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P70428 (EXT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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 homolog
Gene names
Name:Ext2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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

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

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.

Tissue specificity

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

Developmental stage

Expressed in early stages of embryonic development.

Sequence similarities

Belongs to the glycosyltransferase 47 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from mutant phenotype PubMed 16236767. Source: MGI

glycosaminoglycan biosynthetic process

Inferred from electronic annotation. Source: Ensembl

heparan sulfate proteoglycan biosynthetic process

Inferred from mutant phenotype PubMed 16236767. Source: MGI

heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Inferred from electronic annotation. Source: Ensembl

mesoderm formation

Inferred from mutant phenotype PubMed 16236767. Source: MGI

ossification

Inferred from electronic annotation. Source: Ensembl

protein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.7. Source: BHF-UCL

Golgi membrane

Inferred by curator Ref.7. Source: BHF-UCL

endoplasmic reticulum

Inferred from direct assay Ref.7. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred by curator Ref.7. Source: BHF-UCL

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

Inferred by curator Ref.7. Source: BHF-UCL

acetylglucosaminyltransferase activity

Inferred from direct assay Ref.7. Source: BHF-UCL

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

Inferred by curator Ref.7. Source: BHF-UCL

glucuronosyltransferase activity

Inferred from direct assay Ref.7. Source: BHF-UCL

heparan sulfate N-acetylglucosaminyltransferase activity

Inferred by curator Ref.7. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay Ref.7. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Exostosin-2
PRO_0000149652

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

Experimental info

Sequence conflict621S → T in AAC53143. Ref.2
Sequence conflict1601L → V in AAC53143. Ref.2
Sequence conflict3231G → R in AAC53143. Ref.2
Sequence conflict3551V → I in AAC53143. Ref.2
Sequence conflict3601R → K in AAC53143. Ref.2
Sequence conflict3891Q → H in AAC53143. Ref.2
Sequence conflict6221T → A in AAC53143. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70428 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 45D947BF6678378B

FASTA71882,064
        10         20         30         40         50         60 
MCASVKSNIR GPALIPRMKT KHRIYYVTLF SIVLLGLIAT GMFQFWPHSI ESSSDGGVEK 

        70         80         90        100        110        120 
RSIREVPVVR LPTDSPIPER GDLSCRMHTC FDVYRCGFNP KNKIKVYIYP LKKYVDDAGV 

       130        140        150        160        170        180 
PVSSAISREY NELLTAISDS DYYTDDINRA CLFVPSIDVL NQNPLRIKET AQALAQLSRW 

       190        200        210        220        230        240 
DRGTNHLLFN MLPGAPPDYN TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVFSPLSAEM 

       250        260        270        280        290        300 
ALPEKAPGPR RYFLLSSQMA IHPEYREELE ALQAKHQESV LVLDKCTNLS EGVLSVRKRC 

       310        320        330        340        350        360 
HQHQVFDYPQ VLQEATFCTV LRGARLGQAV LSDVLQAGCV PVVIADSYIL PFSEVLDWKR 

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

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

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

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

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

       670        680        690        700        710 
DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL YKDDFPEKLK SFPNIGSL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_034293.2. NM_010163.3.
XP_006498796.1. XM_006498733.1.
UniGeneMm.4336.

3D structure databases

ProteinModelPortalP70428.
SMRP70428. Positions 456-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29858N.

Protein family/group databases

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

PTM databases

PhosphoSiteP70428.

Proteomic databases

PaxDbP70428.
PRIDEP70428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028623; ENSMUSP00000028623; ENSMUSG00000027198.
GeneID14043.
KEGGmmu:14043.
UCSCuc008lgf.2. mouse.

Organism-specific databases

CTD2132.
MGIMGI:108050. Ext2.

Phylogenomic databases

eggNOGNOG272619.
GeneTreeENSGT00550000074496.
HOVERGENHBG101211.
InParanoidQ3TPI7.
KOK02367.
OMAQFGYEVW.
OrthoDBEOG789C9T.
TreeFamTF314231.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeP70428.
CleanExMM_EXT2.
GenevestigatorP70428.

Family and domain databases

InterProIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. HexNAc_Trfase_a.
[Graphical view]
PANTHERPTHR11062. PTHR11062. 1 hit.
PTHR11062:SF6. PTHR11062:SF6. 1 hit.
PfamPF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEXT2. mouse.
NextBio284982.
PROP70428.
SOURCESearch...

Entry information

Entry nameEXT2_MOUSE
AccessionPrimary (citable) accession number: P70428
Secondary accession number(s): P70395, Q3TPI7, Q923D6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot