EXT2
entrez
2132
canonical
uniprot
Q93063
canonical
ensembl
ENSG00000151348
resolver
ensp
ENSP00000351509
resolver
ensp
ENSP00000379032
resolver
ensp
ENSP00000431173
resolver
ensp
ENSP00000530075
resolver
ensp
ENSP00000792015
resolver
genesymbol
EXT2
resolver
hgnc
HGNC:3513
resolver
uniprot
B2R5Z6
resolver
uniprot
C9JU51
resolver
uniprot
J3KPT2
resolver
uniprot
O15288
resolver
uniprot_entry
EXT2_HUMAN
resolver
uniprot_sec
B2R5Z6
resolver
uniprot_sec
C9JU51
resolver
uniprot_sec
J3KPT2
resolver
uniprot_sec
O15288
resolver
amino_acid_sequence
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEKRSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGVSVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRWDRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEVDLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRCHKHQVFDYPQVLQEATFCVVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKRASVVVPEEKMSDVYSILQSIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYPYAAISYEEWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVPSLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDDIIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFYHKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAIDGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
uniprot
proteins
disease_involvement
DISEASE: Hereditary multiple exostoses 2 (EXT2) [MIM:133701]: EXT is a genetically heterogeneous bone disorder caused by genes segregating on human chromosomes 8, 11, and 19 and designated EXT1, EXT2 and EXT3 respectively. EXT is a dominantly inherited skeletal disorder primarily affecting endochondral bone during growth. The disease is characterized by formation of numerous cartilage-capped, benign bone tumors (osteocartilaginous exostoses or osteochondromas) that are often accompanied by skeletal deformities and short stature. In a small percentage of cases exostoses have exhibited malignant transformation resulting in an osteosarcoma or chondrosarcoma. Osteochondromas development can also occur as a sporadic event. {ECO:0000269|PubMed:10429361, ECO:0000269|PubMed:10480354, ECO:0000269|PubMed:10679296, ECO:0000269|PubMed:10738008, ECO:0000269|PubMed:11169766, ECO:0000269|PubMed:11170095, ECO:0000269|PubMed:11432960, ECO:0000269|PubMed:11668521, ECO:0000269|PubMed:19344451, ECO:0000269|PubMed:9326317}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Seizures, scoliosis, and macrocephaly/microcephaly syndrome (SSMS) [MIM:616682]: An autosomal recessive syndrome characterized by seizures, intellectual disability, hypotonia, scoliosis, macrocephaly, hypertelorism and renal dysfunction. {ECO:0000269|PubMed:26246518}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.1.224
uniprot
proteins
function
FUNCTION: Glycosyltransferase forming with EXT1 the heterodimeric heparan sulfate polymerase which catalyzes the elongation of the heparan sulfate glycan backbone (PubMed:22660413, PubMed:36402845, PubMed:36593275). Glycan backbone extension consists in the alternating transfer of (1->4)-beta-D-GlcA and (1->4)-alpha-D-GlcNAc residues from their respective UDP-sugar donors. Both EXT1 and EXT2 are required for the full activity of the polymerase since EXT1 bears the N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity within the complex while EXT2 carries the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity (PubMed:36402845, PubMed:36593275). Heparan sulfate proteoglycans are ubiquitous components of the extracellular matrix and play an important role in tissue homeostasis and signaling (PubMed:19344451, PubMed:22660413). {ECO:0000269|PubMed:19344451, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:36402845, ECO:0000269|PubMed:36593275}.
uniprot
proteins
mass_dalton
82255
uniprot
proteins
mutagenesis
MUTAGEN 266; /note="R->A: No effect on N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity."; /evidence="ECO:0000269|PubMed:36402845"; MUTAGEN 308; /note="Y->A: Increased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. Decreased glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 325; /note="R->A: Increased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. No effect on glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 328; /note="Q->A: No effect on N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. No effect on glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 538; /note="D->A: Decreased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. Loss of glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 538; /note="D->N: Decreased glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; when associated with N-540."; /evidence="ECO:0000269|PubMed:36402845"; MUTAGEN 540; /note="D->A: Increased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. Decreased glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 540; /note="D->N: Decreased glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; when associated with N-538."; /evidence="ECO:0000269|PubMed:36402845"; MUTAGEN 569; /note="R->A: Increased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. Loss of glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275"; MUTAGEN 585; /note="E->A: Decreased N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity. Decreased glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36593275
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:36402845, ECO:0000269|PubMed:36593275}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated at Asn-637. {ECO:0000269|PubMed:36402845, ECO:0000269|PubMed:36593275}.; PTM: A soluble form is generated by proteolytic processing. {ECO:0000250|UniProtKB:O77783}.
uniprot
proteins
protein_family
Glycosyltransferase 47 family
uniprot
proteins
pubmed
10429361
uniprot
proteins
pubmed
10480354
uniprot
proteins
pubmed
10545594
uniprot
proteins
pubmed
10679296
uniprot
proteins
pubmed
10738008
uniprot
proteins
pubmed
11169766
uniprot
proteins
pubmed
11170095
uniprot
proteins
pubmed
11432960
uniprot
proteins
pubmed
11668521
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18337501
uniprot
proteins
pubmed
19344451
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
26246518
uniprot
proteins
pubmed
35137078
uniprot
proteins
pubmed
36402845
uniprot
proteins
pubmed
36593275
uniprot
proteins
pubmed
8782816
uniprot
proteins
pubmed
8894688
uniprot
proteins
pubmed
9110175
uniprot
proteins
pubmed
9326317
uniprot
proteins
sequence_length
718
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:35137078}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:O77783}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus. If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi. {ECO:0000269|PubMed:10679296}.
uniprot
proteins
transmembrane_region
TRANSMEM 26..46; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins