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P70428

- EXT2_MOUSE

UniProt

P70428 - EXT2_MOUSE

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Protein

Exostosin-2

Gene
Ext2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: BHF-UCL
  2. glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Source: BHF-UCL
  3. glucuronosyltransferase activity Source: BHF-UCL
  4. heparan sulfate N-acetylglucosaminyltransferase activity Source: BHF-UCL
  5. N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Source: BHF-UCL
  6. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. cell differentiation Source: MGI
  2. glycosaminoglycan biosynthetic process Source: Ensembl
  3. heparan sulfate proteoglycan biosynthetic process Source: MGI
  4. heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: Ensembl
  5. mesoderm formation Source: MGI
  6. ossification Source: Ensembl
  7. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_198654. 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: Chromosome 2

Organism-specific databases

MGIiMGI:108050. Ext2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei26 – 4621Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini47 – 718672Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: BHF-UCL
  2. endoplasmic reticulum membrane Source: BHF-UCL
  3. Golgi apparatus Source: BHF-UCL
  4. Golgi membrane Source: BHF-UCL
  5. integral component of membrane Source: UniProtKB-KW
  6. intrinsic component of endoplasmic reticulum membrane Source: InterPro
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...) Reviewed prediction
Glycosylationi637 – 6371N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

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.
GenevestigatoriP70428.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-29858N.

Structurei

3D structure databases

ProteinModelPortaliP70428.
SMRiP70428. Positions 456-690.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272619.
GeneTreeiENSGT00550000074496.
HOVERGENiHBG101211.
InParanoidiQ3TPI7.
KOiK02367.
OMAiQFGYEVW.
OrthoDBiEOG789C9T.
TreeFamiTF314231.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11062. PTHR11062. 1 hit.
PTHR11062: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

MCASVKSNIR GPALIPRMKT KHRIYYVTLF SIVLLGLIAT GMFQFWPHSI    50
ESSSDGGVEK RSIREVPVVR LPTDSPIPER GDLSCRMHTC FDVYRCGFNP 100
KNKIKVYIYP LKKYVDDAGV PVSSAISREY NELLTAISDS DYYTDDINRA 150
CLFVPSIDVL NQNPLRIKET AQALAQLSRW DRGTNHLLFN MLPGAPPDYN 200
TALDVPRDRA LLAGGGFSTW TYRQGYDVSI PVFSPLSAEM ALPEKAPGPR 250
RYFLLSSQMA IHPEYREELE ALQAKHQESV LVLDKCTNLS EGVLSVRKRC 300
HQHQVFDYPQ VLQEATFCTV LRGARLGQAV LSDVLQAGCV PVVIADSYIL 350
PFSEVLDWKR ASVVVPEEKM SDVYSILQNI PQRQIEEMQR QARWFWEAYF 400
QSIKAIALAT LQIINDRIYP YAAISYEEWN DPPAVKWASV SNPLFLPLIP 450
PQSQGFTAIV LTYDRVESLF RVITEVSKVP SLSKLLVVWN NQNKNPPEES 500
LWPKIRVPLK VVRTAENKLS NRFFPYDEIE TEAVLAIDDD IIMLTSDELQ 550
FGYEVWREFP DRLVGYPGRL HLWDHEMNKW KYESEWTNEV SMVLTGAAFY 600
HKYFNYLYTY KMPGDIKNWV DTHMNCEDIA MNFLVANVTG KAVIKVTPRK 650
KFKCPECTAI DGLSLDQTHM VERSECINKF ASVFGTMPLK VVEHRADPVL 700
YKDDFPEKLK SFPNIGSL 718
Length:718
Mass (Da):82,064
Last modified:July 27, 2011 - v2
Checksum:i45D947BF6678378B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621S → T in AAC53143. 1 Publication
Sequence conflicti160 – 1601L → V in AAC53143. 1 Publication
Sequence conflicti323 – 3231G → R in AAC53143. 1 Publication
Sequence conflicti355 – 3551V → I in AAC53143. 1 Publication
Sequence conflicti360 – 3601R → K in AAC53143. 1 Publication
Sequence conflicti389 – 3891Q → H in AAC53143. 1 Publication
Sequence conflicti622 – 6221T → A in AAC53143. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006498733.1.
UniGeneiMm.4336.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS16456.1.
RefSeqi NP_034293.2. NM_010163.3.
XP_006498796.1. XM_006498733.1.
UniGenei Mm.4336.

3D structure databases

ProteinModelPortali P70428.
SMRi P70428. Positions 456-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29858N.

Protein family/group databases

CAZyi GT47. Glycosyltransferase Family 47.
GT64. Glycosyltransferase Family 64.

PTM databases

PhosphoSitei P70428.

Proteomic databases

PaxDbi P70428.
PRIDEi P70428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028623 ; ENSMUSP00000028623 ; ENSMUSG00000027198 .
GeneIDi 14043.
KEGGi mmu:14043.
UCSCi uc008lgf.2. mouse.

Organism-specific databases

CTDi 2132.
MGIi MGI:108050. Ext2.

Phylogenomic databases

eggNOGi NOG272619.
GeneTreei ENSGT00550000074496.
HOVERGENi HBG101211.
InParanoidi Q3TPI7.
KOi K02367.
OMAi QFGYEVW.
OrthoDBi EOG789C9T.
TreeFami TF314231.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198654. HS-GAG biosynthesis.

Miscellaneous databases

ChiTaRSi EXT2. mouse.
NextBioi 284982.
PROi P70428.
SOURCEi Search...

Gene expression databases

Bgeei P70428.
CleanExi MM_EXT2.
Genevestigatori P70428.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR004263. Exostosin.
IPR027673. Exostosin-2.
IPR015338. HexNAc_Trfase_a.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR11062. PTHR11062. 1 hit.
PTHR11062:SF6. PTHR11062:SF6. 1 hit.
Pfami PF03016. Exostosin. 1 hit.
PF09258. Glyco_transf_64. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 117 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

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