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Q8BYB9

- PGLT1_MOUSE

UniProt

Q8BYB9 - PGLT1_MOUSE

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Protein

Protein O-glucosyltransferase 1

Gene

Poglut1

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

Functioni

Dual specificity glycosyltransferase. Catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats, such as those found in F7, F9 and NOTCH2, on the consensus sequence C-X-S-X-P-C. Positively regulates Notch signaling without affecting Notch ligand binding.1 Publication

Catalytic activityi

Transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine hydroxy group of an acceptor protein substrate.

Pathwayi

GO - Molecular functioni

  1. glucosyltransferase activity Source: MGI
  2. protein xylosyltransferase activity Source: UniProtKB-EC
  3. UDP-glucosyltransferase activity Source: UniProtKB
  4. UDP-xylosyltransferase activity Source: MGI

GO - Biological processi

  1. cardiovascular system development Source: MGI
  2. protein O-linked glycosylation Source: MGI
  3. regulation of Notch signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT90. Glycosyltransferase Family 90.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein O-glucosyltransferase 1 (EC:2.4.1.-)
Alternative name(s):
CAP10-like 46 kDa protein
KTEL motif-containing protein 1
O-glucosyltransferase Rumi homolog
Short name:
Rumi
Protein O-xylosyltransferase (EC:2.4.2.26)
Gene namesi
Name:Poglut1
Synonyms:Clp46, Ktelc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:2444232. Poglut1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mutant embryos die at or before 9.5 dpc. At 7.0 to 7.5 dpc, they cannot be morphologically distinguished from wild-type littermates. At 8.0 dpc, mutant embryos exhibit an abnormally expanded neural plate that does not fold properly, absence of heart rudiments and posterior axis truncation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi389 – 3924Missing: Significantly more secreted than wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 392369Protein O-glucosyltransferase 1PRO_0000246686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BYB9.
PaxDbiQ8BYB9.
PRIDEiQ8BYB9.

PTM databases

PhosphoSiteiQ8BYB9.

Expressioni

Tissue specificityi

Widely expressed in newborn and adult tissues (at protein level).1 Publication

Gene expression databases

BgeeiQ8BYB9.
CleanExiMM_KTELC1.
ExpressionAtlasiQ8BYB9. baseline and differential.
GenevestigatoriQ8BYB9.

Interactioni

Protein-protein interaction databases

BioGridi230254. 1 interaction.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi389 – 3924Endoplasmic reticulum retention signal

Sequence similaritiesi

Belongs to the glycosyltransferase 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248922.
GeneTreeiENSGT00530000063132.
HOVERGENiHBG069044.
InParanoidiQ8BYB9.
KOiK13667.
OMAiINHLQMD.
OrthoDBiEOG7R831J.
PhylomeDBiQ8BYB9.
TreeFamiTF323280.

Family and domain databases

InterProiIPR006598. LipoPS_modifying.
[Graphical view]
PfamiPF05686. Glyco_transf_90. 1 hit.
[Graphical view]
SMARTiSM00672. CAP10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BYB9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERRAGSRLR AWMLLLLLCP VQGRQKDSGS KWKVFLDQIN RALENYEPCS
60 70 80 90 100
SQNCSCYHGV IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ IIKNRLFRED
110 120 130 140 150
DCMFPSRCSG VEHFILEVIH RLPDMEMVIN VRDYPQVPKW MEPTIPVFSF
160 170 180 190 200
SKTSEYHDIM YPAWTFWEGG PAVWPLYPTG LGRWDLFRED LLRSAAQWPW
210 220 230 240 250
EKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ AWKSMKDTLG
260 270 280 290 300
KPAAKDVHLI DHCKYRYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWVEF
310 320 330 340 350
FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDIAQEIAK RGSQFIINHL
360 370 380 390
QMDDITCYWE NLLTDYSKFL SYNVTRRKDY YQIVPRRLKT EL
Length:392
Mass (Da):46,379
Last modified:July 25, 2006 - v2
Checksum:iCAAD9133E47D3EF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531N → S in BAC30905. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031608 mRNA. Translation: BAC27475.1.
AK035948 mRNA. Translation: BAC29255.1.
AK036224 mRNA. Translation: BAC29351.1.
AK041321 mRNA. Translation: BAC30905.1.
BC026809 mRNA. Translation: AAH26809.1.
CCDSiCCDS28170.1.
RefSeqiNP_759012.1. NM_172380.4.
UniGeneiMm.284366.
Mm.475345.

Genome annotation databases

EnsembliENSMUST00000036210; ENSMUSP00000038166; ENSMUSG00000034064.
GeneIDi224143.
KEGGimmu:224143.
UCSCiuc007zfc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031608 mRNA. Translation: BAC27475.1 .
AK035948 mRNA. Translation: BAC29255.1 .
AK036224 mRNA. Translation: BAC29351.1 .
AK041321 mRNA. Translation: BAC30905.1 .
BC026809 mRNA. Translation: AAH26809.1 .
CCDSi CCDS28170.1.
RefSeqi NP_759012.1. NM_172380.4.
UniGenei Mm.284366.
Mm.475345.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230254. 1 interaction.

Protein family/group databases

CAZyi GT90. Glycosyltransferase Family 90.

PTM databases

PhosphoSitei Q8BYB9.

Proteomic databases

MaxQBi Q8BYB9.
PaxDbi Q8BYB9.
PRIDEi Q8BYB9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000036210 ; ENSMUSP00000038166 ; ENSMUSG00000034064 .
GeneIDi 224143.
KEGGi mmu:224143.
UCSCi uc007zfc.1. mouse.

Organism-specific databases

CTDi 56983.
MGIi MGI:2444232. Poglut1.

Phylogenomic databases

eggNOGi NOG248922.
GeneTreei ENSGT00530000063132.
HOVERGENi HBG069044.
InParanoidi Q8BYB9.
KOi K13667.
OMAi INHLQMD.
OrthoDBi EOG7R831J.
PhylomeDBi Q8BYB9.
TreeFami TF323280.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.

Miscellaneous databases

NextBioi 377117.
PROi Q8BYB9.
SOURCEi Search...

Gene expression databases

Bgeei Q8BYB9.
CleanExi MM_KTELC1.
ExpressionAtlasi Q8BYB9. baseline and differential.
Genevestigatori Q8BYB9.

Family and domain databases

InterProi IPR006598. LipoPS_modifying.
[Graphical view ]
Pfami PF05686. Glyco_transf_90. 1 hit.
[Graphical view ]
SMARTi SM00672. CAP10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, Testis and Thymus.
  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: FVB/N.
    Tissue: Colon.
  3. "Regulation of mammalian Notch signaling and embryonic development by the protein O-glucosyltransferase Rumi."
    Fernandez-Valdivia R., Takeuchi H., Samarghandi A., Lopez M., Leonardi J., Haltiwanger R.S., Jafar-Nejad H.
    Development 138:1925-1934(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  4. Cited for: FUNCTION, MUTAGENESIS OF 389-LYS--LEU-392.

Entry informationi

Entry nameiPGLT1_MOUSE
AccessioniPrimary (citable) accession number: Q8BYB9
Secondary accession number(s): Q8R0H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: November 26, 2014
This is version 94 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3