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C1GALT1-specific chaperone 1 (C38H2-like protein 1) (C38H2-L1) (Core 1 beta1,3-galactosyltransferase 2) (C1Gal-T2) (C1GalT2) (Core 1 beta3-Gal-T2) (Core 1 beta3-galactosyltransferase-specific molecular chaperone)

 C1GLC_HUMAN             Reviewed;         318 AA.
Q96EU7; A8K246; Q8WWS3; Q9NZX1;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
20-JUN-2018, entry version 134.
RecName: Full=C1GALT1-specific chaperone 1;
AltName: Full=C38H2-like protein 1;
Short=C38H2-L1;
AltName: Full=Core 1 beta1,3-galactosyltransferase 2;
Short=C1Gal-T2;
Short=C1GalT2;
Short=Core 1 beta3-Gal-T2;
AltName: Full=Core 1 beta3-galactosyltransferase-specific molecular chaperone;
Name=C1GALT1C1; Synonyms=COSMC;
ORFNames=HSPC067, MSTP143, UNQ273/PRO310;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=12361956; DOI=10.1074/jbc.M205839200;
Kudo T., Iwai T., Kubota T., Iwasaki H., Takayma Y., Hiruma T.,
Inaba N., Zhang Y., Gotoh M., Togayachi A., Narimatsu H.;
"Molecular cloning and characterization of a novel UDP-
Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2),
an enzyme synthesizing a core 1 structure of O-glycan.";
J. Biol. Chem. 277:47724-47731(2002).
[2]
ERRATUM.
Kudo T., Iwai T., Kubota T., Iwasaki H., Takayma Y., Hiruma T.,
Inaba N., Zhang Y., Gotoh M., Togayachi A., Narimatsu H.;
J. Biol. Chem. 281:24999-24999(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH C1GALT1.
PubMed=12464682; DOI=10.1073/pnas.262438199;
Ju T., Cummings R.D.;
"A unique molecular chaperone Cosmc required for activity of the
mammalian core 1 beta 3-galactosyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 99:16613-16618(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Rubboli F., Marchitiello A., Ballabio A., Banfi S.;
"Identification and characterization of C38H2-L1.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Aorta;
Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Ovary;
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).
[12]
VARIANT TNPS LYS-152, VARIANT GLU-131, CHARACTERIZATION OF VARIANT
TNPS LYS-152, AND CHARACTERIZATION OF VARIANT GLU-131.
PubMed=16251947; DOI=10.1038/4371252a;
Ju T., Cummings R.D.;
"Protein glycosylation: chaperone mutation in Tn syndrome.";
Nature 437:1252-1252(2005).
[13]
INVOLVEMENT IN PRODUCTION OF TUMOR-SPECIFIC ANTIGEN.
PubMed=17038624; DOI=10.1126/science.1129200;
Schietinger A., Philip M., Yoshida B.A., Azadi P., Liu H.,
Meredith S.C., Schreiber H.;
"A mutant chaperone converts a wild-type protein into a tumor-specific
antigen.";
Science 314:304-308(2006).
[14]
VARIANTS GLU-131; VAL-143 AND HIS-222, AND VARIANTS TNPS LYS-152 AND
PRO-193.
PubMed=18537974; DOI=10.1111/j.1365-2141.2008.07215.x;
Crew V.K., Singleton B.K., Green C., Parsons S.F., Daniels G.,
Anstee D.J.;
"New mutations in C1GALT1C1 in individuals with Tn positive
phenotype.";
Br. J. Haematol. 142:657-667(2008).
-!- FUNCTION: Probable chaperone required for the generation of 1 O-
glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a
precursor for many extended O-glycans in glycoproteins. Probably
acts as a specific molecular chaperone assisting the
folding/stability of core 1 beta-3-galactosyltransferase
(C1GALT1). {ECO:0000269|PubMed:12464682}.
-!- SUBUNIT: Associates with core 1 beta-3-galactosyltransferase
(C1GALT1), probably not with the soluble active form.
-!- INTERACTION:
Q9NS00:C1GALT1; NbExp=4; IntAct=EBI-2837343, EBI-8628584;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Abundantly expressed
in salivary gland, stomach, small intestine, kidney, and testis
and at intermediate levels in whole brain, cerebellum, spinal
cord, thymus, spleen, trachea, lung, pancreas, ovary, and uterus.
{ECO:0000269|PubMed:12361956}.
