Q93063 (EXT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary multiple exostoses Tumor suppressor
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycosaminoglycan biosynthetic process Inferred from direct assay PubMed 12907669. Source: BHF-UCL heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Inferred from mutant phenotype PubMed 17761672. Source: BHF-UCL 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
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endoplasmic reticulum membrane Traceable author statement PubMed 10639137. Source: ProtInc integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N-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: EC heparan sulfate N-acetylglucosaminyltransferase activity Non-traceable author statement 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 718	718	Exostosin-2		PRO_0000149651
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 46	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	47 – 718	672	Lumenal Potential
Amino acid modifications
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	637	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1	1	M → MSCASGSGGGLRHPLRCQKP WDEECEEEAVCVIM in isoform 3.		VSP_046053
	Alternative sequence	392 – 411	20	ARWFW…ALATL → LFMEPARRENWSAANHQMNS LIWPREQWDS in isoform 2.		VSP_001798
	Natural variant	42	1	M → V. Corresponds to variant rs4755779 [ dbSNP | Ensembl ].		VAR_033921
	Natural variant	85	1	C → R in EXT2. Ref.15		VAR_012823
	Natural variant	152	1	L → R in EXT2. Ref.14		VAR_012824
	Natural variant	179	1	R → S in EXT2. Ref.20		VAR_012825
	Natural variant	202	1	A → V in EXT2. Ref.17		VAR_012826
	Natural variant	223	1	R → P in EXT2. Ref.16		VAR_012827
	Natural variant	227	1	D → N in EXT2; can still form an oligomeric complex. Ref.13 Ref.18 Ref.20		VAR_002378
	Natural variant	380	1	I → T in EXT2. Ref.19		VAR_012828
	Natural variant	576	1	E → K in osteochondroma. Ref.19		VAR_012829
Experimental info
	Sequence conflict	322	1	R → H in BX648142. Ref.5
	Sequence conflict	568	1	G → D in AAB62718. Ref.4
Isoform 2:
	Sequence conflict	397	1	A → V in AAB62718. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 9048CD3A5B63C5CB	FASTA	718	82,255
	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
	Isoform 2 [UniParc]. Checksum: 5CF31DFAB03E4023	FASTA	728	83,570
	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 QLFMEPARRE NWSAANHQMN SLIWPREQWD 430 440 450 460 470 480 SQIINDRIYP YAAISYEEWN DPPAVKWGSV SNPLFLPLIP PQSQGFTAIV LTYDRVESLF 490 500 510 520 530 540 RVITEVSKVP SLSKLLVVWN NQNKNPPEDS LWPKIRVPLK VVRTAENKLS NRFFPYDEIE 550 560 570 580 590 600 TEAVLAIDDD IIMLTSDELQ FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV 610 620 630 640 650 660 SMVLTGAAFY HKYFNYLYTY KMPGDIKNWV DAHMNCEDIA MNFLVANVTG KAVIKVTPRK 670 680 690 700 710 720 KFKCPECTAI DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL
	Isoform 3 [UniParc]. Checksum: FB2DA6738A36F4B8	FASTA	751	85,815
	10 20 30 40 50 60 MSCASGSGGG LRHPLRCQKP WDEECEEEAV CVIMCASVKY NIRGPALIPR MKTKHRIYYI 70 80 90 100 110 120 TLFSIVLLGL IATGMFQFWP HSIESSNDWN VEKRSIRDVP VVRLPADSPI PERGDLSCRM 130 140 150 160 170 180 HTCFDVYRCG FNPKNKIKVY IYALKKYVDD FGVSVSNTIS REYNELLMAI SDSDYYTDDI 190 200 210 220 230 240 NRACLFVPSI DVLNQNTLRI KETAQAMAQL SRWDRGTNHL LFNMLPGGPP DYNTALDVPR 250 260 270 280 290 300 DRALLAGGGF STWTYRQGYD VSIPVYSPLS AEVDLPEKGP GPRQYFLLSS QVGLHPEYRE 310 320 330 340 350 360 DLEALQVKHG ESVLVLDKCT NLSEGVLSVR KRCHKHQVFD YPQVLQEATF CVVLRGARLG 370 380 390 400 410 420 QAVLSDVLQA GCVPVVIADS YILPFSEVLD WKRASVVVPE EKMSDVYSIL QSIPQRQIEE 430 440 450 460 470 480 MQRQARWFWE AYFQSIKAIA LATLQIINDR IYPYAAISYE EWNDPPAVKW GSVSNPLFLP 490 500 510 520 530 540 LIPPQSQGFT AIVLTYDRVE SLFRVITEVS KVPSLSKLLV VWNNQNKNPP EDSLWPKIRV 550 560 570 580 590 600 PLKVVRTAEN KLSNRFFPYD EIETEAVLAI DDDIIMLTSD ELQFGYEVWR EFPDRLVGYP 610 620 630 640 650 660 GRLHLWDHEM NKWKYESEWT NEVSMVLTGA AFYHKYFNYL YTYKMPGDIK NWVDAHMNCE 670 680 690 700 710 720 DIAMNFLVAN VTGKAVIKVT PRKKFKCPEC TAIDGLSLDQ THMVERSECI NKFASVFGTM 730 740 750 PLKVVEHRAD PVLYKDDFPE KLKSFPNIGS L

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62740 mRNA. Translation: AAB07008.1. U64511 mRNA. Translation: AAC50764.1. U67368 , 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.
IPI	IPI00004047. IPI00942173. IPI00953659.
RefSeq	NP_000392.3. NM_000401.3. NP_001171554.1. NM_001178083.1. NP_997005.1. NM_207122.1.
UniGene	Hs.368404.
3D structure databases
ProteinModelPortal	Q93063.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q93063. 3 interactions.
STRING	9606.ENSP00000342656.
Protein family/group databases
CAZy	GT47. Glycosyltransferase Family 47. GT64. Glycosyltransferase Family 64.
PTM databases
PhosphoSite	Q93063.
Polymorphism databases
DMDM	3023739.
Proteomic databases
PaxDb	Q93063.
PRIDE	Q93063.
Protocols and materials databases
DNASU	2132.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343631; ENSP00000342656; ENSG00000151348. ENST00000358681; ENSP00000351509; ENSG00000151348. ENST00000395673; ENSP00000379032; ENSG00000151348. ENST00000533608; ENSP00000431173; ENSG00000151348.
GeneID	2132.
KEGG	hsa:2132.
UCSC	uc001mxz.3. human.
Organism-specific databases
CTD	2132.
GeneCards	GC11P044117.
HGNC	HGNC:3513. EXT2.
MIM	133701. phenotype. 601224. phenotype. 608210. gene.
neXtProt	NX_Q93063.
Orphanet	321. Multiple osteochondromas. 52022. Potocki-Shaffer syndrome.
PharmGKB	PA27925.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG272619.
HOGENOM	HOG000266990.
HOVERGEN	HBG101211.
KO	K02367.
OrthoDB	EOG41VK2B.
Enzyme and pathway databases
BioCyc	MetaCyc:HS07726-MONOMER.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q93063.
Bgee	Q93063.
CleanEx	HS_EXT2.
Genevestigator	Q93063.
GermOnline	ENSG00000151348. Homo sapiens.
Family and domain databases
InterPro	IPR004263. Exostosin. IPR015338. HexNAc_Trfase_a. [Graphical view]
Pfam	PF03016. Exostosin. 1 hit. PF09258. Glyco_transf_64. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EXT2. human.
GenomeRNAi	2132.
NextBio	35535198.
SOURCE	Search...

Entry information

Entry name

EXT2_HUMAN

Accession

Primary (citable) accession number: Q93063
Secondary accession number(s): B2R5Z6 , C9JU51, J3KPT2, O15288

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.