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Q6NVG7

- GT252_MOUSE

UniProt

Q6NVG7 - GT252_MOUSE

Protein

Procollagen galactosyltransferase 2

Gene

Colgalt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen.By similarity

    Catalytic activityi

    UDP-alpha-D-galactose + 5-hydroxy-L-lysine-[procollagen] = UDP + 5-(D-galactosyloxy)-L-lysine-[procollagen].

    GO - Molecular functioni

    1. procollagen galactosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipopolysaccharide biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

    Protein family/group databases

    CAZyiGT25. Glycosyltransferase Family 25.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Procollagen galactosyltransferase 2 (EC:2.4.1.50)
    Alternative name(s):
    Collagen beta(1-O)galactosyltransferase 2
    Glycosyltransferase 25 family member 2
    Hydroxylysine galactosyltransferase 2
    Gene namesi
    Name:Colgalt2
    Synonyms:Glt25d2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2138232. Colgalt2.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 625599Procollagen galactosyltransferase 2PRO_0000309542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi579 – 5791N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ6NVG7.

    PTM databases

    PhosphoSiteiQ6NVG7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6NVG7.
    BgeeiQ6NVG7.
    CleanExiMM_GLT25D2.
    GenevestigatoriQ6NVG7.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000037532.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NVG7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi622 – 6254Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyltransferase 25 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3306.
    GeneTreeiENSGT00550000074427.
    HOGENOMiHOG000007198.
    HOVERGENiHBG058097.
    InParanoidiQ6NVG7.
    KOiK11703.
    OMAiQIREWKR.
    OrthoDBiEOG7060RC.
    PhylomeDBiQ6NVG7.
    TreeFamiTF313826.

    Family and domain databases

    Gene3Di3.90.550.10. 2 hits.
    InterProiIPR002654. Glyco_trans_25.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF01755. Glyco_transf_25. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6NVG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARLATVAC ALFLLSSALL RLGCRARFAA EPDSDEDGEE TVAFPESPPQ    50
    KPTVFVVVLA RNAAHTLPYF LGCLERLDYP KSRMAIWAAT DHNVDNTTEI 100
    LREWLKSVQR LYHYVEWRPM NEPESYPDEI GPKHWPNSRF SHVMKLRQAA 150
    LRTAREKWSD YILFIDVDNF LTNPQTLNLM IVENKTIVAP MLESRGLYSN 200
    FWCGITPQGF YKRTPDYLQI REWKRMGCFP VPMVHSTFLI DLRKEASDKL 250
    AFYPPHQDYT WTFDDIIVFA FSSRQAGIQM YLCNKEHYGY LPIPLKPHQT 300
    LQEDVENLIH VQIEAMIDHP PMEPSQFVSV VPKYPDKMGF DEIFMINLKR 350
    RKDRRDRMLR TLYEQEIEVK IVEAVDGKAL NTSQLKAWNI EMLPGYRDPY 400
    SSRPLTRGEI GCFLSHFSVW KEVIDRELEK TLVIEDDVRF EHQFKRKLMK 450
    LMEDIDKAQL DWELIYIGRK RMQVKEPEKA VPNVVNLVEA DYSYWTLGYA 500
    ISLEGAQKLV GADPFGKMLP VDEFLPIMYN KHPVAEYKEY YESRDLKAFS 550
    AEPLLIYPTH YTGQPGYLSD TETSTIWDNE TVATDWDRTH SWKSRKQGHI 600
    RSTAKNTEAL PPPTSLDTVP SRDEL 625
    Length:625
    Mass (Da):72,788
    Last modified:November 13, 2007 - v2
    Checksum:iCEEAB275790C1F3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti398 – 3981D → G in BAC35169. (PubMed:16141072)Curated
    Sequence conflicti616 – 6161L → V in AAH68118. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK052838 mRNA. Translation: BAC35169.1.
    BC068118 mRNA. Translation: AAH68118.1.
    CCDSiCCDS15364.1.
    RefSeqiNP_808424.3. NM_177756.4.
    UniGeneiMm.23782.

    Genome annotation databases

    EnsembliENSMUST00000044311; ENSMUSP00000037532; ENSMUSG00000032649.
    GeneIDi269132.
    KEGGimmu:269132.
    UCSCiuc007czg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK052838 mRNA. Translation: BAC35169.1 .
    BC068118 mRNA. Translation: AAH68118.1 .
    CCDSi CCDS15364.1.
    RefSeqi NP_808424.3. NM_177756.4.
    UniGenei Mm.23782.

    3D structure databases

    ProteinModelPortali Q6NVG7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000037532.

    Protein family/group databases

    CAZyi GT25. Glycosyltransferase Family 25.

    PTM databases

    PhosphoSitei Q6NVG7.

    Proteomic databases

    PRIDEi Q6NVG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000044311 ; ENSMUSP00000037532 ; ENSMUSG00000032649 .
    GeneIDi 269132.
    KEGGi mmu:269132.
    UCSCi uc007czg.2. mouse.

    Organism-specific databases

    CTDi 23127.
    MGIi MGI:2138232. Colgalt2.

    Phylogenomic databases

    eggNOGi COG3306.
    GeneTreei ENSGT00550000074427.
    HOGENOMi HOG000007198.
    HOVERGENi HBG058097.
    InParanoidi Q6NVG7.
    KOi K11703.
    OMAi QIREWKR.
    OrthoDBi EOG7060RC.
    PhylomeDBi Q6NVG7.
    TreeFami TF313826.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    NextBioi 392706.
    PROi Q6NVG7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6NVG7.
    Bgeei Q6NVG7.
    CleanExi MM_GLT25D2.
    Genevestigatori Q6NVG7.

    Family and domain databases

    Gene3Di 3.90.550.10. 2 hits.
    InterProi IPR002654. Glyco_trans_25.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    Pfami PF01755. Glyco_transf_25. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Mammary gland.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiGT252_MOUSE
    AccessioniPrimary (citable) accession number: Q6NVG7
    Secondary accession number(s): Q8BWD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 74 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3