-!- DISEASE: Tn polyagglutination syndrome (TNPS) [MIM:300622]: A
clonal disorder characterized by the polyagglutination of red
blood cells by naturally occurring anti-Tn antibodies following
exposure of the Tn antigen on the surface of erythrocytes. Only a
subset of red cells express the antigen, which can also be
expressed on platelets and leukocytes. This condition may occur in
healthy individuals who manifest asymptomatic anemia, leukopenia,
or thrombocytopenia. However, there is also an association between
the Tn antigen and leukemia or myelodysplastic disorders.
{ECO:0000269|PubMed:16251947, ECO:0000269|PubMed:18537974}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Defects in C1GALT1C1 in Ag104A cell line create a
tumor-specific glycopeptidic neo-epitope. This epitope induces a
high-affinity, highly specific, syngeneic monoclonal antibody.
This is caused by the abolition of function of a
glycosyltransferase, disrupting O-glycan Core 1 synthesis.
-!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-
Gal-T subfamily. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:12361956) assigned to be a
glycosyltransferase. However, it was later shown (Ref.2 and
PubMed:12464682) that it has no transferase activity and rather
acts as a chaperone. {ECO:0000305|PubMed:12361956}.
-!- SEQUENCE CAUTION:
Sequence=AAF29039.1; Type=Frameshift; Positions=16, 22, 24, 25; Evidence={ECO:0000305};
Sequence=CAC80277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=C1GALT1-specific chaperone 1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_443";
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EMBL; AB084170; BAC41493.1; -; mRNA.
EMBL; AY159319; AAN78129.1; -; mRNA.
EMBL; AJ238398; CAC80277.1; ALT_INIT; mRNA.
EMBL; AF161552; AAF29039.1; ALT_FRAME; mRNA.
EMBL; AF177284; AAQ13670.1; -; mRNA.
EMBL; AY358642; AAQ89005.1; -; mRNA.
EMBL; AC011890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK290111; BAF82800.1; -; mRNA.
EMBL; CH471107; EAX11873.1; -; Genomic_DNA.
EMBL; BC011930; AAH11930.1; -; mRNA.
EMBL; BC050441; AAH50441.1; -; mRNA.
CCDS; CCDS14602.1; -.
RefSeq; NP_001011551.1; NM_001011551.2.
RefSeq; NP_689905.1; NM_152692.4.
UniGene; Hs.643920; -.
ProteinModelPortal; Q96EU7; -.
SMR; Q96EU7; -.
BioGrid; 118844; 17.
IntAct; Q96EU7; 3.
MINT; Q96EU7; -.
STRING; 9606.ENSP00000304364; -.
CAZy; GT31; Glycosyltransferase Family 31.
iPTMnet; Q96EU7; -.
PhosphoSitePlus; Q96EU7; -.
BioMuta; C1GALT1C1; -.
DMDM; 74751849; -.
EPD; Q96EU7; -.
MaxQB; Q96EU7; -.
PaxDb; Q96EU7; -.
PeptideAtlas; Q96EU7; -.
PRIDE; Q96EU7; -.
ProteomicsDB; 76452; -.
DNASU; 29071; -.
Ensembl; ENST00000304661; ENSP00000304364; ENSG00000171155.
Ensembl; ENST00000371313; ENSP00000360363; ENSG00000171155.
GeneID; 29071; -.
KEGG; hsa:29071; -.
UCSC; uc004esy.4; human.
CTD; 29071; -.
DisGeNET; 29071; -.
EuPathDB; HostDB:ENSG00000171155.7; -.
GeneCards; C1GALT1C1; -.
HGNC; HGNC:24338; C1GALT1C1.
HPA; HPA015632; -.
MalaCards; C1GALT1C1; -.
MIM; 300611; gene.
MIM; 300622; phenotype.
neXtProt; NX_Q96EU7; -.
OpenTargets; ENSG00000171155; -.
PharmGKB; PA134974626; -.
eggNOG; KOG2246; Eukaryota.
eggNOG; ENOG410YRJG; LUCA.
GeneTree; ENSGT00530000063264; -.
HOGENOM; HOG000013033; -.
HOVERGEN; HBG059493; -.
InParanoid; Q96EU7; -.
KO; K09653; -.
OMA; CLKYTGV; -.
OrthoDB; EOG091G0F36; -.
PhylomeDB; Q96EU7; -.
TreeFam; TF317293; -.
BRENDA; 2.4.1.122; 2681.
Reactome; R-HSA-5083632; Defective C1GALT1C1 causes Tn polyagglutination syndrome (TNPS).
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
ChiTaRS; C1GALT1C1; human.
GenomeRNAi; 29071; -.
PRO; PR:Q96EU7; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000171155; -.
