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Q8IYK4 (GT252_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:COLGALT2
Synonyms:C1orf17, GLT25D2, KIAA0584
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen. Ref.6

Catalytic activity

UDP-alpha-D-galactose + 5-hydroxy-L-lysine-[procollagen] = UDP + 5-(D-galactosyloxy)-L-lysine-[procollagen]. Ref.6

Subcellular location

Endoplasmic reticulum lumen Potential.

Tissue specificity

Expressed in brain and skeletal muscle. Ref.6

Sequence similarities

Belongs to the glycosyltransferase 25 family.

Caution

Has no glucosyltransferase activity.

Biophysicochemical properties

Kinetic parameters:

KM=33.5 µM for UDP-galactose Ref.6

Sequence caution

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

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processextracellular matrix organization

Traceable author statement. Source: Reactome

lipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Traceable author statement. Source: Reactome

   Molecular_functionprocollagen galactosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 626599Procollagen galactosyltransferase 2
PRO_0000309541

Regions

Motif623 – 6264Prevents secretion from ER Potential

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential

Natural variations

Natural variant4751V → I in a breast cancer sample; somatic mutation. Ref.8
VAR_036978

Sequences

Sequence LengthMass (Da)Tools
Q8IYK4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 697A76DB73F67539

FASTA62672,924
        10         20         30         40         50         60 
MAARPAATLA WSLLLLSSAL LREGCRARFV AERDSEDDGE EPVVFPESPL QSPTVLVAVL 

        70         80         90        100        110        120 
ARNAAHTLPH FLGCLERLDY PKSRMAIWAA TDHNVDNTTE IFREWLKNVQ RLYHYVEWRP 

       130        140        150        160        170        180 
MDEPESYPDE IGPKHWPTSR FAHVMKLRQA ALRTAREKWS DYILFIDVDN FLTNPQTLNL 

       190        200        210        220        230        240 
LIAENKTIVA PMLESRGLYS NFWCGITPKG FYKRTPDYVQ IREWKRTGCF PVPMVHSTFL 

       250        260        270        280        290        300 
IDLRKEASDK LTFYPPHQDY TWTFDDIIVF AFSSRQAGIQ MYLCNREHYG YLPIPLKPHQ 

       310        320        330        340        350        360 
TLQEDIENLI HVQIEAMIDR PPMEPSQYVS VVPKYPDKMG FDEIFMINLK RRKDRRDRML 

       370        380        390        400        410        420 
RTLYEQEIEV KIVEAVDGKA LNTSQLKALN IEMLPGYRDP YSSRPLTRGE IGCFLSHYSV 

       430        440        450        460        470        480 
WKEVIDRELE KTLVIEDDVR FEHQFKKKLM KLMDNIDQAQ LDWELIYIGR KRMQVKEPEK 

       490        500        510        520        530        540 
AVPNVANLVE ADYSYWTLGY VISLEGAQKL VGANPFGKML PVDEFLPVMY NKHPVAEYKE 

       550        560        570        580        590        600 
YYESRDLKAF SAEPLLIYPT HYTGQPGYLS DTETSTIWDN ETVATDWDRT HAWKSRKQSR 

       610        620 
IYSNAKNTEA LPPPTSLDTV PSRDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-475.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1360.1.
PIRT00343.
RefSeqNP_055916.1. NM_015101.2.
UniGeneHs.387995.

3D structure databases

ProteinModelPortalQ8IYK4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116746. 1 interaction.
STRING9606.ENSP00000354960.

Protein family/group databases

CAZyGT25. Glycosyltransferase Family 25.

PTM databases

PhosphoSiteQ8IYK4.

Polymorphism databases

DMDM74750765.

Proteomic databases

MaxQBQ8IYK4.
PaxDbQ8IYK4.
PRIDEQ8IYK4.

Protocols and materials databases

DNASU23127.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361927; ENSP00000354960; ENSG00000198756.
GeneID23127.
KEGGhsa:23127.
UCSCuc001gqr.3. human.

Organism-specific databases

CTD23127.
GeneCardsGC01M183899.
HGNCHGNC:16790. COLGALT2.
HPAHPA031749.
HPA031750.
neXtProtNX_Q8IYK4.
PharmGKBPA25606.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3306.
HOGENOMHOG000007198.
HOVERGENHBG058097.
KOK11703.
OMAQIREWKR.
OrthoDBEOG7060RC.
PhylomeDBQ8IYK4.
TreeFamTF313826.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SABIO-RKQ8IYK4.

Gene expression databases

ArrayExpressQ8IYK4.
BgeeQ8IYK4.
CleanExHS_GLT25D2.
GenevestigatorQ8IYK4.

Family and domain databases

InterProIPR002654. Glyco_trans_25.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF01755. Glyco_transf_25. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23127.
NextBio44367.
PROQ8IYK4.

Entry information

Entry nameGT252_HUMAN
AccessionPrimary (citable) accession number: Q8IYK4
Secondary accession number(s): O60327, Q9BZR0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM