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Protein

Exostosin-2

Gene

Ext2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei490 – 4901SubstrateBy similarity
Metal bindingi540 – 5401Manganese; catalyticBy similarity
Binding sitei569 – 5691SubstrateBy similarity
Active sitei628 – 6281By similarity

GO - Molecular functioni

  • acetylglucosaminyltransferase activity Source: BHF-UCL
  • glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: BHF-UCL
  • glucuronosyltransferase activity Source: BHF-UCL
  • heparan sulfate N-acetylglucosaminyltransferase activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Source: BHF-UCL
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: BHF-UCL
  • transferase activity, transferring glycosyl groups Source: MGI

GO - Biological processi

  • cell differentiation Source: MGI
  • cellular polysaccharide biosynthetic process Source: MGI
  • glycosaminoglycan biosynthetic process Source: MGI
  • heparan sulfate proteoglycan biosynthetic process Source: MGI
  • heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: MGI
  • mesoderm formation Source: MGI
  • ossification Source: MGI
  • protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_324389. HS-GAG biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

Names & Taxonomyi

Protein namesi
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 homolog
Gene namesi
Name:Ext2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:108050. Ext2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei26 – 4621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini47 – 718672LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: BHF-UCL
  • endoplasmic reticulum membrane Source: BHF-UCL
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: BHF-UCL
  • Golgi membrane Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • UDP-N-acetylglucosamine transferase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 718718Exostosin-2PRO_0000149652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi626 ↔ 676By similarity
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP70428.
PaxDbiP70428.
PRIDEiP70428.

PTM databases

PhosphoSiteiP70428.

Expressioni

Tissue specificityi

Heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.

Developmental stagei

Expressed in early stages of embryonic development.

Gene expression databases

BgeeiP70428.
CleanExiMM_EXT2.
ExpressionAtlasiP70428. baseline and differential.
GenevestigatoriP70428.

Interactioni

Subunit structurei

Interacts with GALNT5 (By similarity). Forms a homo/hetero-oligomeric complex with EXT1.By similarity

Protein-protein interaction databases

DIPiDIP-29858N.

Structurei

3D structure databases

ProteinModelPortaliP70428.
SMRiP70428. Positions 456-690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni517 – 5226Substrate bindingBy similarity
Regioni538 – 5403Substrate bindingBy similarity
Regioni624 – 6285Substrate bindingBy similarity
Regioni662 – 67312Substrate bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
HOVERGENiHBG101211.
InParanoidiP70428.
KOiK02367.
OMAiQFGYEVW.
OrthoDBiEOG789C9T.
TreeFamiTF314231.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P70428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCASVKSNIR GPALIPRMKT KHRIYYVTLF SIVLLGLIAT GMFQFWPHSI
60 70 80 90 100
ESSSDGGVEK RSIREVPVVR LPTDSPIPER GDLSCRMHTC FDVYRCGFNP
110 120 130 140 150
KNKIKVYIYP LKKYVDDAGV PVSSAISREY NELLTAISDS DYYTDDINRA
160 170 180 190 200
CLFVPSIDVL NQNPLRIKET AQALAQLSRW DRGTNHLLFN MLPGAPPDYN
210 220 230 240 250
TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVFSPLSAEM ALPEKAPGPR
260 270 280 290 300
RYFLLSSQMA IHPEYREELE ALQAKHQESV LVLDKCTNLS EGVLSVRKRC
310 320 330 340 350
HQHQVFDYPQ VLQEATFCTV LRGARLGQAV LSDVLQAGCV PVVIADSYIL
360 370 380 390 400
PFSEVLDWKR ASVVVPEEKM SDVYSILQNI PQRQIEEMQR QARWFWEAYF
410 420 430 440 450
QSIKAIALAT LQIINDRIYP YAAISYEEWN DPPAVKWASV SNPLFLPLIP
460 470 480 490 500
PQSQGFTAIV LTYDRVESLF RVITEVSKVP SLSKLLVVWN NQNKNPPEES
510 520 530 540 550
LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD IIMLTSDELQ
560 570 580 590 600
FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY
610 620 630 640 650
HKYFNYLYTY KMPGDIKNWV DTHMNCEDIA MNFLVANVTG KAVIKVTPRK
660 670 680 690 700
KFKCPECTAI DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL
710
YKDDFPEKLK SFPNIGSL
Length:718
Mass (Da):82,064
Last modified:July 27, 2011 - v2
Checksum:i45D947BF6678378B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621S → T in AAC53143 (PubMed:9110175).Curated
Sequence conflicti160 – 1601L → V in AAC53143 (PubMed:9110175).Curated
Sequence conflicti323 – 3231G → R in AAC53143 (PubMed:9110175).Curated
Sequence conflicti355 – 3551V → I in AAC53143 (PubMed:9110175).Curated
Sequence conflicti360 – 3601R → K in AAC53143 (PubMed:9110175).Curated
Sequence conflicti389 – 3891Q → H in AAC53143 (PubMed:9110175).Curated
Sequence conflicti622 – 6221T → A in AAC53143 (PubMed:9110175).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72141 mRNA. Translation: AAB17006.1.
U67837 mRNA. Translation: AAC53143.1.
AK164342 mRNA. Translation: BAE37749.1.
AL732493, AL732472 Genomic DNA. Translation: CAM22097.1.
AL732472, AL732493 Genomic DNA. Translation: CAM23881.1.
CH466519 Genomic DNA. Translation: EDL27629.1.
BC006597 mRNA. Translation: AAH06597.1.
CCDSiCCDS16456.1.
RefSeqiNP_034293.2. NM_010163.3.
XP_006498796.1. XM_006498733.2.
UniGeneiMm.4336.

Genome annotation databases

EnsembliENSMUST00000028623; ENSMUSP00000028623; ENSMUSG00000027198.
GeneIDi14043.
KEGGimmu:14043.
UCSCiuc008lgf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72141 mRNA. Translation: AAB17006.1.
U67837 mRNA. Translation: AAC53143.1.
AK164342 mRNA. Translation: BAE37749.1.
AL732493, AL732472 Genomic DNA. Translation: CAM22097.1.
AL732472, AL732493 Genomic DNA. Translation: CAM23881.1.
CH466519 Genomic DNA. Translation: EDL27629.1.
BC006597 mRNA. Translation: AAH06597.1.
CCDSiCCDS16456.1.
RefSeqiNP_034293.2. NM_010163.3.
XP_006498796.1. XM_006498733.2.
UniGeneiMm.4336.

3D structure databases

ProteinModelPortaliP70428.
SMRiP70428. Positions 456-690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29858N.

Protein family/group databases

CAZyiGT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSiteiP70428.

Proteomic databases

MaxQBiP70428.
PaxDbiP70428.
PRIDEiP70428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028623; ENSMUSP00000028623; ENSMUSG00000027198.
GeneIDi14043.
KEGGimmu:14043.
UCSCiuc008lgf.2. mouse.

Organism-specific databases

CTDi2132.
MGIiMGI:108050. Ext2.

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
HOVERGENiHBG101211.
InParanoidiP70428.
KOiK02367.
OMAiQFGYEVW.
OrthoDBiEOG789C9T.
TreeFamiTF314231.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_324389. HS-GAG biosynthesis.

Miscellaneous databases

ChiTaRSiExt2. mouse.
NextBioi284982.
PROiP70428.
SOURCEiSearch...

Gene expression databases

BgeeiP70428.
CleanExiMM_EXT2.
ExpressionAtlasiP70428. baseline and differential.
GenevestigatoriP70428.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. EXT_C.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamiPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the murine homolog of the human EXT2 multiple exostoses gene."
    Stickens D.J., Evans G.A.
    Biochem. Mol. Med. 61:16-21(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 [MRNA].
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Mammary gland.
  7. "The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate."
    McCormick C., Duncan G., Goutsos K.T., Tufaro F.
    Proc. Natl. Acad. Sci. U.S.A. 97:668-673(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiEXT2_MOUSE
AccessioniPrimary (citable) accession number: P70428
Secondary accession number(s): P70395, Q3TPI7, Q923D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.