CleanEx; HS_C1GALT1C1; -.
Genevisible; Q96EU7; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IBA:GO_Central.
GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
GO; GO:0030168; P:platelet activation; IEA:Ensembl.
GO; GO:0036344; P:platelet morphogenesis; IEA:Ensembl.
GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
InterPro; IPR026731; C1GALT1C1.
PANTHER; PTHR23033:SF2; PTHR23033:SF2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Disease mutation; Membrane;
Polymorphism; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 318 C1GALT1-specific chaperone 1.
/FTId=PRO_0000285074.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 26 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 27 318 Lumenal. {ECO:0000255}.
VARIANT 131 131 D -> E (common polymorphism; retains
capacity to promote Tn synthase activity;
dbSNP:rs17261572).
{ECO:0000269|PubMed:16251947,
ECO:0000269|PubMed:18537974}.
/FTId=VAR_031910.
VARIANT 143 143 A -> V (in dbSNP:rs45557031).
{ECO:0000269|PubMed:18537974}.
/FTId=VAR_069274.
VARIANT 152 152 E -> K (in TNPS; loss capacity to promote
Tn synthase activity; dbSNP:rs137853599).
{ECO:0000269|PubMed:16251947,
ECO:0000269|PubMed:18537974}.
/FTId=VAR_031911.
VARIANT 193 193 S -> P (in TNPS; dbSNP:rs397514537).
{ECO:0000269|PubMed:18537974}.
/FTId=VAR_069275.
VARIANT 222 222 Q -> H (in dbSNP:rs200973382).
{ECO:0000269|PubMed:18537974}.
/FTId=VAR_069276.
CONFLICT 76 76 K -> E (in Ref. 4; CAC80277).
{ECO:0000305}.
CONFLICT 107 107 V -> E (in Ref. 5; AAF29039).
{ECO:0000305}.
CONFLICT 108 108 F -> L (in Ref. 4; CAC80277).
{ECO:0000305}.
SEQUENCE 318 AA; 36382 MW; 5D766966A872CA84 CRC64;
MLSESSSFLK GVMLGSIFCA LITMLGHIRI GHGNRMHHHE HHHLQAPNKE DILKISEDER
MELSKSFRVY CIILVKPKDV SLWAAVKETW TKHCDKAEFF SSENVKVFES INMDTNDMWL
MMRKAYKYAF DKYRDQYNWF FLARPTTFAI IENLKYFLLK KDPSQPFYLG HTIKSGDLEY
VGMEGGIVLS VESMKRLNSL LNIPEKCPEQ GGMIWKISED KQLAVCLKYA GVFAENAEDA
DGKDVFNTKS VGLSIKEAMT YHPNQVVEGC CSDMAVTFNG LTPNQMHVMM YGVYRLRAFG
HIFNDALVFL PPNGSDND


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E1908p ELISA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Pig,Sus scrofa 96T
U1908p CLIA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Pig,Sus scrofa 96T
E1908p ELISA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Pig,Sus scrofa 96T
U1908p CLIA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Pig,Sus scrofa 96T
E1908b ELISA ACAN,AGC1,Aggrecan core protein,Bos taurus,Bovine,Cartilage-specific proteoglycan core protein,CSPCP 96T
E1908r ELISA Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Rat,Rattus norvegicus 96T
U1908b CLIA kit ACAN,AGC1,Aggrecan core protein,Bos taurus,Bovine,Cartilage-specific proteoglycan core protein,CSPCP 96T
E1908m ELISA kit Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Mouse,Mus musculus 96T
E1908r ELISA kit Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Rat,Rattus norvegicus 96T
U1908r CLIA Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Rat,Rattus norvegicus 96T
U1908r CLIA kit Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Rat,Rattus norvegicus 96T
U1908m CLIA Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Mouse,Mus musculus 96T
E1908m ELISA Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Mouse,Mus musculus 96T
E1908b ELISA kit ACAN,AGC1,Aggrecan core protein,Bos taurus,Bovine,Cartilage-specific proteoglycan core protein,CSPCP 96T
U1908m CLIA kit Acan,Agc,Agc1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Mouse,Mus musculus 96T
U1908b CLIA ACAN,AGC1,Aggrecan core protein,Bos taurus,Bovine,Cartilage-specific proteoglycan core protein,CSPCP 96T
U1908Rb CLIA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Oryctolagus cuniculus,Rabbit 96T
U1908Rb CLIA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Oryctolagus cuniculus,Rabbit 96T
E1908Rb ELISA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,CSPCP,Oryctolagus cuniculus,Rabbit 96T


 

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