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Q16394 (EXT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-1

EC=2.4.1.224
EC=2.4.1.225
Alternative name(s):
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses protein 1
Putative tumor suppressor protein EXT1
Gene names
Name:EXT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Ref.7

Catalytic activity

UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan.

UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Forms a homo/hetero-oligomeric complex with EXT2. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note: The EXT1/EXT2 complex is localized in the Golgi apparatus. Ref.6

Tissue specificity

Ubiquitous.

Involvement in disease

Hereditary multiple exostoses 1 (EXT1) [MIM:133700]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A syndrome that combines the clinical features of tricho-rhino-phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation.
Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.

Chondrosarcoma (CHDSA) [MIM:215300]: A malignant neoplasm derived from cartilage cells. Chondrosarcomas range from slow-growing non-metastasizing lesions to highly aggressive metastasizing sarcomas.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   DiseaseDisease mutation
Hereditary multiple exostoses
Tumor suppressor
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular polysaccharide biosynthetic process

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

embryonic skeletal joint development

Inferred from electronic annotation. Source: Ensembl

endoderm development

Inferred from electronic annotation. Source: Ensembl

gastrulation

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan biosynthetic process

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

heparan sulfate proteoglycan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Inferred from mutant phenotype PubMed 17761672. Source: BHF-UCL

mesoderm development

Inferred from electronic annotation. Source: Ensembl

olfactory bulb development

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

protein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

signal transduction

Traceable author statement PubMed 10878610. Source: ProtInc

skeletal system development

Traceable author statement PubMed 9620772. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 10639137. Source: BHF-UCL

Golgi membrane

Traceable author statement PubMed 12907669. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay PubMed 9620772. Source: BHF-UCL

endoplasmic reticulum membrane

Non-traceable author statement PubMed 9620772. Source: BHF-UCL

integral component of endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Traceable author statement PubMed 9620772. Source: ProtInc

   Molecular_functionN-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

acetylglucosaminyltransferase activity

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

glucuronosyltransferase activity

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

heparan sulfate N-acetylglucosaminyltransferase activity

Non-traceable author statement PubMed 12907669. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 12907669. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

transferase activity, transferring glycosyl groups

Inferred from direct assay PubMed 12907669. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Exostosin-1
PRO_0000149648

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 746718Lumenal Potential

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential

Natural variations

Natural variant271Q → K in EXT1; no loss of activity.
VAR_012815
Natural variant1641D → H in EXT1; loss of activity. Ref.14
VAR_012816
Natural variant215 – 2228MLAKASIS → I in isolated osteochondroma; somatic mutation.
VAR_012818
Natural variant215 – 2217Missing in EXT1.
VAR_012817
Natural variant235 – 2395Missing in multiple osteochondromas.
VAR_012819
Natural variant2801R → G in EXT1; loss of activity. Ref.9 Ref.12 Ref.13
VAR_002370
Natural variant2801R → S in EXT1; loss of activity. Ref.13
VAR_002371
Natural variant3161N → S in chondrosarcoma; no loss of activity. Ref.14
VAR_012820
Natural variant3391G → D in EXT1; loss of activity. Ref.11
VAR_002372
Natural variant3401R → C in EXT1; loss of activity; still able to form an oligomeric complex. Ref.11
VAR_002373
Natural variant3401R → H in EXT1; loss of activity. Ref.9 Ref.13
VAR_002374
Natural variant3401R → L in EXT1; loss of activity. Ref.10
VAR_002375
Natural variant3401R → S in EXT1; loss of activity. Ref.12
VAR_002376
Natural variant4861A → V in EXT1; no loss of activity. Ref.15
Corresponds to variant rs188859975 [ dbSNP | Ensembl ].
VAR_012821
Natural variant4961P → L in EXT1; no loss of activity. Ref.15
VAR_012822
Natural variant6271Missing in EXT1; loss of activity. Ref.13
VAR_002377

Experimental info

Mutagenesis271Q → A or P: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis271Missing: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis1641D → E: Abolishes heparan-sulfate biosynthesis. Ref.17
Mutagenesis1641Missing: Abolishes heparan-sulfate biosynthesis. Ref.17
Mutagenesis3161N → A: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis3161Missing: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis4861A → H: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis4861Missing: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis4961P → H: No effect on heparan-sulfate biosynthesis. Ref.17
Mutagenesis4961Missing: No effect on heparan-sulfate biosynthesis. Ref.17
Sequence conflict60 – 612DA → EP Ref.1
Sequence conflict60 – 612DA → EP Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q16394 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 842CD7E6C1312C1A

FASTA74686,255
        10         20         30         40         50         60 
MQAKKRYFIL LSAGSCLALL FYFGGLQFRA SRSHSRREEH SGRNGLHHPS PDHFWPRFPD 

        70         80         90        100        110        120 
ALRPFVPWDQ LENEDSSVHI SPRQKRDANS SIYKGKKCRM ESCFDFTLCK KNGFKVYVYP 

       130        140        150        160        170        180 
QQKGEKIAES YQNILAAIEG SRFYTSDPSQ ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS 

       190        200        210        220        230        240 
LHLWNNGRNH LIFNLYSGTW PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD 

       250        260        270        280        290        300 
HPRTGGERGF LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVVLLTTCKH 

       310        320        330        340        350        360 
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA LQAACVPVML 

       370        380        390        400        410        420 
SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK ILALRQQTQF LWEAYFSSVE 

       430        440        450        460        470        480 
KIVLTTLEII QDRIFKHISR NSLIWNKHPG GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF 

       490        500        510        520        530        540 
TAVIHAVTPL VSQSQPVLKL LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVVVIE 

       550        560        570        580        590        600 
GESKVMSSRF LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWQSFPERIV GYPARSHFWD 

       610        620        630        640        650        660 
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYSHYLPA SLKNMVDQLA NCEDILMNFL 

       670        680        690        700        710        720 
VSAVTKLPPI KVTQKKQYKE TMMGQTSRAS RWADPDHFAQ RQSCMNTFAS WFGYMPLIHS 

       730        740 
QMRLDPVLFK DQVSILRKKY RDIERL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the putative tumour suppressor gene for hereditary multiple exostoses (EXT1)."
Ahn J., Luedecke H.-J., Lindow S., Horton W.A., Lee B., Wagner M.J., Horsthemke B., Wells D.E.
Nat. Genet. 11:137-143(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Genomic organization and promoter structure of the human EXT1 gene."
Luedecke H.-J., Ahn J., Lin X., Hill A., Wagner M.J., Schomburg L., Horsthemke B., Wells D.E.
Genomics 40:351-354(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-320.
Tissue: Lung.
[6]"Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus."
Kobayashi S., Morimoto K., Shimizu T., Takahashi M., Kurosawa H., Shirasawa T.
Biochem. Biophys. Res. Commun. 268:860-867(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[7]"The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins."
Duncan G., McCormick C., Tufaro F.
J. Clin. Invest. 108:511-516(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes."
Wuyts W., Van Hul W.
Hum. Mutat. 15:220-227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[9]"Spectrum of EXT1 mutations in hereditary multiple exostoses."
Raskind W.H., Matsushita M., Conrad E.U. III, Wells D.E., Sandell L.J., Wagner M.J., Houck J.
Am. J. Hum. Genet. 59:A280-A280(1996)
Cited for: VARIANTS EXT1 GLY-280 AND HIS-340.
[10]"Hereditary multiple exostoses (EXT): mutational studies of familial EXT1 cases and EXT-associated malignancies."
Hecht J.T., Hogue D.A., Wang Y., Blanton S.H., Wagner M.J., Strong L.C., Raskind W.H., Hansen M.F., Wells D.E.
Am. J. Hum. Genet. 60:80-86(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT1 LEU-340.
[11]"Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses."
Philippe C., Porter D.E., Emerton M.E., Wells D.E., Simpson A.H.R.W., Monaco A.P.
Am. J. Hum. Genet. 61:520-528(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT1 ASP-339 AND CYS-340.
[12]"Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses."
Wuyts W., van Hul W., de Boulle K., Hendrickx J., Bakker E., Vanhoenacker F., Mollica F., Luedecke H.-J., Sayli B.S., Pazzaglia U.E., Mortier G., Hamel B.C.J., Conrad E.U. III, Matsushita M., Raskind W.H., Willems P.J.
Am. J. Hum. Genet. 62:346-354(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT1 GLY-280 AND SER-340.
[13]"Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses."
Raskind W.H., Conrad E.U. III, Matsushita M., Wijsman E.M., Wells D.E., Chapman N., Sandell L.J., Wagner M.J., Houck J.
Hum. Mutat. 11:231-239(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT1 GLY-280; SER-280; HIS-340 AND HIS-627 DEL.
[14]"EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas."
Bovee J.V.M.G., Cleton-Jansen A.-M., Wuyts W., Caethoven G., Taminiau A.H.M., Bakker E., van Hul W., Cornelisse C.J., Hogendoorn P.C.W.
Am. J. Hum. Genet. 65:689-698(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT1 HIS-164; 235-PRO--LYS-239 DEL AND SER-316.
[15]"Mutation analysis of hereditary multiple exostoses in the Chinese."
Xu L., Xia J., Jiang H., Zhou J., Li H., Wang D., Pan Q., Long Z., Fan C., Deng H.-X.
Hum. Genet. 105:45-50(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT1 VAL-486 AND LEU-496.
[16]"Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes."
Bernard M.A., Hall C.E., Hogue D.A., Cole W.G., Scott A., Snuggs M.B., Clines G.A., Luedecke H.-J., Lovett M., Van Winkle W.B., Hecht J.T.
Cell Motil. Cytoskeleton 48:149-162(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT1 215-MET--SER-221 DEL, VARIANT OSTEOCHONDROMA 215-MET--SER-222 DELINS ILE.
[17]"Etiological point mutations in the hereditary multiple exostoses gene EXT1: a functional analysis of heparan sulfate polymerase activity."
Cheung P.K., McCormick C., Crawford B.E., Esko J.D., Tufaro F., Duncan G.
Am. J. Hum. Genet. 69:55-66(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS, MUTAGENESIS OF GLN-27; ASP-164; ASN-316; ALA-486 AND PRO-496.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S79639 mRNA. Translation: AAB62283.1.
AK313129 mRNA. Translation: BAG35949.1.
CH471060 Genomic DNA. Translation: EAW91972.1.
BC001174 mRNA. Translation: AAH01174.1.
U70539 Genomic DNA. Translation: AAC51154.1.
RefSeqNP_000118.2. NM_000127.2.
UniGeneHs.492618.

3D structure databases

ProteinModelPortalQ16394.
SMRQ16394. Positions 478-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108432. 5 interactions.
IntActQ16394. 1 interaction.
MINTMINT-120274.
STRING9606.ENSP00000367446.

Protein family/group databases

CAZyGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSiteQ16394.

Polymorphism databases

DMDM20141422.

Proteomic databases

PaxDbQ16394.
PRIDEQ16394.

Protocols and materials databases

DNASU2131.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378204; ENSP00000367446; ENSG00000182197.
GeneID2131.
KEGGhsa:2131.
UCSCuc003yok.1. human.

Organism-specific databases

CTD2131.
GeneCardsGC08M118880.
HGNCHGNC:3512. EXT1.
HPAHPA044394.
MIM133700. phenotype.
150230. phenotype.
215300. phenotype.
608177. gene.
neXtProtNX_Q16394.
Orphanet55880. Chondrosarcoma.
502. Langer-Giedion syndrome.
321. Multiple osteochondromas.
PharmGKBPA27924.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272619.
HOGENOMHOG000266990.
HOVERGENHBG003459.
InParanoidQ16394.
KOK02366.
OMAVTTCKHG.
OrthoDBEOG7RBZ7Z.
PhylomeDBQ16394.
TreeFamTF314231.

Enzyme and pathway databases

BioCycMetaCyc:HS00012-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ16394.
BgeeQ16394.
CleanExHS_EXT1.
GenevestigatorQ16394.

Family and domain databases

InterProIPR004263. Exostosin.
IPR027670. Exostosin-1.
IPR015338. HexNAc_Trfase_a.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF7. PTHR11062:SF7. 1 hit.
PfamPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEXT1. human.
GeneWikiEXT1.
GenomeRNAi2131.
NextBio8611.
PROQ16394.
SOURCESearch...

Entry information

Entry nameEXT1_HUMAN
AccessionPrimary (citable) accession number: Q16394
Secondary accession number(s): B2R7V2, Q9BVI9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM