Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein O-glucosyltransferase 1 (EC 2.4.1.-) (CAP10-like 46 kDa protein) (KTEL motif-containing protein 1) (O-glucosyltransferase Rumi homolog) (Rumi) (Protein O-xylosyltransferase POGLUT1) (EC 2.4.2.26) (Wing-shaped neural plate protein) (Wsnp)

 PGLT1_MOUSE             Reviewed;         392 AA.
Q8BYB9; Q8R0H7;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
28-FEB-2018, entry version 117.
RecName: Full=Protein O-glucosyltransferase 1 {ECO:0000305};
EC=2.4.1.- {ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195};
AltName: Full=CAP10-like 46 kDa protein;
AltName: Full=KTEL motif-containing protein 1;
AltName: Full=O-glucosyltransferase Rumi homolog {ECO:0000303|PubMed:21490058};
Short=Rumi {ECO:0000303|PubMed:21490058};
AltName: Full=Protein O-xylosyltransferase POGLUT1;
EC=2.4.2.26 {ECO:0000269|PubMed:21949356};
AltName: Full=Wing-shaped neural plate protein {ECO:0000303|PubMed:26496195};
Short=Wsnp {ECO:0000303|PubMed:26496195};
Flags: Precursor;
Name=Poglut1 {ECO:0000312|MGI:MGI:2444232}; Synonyms=Clp46, Ktelc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=21490058; DOI=10.1242/dev.060020;
Fernandez-Valdivia R., Takeuchi H., Samarghandi A., Lopez M.,
Leonardi J., Haltiwanger R.S., Jafar-Nejad H.;
"Regulation of mammalian Notch signaling and embryonic development by
the protein O-glucosyltransferase Rumi.";
Development 138:1925-1934(2011).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 389-LYS--LEU-392.
PubMed=21949356; DOI=10.1073/pnas.1109696108;
Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A.,
Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A.,
Jafar-Nejad H., Haltiwanger R.S.;
"Rumi functions as both a protein O-glucosyltransferase and a protein
O-xylosyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=26496195; DOI=10.1371/journal.pgen.1005551;
Ramkumar N., Harvey B.M., Lee J.D., Alcorn H.L., Silva-Gagliardi N.F.,
McGlade C.J., Bestor T.H., Wijnholds J., Haltiwanger R.S.,
Anderson K.V.;
"Protein O-glucosyltransferase 1 (POGLUT1) promotes mouse gastrulation
through modification of the apical polarity protein CRUMBS2.";
PLoS Genet. 11:E1005551-E1005551(2015).
-!- FUNCTION: Dual specificity glycosyltransferase that catalyzes the
transfer of glucose and xylose from UDP-glucose and UDP-xylose,
respectively, to a serine residue found in the consensus sequence
of C-X-S-X-P-C (PubMed:21949356, PubMed:26496195). Specifically
targets extracellular EGF repeats of protein such as CRB2, F7, F9
and NOTCH2 (PubMed:21949356, PubMed:26496195). Acts as a positive
regulator of Notch signaling by mediating O-glucosylation of
Notch, leading to regulate muscle development (By similarity).
Notch glucosylation does not affect Notch ligand binding (By
similarity). Required during early development to promote
gastrulation: acts by mediating O-glucosylation of CRB2, which is
required for CRB2 localization to the cell membrane
(PubMed:26496195). {ECO:0000250|UniProtKB:Q8NBL1,
ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-xylose + [protein]-L-serine = UDP
+ [protein]-3-O-(beta-D-xylosyl)-L-serine.
{ECO:0000269|PubMed:21949356}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000250|UniProtKB:Q8NBL1}.
-!- TISSUE SPECIFICITY: Widely expressed in newborn and adult tissues
(at protein level). {ECO:0000269|PubMed:21490058,
ECO:0000269|PubMed:26496195}.
-!- DISRUPTION PHENOTYPE: 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 (PubMed:21490058, PubMed:26496195). 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 (PubMed:21490058). Defects are caused by
a deficit of mesoderm caused by impaired gastrulation.
{ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:26496195}.
-!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK031608; BAC27475.1; -; mRNA.
EMBL; AK035948; BAC29255.1; -; mRNA.
EMBL; AK036224; BAC29351.1; -; mRNA.
EMBL; AK041321; BAC30905.1; -; mRNA.
EMBL; BC026809; AAH26809.1; -; mRNA.
CCDS; CCDS28170.1; -.
RefSeq; NP_759012.1; NM_172380.4.
UniGene; Mm.284366; -.
UniGene; Mm.475345; -.
SMR; Q8BYB9; -.
BioGrid; 230254; 1.
STRING; 10090.ENSMUSP00000038166; -.
CAZy; GT90; Glycosyltransferase Family 90.
iPTMnet; Q8BYB9; -.
PhosphoSitePlus; Q8BYB9; -.
EPD; Q8BYB9; -.
MaxQB; Q8BYB9; -.
PaxDb; Q8BYB9; -.
PeptideAtlas; Q8BYB9; -.
PRIDE; Q8BYB9; -.
Ensembl; ENSMUST00000036210; ENSMUSP00000038166; ENSMUSG00000034064.
GeneID; 224143; -.
KEGG; mmu:224143; -.
UCSC; uc007zfc.2; mouse.
CTD; 56983; -.
MGI; MGI:2444232; Poglut1.
eggNOG; KOG2458; Eukaryota.
eggNOG; ENOG410XT5U; LUCA.
GeneTree; ENSGT00530000063132; -.
HOVERGEN; HBG069044; -.
InParanoid; Q8BYB9; -.
KO; K13667; -.
OMA; IPLVDHC; -.
OrthoDB; EOG091G0BPU; -.
PhylomeDB; Q8BYB9; -.
TreeFam; TF323280; -.
UniPathway; UPA00378; -.
PRO; PR:Q8BYB9; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000034064; -.
CleanEx; MM_KTELC1; -.
Genevisible; Q8BYB9; MM.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0046527; F:glucosyltransferase activity; IMP:MGI.
GO; GO:0030158; F:protein xylosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:MGI.
GO; GO:0048318; P:axial mesoderm development; IMP:MGI.
GO; GO:0072358; P:cardiovascular system development; IMP:MGI.
GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
GO; GO:0006664; P:glycolipid metabolic process; IBA:GO_Central.
GO; GO:0060537; P:muscle tissue development; ISS:UniProtKB.
GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB.
GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
InterPro; IPR006598; LipoPS_modifying.
Pfam; PF05686; Glyco_transf_90; 1.
SMART; SM00672; CAP10; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Endoplasmic reticulum;
Gastrulation; Glycoprotein; Glycosyltransferase; Reference proteome;
Signal; Transferase.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 392 Protein O-glucosyltransferase 1.
/FTId=PRO_0000246686.
MOTIF 389 392 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 389 392 Missing: Significantly more secreted than
wild-type. {ECO:0000269|PubMed:21949356}.
CONFLICT 53 53 N -> S (in Ref. 1; BAC30905).
{ECO:0000305}.
SEQUENCE 392 AA; 46379 MW; CAAD9133E47D3EF0 CRC64;
MERRAGSRLR AWMLLLLLCP VQGRQKDSGS KWKVFLDQIN RALENYEPCS SQNCSCYHGV
IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ IIKNRLFRED DCMFPSRCSG VEHFILEVIH
RLPDMEMVIN VRDYPQVPKW MEPTIPVFSF SKTSEYHDIM YPAWTFWEGG PAVWPLYPTG
LGRWDLFRED LLRSAAQWPW EKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ
AWKSMKDTLG KPAAKDVHLI DHCKYRYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWVEF
FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDIAQEIAK RGSQFIINHL QMDDITCYWE
NLLTDYSKFL SYNVTRRKDY YQIVPRRLKT EL


Related products :

Catalog number Product name Quantity
EIAAB30730 CAP10-like 46 kDa protein,Clp46,KTEL motif-containing protein 1,Ktelc1,Mouse,Mus musculus,Poglut1,Protein O-glucosyltransferase 1
EIAAB30731 Bos taurus,Bovine,CAP10-like 46 kDa protein,CLP46,KTEL motif-containing protein 1,KTELC1,POGLUT1,Protein O-glucosyltransferase 1
EIAAB30732 C3orf9,CAP10-like 46 kDa protein,CLP46,hCLP46,Homo sapiens,Human,KTEL motif-containing protein 1,KTELC1,MDS010,MDSRP,Myelodysplastic syndromes relative protein,POGLUT1,Protein O-glucosyltransferase 1,
E2001Hu Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 96T
YHB1127Mo Mouse Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 96T
E0719Mo Mouse Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
YHB1127Mo Mouse Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
QY-E03888 Human Protein O-Glucosyltransferase 1(POGLUT1)ELISA Kit 96T
YHB2495Hu Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
E2001Hu Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
201-12-2002 Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
UB-E03888 Human Protein O-Glucosyltransferase 1(POGLUT1)ELISA Kit 96T
E0720Mo Mouse Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 96T
201-12-2002 Human Protein O-Glucosyltransferase 1(POGLUT1)ELISA Kit 96T
E0720Mo Mouse Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 48T
201-02-0721 Mouse Protein O-Glucosyltransferase 1(POGLUT1)ELISA kit 96T
YHB2495Hu Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 96T
201-12-2002 Human Protein O-Glucosyltransferase 1 (POGLUT1)ELISA kit 96T
PGLT1_MOUSE ELISA Kit FOR Protein O-glucosyltransferase 1; organism: Mouse; gene name: Poglut1 96T
PGLT1_HUMAN ELISA Kit FOR Protein O-glucosyltransferase 1; organism: Human; gene name: POGLUT1 96T
EIAAB43986 E3 ubiquitin-protein ligase TRIM2,Kiaa0517,Mouse,Mus musculus,Narf,Neural activity-related RING finger protein,Trim2,Tripartite motif-containing protein 2
EIAAB46728 5'OY11.1,Homo sapiens,Human,SUHW2,Suppressor of hairy wing homolog 2,Zinc finger protein 279,Zinc finger protein 280B,Zinc finger protein 632,ZNF279,ZNF280B,ZNF632
30-657 The predicted protein ZNF280A is similar to Drosophila suppressor of hairy wing protein, a leucine zipper protein which represses the function of transcriptional enhancers of the gypsy retrotransposon 0.05 mg
U1742h CLIA Ceramide glucosyltransferase,GCS,GLCT-1,Glucosylceramide synthase,Homo sapiens,Human,UDP-glucose ceramide glucosyltransferase,UDP-glucose N-acylsphingosine D-glucosyltransferase,UGCG 96T
E1742h ELISA Ceramide glucosyltransferase,GCS,GLCT-1,Glucosylceramide synthase,Homo sapiens,Human,UDP-glucose ceramide glucosyltransferase,UDP-glucose N-acylsphingosine D-glucosyltransferase,UGCG 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur