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Q8IYK4

- GT252_HUMAN

UniProt

Q8IYK4 - GT252_HUMAN

Protein

Procollagen galactosyltransferase 2

Gene

COLGALT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen.1 Publication

    Catalytic activityi

    UDP-alpha-D-galactose + 5-hydroxy-L-lysine-[procollagen] = UDP + 5-(D-galactosyloxy)-L-lysine-[procollagen].1 Publication

    Kineticsi

    1. KM=33.5 µM for UDP-galactose1 Publication

    GO - Molecular functioni

    1. procollagen galactosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. extracellular matrix organization Source: Reactome
    2. lipopolysaccharide biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    SABIO-RKQ8IYK4.

    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:C1orf17, GLT25D2, KIAA0584
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16790. COLGALT2.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25606.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 626599Procollagen galactosyltransferase 2PRO_0000309541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi580 – 5801N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8IYK4.
    PaxDbiQ8IYK4.
    PRIDEiQ8IYK4.

    PTM databases

    PhosphoSiteiQ8IYK4.

    Expressioni

    Tissue specificityi

    Expressed in brain and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ8IYK4.
    BgeeiQ8IYK4.
    CleanExiHS_GLT25D2.
    GenevestigatoriQ8IYK4.

    Organism-specific databases

    HPAiHPA031749.
    HPA031750.

    Interactioni

    Protein-protein interaction databases

    BioGridi116746. 1 interaction.
    STRINGi9606.ENSP00000354960.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IYK4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi623 – 6264Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyltransferase 25 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3306.
    HOGENOMiHOG000007198.
    HOVERGENiHBG058097.
    KOiK11703.
    OMAiQIREWKR.
    OrthoDBiEOG7060RC.
    PhylomeDBiQ8IYK4.
    TreeFamiTF313826.

    Family and domain databases

    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.

    Q8IYK4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARPAATLA WSLLLLSSAL LREGCRARFV AERDSEDDGE EPVVFPESPL    50
    QSPTVLVAVL ARNAAHTLPH FLGCLERLDY PKSRMAIWAA TDHNVDNTTE 100
    IFREWLKNVQ RLYHYVEWRP MDEPESYPDE IGPKHWPTSR FAHVMKLRQA 150
    ALRTAREKWS DYILFIDVDN FLTNPQTLNL LIAENKTIVA PMLESRGLYS 200
    NFWCGITPKG FYKRTPDYVQ IREWKRTGCF PVPMVHSTFL IDLRKEASDK 250
    LTFYPPHQDY TWTFDDIIVF AFSSRQAGIQ MYLCNREHYG YLPIPLKPHQ 300
    TLQEDIENLI HVQIEAMIDR PPMEPSQYVS VVPKYPDKMG FDEIFMINLK 350
    RRKDRRDRML RTLYEQEIEV KIVEAVDGKA LNTSQLKALN IEMLPGYRDP 400
    YSSRPLTRGE IGCFLSHYSV WKEVIDRELE KTLVIEDDVR FEHQFKKKLM 450
    KLMDNIDQAQ LDWELIYIGR KRMQVKEPEK AVPNVANLVE ADYSYWTLGY 500
    VISLEGAQKL VGANPFGKML PVDEFLPVMY NKHPVAEYKE YYESRDLKAF 550
    SAEPLLIYPT HYTGQPGYLS DTETSTIWDN ETVATDWDRT HAWKSRKQSR 600
    IYSNAKNTEA LPPPTSLDTV PSRDEL 626
    Length:626
    Mass (Da):72,924
    Last modified:March 1, 2003 - v1
    Checksum:i697A76DB73F67539
    GO

    Sequence cautioni

    The sequence BAA25510.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti475 – 4751V → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036978

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288389 mRNA. Translation: AAG60609.1.
    AB011156 mRNA. Translation: BAA25510.1. Different initiation.
    AL592299, AL157943 Genomic DNA. Translation: CAI14722.1.
    AL157943, AL592299 Genomic DNA. Translation: CAI17872.1.
    CH471067 Genomic DNA. Translation: EAW91172.1.
    BC035672 mRNA. Translation: AAH35672.1.
    CCDSiCCDS1360.1.
    PIRiT00343.
    RefSeqiNP_055916.1. NM_015101.2.
    UniGeneiHs.387995.

    Genome annotation databases

    EnsembliENST00000361927; ENSP00000354960; ENSG00000198756.
    GeneIDi23127.
    KEGGihsa:23127.
    UCSCiuc001gqr.3. human.

    Polymorphism databases

    DMDMi74750765.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288389 mRNA. Translation: AAG60609.1 .
    AB011156 mRNA. Translation: BAA25510.1 . Different initiation.
    AL592299 , AL157943 Genomic DNA. Translation: CAI14722.1 .
    AL157943 , AL592299 Genomic DNA. Translation: CAI17872.1 .
    CH471067 Genomic DNA. Translation: EAW91172.1 .
    BC035672 mRNA. Translation: AAH35672.1 .
    CCDSi CCDS1360.1.
    PIRi T00343.
    RefSeqi NP_055916.1. NM_015101.2.
    UniGenei Hs.387995.

    3D structure databases

    ProteinModelPortali Q8IYK4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116746. 1 interaction.
    STRINGi 9606.ENSP00000354960.

    Protein family/group databases

    CAZyi GT25. Glycosyltransferase Family 25.

    PTM databases

    PhosphoSitei Q8IYK4.

    Polymorphism databases

    DMDMi 74750765.

    Proteomic databases

    MaxQBi Q8IYK4.
    PaxDbi Q8IYK4.
    PRIDEi Q8IYK4.

    Protocols and materials databases

    DNASUi 23127.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361927 ; ENSP00000354960 ; ENSG00000198756 .
    GeneIDi 23127.
    KEGGi hsa:23127.
    UCSCi uc001gqr.3. human.

    Organism-specific databases

    CTDi 23127.
    GeneCardsi GC01M183899.
    HGNCi HGNC:16790. COLGALT2.
    HPAi HPA031749.
    HPA031750.
    neXtProti NX_Q8IYK4.
    PharmGKBi PA25606.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3306.
    HOGENOMi HOG000007198.
    HOVERGENi HBG058097.
    KOi K11703.
    OMAi QIREWKR.
    OrthoDBi EOG7060RC.
    PhylomeDBi Q8IYK4.
    TreeFami TF313826.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    SABIO-RK Q8IYK4.

    Miscellaneous databases

    GenomeRNAii 23127.
    NextBioi 44367.
    PROi Q8IYK4.

    Gene expression databases

    ArrayExpressi Q8IYK4.
    Bgeei Q8IYK4.
    CleanExi HS_GLT25D2.
    Genevestigatori Q8IYK4.

    Family and domain databases

    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. "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
      Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
      Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Duodenum.
    6. "Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases."
      Schegg B., Huelsmeier A.J., Rutschmann C., Maag C., Hennet T.
      Mol. Cell. Biol. 29:943-952(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-475.

    Entry informationi

    Entry nameiGT252_HUMAN
    AccessioniPrimary (citable) accession number: Q8IYK4
    Secondary accession number(s): O60327, Q9BZR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Has no glucosyltransferase activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3