Q8IYK4 (GT252_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	COLGALT2
Synonyms:	C1orf17, GLT25D2, KIAA0584

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	extracellular matrix organization Traceable author statement. Source: Reactome lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	procollagen galactosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 626	599	Procollagen galactosyltransferase 2		PRO_0000309541
Regions
	Motif	623 – 626	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	185	1	N-linked (GlcNAc...) Potential
	Glycosylation	382	1	N-linked (GlcNAc...) Potential
	Glycosylation	580	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	475	1	V → I in a breast cancer sample; somatic mutation. Ref.8		VAR_036978

Sequences

	Sequence		Length	Mass (Da)
	Q8IYK4 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 697A76DB73F67539	FASTA	626	72,924
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00514694.
PIR	T00343.
RefSeq	NP_055916.1. NM_015101.2.
UniGene	Hs.387995.
3D structure databases
ProteinModelPortal	Q8IYK4.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000354960.
Protein family/group databases
CAZy	GT25. Glycosyltransferase Family 25.
PTM databases
PhosphoSite	Q8IYK4.
Polymorphism databases
DMDM	74750765.
Proteomic databases
PaxDb	Q8IYK4.
PRIDE	Q8IYK4.
Protocols and materials databases
DNASU	23127.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361927; ENSP00000354960; ENSG00000198756.
GeneID	23127.
KEGG	hsa:23127.
UCSC	uc001gqr.3. human.
Organism-specific databases
CTD	23127.
GeneCards	GC01M183898.
HGNC	HGNC:16790. COLGALT2.
HPA	HPA031749. HPA031750.
neXtProt	NX_Q8IYK4.
PharmGKB	PA25606.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3306.
HOGENOM	HOG000007198.
HOVERGEN	HBG058097.
KO	K11703.
OMA	LPHFLGC.
OrthoDB	EOG4B2SWX.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
SABIO-RK	Q8IYK4.
Gene expression databases
ArrayExpress	Q8IYK4.
Bgee	Q8IYK4.
CleanEx	HS_GLT25D2.
Genevestigator	Q8IYK4.
Family and domain databases
InterPro	IPR002654. Glyco_trans_25. [Graphical view]
Pfam	PF01755. Glyco_transf_25. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23127.
NextBio	44367.

Entry information

Entry name

GT252_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.