ID   DPM1_HUMAN              Reviewed;         260 AA.
AC   O60762; O15157; Q6IB78; Q96HK0;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-NOV-2024, entry version 214.
DE   RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1;
DE            EC=2.4.1.83 {ECO:0000305|PubMed:10835346};
DE   AltName: Full=Dolichol-phosphate mannose synthase subunit 1;
DE            Short=DPM synthase subunit 1;
DE   AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 1;
DE   AltName: Full=Mannose-P-dolichol synthase subunit 1;
DE            Short=MPD synthase subunit 1;
GN   Name=DPM1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Placenta;
RX   PubMed=9535917; DOI=10.1074/jbc.273.15.9249;
RA   Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., Kinoshita T.;
RT   "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for
RT   synthesis of dolichol-phosphate-mannose in mammalian cells.";
RL   J. Biol. Chem. 273:9249-9254(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Urinary bladder;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-260.
RX   PubMed=9223280; DOI=10.1073/pnas.94.15.7873;
RA   Colussi P.A., Taron C.H., Mack J.C., Orlean P.;
RT   "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases
RT   represent two classes of the enzyme, but both function in
RT   Schizosaccharomyces pombe.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997).
RN   [7]
RP   SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10835346; DOI=10.1093/emboj/19.11.2475;
RA   Maeda Y., Tanaka S., Hino J., Kangawa K., Kinoshita T.;
RT   "Human dolichol-phosphate-mannose synthase consists of three subunits,
RT   DPM1, DPM2 and DPM3.";
RL   EMBO J. 19:2475-2482(2000).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   INTERACTION WITH DPM3.
RX   PubMed=16280320; DOI=10.1074/jbc.m511311200;
RA   Ashida H., Maeda Y., Kinoshita T.;
RT   "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is
RT   tethered to and stabilized on the endoplasmic reticulum membrane by DPM3.";
RL   J. Biol. Chem. 281:896-904(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-9, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [18]
RP   VARIANT CDG1E GLY-92.
RX   PubMed=10642597; DOI=10.1172/jci7302;
RA   Kim S., Westphal V., Srikrishna G., Mehta D.P., Peterson S., Filiano J.,
RA   Karnes P.S., Patterson M.C., Freeze H.H.;
RT   "Dolichol phosphate mannose synthase (DPM1) mutations define congenital
RT   disorder of glycosylation Ie (CDG-Ie).";
RL   J. Clin. Invest. 105:191-198(2000).
RN   [19]
RP   VARIANT CDG1E GLY-92.
RX   PubMed=10642602; DOI=10.1172/jci8691;
RA   Imbach T., Schenk B., Schollen E., Burda P., Stutz A., Gruenewald S.,
RA   Bailie N.M., King M.D., Jaeken J., Matthijs G., Berger E.G., Aebi M.,
RA   Hennet T.;
RT   "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital
RT   disorder of glycosylation type Ie.";
RL   J. Clin. Invest. 105:233-239(2000).
RN   [20]
RP   VARIANT CDG1E PRO-248.
RX   PubMed=15669674; DOI=10.1023/b:boli.0000042984.42433.d8;
RA   Garcia-Silva M.T., Matthijs G., Schollen E., Cabrera J.C.,
RA   Sanchez Del Pozo J., Herreros M.M., Simon R., Maties M., Hernandez E.M.,
RA   Hennet T., Briones P.;
RT   "Congenital disorder of glycosylation (CDG) type Ie. A new patient.";
RL   J. Inherit. Metab. Dis. 27:591-600(2004).
RN   [21]
RP   VARIANT CDG1E VAL-152, AND CHARACTERIZATION OF VARIANT CDG1E VAL-152.
RX   PubMed=23856421; DOI=10.1016/j.ymgme.2013.06.016;
RA   Yang A.C., Ng B.G., Moore S.A., Rush J., Waechter C.J., Raymond K.M.,
RA   Willer T., Campbell K.P., Freeze H.H., Mehta L.;
RT   "Congenital disorder of glycosylation due to DPM1 mutations presenting with
RT   dystroglycanopathy-type congenital muscular dystrophy.";
RL   Mol. Genet. Metab. 110:345-351(2013).
RN   [22]
RP   INTERACTION WITH DPM3.
RX   PubMed=19576565; DOI=10.1016/j.ajhg.2009.06.006;
RA   Lefeber D.J., Schonberger J., Morava E., Guillard M., Huyben K.M.,
RA   Verrijp K., Grafakou O., Evangeliou A., Preijers F.W., Manta P., Yildiz J.,
RA   Grunewald S., Spilioti M., van den Elzen C., Klein D., Hess D., Ashida H.,
RA   Hofsteenge J., Maeda Y., van den Heuvel L., Lammens M., Lehle L.,
RA   Wevers R.A.;
RT   "Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital
RT   disorders of glycosylation with the dystroglycanopathies.";
RL   Am. J. Hum. Genet. 85:76-86(2009).
