5GGI

Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with Mn, UDP and Mannosyl-peptide

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	FAM3B/PANDER-like	8055726	3002300	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)
A	GNT-I	e5ggiA1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: GNT-I	ECOD (1.6)
B	ILEI	e5ggiB1	A: a+b two layers	X: FAM3 superfamily (From Topology)	H: FAM3 superfamily (From Topology)	T: FAM3 superfamily	F: ILEI	ECOD (1.6)
B	GNT-I	e5ggiB2	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: GNT-I	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03071	GNT-I family (GNT-I)	GNT-I family	-	Family
A, B	PF15711	Interleukin-like EMT inducer (ILEI)	Interleukin-like EMT inducer	ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fib ...	ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localisation, is associated with EMT in human cancerous tissue [1]. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1	binding carbohydrate binding UDP-glycosyltransferase activity beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity glycosyltransferase activity catalytic activity, acting on a protein catalytic activity, acting on a glycoprotein acetylglucosaminyltransferase activity transferase activity hexosyltransferase activity catalytic activity cation binding manganese ion binding transition metal ion binding binding carbohydrate binding UDP-glycosyltransferase activity beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity glycosyltransferase activity catalytic activity, acting on a protein catalytic activity, acting on a glycoprotein acetylglucosaminyltransferase activity transferase activity hexosyltransferase activity catalytic activity cation binding manganese ion binding transition metal ion binding ion binding metal ion binding small molecule binding	biosynthetic process metabolic process cellular process macromolecule metabolic process gene expression macromolecule biosynthetic process localization localization of cell multicellular organismal process system process sensory perception nervous system process sensory perception of sound sensory perception of mechanical stimulus biosynthetic process metabolic process cellular process macromolecule metabolic process gene expression macromolecule biosynthetic process localization localization of cell multicellular organismal process system process sensory perception nervous system process sensory perception of sound sensory perception of mechanical stimulus developmental process head development forebrain development animal organ development brain development nervous system development dentate gyrus development pallium development multicellular organism development central nervous system development anatomical structure development telencephalon development hippocampus development limbic system development system development myelination axon ensheathment ensheathment of neurons carbohydrate derivative biosynthetic process protein mannosylation glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein glycosylation protein O-linked mannosylation glycosylation mannosylation macromolecule modification macromolecule glycosylation protein O-linked glycosylation protein metabolic process protein modification process O-glycan processing response to stimulus defense response response to stress reactive gliosis inflammatory response neuroinflammatory response cellular component organization extracellular matrix organization cellular component organization or biogenesis basement membrane organization extracellular structure organization external encapsulating structure organization	cellular anatomical structure membrane membrane-bounded organelle Golgi membrane intracellular anatomical structure Golgi apparatus intracellular membrane-bounded organelle endomembrane system intracellular organelle bounding membrane of organelle organelle cytoplasm organelle membrane
C [auth F], D [auth G]	mannosyl-peptide	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR039477	ILEI/PANDER domain	Domain
A, B	IPR004139	Glycosyl transferase, family 13	Family
A, B	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily
A, B	IPR039474	Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1, PANDER-like domain	Domain
A, B	IPR052463	O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: Q8WZA1	autosomal recessive limb-girdle muscular dystrophy type 2O limb-girdle muscular dystrophy retinitis pigmentosa muscular dystrophy-dystroglycanopathy, type A muscular dystrophy-dystroglycanopathy (congenital with brain and eye anomalies), type A3 congenital muscular dystrophy muscular dystrophy-dystroglycanopathy (congenital with intellectual disability), type B3 retinitis pigmentosa 76 lissencephaly spectrum disorders malignant glioma muscle tissue disease muscular dystrophy alpha-Dystroglycanopathies retinal degeneration cerebrovascular disorder autosomal recessive limb-girdle muscular dystrophy type 2O limb-girdle muscular dystrophy retinitis pigmentosa muscular dystrophy-dystroglycanopathy, type A muscular dystrophy-dystroglycanopathy (congenital with brain and eye anomalies), type A3 congenital muscular dystrophy muscular dystrophy-dystroglycanopathy (congenital with intellectual disability), type B3 retinitis pigmentosa 76 lissencephaly spectrum disorders malignant glioma muscle tissue disease muscular dystrophy alpha-Dystroglycanopathies retinal degeneration cerebrovascular disorder hydrocephalus medulloblastoma muscle-eye-brain disease muscular dystrophy-dystroglycanopathy arthrogryposis myopathy cataract cone-rod dystrophy intellectual disability malignant ependymoma muscular disease muscular dystrophy-dystroglycanopathy (congenital with brain and eye anomalies), type A, 4 atypical teratoid rhabdoid tumor osteosarcoma congenital disorder of glycosylation glioblastoma large cell medulloblastoma lung carcinoma

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C [auth F], D [auth G]	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359
C [auth F], D [auth G]	NH2	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 , L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.