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Q93063 (EXT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exostosin-2

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 2
Putative tumor suppressor protein EXT2
Gene names
Name:EXT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length718 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.

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 EXT1. Interacts with GALNT5. Ref.10 Ref.11

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.10

Tissue specificity

Ubiquitous.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Potocki-Shaffer syndrome (POSHS) [MIM:601224]: A syndrome characterized by foramina parietalia permagna, multiple exostoses, and craniofacial dysostosis and mental retardation in some cases.
Note: The gene represented in this entry is involved in disease pathogenesis.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   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_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular polysaccharide biosynthetic process

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

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 mutant phenotype PubMed 17761672. Source: BHF-UCL

heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

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

mesoderm formation

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

protein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

signal transduction

Traceable author statement PubMed 10878610. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: BHF-UCL

Golgi membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

endoplasmic reticulum membrane

Traceable author statement PubMed 10639137. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionN-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity

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

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

Inferred from electronic annotation. Source: UniProtKB-EC

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

transferase activity, transferring glycosyl groups

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

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q93063-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q93063-2)

The sequence of this isoform differs from the canonical sequence as follows:
     392-411: ARWFWEAYFQSIKAIALATL → LFMEPARRENWSAANHQMNSLIWPREQWDS
Isoform 3 (identifier: Q93063-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSCASGSGGGLRHPLRCQKPWDEECEEEAVCVIM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Exostosin-2
PRO_0000149651

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain47 – 718672Lumenal Potential

Amino acid modifications

Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation6371N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MSCASGSGGGLRHPLRCQKP WDEECEEEAVCVIM in isoform 3.
VSP_046053
Alternative sequence392 – 41120ARWFW…ALATL → LFMEPARRENWSAANHQMNS LIWPREQWDS in isoform 2.
VSP_001798
Natural variant421M → V.
Corresponds to variant rs4755779 [ dbSNP | Ensembl ].
VAR_033921
Natural variant851C → R in EXT2. Ref.15
VAR_012823
Natural variant1521L → R in EXT2. Ref.14
VAR_012824
Natural variant1791R → S in EXT2. Ref.20
VAR_012825
Natural variant2021A → V in EXT2. Ref.17
VAR_012826
Natural variant2231R → P in EXT2. Ref.16
VAR_012827
Natural variant2271D → N in EXT2; can still form an oligomeric complex. Ref.13 Ref.18 Ref.20
VAR_002378
Natural variant3801I → T in EXT2. Ref.19
VAR_012828
Natural variant5761E → K in osteochondroma. Ref.19
VAR_012829

Experimental info

Sequence conflict3221R → H in BX648142. Ref.5
Sequence conflict5681G → D in AAB62718. Ref.4
Isoform 2:
Sequence conflict3971A → V in AAB62718. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9048CD3A5B63C5CB

FASTA71882,255
        10         20         30         40         50         60 
MCASVKYNIR GPALIPRMKT KHRIYYITLF SIVLLGLIAT GMFQFWPHSI ESSNDWNVEK 

        70         80         90        100        110        120 
RSIRDVPVVR LPADSPIPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYA LKKYVDDFGV 

       130        140        150        160        170        180 
SVSNTISREY NELLMAISDS DYYTDDINRA CLFVPSIDVL NQNTLRIKET AQAMAQLSRW 

       190        200        210        220        230        240 
DRGTNHLLFN MLPGGPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVYSPLSAEV 

       250        260        270        280        290        300 
DLPEKGPGPR QYFLLSSQVG LHPEYREDLE ALQVKHGESV LVLDKCTNLS EGVLSVRKRC 

       310        320        330        340        350        360 
HKHQVFDYPQ VLQEATFCVV LRGARLGQAV LSDVLQAGCV PVVIADSYIL PFSEVLDWKR 

       370        380        390        400        410        420 
ASVVVPEEKM SDVYSILQSI PQRQIEEMQR QARWFWEAYF QSIKAIALAT LQIINDRIYP 

       430        440        450        460        470        480 
YAAISYEEWN DPPAVKWGSV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF RVITEVSKVP 

       490        500        510        520        530        540 
SLSKLLVVWN NQNKNPPEDS LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD 

       550        560        570        580        590        600 
IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY 

       610        620        630        640        650        660 
HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK KFKCPECTAI 

       670        680        690        700        710 
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL 

« Hide

Isoform 2 [UniParc].

Checksum: 5CF31DFAB03E4023
Show »

FASTA72883,570
Isoform 3 [UniParc].

Checksum: FB2DA6738A36F4B8
Show »

FASTA75185,815

References

« Hide 'large scale' references
[1]"The EXT2 multiple exostoses gene defines a family of putative tumour suppressor genes."
Stickens D.J., Clines G., Burbee D.G., Ramos P., Thomas S., Hogue D., Hecht J.T., Lovett M., Evans G.A.
Nat. Genet. 14:25-32(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Positional cloning of a gene involved in hereditary multiple exostoses."
Wuyts W., van Hul W., Wauters J., Nemtsova M., Reyniers E., van Hul E., de Boulle K., de Vries B.B.A., Hendrickx J., Herrygers I., Bossuyt P., Balemans W., Fransen E., Vits L., Coucke P., Nowak N.J., Mallet L., van den Ouweland A.M.W. expand/collapse author list , McGaughran J., Halley D.J.J., Willems P.J.
Hum. Mol. Genet. 5:1547-1557(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans."
Clines G.A., Ashley J.A., Shah S., Lovett M.
Genome Res. 7:359-367(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Molecular cloning of a candidate gene for hereditary multiple exostoses type II."
Deng H.-X., Fan C., Xia J.H., Xu L., He X.X., Ruan Q.G., Yang Y., Huang L.
Prog. Nat. Sci. 6:692-699(1996)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[5]"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] (ISOFORM 1).
Tissue: Amygdala.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Endometrial cancer.
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Ovary.
[10]"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.
[11]"A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses."
Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.
Hum. Mol. Genet. 8:2155-2164(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GALNT5.
[12]"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.
[13]"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: VARIANT EXT2 ASN-227.
[14]"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: VARIANT EXT2 ARG-152, ALTERNATIVE SPLICING.
[15]"Germline mutations in the EXT1 and EXT2 genes in Korean patients with hereditary multiple exostoses."
Park K.J., Shin K.-H., Ku J.-L., Cho T.-J., Lee S.H., Choi I.H., Philippe C., Monaco A.P., Porter D.E., Park J.-G.
J. Hum. Genet. 44:230-234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT2 ARG-85.
[16]"An R223P mutation in EXT2 gene causes hereditary multiple exostoses."
Shi Y.-R., Wu J.-Y., Tsai F.-J., Lee C.-C., Tsai C.-H.
Hum. Mutat. 15:390-391(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT2 PRO-223.
[17]"Mutation frequencies of EXT1 and EXT2 in 43 Japanese families with hereditary multiple exostoses."
Seki H., Kubota T., Ikegawa S., Haga N., Fujioka F., Ohzeki S., Wakui K., Yoshikawa H., Takaoka K., Fukushima Y.
Am. J. Med. Genet. 99:59-62(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT2 VAL-202.
[18]"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 EXT2 ASN-227.
[19]"Ext-mutation analysis in Italian sporadic and hereditary osteochondromas."
Gigante M., Matera M.G., Seripa D., Izzo A.M., Venanzi R., Giannotti A., Digilio M.C., Gravina C., Lazzari M., Monteleone G., Monteleone M., Dallapiccola B., Fazio V.M.
Int. J. Cancer 95:378-383(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EXT2 THR-380, VARIANT OSTEOCHONDROMA LYS-576.
[20]"Genotype-phenotype correlation in hereditary multiple exostoses."
Francannet C., Cohen-Tanugi A., Le Merrer M., Munnich A., Bonaventure J., Legeai-Mallet L.
J. Med. Genet. 38:430-434(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EXT2 SER-179 AND ASN-227.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62740 mRNA. Translation: AAB07008.1.
U64511 mRNA. Translation: AAC50764.1.
U67368 expand/collapse EMBL AC list , U67356, U67357, U67358, U67360, U67361, U67362, U67363, U67364, U67365, U67366, U67367 Genomic DNA. Translation: AAC51219.1.
U72263 mRNA. Translation: AAB62718.1.
AK312375 mRNA. Translation: BAG35293.1.
BX648142 mRNA. No translation available.
AC068457 Genomic DNA. No translation available.
AC103854 Genomic DNA. No translation available.
AC134775 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68068.1.
CH471064 Genomic DNA. Translation: EAW68070.1.
CH471064 Genomic DNA. Translation: EAW68071.1.
BC010058 mRNA. Translation: AAH10058.1.
CCDSCCDS53618.1. [Q93063-3]
CCDS53619.1. [Q93063-2]
CCDS7908.1. [Q93063-1]
RefSeqNP_000392.3. NM_000401.3. [Q93063-3]
NP_001171554.1. NM_001178083.1. [Q93063-2]
NP_997005.1. NM_207122.1. [Q93063-1]
UniGeneHs.368404.

3D structure databases

ProteinModelPortalQ93063.
SMRQ93063. Positions 456-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108433. 23 interactions.
IntActQ93063. 8 interactions.
MINTMINT-120303.
STRING9606.ENSP00000342656.

Protein family/group databases

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

PTM databases

PhosphoSiteQ93063.

Polymorphism databases

DMDM3023739.

Proteomic databases

MaxQBQ93063.
PaxDbQ93063.
PRIDEQ93063.

Protocols and materials databases

DNASU2132.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343631; ENSP00000342656; ENSG00000151348. [Q93063-1]
ENST00000358681; ENSP00000351509; ENSG00000151348. [Q93063-2]
ENST00000395673; ENSP00000379032; ENSG00000151348. [Q93063-3]
ENST00000533608; ENSP00000431173; ENSG00000151348. [Q93063-1]
GeneID2132.
KEGGhsa:2132.
UCSCuc001mxz.3. human. [Q93063-1]
uc001mya.3. human.
uc009ykt.3. human. [Q93063-2]

Organism-specific databases

CTD2132.
GeneCardsGC11P044117.
GeneReviewsEXT2.
HGNCHGNC:3513. EXT2.
HPAHPA051715.
MIM133701. phenotype.
601224. phenotype.
608210. gene.
neXtProtNX_Q93063.
Orphanet321. Multiple osteochondromas.
52022. Potocki-Shaffer syndrome.
PharmGKBPA27925.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272619.
HOGENOMHOG000266990.
HOVERGENHBG101211.
KOK02367.
OMAQFGYEVW.
OrthoDBEOG789C9T.
PhylomeDBQ93063.
TreeFamTF314231.

Enzyme and pathway databases

BioCycMetaCyc:HS07726-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ93063.
BgeeQ93063.
CleanExHS_EXT2.
GenevestigatorQ93063.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEXT2. human.
GeneWikiEXT2_(gene).
GenomeRNAi2132.
NextBio35535198.
PROQ93063.
SOURCESearch...

Entry information

Entry nameEXT2_HUMAN
AccessionPrimary (citable) accession number: Q93063
Secondary accession number(s): B2R5Z6 expand/collapse secondary AC list , C9JU51, J3KPT2, O15288
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 143 of the entry and version 1 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

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PATHWAY comments

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