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P70428

- EXT2_MOUSE

UniProt

P70428 - EXT2_MOUSE

Protein

Exostosin-2

Gene

Ext2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    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
    Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis

    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.By similarity

    Protein-protein interaction databases

    DIPiDIP-29858N.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini47 – 718672LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei26 – 4621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 47 family.Curated

    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

    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:
    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

    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: October 1, 2014
    This is version 118 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