4R67

Human constitutive 20S proteasome in complex with carfilzomib

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4r67a_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
O	d4r67o_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4r67b_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
DA [auth d]	d4r67d_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
P	d4r67p_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
RA [auth r]	d4r67r_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d4r67c_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	automated matches	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
Q	d4r67q_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	automated matches	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d4r67e_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
S	d4r67s_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d4r67f_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
T	d4r67t_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d4r67g_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
U	d4r67u_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d4r67h_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
V	d4r67v_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
W	d4r67w_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
I	d4r67i_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
J	d4r67j_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
X	d4r67x_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
AB [auth 0]	d4r670_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
K	d4r67k_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
Y	d4r67y_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
BB [auth 3]	d4r673_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
L	d4r67l_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
Z	d4r67z_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
AA [auth 1]	d4r671_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
M	d4r67m_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
BA [auth 2]	d4r672_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
N	d4r67n_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Class II glutamine amidotransferases	8064014	3000131	SCOP2B (2022-06-29)
DA [auth d]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064014	3000131	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Class II glutamine amidotransferases	8064014	3000131	SCOP2B (2022-06-29)
RA [auth r]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064014	3000131	SCOP2B (2022-06-29)
EA [auth e]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064036	3000131	SCOP2B (2022-06-29)
SA [auth s]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064036	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class II glutamine amidotransferases	8064036	3000131	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	Class II glutamine amidotransferases	8064036	3000131	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class II glutamine amidotransferases	8064004	3000131	SCOP2B (2022-06-29)
FA [auth f]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064004	3000131	SCOP2B (2022-06-29)
R	SCOP2B Superfamily	Class II glutamine amidotransferases	8064004	3000131	SCOP2B (2022-06-29)
TA [auth t]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064004	3000131	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Class II glutamine amidotransferases	8064022	3000131	SCOP2B (2022-06-29)
GA [auth g]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064022	3000131	SCOP2B (2022-06-29)
S	SCOP2B Superfamily	Class II glutamine amidotransferases	8064022	3000131	SCOP2B (2022-06-29)
UA [auth u]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064022	3000131	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Class II glutamine amidotransferases	8064060	3000131	SCOP2B (2022-06-29)
HA [auth h]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064060	3000131	SCOP2B (2022-06-29)
T	SCOP2B Superfamily	Class II glutamine amidotransferases	8064060	3000131	SCOP2B (2022-06-29)
VA [auth v]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064060	3000131	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Class II glutamine amidotransferases	8064054	3000131	SCOP2B (2022-06-29)
IA [auth i]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064054	3000131	SCOP2B (2022-06-29)
U	SCOP2B Superfamily	Class II glutamine amidotransferases	8064054	3000131	SCOP2B (2022-06-29)
WA [auth w]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064054	3000131	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Class II glutamine amidotransferases	8079175	3000131	SCOP2B (2022-06-29)
JA [auth j]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079175	3000131	SCOP2B (2022-06-29)
V	SCOP2B Superfamily	Class II glutamine amidotransferases	8079175	3000131	SCOP2B (2022-06-29)
XA [auth x]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079175	3000131	SCOP2B (2022-06-29)
KA [auth k]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064074	3000131	SCOP2B (2022-06-29)
W	SCOP2B Superfamily	Class II glutamine amidotransferases	8064074	3000131	SCOP2B (2022-06-29)
YA [auth y]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064074	3000131	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Class II glutamine amidotransferases	8064074	3000131	SCOP2B (2022-06-29)
BB [auth 3]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079492	3000131	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Class II glutamine amidotransferases	8079492	3000131	SCOP2B (2022-06-29)