CC   -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC       to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC       donor in pathways leading to N-glycosylation, glycosyl
CC       phosphatidylinositol membrane anchoring, and O-mannosylation of
CC       proteins; catalytic subunit of the dolichol-phosphate mannose (DPM)
CC       synthase complex. {ECO:0000269|PubMed:10835346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl phosphate + GDP-alpha-D-mannose =
CC         a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + GDP;
CC         Xref=Rhea:RHEA:21184, Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:57683, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58211; EC=2.4.1.83;
CC         Evidence={ECO:0000305|PubMed:10835346};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21185;
CC         Evidence={ECO:0000305|PubMed:10835346};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8U4M3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8U4M3};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q8U4M3};
CC       Note=Binds 1 divalent metal cation. {ECO:0000250|UniProtKB:Q8U4M3};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:10835346}.
CC   -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC       complex composed of DPM1, DPM2 and DPM3; within the complex, directly
CC       interacts with DPM3 (PubMed:10835346, PubMed:16280320). This
CC       interaction stabilizes DPM1 (PubMed:10835346, PubMed:19576565).
CC       {ECO:0000269|PubMed:10835346, ECO:0000269|PubMed:16280320,
CC       ECO:0000269|PubMed:19576565}.
CC   -!- INTERACTION:
CC       O60762; Q9P2X0: DPM3; NbExp=5; IntAct=EBI-719526, EBI-9087337;
CC       O60762; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-719526, EBI-16439278;
CC       O60762; P48775: TDO2; NbExp=6; IntAct=EBI-719526, EBI-743494;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000305|PubMed:10835346}.
CC   -!- DISEASE: Congenital disorder of glycosylation 1E (CDG1E) [MIM:608799]:
CC       A form of congenital disorder of glycosylation, a multisystem disorder
CC       caused by a defect in glycoprotein biosynthesis and characterized by
CC       under-glycosylated serum glycoproteins. Congenital disorders of
CC       glycosylation result in a wide variety of clinical features, such as
CC       defects in the nervous system development, psychomotor retardation,
CC       dysmorphic features, hypotonia, coagulation disorders, and
CC       immunodeficiency. The broad spectrum of features reflects the critical
CC       role of N-glycoproteins during embryonic development, differentiation,
CC       and maintenance of cell functions. Some CDG1E patients have features
CC       consistent with a dystroglycanopathy and congenital muscular dystrophy,
CC       including O-mannosylation defect, camptodactyly, elevated creatine
CC       kinase, motor delay and dystrophic changes on muscel biopsy.
CC       {ECO:0000269|PubMed:10642597, ECO:0000269|PubMed:10642602,
CC       ECO:0000269|PubMed:15669674, ECO:0000269|PubMed:23856421}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; D86198; BAA25646.1; -; mRNA.
DR   EMBL; D86202; BAA25647.1; -; Genomic_DNA.
DR   EMBL; CR456926; CAG33207.1; -; mRNA.
DR   EMBL; AK289569; BAF82258.1; -; mRNA.
DR   EMBL; AL034553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007073; AAH07073.1; -; mRNA.
DR   EMBL; BC008466; AAH08466.1; -; mRNA.
DR   EMBL; BC016322; AAH16322.1; -; mRNA.
DR   EMBL; AF007875; AAC98797.1; -; mRNA.
DR   CCDS; CCDS13434.1; -.
DR   RefSeq; NP_001303963.1; NM_001317034.1.
DR   RefSeq; NP_001303964.1; NM_001317035.1.
DR   RefSeq; NP_001303965.1; NM_001317036.1.
DR   RefSeq; NP_003850.1; NM_003859.2.
DR   AlphaFoldDB; O60762; -.
DR   SMR; O60762; -.
DR   BioGRID; 114340; 181.
DR   ComplexPortal; CPX-6268; Dolichol-phosphate mannosyltransferase complex.
DR   CORUM; O60762; -.
DR   IntAct; O60762; 79.
DR   MINT; O60762; -.
DR   STRING; 9606.ENSP00000360638; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GlyGen; O60762; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60762; -.
DR   PhosphoSitePlus; O60762; -.
DR   SwissPalm; O60762; -.
DR   BioMuta; DPM1; -.
DR   jPOST; O60762; -.
DR   MassIVE; O60762; -.
DR   PaxDb; 9606-ENSP00000360644; -.
DR   PeptideAtlas; O60762; -.
DR   ProteomicsDB; 49589; -.
DR   Pumba; O60762; -.
DR   Antibodypedia; 28594; 143 antibodies from 28 providers.
DR   DNASU; 8813; -.
DR   Ensembl; ENST00000371588.10; ENSP00000360644.5; ENSG00000000419.14.
DR   GeneID; 8813; -.
DR   KEGG; hsa:8813; -.
