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Q8IYK4

- GT252_HUMAN

UniProt

Q8IYK4 - GT252_HUMAN

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Protein

Procollagen galactosyltransferase 2

Gene

COLGALT2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. procollagen galactosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

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

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
Complete GO annotation...

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

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

Organism-specific databases

HPAiHPA031749.
HPA031750.

Interactioni

Protein-protein interaction databases

BioGridi116746. 15 interactions.
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.
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 [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.

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. 15 interactions.
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.
GeneTreei ENSGT00550000074427.
HOGENOMi HOG000007198.
HOVERGENi HBG058097.
InParanoidi Q8IYK4.
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

Bgeei Q8IYK4.
CleanExi HS_GLT25D2.
ExpressionAtlasi Q8IYK4. baseline and differential.
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

« 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: October 29, 2014
This is version 103 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