NA [auth n]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079492	3000131	SCOP2B (2022-06-29)
Z	SCOP2B Superfamily	Class II glutamine amidotransferases	8079492	3000131	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
CA [auth c]	Proteasome	e4r67c1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
QA [auth q]	Proteasome	e4r67q1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
A	Proteasome	e4r67A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O	Proteasome	e4r67O1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B	Proteasome	e4r67B1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DA [auth d]	Proteasome	e4r67d1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P	Proteasome	e4r67P1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
RA [auth r]	Proteasome	e4r67r1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
EA [auth e]	Proteasome	e4r67e1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
SA [auth s]	Proteasome	e4r67s1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C	Proteasome	e4r67C1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q	Proteasome	e4r67Q1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D	Proteasome	e4r67D1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
FA [auth f]	Proteasome	e4r67f1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R	Proteasome	e4r67R1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
TA [auth t]	Proteasome	e4r67t1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E	Proteasome	e4r67E1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
GA [auth g]	Proteasome	e4r67g1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S	Proteasome	e4r67S1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
UA [auth u]	Proteasome	e4r67u1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F	Proteasome	e4r67F1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
HA [auth h]	Proteasome	e4r67h1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T	Proteasome	e4r67T1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
VA [auth v]	Proteasome	e4r67v1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G	Proteasome	e4r67G1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
IA [auth i]	Proteasome	e4r67i1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U	Proteasome	e4r67U1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
WA [auth w]	Proteasome	e4r67w1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H	Proteasome	e4r67H1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
JA [auth j]	Proteasome	e4r67j1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V	Proteasome	e4r67V1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
XA [auth x]	Proteasome	e4r67x1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
KA [auth k]	Proteasome	e4r67k1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W	Proteasome	e4r67W1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
YA [auth y]	Proteasome	e4r67y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I	Proteasome	e4r67I1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J	Proteasome	e4r67J1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
LA [auth l]	Proteasome	e4r67l1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X	Proteasome	e4r67X1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
ZA [auth z]	Proteasome	e4r67z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AB [auth 0]	Proteasome	e4r6701	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K	Proteasome	e4r67K1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
MA [auth m]	Proteasome	e4r67m1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y	Proteasome	e4r67Y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BB [auth 3]	Proteasome	e4r6731	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L	Proteasome	e4r67L1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
NA [auth n]	Proteasome	e4r67n1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z	Proteasome	e4r67Z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth 1]	Proteasome	e4r6711	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
CB [auth a]	Proteasome	e4r67a1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
OA [auth o]	Proteasome	e4r67o1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M	Proteasome	e4r67M1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth 2]	Proteasome	e4r6721	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DB [auth b]	Proteasome	e4r67b1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
PA [auth p]	Proteasome	e4r67p1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N	Proteasome	e4r67N1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
CA [auth c]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
QA [auth q]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
A	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
O	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
B	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
DA [auth d]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
P	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
RA [auth r]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
EA [auth e]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
SA [auth s]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
C	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
Q	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
D	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
FA [auth f]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
R	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
TA [auth t]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
E	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
GA [auth g]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
S	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
UA [auth u]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
F	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
HA [auth h]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
T	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
VA [auth v]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
G	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
IA [auth i]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
U	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
WA [auth w]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
H	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
JA [auth j]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
V	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
XA [auth x]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
KA [auth k]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
W	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
YA [auth y]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
I	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
J	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
LA [auth l]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
X	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
ZA [auth z]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
AB [auth 0]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
K	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
MA [auth m]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
Y	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
BB [auth 3]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
L	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
NA [auth n]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
Z	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
AA [auth 1]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
CB [auth a]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
OA [auth o]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
M	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
BA [auth 2]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
DB [auth b]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
PA [auth p]	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
N	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, CA [auth c], O, QA [auth q]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
A, CA [auth c], O, QA [auth q]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
B, DA [auth d], P, RA [auth r]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
B, DA [auth d], P, RA [auth r]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
C, EA [auth e], Q, SA [auth s]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
C, EA [auth e], Q, SA [auth s]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
D, FA [auth f], R, TA [auth t]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
D, FA [auth f], R, TA [auth t]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
E, GA [auth g], S, UA [auth u]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
E, GA [auth g], S, UA [auth u]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
F, HA [auth h], T, VA [auth v]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
F, HA [auth h], T, VA [auth v]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
G, IA [auth i], U, WA [auth w]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
G, IA [auth i], U, WA [auth w]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
H, JA [auth j], V, XA [auth x]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
H, JA [auth j], V, XA [auth x]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
I, KA [auth k], W, YA [auth y]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
I, KA [auth k], W, YA [auth y]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
I, KA [auth k], W, YA [auth y]	PF12465	Proteasome beta subunits C terminal (Pr_beta_C)	Proteasome beta subunits C terminal	-	Family
J, LA [auth l], X, ZA [auth z]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
AB [auth 0], K, MA [auth m], Y	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
AB [auth 0], K, MA [auth m], Y	PF12465	Proteasome beta subunits C terminal (Pr_beta_C)	Proteasome beta subunits C terminal	-	Family
BB [auth 3], L, NA [auth n], Z	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
AA [auth 1], CB [auth a], M, OA [auth o]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
