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

Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Dolichyl-phosphate beta-D-mannosyltransferase subunit 1) (Mannose-P-dolichol synthase subunit 1) (MPD synthase subunit 1)

 DPM1_HUMAN              Reviewed;         260 AA.
O60762; O15157; Q6IB78; Q96HK0;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
27-SEP-2017, entry version 168.
RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1;
EC=2.4.1.83;
AltName: Full=Dolichol-phosphate mannose synthase subunit 1;
Short=DPM synthase subunit 1;
AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 1;
AltName: Full=Mannose-P-dolichol synthase subunit 1;
Short=MPD synthase subunit 1;
Name=DPM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Placenta;
PubMed=9535917; DOI=10.1074/jbc.273.15.9249;
Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., Kinoshita T.;
"A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for
synthesis of dolichol-phosphate-mannose in mammalian cells.";
J. Biol. Chem. 273:9249-9254(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Urinary bladder;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-260.
PubMed=9223280; DOI=10.1073/pnas.94.15.7873;
Colussi P.A., Taron C.H., Mack J.C., Orlean P.;
"Human and Saccharomyces cerevisiae dolichol phosphate mannose
synthases represent two classes of the enzyme, but both function in
Schizosaccharomyces pombe.";
Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997).
[7]
SUBUNIT.
PubMed=10835346; DOI=10.1093/emboj/19.11.2475;
Maeda Y., Tanaka S., Hino J., Kangawa K., Kinoshita T.;
"Human dolichol-phosphate-mannose synthase consists of three subunits,
DPM1, DPM2 and DPM3.";
EMBO J. 19:2475-2482(2000).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
INTERACTION WITH DPM3.
PubMed=16280320; DOI=10.1074/jbc.M511311200;
Ashida H., Maeda Y., Kinoshita T.;
"DPM1, the catalytic subunit of dolichol-phosphate mannose synthase,
is tethered to and stabilized on the endoplasmic reticulum membrane by
DPM3.";
J. Biol. Chem. 281:896-904(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-9, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
VARIANT CDG1E GLY-92.
PubMed=10642597; DOI=10.1172/JCI7302;
Kim S., Westphal V., Srikrishna G., Mehta D.P., Peterson S.,
Filiano J., Karnes P.S., Patterson M.C., Freeze H.H.;
"Dolichol phosphate mannose synthase (DPM1) mutations define
congenital disorder of glycosylation Ie (CDG-Ie).";
J. Clin. Invest. 105:191-198(2000).
[19]
VARIANT CDG1E GLY-92.
PubMed=10642602; DOI=10.1172/JCI8691;
Imbach T., Schenk B., Schollen E., Burda P., Stutz A., Gruenewald S.,
Bailie N.M., King M.D., Jaeken J., Matthijs G., Berger E.G., Aebi M.,
Hennet T.;
"Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital
disorder of glycosylation type Ie.";
J. Clin. Invest. 105:233-239(2000).
[20]
VARIANT CDG1E PRO-248.
PubMed=15669674; DOI=10.1023/B:BOLI.0000042984.42433.d8;
Garcia-Silva M.T., Matthijs G., Schollen E., Cabrera J.C.,
Sanchez Del Pozo J., Herreros M.M., Simon R., Maties M.,
Hernandez E.M., Hennet T., Briones P.;
"Congenital disorder of glycosylation (CDG) type Ie. A new patient.";
J. Inherit. Metab. Dis. 27:591-600(2004).
[21]
VARIANT CDG1E VAL-152, AND CHARACTERIZATION OF VARIANT CDG1E VAL-152.
PubMed=23856421; DOI=10.1016/j.ymgme.2013.06.016;
Yang A.C., Ng B.G., Moore S.A., Rush J., Waechter C.J., Raymond K.M.,
Willer T., Campbell K.P., Freeze H.H., Mehta L.;
"Congenital disorder of glycosylation due to DPM1 mutations presenting
with dystroglycanopathy-type congenital muscular dystrophy.";
Mol. Genet. Metab. 110:345-351(2013).
-!- FUNCTION: Transfers mannose from GDP-mannose to dolichol
monophosphate to form dolichol phosphate mannose (Dol-P-Man) which
is the mannosyl donor in pathways leading to N-glycosylation,
glycosyl phosphatidylinositol membrane anchoring, and O-
mannosylation of proteins; catalytic subunit of the dolichol-
phosphate mannose (DPM) synthase complex.
-!- CATALYTIC ACTIVITY: GDP-mannose + dolichyl phosphate = GDP +
dolichyl D-mannosyl phosphate.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM)
synthase complex composed of DPM1, DPM2 and DPM3; in the complex
interacts directly with DPM3. {ECO:0000269|PubMed:10835346,
ECO:0000269|PubMed:16280320}.
-!- INTERACTION:
Q9P2X0:DPM3; NbExp=4; IntAct=EBI-719526, EBI-9087337;
Q13418:ILK; NbExp=3; IntAct=EBI-719526, EBI-747644;
P48775:TDO2; NbExp=6; IntAct=EBI-719526, EBI-743494;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
-!- DISEASE: Congenital disorder of glycosylation 1E (CDG1E)
[MIM:608799]: A form of congenital disorder of glycosylation, a
multisystem disorder caused by a defect in glycoprotein
biosynthesis and characterized by under-glycosylated serum
glycoproteins. Congenital disorders of glycosylation result in a
