Q8NBJ5 (GT251_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Procollagen galactosyltransferase 1
EC=2.4.1.50

Alternative name(s):
Collagen beta(1-O)galactosyltransferase 1
Glycosyltransferase 25 family member 1
Hydroxylysine galactosyltransferase 1

Gene names

Name:	COLGALT1
Synonyms:	GLT25D1
ORF Names:	PSEC0241

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	622 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 of 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. Note: Colocalized with PLOD3 and mannose binding lectin. Ref.7
Tissue specificity	Ubiquitous with higher levels in placenta, heart, lung and spleen. Ref.6
Post-translational modification	N-glycosylated. Ref.7
Sequence similarities	Belongs to the glycosyltransferase 25 family.
Caution	Has no glucosyltransferase activity.
Biophysicochemical properties	Kinetic parameters: KM=18.7 µM for UDP-galactose Ref.6

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
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 Inferred from direct assay Ref.7. Source: UniProtKB
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 – 29	29	Potential
	Chain	30 – 622	593	Procollagen galactosyltransferase 1		PRO_0000309536
Regions
	Motif	619 – 622	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	184	1	N-linked (GlcNAc...) Potential
	Glycosylation	381	1	N-linked (GlcNAc...) Ref.5
Experimental info
	Sequence conflict	100	1	V → E in BAC11307. Ref.1
	Sequence conflict	220	1	I → T in BAC11307. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8NBJ5 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: C430974CB1CF5280	FASTA	622	71,636
	10 20 30 40 50 60 MAAAPRAGRR RGQPLLALLL LLLAPLPPGA PPGADAYFPE ERWSPESPLQ APRVLIALLA 70 80 90 100 110 120 RNAAHALPTT LGALERLRHP RERTALWVAT DHNMDNTSTV LREWLVAVKS LYHSVEWRPA 130 140 150 160 170 180 EEPRSYPDEE GPKHWSDSRY EHVMKLRQAA LKSARDMWAD YILFVDADNL ILNPDTLSLL 190 200 210 220 230 240 IAENKTVVAP MLDSRAAYSN FWCGMTSQGY YKRTPAYIPI RKRDRRGCFA VPMVHSTFLI 250 260 270 280 290 300 DLRKAASRNL AFYPPHPDYT WSFDDIIVFA FSCKQAEVQM YVCNKEEYGF LPVPLRAHST 310 320 330 340 350 360 LQDEAESFMH VQLEVMVKHP PAEPSRFISA PTKTPDKMGF DEVFMINLRR RQDRRERMLR 370 380 390 400 410 420 ALQAQEIECR LVEAVDGKAM NTSQVEALGI QMLPGYRDPY HGRPLTKGEL GCFLSHYNIW 430 440 450 460 470 480 KEVVDRGLQK SLVFEDDLRF EIFFKRRLMN LMRDVEREGL DWDLIYVGRK RMQVEHPEKA 490 500 510 520 530 540 VPRVRNLVEA DYSYWTLAYV ISLQGARKLL AAEPLSKMLP VDEFLPVMFD KHPVSEYKAH 550 560 570 580 590 600 FSLRNLHAFS VEPLLIYPTH YTGDDGYVSD TETSVVWNNE HVKTDWDRAK SQKMREQQAL 610 620 SREAKNSDVL QSPLDSAARD EL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: Cervix.
[5]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96 AND ASN-381, MASS SPECTROMETRY. Tissue: Liver.
[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]	"The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein." Liefhebber J.M., Punt S., Spaan W.J., van Leeuwen H.C. BMC Cell Biol. 11:33-33(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, MASS SPECTROMETRY.
[8]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK074941 mRNA. Translation: BAC11307.1. AK075541 mRNA. Translation: BAC11684.1. AC010618 Genomic DNA. No translation available. CH471106 Genomic DNA. Translation: EAW84622.1. BC108308 mRNA. Translation: AAI08309.1.
IPI	IPI00168262.
RefSeq	NP_078932.2. NM_024656.2.
UniGene	Hs.418795.
3D structure databases
ProteinModelPortal	Q8NBJ5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NBJ5. 3 interactions.
STRING	9606.ENSP00000252599.
Protein family/group databases
CAZy	GT25. Glycosyltransferase Family 25.
PTM databases
PhosphoSite	Q8NBJ5.
Polymorphism databases
DMDM	74715064.
Proteomic databases
PaxDb	Q8NBJ5.
PeptideAtlas	Q8NBJ5.
PRIDE	Q8NBJ5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252599; ENSP00000252599; ENSG00000130309.
GeneID	79709.
KEGG	hsa:79709.
UCSC	uc002nhc.1. human.
Organism-specific databases
CTD	79709.
GeneCards	GC19P017666.
HGNC	HGNC:26182. COLGALT1.
HPA	HPA047821.
neXtProt	NX_Q8NBJ5.
PharmGKB	PA134991138.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG293154.
HOGENOM	HOG000007198.
HOVERGEN	HBG058097.
InParanoid	Q8NBJ5.
KO	K11703.
OMA	QLEVMVK.
OrthoDB	EOG4B2SWX.
PhylomeDB	Q8NBJ5.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
SABIO-RK	Q8NBJ5.
Gene expression databases
ArrayExpress	Q8NBJ5.
Bgee	Q8NBJ5.
CleanEx	HS_GLT25D1.
Genevestigator	Q8NBJ5.
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
ChiTaRS	GLT25D1. human.
GenomeRNAi	79709.
NextBio	69027.

Entry information

Entry name

GT251_HUMAN

Accession

Primary (citable) accession number: Q8NBJ5
Secondary accession number(s): Q8NC64

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 86 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.