BA [auth 2], DB [auth b], N, PA [auth p]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, CA [auth c], O, QA [auth q]	Proteasome subunit alpha type-6	transcription factor binding RNA polymerase II-specific DNA-binding transcription factor binding protein binding binding DNA-binding transcription factor binding NF-kappaB binding RNA binding organic cyclic compound binding nucleic acid binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity transcription factor binding RNA polymerase II-specific DNA-binding transcription factor binding protein binding binding DNA-binding transcription factor binding NF-kappaB binding RNA binding organic cyclic compound binding nucleic acid binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding anion binding heterocyclic compound binding small molecule binding	catabolic process proteolysis involved in protein catabolic process proteolysis metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteasomal protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process catabolic process proteolysis involved in protein catabolic process proteolysis metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteasomal protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process positive regulation of DNA-binding transcription factor activity regulation of cellular process cellular biosynthetic process positive regulation of NF-kappaB transcription factor activity RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process positive regulation of molecular function nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process cellular metabolic process biological regulation regulation of cellular metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process regulation of molecular function regulation of gene expression biosynthetic process regulation of DNA-binding transcription factor activity regulation of macromolecule biosynthetic process cellular process regulation of DNA-templated transcription regulation of metabolic process regulation of defense response response to stimulus regulation of response to external stimulus defense response regulation of inflammatory response response to external stimulus regulation of response to stimulus response to stress regulation of response to stress inflammatory response	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity intracellular organelle lumen intracellular organelle organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix protein-containing complex membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity intracellular organelle lumen intracellular organelle organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix protein-containing complex proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytoplasm cytosol nucleoplasm intracellular non-membrane-bounded organelle ribosome non-membrane-bounded organelle sarcomere contractile muscle fiber supramolecular fiber myofibril supramolecular polymer supramolecular complex cytoplasmic ribonucleoprotein granule ribonucleoprotein granule P-body
B, DA [auth d], P, RA [auth r]	Proteasome subunit alpha type-2	-	biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to external stimulus response to external biotic stimulus response to virus response to biotic stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to external stimulus response to external biotic stimulus response to virus response to biotic stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex extracellular exosome membrane-bounded organelle extracellular vesicle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle vesicle lumen intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen secretory granule secretory vesicle cytoplasm cytosol cytoplasmic ribonucleoprotein granule ribonucleoprotein granule intracellular non-membrane-bounded organelle supramolecular complex P-body non-membrane-bounded organelle ficolin-1-rich granule ficolin-1-rich granule lumen nucleus nucleoplasm nuclear lumen
C, EA [auth e], Q, SA [auth s]	Proteasome subunit alpha type-4	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle cytoplasm cytosol intracellular organelle intracellular membrane-bounded organelle cytoplasmic ribonucleoprotein granule ribonucleoprotein granule intracellular non-membrane-bounded organelle supramolecular complex P-body non-membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
D, FA [auth f], R, TA [auth t]	Proteasome subunit alpha type-7	identical protein binding protein binding binding	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle cytoplasm cytosol postsynapse synapse cell junction nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen
E, GA [auth g], S, UA [auth u]	Proteasome subunit alpha type-5	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex extracellular exosome membrane-bounded organelle extracellular vesicle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle vesicle lumen intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen secretory granule secretory vesicle cytoplasm cytosol ficolin-1-rich granule ficolin-1-rich granule lumen nucleus nucleoplasm nuclear lumen
F, HA [auth h], T, VA [auth v]	Proteasome subunit alpha type-1	binding lipid binding lipopolysaccharide binding carbohydrate derivative binding	immune system process regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response immune system process regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus negative regulation of immune response regulation of inflammatory response to antigenic stimulus biological regulation response to external stimulus regulation of inflammatory response regulation of response to stimulus negative regulation of immune system process negative regulation of response to external stimulus negative regulation of defense response regulation of immune response inflammatory response catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular organelle centrosome microtubule organizing center cytoskeleton intracellular non-membrane-bounded organelle microtubule cytoskeleton non-membrane-bounded organelle cytoplasm cytosol nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
G, IA [auth i], U, WA [auth w]	Proteasome subunit alpha type-3	ubiquitin protein ligase binding protein binding binding ubiquitin-like protein ligase binding enzyme binding	regulation of biological process regulation of catalytic activity regulation of protein metabolic process regulation of peptidase activity biological regulation primary metabolic process regulation of macromolecule metabolic process regulation of primary metabolic process regulation of molecular function regulation of proteolysis proteolysis regulation of hydrolase activity regulation of endopeptidase activity metabolic process regulation of biological process regulation of catalytic activity regulation of protein metabolic process regulation of peptidase activity biological regulation primary metabolic process regulation of macromolecule metabolic process regulation of primary metabolic process regulation of molecular function regulation of proteolysis proteolysis regulation of hydrolase activity regulation of endopeptidase activity metabolic process protein metabolic process macromolecule metabolic process regulation of metabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle synapse cell junction cytoplasm cytosol nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen
H, JA [auth j], V, XA [auth x]	Proteasome subunit beta type-6	cell adhesion molecule binding cadherin binding protein binding binding peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
I, KA [auth k], W, YA [auth y]	Proteasome subunit beta type-7	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen organelle secretory granule secretory vesicle cytoplasm vesicle cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus nuclear body nucleoplasm nuclear lumen ficolin-1-rich granule ficolin-1-rich granule lumen
J, LA [auth l], X, ZA [auth z]	Proteasome subunit beta type-3	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen
AB [auth 0], K, MA [auth m], Y	Proteasome subunit beta type-2	-	response to stimulus response to chemical response to organic cyclic compound catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process response to stimulus response to chemical response to organic cyclic compound catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen
BB [auth 3], L, NA [auth n], Z	Proteasome subunit beta type-5	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	response to oxidative stress response to stimulus response to stress proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process response to oxidative stress response to stimulus response to stress proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular organelle centrosome microtubule organizing center intracellular anatomical structure cytoskeleton intracellular non-membrane-bounded organelle microtubule cytoskeleton non-membrane-bounded organelle cytoplasm cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
AA [auth 1], CB [auth a], M, OA [auth o]	Proteasome subunit beta type-1	-	catabolic process proteolysis involved in protein catabolic process proteolysis metabolic process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteasomal protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular region cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen secretory granule secretory vesicle cytoplasm cytosol proteasome core complex proteasome core complex, beta-subunit complex ficolin-1-rich granule ficolin-1-rich granule lumen nucleus nucleoplasm nuclear lumen
BA [auth 2], DB [auth b], N, PA [auth p]	Proteasome subunit beta type-4	binding lipid binding lipopolysaccharide binding carbohydrate derivative binding	regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus negative regulation of immune response regulation of inflammatory response to antigenic stimulus biological regulation response to external stimulus regulation of inflammatory response regulation of response to stimulus negative regulation of immune system process immune system process negative regulation of response to external stimulus negative regulation of defense response regulation of immune response inflammatory response catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytosol proteasome core complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen cilium plasma membrane bounded cell projection ciliary basal body cell projection microtubule organizing center cytoskeleton intracellular non-membrane-bounded organelle microtubule cytoskeleton non-membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, CA [auth c], O, QA [auth q]	IPR034642	Proteasome subunit alpha6	Family
A, CA [auth c], O, QA [auth q]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
A, CA [auth c], O, QA [auth q]	IPR050115	Proteasome subunit alpha	Family
A, CA [auth c], O, QA [auth q]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, CA [auth c], O, QA [auth q]	IPR023332	Proteasome alpha-type subunit	Family
A, CA [auth c], O, QA [auth q]	IPR001353	Proteasome, subunit alpha/beta	Family
B, DA [auth d], P, RA [auth r]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
B, DA [auth d], P, RA [auth r]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
B, DA [auth d], P, RA [auth r]	IPR050115	Proteasome subunit alpha	Family
B, DA [auth d], P, RA [auth r]	IPR023332	Proteasome alpha-type subunit	Family
B, DA [auth d], P, RA [auth r]	IPR001353	Proteasome, subunit alpha/beta	Family
C, EA [auth e], Q, SA [auth s]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
C, EA [auth e], Q, SA [auth s]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
C, EA [auth e], Q, SA [auth s]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