wide variety of clinical features, such as defects in the nervous
system development, psychomotor retardation, dysmorphic features,
hypotonia, coagulation disorders, and immunodeficiency. The broad
spectrum of features reflects the critical role of N-glycoproteins
during embryonic development, differentiation, and maintenance of
cell functions. Some CDG1E patients have features consistent with
a dystroglycanopathy and congenital muscular dystrophy, including
O-mannosylation defect, camptodactyly, elevated creatine kinase,
motor delay and dystrophic changes on muscel biopsy.
{ECO:0000269|PubMed:10642597, ECO:0000269|PubMed:10642602,
ECO:0000269|PubMed:15669674, ECO:0000269|PubMed:23856421}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D86198; BAA25646.1; -; mRNA.
EMBL; D86202; BAA25647.1; -; Genomic_DNA.
EMBL; CR456926; CAG33207.1; -; mRNA.
EMBL; AK289569; BAF82258.1; -; mRNA.
EMBL; AL034553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007073; AAH07073.1; -; mRNA.
EMBL; BC008466; AAH08466.1; -; mRNA.
EMBL; BC016322; AAH16322.1; -; mRNA.
EMBL; AF007875; AAC98797.1; -; mRNA.
CCDS; CCDS13434.1; -.
RefSeq; NP_001303963.1; NM_001317034.1.
RefSeq; NP_001303964.1; NM_001317035.1.
RefSeq; NP_001303965.1; NM_001317036.1.
RefSeq; NP_003850.1; NM_003859.2.
UniGene; Hs.654951; -.
ProteinModelPortal; O60762; -.
SMR; O60762; -.
BioGrid; 114340; 26.
CORUM; O60762; -.
IntAct; O60762; 36.
STRING; 9606.ENSP00000360644; -.
CAZy; GT2; Glycosyltransferase Family 2.
iPTMnet; O60762; -.
PhosphoSitePlus; O60762; -.
BioMuta; DPM1; -.
EPD; O60762; -.
MaxQB; O60762; -.
PaxDb; O60762; -.
PeptideAtlas; O60762; -.
PRIDE; O60762; -.
DNASU; 8813; -.
Ensembl; ENST00000371588; ENSP00000360644; ENSG00000000419.
GeneID; 8813; -.
KEGG; hsa:8813; -.
UCSC; uc002xvw.2; human.
CTD; 8813; -.
DisGeNET; 8813; -.
EuPathDB; HostDB:ENSG00000000419.12; -.
GeneCards; DPM1; -.
GeneReviews; DPM1; -.
HGNC; HGNC:3005; DPM1.
HPA; HPA051818; -.
MalaCards; DPM1; -.
MIM; 603503; gene.
MIM; 608799; phenotype.
neXtProt; NX_O60762; -.
OpenTargets; ENSG00000000419; -.
Orphanet; 79322; DPM1-CDG.
PharmGKB; PA27463; -.
eggNOG; KOG2978; Eukaryota.
eggNOG; COG0463; LUCA.
GeneTree; ENSGT00550000075000; -.
HOGENOM; HOG000283250; -.
HOVERGEN; HBG018967; -.
InParanoid; O60762; -.
KO; K00721; -.
PhylomeDB; O60762; -.
TreeFam; TF105617; -.
BRENDA; 2.4.1.83; 2681.
Reactome; R-HSA-162699; Synthesis of dolichyl-phosphate mannose.
UniPathway; UPA00378; -.
ChiTaRS; DPM1; human.
GeneWiki; DPM1; -.
GenomeRNAi; 8813; -.
PRO; PR:O60762; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000000419; -.
CleanEx; HS_DPM1; -.
ExpressionAtlas; O60762; baseline and differential.
Genevisible; O60762; HS.
GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IDA:UniProtKB.
GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:HGNC.
GO; GO:0019348; P:dolichol metabolic process; IDA:MGI.
GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:UniProtKB.
GO; GO:0035268; P:protein mannosylation; IDA:HGNC.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
GO; GO:0035269; P:protein O-linked mannosylation; IDA:HGNC.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF00535; Glycos_transf_2; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Congenital disorder of glycosylation;
Congenital muscular dystrophy; Disease mutation; Dystroglycanopathy;
Endoplasmic reticulum; Glycosyltransferase; Phosphoprotein;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
CHAIN 2 260 Dolichol-phosphate mannosyltransferase
subunit 1.
/FTId=PRO_0000059170.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VARIANT 92 92 R -> G (in CDG1E; dbSNP:rs121908583).
{ECO:0000269|PubMed:10642597,
ECO:0000269|PubMed:10642602}.
/FTId=VAR_012341.
VARIANT 152 152 G -> V (in CDG1E; abolishes interaction
with DPM3; dbSNP:rs587777116).
{ECO:0000269|PubMed:23856421}.
/FTId=VAR_070592.
VARIANT 248 248 S -> P (in CDG1E; dbSNP:rs587777114).
{ECO:0000269|PubMed:15669674}.
/FTId=VAR_019841.
CONFLICT 9 9 S -> G (in Ref. 5; AAH08466).
{ECO:0000305}.
CONFLICT 15 15 R -> W (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 135 135 Q -> K (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 143 143 V -> A (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 154 154 V -> I (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 177 177 R -> T (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 191 191 R -> P (in Ref. 6; AAC98797).
{ECO:0000305}.
CONFLICT 220 220 L -> M (in Ref. 5; AAH08466).
{ECO:0000305}.
SEQUENCE 260 AA; 29634 MW; 9792145BFC8F0514 CRC64;
MASLEVSRSP RRSRRELEVR SPRQNKYSVL LPTYNERENL PLIVWLLVKS FSESGINYEI
IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT AYIHGMKHAT GNYIIIMDAD
LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRGANF LTQILLRPGA
SDLTGSFRLY RKEVLEKLIE KCVSKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK
LGGNEIVSFL KGLLTLFATT


Related products :

Catalog number Product name Quantity
EIAAB11782 Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,DPM3,Homo sapiens,
EIAAB11783 Bos taurus,Bovine,Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,
EIAAB11781 Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,Dpm3,Mannose-P-dol
EIAAB11775 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Homo sapiens,Human,Mannose-P-dolichol synthase,MPD synthase
EIAAB11774 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,Dpm1,Mannose-P-dolichol synthase,Mouse,MPD synthase,Mus musculus
EIAAB11776 Bos taurus,Bovine,Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase
EIAAB11773 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase,Pig,Sus scrofa
DPM3_BOVIN Bovine ELISA Kit FOR Dolichol-phosphate mannosyltransferase subunit 3 96T
CSB-EL007136HU Human Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit 96T
CSB-EL007136MO Mouse Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit 96T
CSB-EL007136BO Bovine Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit 96T
CSB-EL007136HU Human Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit SpeciesHuman 96T
CSB-EL007136BO Bovine Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit SpeciesBovine 96T
CSB-EL007136MO Mouse Dolichol-phosphate mannosyltransferase subunit 3(DPM3) ELISA kit SpeciesMouse 96T
DPM3_BOVIN ELISA Kit FOR Dolichol-phosphate mannosyltransferase subunit 3; organism: Bovine; gene name: DPM3 96T
DPM3_MOUSE ELISA Kit FOR Dolichol-phosphate mannosyltransferase subunit 3; organism: Mouse; gene name: Dpm3 96T
EIAAB11423 All-trans-decaprenyl-diphosphate synthase subunit 2,C6orf210,Candidate tumor suppressor protein,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,DLP1,Homo sapiens,
EIAAB11864 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,Dps1,Mouse,Mus musculus,Pdss1,Solanesyl-diphosphate synthase s
EIAAB11424 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Mouse,Mus musculus,Pdss2,Solanesyl-diphosphate synthase s
EIAAB11422 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Pdss2,Rat,Rattus norvegicus
EIAAB11863 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,DPS1,Homo sapiens,Human,PDSS1,TPRT,TPT 1,Trans-prenyltransfera
15-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 Polyclonal 0.1 mg
15-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 Polyclonal 0.05 mg
25-595 ATP5G2 is a subunit of mitochondrial ATP synthase. ATP synthase is composed of two linked multi-subunit complexes the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising t 0.05 mg
DPP10 DPM2 Gene dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit


 

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