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Q8K297

- GT251_MOUSE

UniProt

Q8K297 - GT251_MOUSE

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Protein

Procollagen galactosyltransferase 1

Gene

Colgalt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen.By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. procollagen galactosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipopolysaccharide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Colgalt1
Synonyms:Glt25d1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1924348. Colgalt1.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation
Note: Colocalized with PLOD3 and mannose binding lectin.By similarity

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 617586Procollagen galactosyltransferase 1PRO_0000309537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)1 Publication
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8K297.
PaxDbiQ8K297.
PRIDEiQ8K297.

PTM databases

PhosphoSiteiQ8K297.

Expressioni

Gene expression databases

BgeeiQ8K297.
CleanExiMM_GLT25D1.
GenevestigatoriQ8K297.

Interactioni

Protein-protein interaction databases

BioGridi231529. 2 interactions.
IntActiQ8K297. 1 interaction.
MINTiMINT-1866727.

Structurei

3D structure databases

ProteinModelPortaliQ8K297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi614 – 6174Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase 25 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
InParanoidiQ8K297.
KOiK11703.
OMAiMWADYIL.
OrthoDBiEOG7060RC.
PhylomeDBiQ8K297.
TreeFamiTF313826.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
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.

Q8K297-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALPRGSRG LPLLPLLLLL PPLGGPRGAD GYFPEERWSP ESPLQAPRVL
60 70 80 90 100
IALLARNAAP ALPATLGALE QLRHPRERTA LWVATDHNTD NTSAILREWL
110 120 130 140 150
VAVKGLYHSV EWRPAEEPSS YPDEEGPKHW SDSRYEHVMK LRQAALKSAR
160 170 180 190 200
DMWADYILFM DIDNLITNPD TLSLLIAENK TVVAPMLDSR AAYSNFWCGM
210 220 230 240 250
TSQGYYKRTP AYIPIRKRDR RGCFAVPMVH STFLIDLRKA ASRNLAFYPT
260 270 280 290 300
HPDYTWSFDD IIVFAFSCKQ AEVQMYVCNK EVYGFLPVPL RAHSSLQDEA
310 320 330 340 350
ESFMHVQLEV MVKHPPVQLS RFISAPRKTS DKMGFDEVFM INLKRRRDRR
360 370 380 390 400
ERMLRALHEQ EIDCQLVEAV DGKAMNTSQV EAMGIQMLPG YRDPYHGRPL
410 420 430 440 450
TKGELGCFLS HYNIWKEVVD RGLQKSLVFE DDLRFEIFFK RRLMNLMRDV
460 470 480 490 500
EREGLDWDLI YVGRKRMQVE HPEKAVPHVR NLVEADYSYW TLAYVISLQG
510 520 530 540 550
AQKLLAAKPL AKMLPVDEFL PVMFDKHPMS EYKSHFSPRN LRAFSVEPLL
560 570 580 590 600
IYPTHYTGDD GYVSDTETSV VWNNEQVKTD WDRAKSQKMR EQQALSREAK
610
NSDVLQSPLD STARDEL
Length:617
Mass (Da):71,061
Last modified:November 13, 2007 - v2
Checksum:i828D28E3300D9CC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81S → L in BAE43293. (PubMed:16141072)Curated
Sequence conflicti30 – 301D → A in BAE43293. (PubMed:16141072)Curated
Sequence conflicti250 – 2501T → P in AAH32165. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK035788 mRNA. Translation: BAE43293.1.
BC032165 mRNA. Translation: AAH32165.1.
BC056951 mRNA. Translation: AAH56951.1.
CCDSiCCDS22401.1.
RefSeqiNP_666323.2. NM_146211.3.
UniGeneiMm.273836.
Mm.334606.

Genome annotation databases

EnsembliENSMUST00000047903; ENSMUSP00000047923; ENSMUSG00000034807.
GeneIDi234407.
KEGGimmu:234407.
UCSCiuc009mee.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK035788 mRNA. Translation: BAE43293.1 .
BC032165 mRNA. Translation: AAH32165.1 .
BC056951 mRNA. Translation: AAH56951.1 .
CCDSi CCDS22401.1.
RefSeqi NP_666323.2. NM_146211.3.
UniGenei Mm.273836.
Mm.334606.

3D structure databases

ProteinModelPortali Q8K297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 231529. 2 interactions.
IntActi Q8K297. 1 interaction.
MINTi MINT-1866727.

Protein family/group databases

CAZyi GT25. Glycosyltransferase Family 25.

PTM databases

PhosphoSitei Q8K297.

Proteomic databases

MaxQBi Q8K297.
PaxDbi Q8K297.
PRIDEi Q8K297.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047903 ; ENSMUSP00000047923 ; ENSMUSG00000034807 .
GeneIDi 234407.
KEGGi mmu:234407.
UCSCi uc009mee.2. mouse.

Organism-specific databases

CTDi 234407.
MGIi MGI:1924348. Colgalt1.

Phylogenomic databases

eggNOGi NOG293154.
GeneTreei ENSGT00550000074427.
HOGENOMi HOG000007198.
HOVERGENi HBG058097.
InParanoidi Q8K297.
KOi K11703.
OMAi MWADYIL.
OrthoDBi EOG7060RC.
PhylomeDBi Q8K297.
TreeFami TF313826.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSi GLT25D1. mouse.
NextBioi 382175.
PROi Q8K297.
SOURCEi Search...

Gene expression databases

Bgeei Q8K297.
CleanExi MM_GLT25D1.
Genevestigatori Q8K297.

Family and domain databases

Gene3Di 3.90.550.10. 2 hits.
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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91.

Entry informationi

Entry nameiGT251_MOUSE
AccessioniPrimary (citable) accession number: Q8K297
Secondary accession number(s): Q3V3R5, Q6PGL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: October 1, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3