C, EA [auth e], Q, SA [auth s]	IPR050115	Proteasome subunit alpha	Family
C, EA [auth e], Q, SA [auth s]	IPR023332	Proteasome alpha-type subunit	Family
C, EA [auth e], Q, SA [auth s]	IPR001353	Proteasome, subunit alpha/beta	Family
D, FA [auth f], R, TA [auth t]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
D, FA [auth f], R, TA [auth t]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
D, FA [auth f], R, TA [auth t]	IPR050115	Proteasome subunit alpha	Family
D, FA [auth f], R, TA [auth t]	IPR023332	Proteasome alpha-type subunit	Family
D, FA [auth f], R, TA [auth t]	IPR001353	Proteasome, subunit alpha/beta	Family
E, GA [auth g], S, UA [auth u]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
E, GA [auth g], S, UA [auth u]	IPR033812	Proteasome subunit alpha5	Family
E, GA [auth g], S, UA [auth u]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
E, GA [auth g], S, UA [auth u]	IPR050115	Proteasome subunit alpha	Family
E, GA [auth g], S, UA [auth u]	IPR023332	Proteasome alpha-type subunit	Family
E, GA [auth g], S, UA [auth u]	IPR001353	Proteasome, subunit alpha/beta	Family
F, HA [auth h], T, VA [auth v]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
F, HA [auth h], T, VA [auth v]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
F, HA [auth h], T, VA [auth v]	IPR050115	Proteasome subunit alpha	Family
F, HA [auth h], T, VA [auth v]	IPR035144	Proteasome subunit alpha 1	Family
F, HA [auth h], T, VA [auth v]	IPR023332	Proteasome alpha-type subunit	Family
F, HA [auth h], T, VA [auth v]	IPR001353	Proteasome, subunit alpha/beta	Family
G, IA [auth i], U, WA [auth w]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
G, IA [auth i], U, WA [auth w]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
G, IA [auth i], U, WA [auth w]	IPR050115	Proteasome subunit alpha	Family
G, IA [auth i], U, WA [auth w]	IPR023332	Proteasome alpha-type subunit	Family
G, IA [auth i], U, WA [auth w]	IPR001353	Proteasome, subunit alpha/beta	Family
H, JA [auth j], V, XA [auth x]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
H, JA [auth j], V, XA [auth x]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
H, JA [auth j], V, XA [auth x]	IPR023333	Proteasome B-type subunit	Family
H, JA [auth j], V, XA [auth x]	IPR001353	Proteasome, subunit alpha/beta	Family
H, JA [auth j], V, XA [auth x]	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
I, KA [auth k], W, YA [auth y]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
I, KA [auth k], W, YA [auth y]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
I, KA [auth k], W, YA [auth y]	IPR024689	Proteasome beta subunit, C-terminal	Domain
I, KA [auth k], W, YA [auth y]	IPR023333	Proteasome B-type subunit	Family
I, KA [auth k], W, YA [auth y]	IPR001353	Proteasome, subunit alpha/beta	Family
I, KA [auth k], W, YA [auth y]	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
J, LA [auth l], X, ZA [auth z]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
J, LA [auth l], X, ZA [auth z]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
J, LA [auth l], X, ZA [auth z]	IPR023333	Proteasome B-type subunit	Family
J, LA [auth l], X, ZA [auth z]	IPR001353	Proteasome, subunit alpha/beta	Family
J, LA [auth l], X, ZA [auth z]	IPR033811	Proteasome beta 3 subunit	Family
AB [auth 0], K, MA [auth m], Y	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
AB [auth 0], K, MA [auth m], Y	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AB [auth 0], K, MA [auth m], Y	IPR023333	Proteasome B-type subunit	Family
AB [auth 0], K, MA [auth m], Y	IPR050115	Proteasome subunit alpha	Family
AB [auth 0], K, MA [auth m], Y	IPR001353	Proteasome, subunit alpha/beta	Family
AB [auth 0], K, MA [auth m], Y	IPR035206	Proteasome subunit beta 2	Family
BB [auth 3], L, NA [auth n], Z	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
BB [auth 3], L, NA [auth n], Z	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
BB [auth 3], L, NA [auth n], Z	IPR023333	Proteasome B-type subunit	Family
BB [auth 3], L, NA [auth n], Z	IPR001353	Proteasome, subunit alpha/beta	Family
BB [auth 3], L, NA [auth n], Z	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
AA [auth 1], CB [auth a], M, OA [auth o]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
AA [auth 1], CB [auth a], M, OA [auth o]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AA [auth 1], CB [auth a], M, OA [auth o]	IPR023333	Proteasome B-type subunit	Family
AA [auth 1], CB [auth a], M, OA [auth o]	IPR001353	Proteasome, subunit alpha/beta	Family
BA [auth 2], DB [auth b], N, PA [auth p]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
BA [auth 2], DB [auth b], N, PA [auth p]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
BA [auth 2], DB [auth b], N, PA [auth p]	IPR023333	Proteasome B-type subunit	Family
BA [auth 2], DB [auth b], N, PA [auth p]	IPR016295	Proteasome subunit beta 4	Family
BA [auth 2], DB [auth b], N, PA [auth p]	IPR001353	Proteasome, subunit alpha/beta	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, CA [auth c], O, QA [auth q]	Pharos: P60900	HIV infectious disease myocardial infarction HIV Coinfection psoriasis
B, DA [auth d], P, RA [auth r]	Pharos: P25787	osteoporosis heart disease breast cancer malignant mesothelioma Osteoporosis, Senile psoriasis colorectal cancer ovarian cancer
C, EA [auth e], Q, SA [auth s]	Pharos: P25789	Mammary Neoplasms, Experimental sarcomatoid carcinoma adult acute respiratory distress syndrome carcinoma HIV infectious disease liver cancer lung carcinoma mammary neoplasms, animal ovarian cancer polycystic ovary syndrome abdominal aortic aneurysm small cell lung carcinoma bipolar disorder bronchitis chronic obstructive pulmonary disease Mammary Neoplasms, Experimental sarcomatoid carcinoma adult acute respiratory distress syndrome carcinoma HIV infectious disease liver cancer lung carcinoma mammary neoplasms, animal ovarian cancer polycystic ovary syndrome abdominal aortic aneurysm small cell lung carcinoma bipolar disorder bronchitis chronic obstructive pulmonary disease liver neoplasm lymphoplasmacytic lymphoma peripheral arterial disease squamous cell lung carcinoma anorexia nervosa brain aneurysm dental caries lung adenocarcinoma nicotine dependence plasma cell myeloma Sjogren syndrome undifferentiated carcinoma autism spectrum disorder breast cancer dermatomyositis
D, FA [auth f], R, TA [auth t]	Pharos: O14818	breast cancer lung cancer pancreatic intraductal papillary-mucinous carcinoma glioblastoma medulloblastoma plasma cell myeloma intellectual disability ovarian cancer Sjogren syndrome
E, GA [auth g], S, UA [auth u]	Pharos: P28066	HIV infectious disease osteoporosis non-small cell lung carcinoma Osteoporosis, Age-Related ovarian cancer pancreatic intraductal papillary-mucinous neoplasm Alzheimer disease pilocytic astrocytoma cystic fibrosis primitive neuroectodermal tumor fatty liver disease tuberculosis glioblastoma lung cancer malignant glioma HIV infectious disease osteoporosis non-small cell lung carcinoma Osteoporosis, Age-Related ovarian cancer pancreatic intraductal papillary-mucinous neoplasm Alzheimer disease pilocytic astrocytoma cystic fibrosis primitive neuroectodermal tumor fatty liver disease tuberculosis glioblastoma lung cancer malignant glioma oligodendroglioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia astrocytic tumor pituitary cancer diabetes mellitus psoriasis gastric cancer hepatocellular carcinoma invasive ductal breast carcinoma lymphoplasmacytic lymphoma medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma Pick disease atypical teratoid rhabdoid tumor gastric carcinoma large cell medulloblastoma malignant ependymoma
F, HA [auth h], T, VA [auth v]	Pharos: P25786	mantle cell lymphoma plasma cell myeloma Systemic AL amyloidosis
G, IA [auth i], U, WA [auth w]	Pharos: P25788	attention deficit hyperactivity disorder, inattentive type lymphoplasmacytic lymphoma pancreatic ductal adenocarcinoma Sjogren syndrome dermatomyositis osteosarcoma plasma cell myeloma heart disease ovarian cancer psoriasis
H, JA [auth j], V, XA [auth x]	Pharos: P28072	attention deficit hyperactivity disorder, inattentive type ovarian cancer psoriasis brain aneurysm pancreatic ductal adenocarcinoma Sjogren syndrome lung cancer plasma cell myeloma systemic lupus erythematosus
I, KA [auth k], W, YA [auth y]	Pharos: Q99436	atrial fibrillation allergic rhinitis hepatocellular carcinoma malignant ependymoma pancreatic intraductal papillary-mucinous carcinoma peripheral nervous system disease plasma cell myeloma astrocytic tumor hypothyroidism oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm peripheral neuropathy vitiligo lymphoplasmacytic lymphoma ovarian cancer atrial fibrillation allergic rhinitis hepatocellular carcinoma malignant ependymoma pancreatic intraductal papillary-mucinous carcinoma peripheral nervous system disease plasma cell myeloma astrocytic tumor hypothyroidism oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm peripheral neuropathy vitiligo lymphoplasmacytic lymphoma ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia Pick disease
J, LA [auth l], X, ZA [auth z]	Pharos: P49720	chronic obstructive pulmonary disease lymphoplasmacytic lymphoma diabetes mellitus ovarian cancer glioblastoma plasma cell myeloma
AB [auth 0], K, MA [auth m], Y	Pharos: P49721	urinary bladder cancer atypical teratoid rhabdoid tumor glioblastoma lung carcinoma osteosarcoma Sjogren syndrome breast cancer invasive ductal breast carcinoma malignant mesothelioma ovarian cancer Systemic AL amyloidosis urinary bladder neoplasm diabetes mellitus large cell medulloblastoma mantle cell lymphoma urinary bladder cancer atypical teratoid rhabdoid tumor glioblastoma lung carcinoma osteosarcoma Sjogren syndrome breast cancer invasive ductal breast carcinoma malignant mesothelioma ovarian cancer Systemic AL amyloidosis urinary bladder neoplasm diabetes mellitus large cell medulloblastoma mantle cell lymphoma plasma cell myeloma systemic lupus erythematosus
BB [auth 3], L, NA [auth n], Z	Pharos: P28074	plasma cell myeloma acute lymphoblastic leukemia diabetes mellitus mantle cell lymphoma ovarian cancer Relapse multiple myeloma B-cell acute lymphoblastic leukemia hypertensive disorder medulloblastoma coronary artery disease lung cancer myocardial ischemia psoriasis
AA [auth 1], CB [auth a], M, OA [auth o]	Pharos: P20618	acute coronary syndrome peripheral neuropathy plasma cell myeloma peripheral nervous system disease lymphoplasmacytic lymphoma osteoarthritis ovarian cancer dermatomyositis malignant colon neoplasm osteoarthritis susceptibility 1 pancreatic ductal adenocarcinoma glioblastoma mantle cell lymphoma Osteoarthrosis Deformans
BA [auth 2], DB [auth b], N, PA [auth p]	Pharos: P28070	HIV infectious disease HIV Coinfection lymphoplasmacytic lymphoma plasma cell myeloma Sjogren syndrome major depressive disorder proteasome-associated autoinflammatory syndrome 3 lung cancer ovarian cancer psoriasis