Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B Superfamily14-3-3 protein 8034961 3001329 SCOP2B (2022-06-29)
BSCOP2B Superfamily14-3-3 protein 8034961 3001329 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyProtein kinase-like (PK-like) 8035244 3000066 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyProtein kinase-like (PK-like) 8035244 3000066 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A14-3-3e6u2hA1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: 14-3-3ECOD (1.6)
B14-3-3e6u2hB1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: 14-3-3ECOD (1.6)
CPkinase_Tyre6u2hC1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: Pkinase_TyrECOD (1.6)
DPkinase_Tyre6u2hD1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: Pkinase_TyrECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.20.190.20 Mainly Alpha Up-down Bundle Delta-Endotoxin domain 1CATH (utative)
B1.20.190.20 Mainly Alpha Up-down Bundle Delta-Endotoxin domain 1CATH (utative)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF0024414-3-3 protein (14-3-3)14-3-3 protein- Repeat
C, D
PF07714Protein tyrosine and serine/threonine kinase (PK_Tyr_Ser-Thr)Protein tyrosine and serine/threonine kinaseProtein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosph ...Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
14-3-3 protein zeta/delta
C, D
Serine/threonine-protein kinase B-raf

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP63104
C, D
PharosP15056

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
C, D
SEP Parent Component: SER

RESIDAA0037

PSI-MOD :  O-phospho-L-serine MOD:00046