DR   MANE-Select; ENST00000371588.10; ENSP00000360644.5; NM_003859.3; NP_003850.1.
DR   UCSC; uc002xvw.2; human.
DR   AGR; HGNC:3005; -.
DR   CTD; 8813; -.
DR   DisGeNET; 8813; -.
DR   GeneCards; DPM1; -.
DR   GeneReviews; DPM1; -.
DR   HGNC; HGNC:3005; DPM1.
DR   HPA; ENSG00000000419; Low tissue specificity.
DR   MalaCards; DPM1; -.
DR   MIM; 603503; gene.
DR   MIM; 608799; phenotype.
DR   neXtProt; NX_O60762; -.
DR   OpenTargets; ENSG00000000419; -.
DR   Orphanet; 79322; DPM1-CDG.
DR   PharmGKB; PA27463; -.
DR   VEuPathDB; HostDB:ENSG00000000419; -.
DR   eggNOG; KOG2978; Eukaryota.
DR   GeneTree; ENSGT00940000153481; -.
DR   HOGENOM; CLU_033536_13_3_1; -.
DR   InParanoid; O60762; -.
DR   OMA; VNVINWP; -.
DR   OrthoDB; 604at2759; -.
DR   PhylomeDB; O60762; -.
DR   TreeFam; TF105617; -.
DR   BioCyc; MetaCyc:ENSG00000000419-MONOMER; -.
DR   BRENDA; 2.4.1.83; 2681.
DR   PathwayCommons; O60762; -.
DR   Reactome; R-HSA-162699; Synthesis of dolichyl-phosphate mannose.
DR   Reactome; R-HSA-4717374; Defective DPM1 causes DPM1-CDG.
DR   Reactome; R-HSA-4719360; Defective DPM3 causes DPM3-CDG.
DR   Reactome; R-HSA-4719377; Defective DPM2 causes DPM2-CDG.
DR   SignaLink; O60762; -.
DR   SIGNOR; O60762; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 8813; 108 hits in 1168 CRISPR screens.
DR   ChiTaRS; DPM1; human.
DR   GeneWiki; DPM1; -.
DR   GenomeRNAi; 8813; -.
DR   Pharos; O60762; Tbio.
DR   PRO; PR:O60762; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; O60762; protein.
DR   Bgee; ENSG00000000419; Expressed in epithelium of nasopharynx and 215 other cell types or tissues.
DR   ExpressionAtlas; O60762; baseline and differential.
DR   GO; GO:0033185; C:dolichol-phosphate-mannose synthase complex; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC-UCL.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0043178; F:alcohol binding; IEA:Ensembl.
DR   GO; GO:0005537; F:D-mannose binding; IEA:Ensembl.
DR   GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:HGNC-UCL.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR   GO; GO:0019348; P:dolichol metabolic process; IDA:MGI.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IEA:Ensembl.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0035268; P:protein mannosylation; IDA:HGNC-UCL.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IDA:HGNC-UCL.
DR   GO; GO:0070482; P:response to oxygen levels; IEA:Ensembl.
DR   CDD; cd06442; DPM1_like; 1.
DR   FunFam; 3.90.550.10:FF:000036; Dolichol-phosphate mannosyltransferase subunit 1; 1.
DR   InterPro; IPR039528; DPM1-like.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43398; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR   PANTHER; PTHR43398:SF1; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Congenital disorder of glycosylation;
KW   Congenital muscular dystrophy; Disease variant; Dystroglycanopathy;
KW   Endoplasmic reticulum; Glycosyltransferase; Magnesium; Manganese;
KW   Metal-binding; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..260
FT                   /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT                   /id="PRO_0000059170"
FT   BINDING         32
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         34
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         36
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         63
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         65
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         118
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         119
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         120
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         147
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         234
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   BINDING         240
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U4M3"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   VARIANT         92
FT                   /note="R -> G (in CDG1E; dbSNP:rs121908583)"
FT                   /evidence="ECO:0000269|PubMed:10642597,
FT                   ECO:0000269|PubMed:10642602"
FT                   /id="VAR_012341"
FT   VARIANT         152
FT                   /note="G -> V (in CDG1E; abolishes interaction with DPM3;
FT                   dbSNP:rs587777116)"
FT                   /evidence="ECO:0000269|PubMed:23856421"
FT                   /id="VAR_070592"
FT   VARIANT         248
FT                   /note="S -> P (in CDG1E; dbSNP:rs587777114)"
FT                   /evidence="ECO:0000269|PubMed:15669674"
FT                   /id="VAR_019841"
FT   CONFLICT        9
FT                   /note="S -> G (in Ref. 5; AAH08466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="R -> W (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="Q -> K (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="V -> A (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="V -> I (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="R -> T (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="R -> P (in Ref. 6; AAC98797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="L -> M (in Ref. 5; AAH08466)"
FT                   /evidence="ECO:0000305"
SQ   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
//