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Protein

Procollagen galactosyltransferase 2

Gene

COLGALT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.50. 2681.
    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 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16790. COLGALT2.

    Subcellular locationi

    • Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25606.

    Polymorphism and mutation databases

    BioMutaiCOLGALT2.
    DMDMi74750765.

    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

    BgeeiQ8IYK4.
    CleanExiHS_GLT25D2.
    ExpressionAtlasiQ8IYK4. baseline and differential.
    GenevestigatoriQ8IYK4.

    Organism-specific databases

    HPAiHPA031749.
    HPA031750.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBQLN1Q9UMX0-23EBI-10263496,EBI-10173939

    Protein-protein interaction databases

    BioGridi116746. 28 interactions.
    IntActiQ8IYK4. 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.
    GeneTreeiENSGT00550000074427.
    HOGENOMiHOG000007198.
    HOVERGENiHBG058097.
    InParanoidiQ8IYK4.
    KOiK11703.
    OMAiMAIWAAT.
    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

            10         20         30         40         50
    MAARPAATLA WSLLLLSSAL LREGCRARFV AERDSEDDGE EPVVFPESPL
    60 70 80 90 100
    QSPTVLVAVL ARNAAHTLPH FLGCLERLDY PKSRMAIWAA TDHNVDNTTE
    110 120 130 140 150
    IFREWLKNVQ RLYHYVEWRP MDEPESYPDE IGPKHWPTSR FAHVMKLRQA
    160 170 180 190 200
    ALRTAREKWS DYILFIDVDN FLTNPQTLNL LIAENKTIVA PMLESRGLYS
    210 220 230 240 250
    NFWCGITPKG FYKRTPDYVQ IREWKRTGCF PVPMVHSTFL IDLRKEASDK
    260 270 280 290 300
    LTFYPPHQDY TWTFDDIIVF AFSSRQAGIQ MYLCNREHYG YLPIPLKPHQ
    310 320 330 340 350
    TLQEDIENLI HVQIEAMIDR PPMEPSQYVS VVPKYPDKMG FDEIFMINLK
    360 370 380 390 400
    RRKDRRDRML RTLYEQEIEV KIVEAVDGKA LNTSQLKALN IEMLPGYRDP
    410 420 430 440 450
    YSSRPLTRGE IGCFLSHYSV WKEVIDRELE KTLVIEDDVR FEHQFKKKLM
    460 470 480 490 500
    KLMDNIDQAQ LDWELIYIGR KRMQVKEPEK AVPNVANLVE ADYSYWTLGY
    510 520 530 540 550
    VISLEGAQKL VGANPFGKML PVDEFLPVMY NKHPVAEYKE YYESRDLKAF
    560 570 580 590 600
    SAEPLLIYPT HYTGQPGYLS DTETSTIWDN ETVATDWDRT HAWKSRKQSR
    610 620
    IYSNAKNTEA LPPPTSLDTV PSRDEL
    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.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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_001290349.1. NM_001303420.1.
    NP_001290350.1. NM_001303421.1.
    NP_055916.1. NM_015101.3.
    UniGeneiHs.387995.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_001290349.1. NM_001303420.1.
    NP_001290350.1. NM_001303421.1.
    NP_055916.1. NM_015101.3.
    UniGeneiHs.387995.

    3D structure databases

    ProteinModelPortaliQ8IYK4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116746. 28 interactions.
    IntActiQ8IYK4. 1 interaction.
    STRINGi9606.ENSP00000354960.

    Protein family/group databases

    CAZyiGT25. Glycosyltransferase Family 25.

    PTM databases

    PhosphoSiteiQ8IYK4.

    Polymorphism and mutation databases

    BioMutaiCOLGALT2.
    DMDMi74750765.

    Proteomic databases

    MaxQBiQ8IYK4.
    PaxDbiQ8IYK4.
    PRIDEiQ8IYK4.

    Protocols and materials databases

    DNASUi23127.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi23127.
    GeneCardsiGC01M183899.
    HGNCiHGNC:16790. COLGALT2.
    HPAiHPA031749.
    HPA031750.
    neXtProtiNX_Q8IYK4.
    PharmGKBiPA25606.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3306.
    GeneTreeiENSGT00550000074427.
    HOGENOMiHOG000007198.
    HOVERGENiHBG058097.
    InParanoidiQ8IYK4.
    KOiK11703.
    OMAiMAIWAAT.
    OrthoDBiEOG7060RC.
    PhylomeDBiQ8IYK4.
    TreeFamiTF313826.

    Enzyme and pathway databases

    BRENDAi2.4.1.50. 2681.
    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    SABIO-RKQ8IYK4.

    Miscellaneous databases

    ChiTaRSiCOLGALT2. human.
    GenomeRNAii23127.
    NextBioi44367.
    PROiQ8IYK4.

    Gene expression databases

    BgeeiQ8IYK4.
    CleanExiHS_GLT25D2.
    ExpressionAtlasiQ8IYK4. baseline and differential.
    GenevestigatoriQ8IYK4.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: April 29, 2015
    This is version 109 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.