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O60762 (DPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichol-phosphate mannosyltransferase subunit 1

EC=2.4.1.83
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 1
Short name=DPM synthase subunit 1
Dolichyl-phosphate beta-D-mannosyltransferase subunit 1
Mannose-P-dolichol synthase subunit 1
Short name=MPD synthase subunit 1
Gene names
Name:DPM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3. Ref.7 Ref.9

Subcellular location

Endoplasmic reticulum.

Involvement in disease

Congenital disorder of glycosylation 1E (CDG1E) [MIM:608799]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DiseaseCongenital disorder of glycosylation
Congenital muscular dystrophy
Disease mutation
Dystroglycanopathy
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

GDP-mannose metabolic process

Inferred from electronic annotation. Source: Ensembl

GPI anchor biosynthetic process

Inferred from direct assay Ref.7. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

dolichol metabolic process

Inferred from direct assay Ref.1PubMed 9724629. Source: MGI

dolichol-linked oligosaccharide biosynthetic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein O-linked mannosylation

Inferred from direct assay Ref.1. Source: HGNC

protein mannosylation

Inferred from direct assay Ref.1. Source: HGNC

   Cellular_componentdolichol-phosphate-mannose synthase complex

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 9724629. Source: MGI

endoplasmic reticulum membrane

Inferred from direct assay PubMed 9724629. Source: HGNC

membrane

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functionalcohol binding

Inferred from electronic annotation. Source: Ensembl

dolichyl-phosphate beta-D-mannosyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

dolichyl-phosphate-mannose-protein mannosyltransferase activity

Inferred from direct assay Ref.1. Source: HGNC

mannose binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DPM3Q9P2X04EBI-719526,EBI-9087337

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 260259Dolichol-phosphate mannosyltransferase subunit 1
PRO_0000059170

Amino acid modifications

Modified residue21N-acetylalanine Ref.11 Ref.13 Ref.14
Modified residue91Phosphoserine Ref.11 Ref.13

Natural variations

Natural variant921R → G in CDG1E. Ref.15 Ref.16
VAR_012341
Natural variant1521G → V in CDG1E; abolishes interaction with DPM3. Ref.18
VAR_070592
Natural variant2481S → P in CDG1E. Ref.17
VAR_019841

Experimental info

Sequence conflict91S → G in AAH08466. Ref.5
Sequence conflict151R → W in AAC98797. Ref.6
Sequence conflict1351Q → K in AAC98797. Ref.6
Sequence conflict1431V → A in AAC98797. Ref.6
Sequence conflict1541V → I in AAC98797. Ref.6
Sequence conflict1771R → T in AAC98797. Ref.6
Sequence conflict1911R → P in AAC98797. Ref.6
Sequence conflict2201L → M in AAH08466. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O60762 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9792145BFC8F0514

FASTA26029,634
        10         20         30         40         50         60 
MASLEVSRSP RRSRRELEVR SPRQNKYSVL LPTYNERENL PLIVWLLVKS FSESGINYEI 

        70         80         90        100        110        120 
IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT AYIHGMKHAT GNYIIIMDAD 

       130        140        150        160        170        180 
LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRGANF LTQILLRPGA 

       190        200        210        220        230        240 
SDLTGSFRLY RKEVLEKLIE KCVSKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK 

       250        260 
LGGNEIVSFL KGLLTLFATT 

« Hide

References

« Hide 'large scale' references
[1]"A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells."
Tomita S., Inoue N., Maeda Y., Ohishi K., Takeda J., Kinoshita T.
J. Biol. Chem. 273:9249-9254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Placenta.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain and Urinary bladder.
[6]"Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe."
Colussi P.A., Taron C.H., Mack J.C., Orlean P.
Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-260.
[7]"Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3."
Maeda Y., Tanaka S., Hino J., Kangawa K., Kinoshita T.
EMBO J. 19:2475-2482(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3."
Ashida H., Maeda Y., Kinoshita T.
J. Biol. Chem. 281:896-904(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPM3.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)."
Kim S., Westphal V., Srikrishna G., Mehta D.P., Peterson S., Filiano J., Karnes P.S., Patterson M.C., Freeze H.H.
J. Clin. Invest. 105:191-198(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1E GLY-92.
[16]"Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie."
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.
J. Clin. Invest. 105:233-239(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1E GLY-92.
[17]"Congenital disorder of glycosylation (CDG) type Ie. A new patient."
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.
J. Inherit. Metab. Dis. 27:591-600(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1E PRO-248.
[18]"Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy."
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.
Mol. Genet. Metab. 110:345-351(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1E VAL-152, CHARACTERIZATION OF VARIANT CDG1E VAL-152.

Web resources

GeneReviews
GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86198 mRNA. Translation: BAA25646.1.
D86202 Genomic DNA. Translation: BAA25647.1.
CR456926 mRNA. Translation: CAG33207.1.
AK289569 mRNA. Translation: BAF82258.1.
AL034553 Genomic DNA. Translation: CAB53749.1.
BC007073 mRNA. Translation: AAH07073.1.
BC008466 mRNA. Translation: AAH08466.1.
BC016322 mRNA. Translation: AAH16322.1.
AF007875 mRNA. Translation: AAC98797.1.
RefSeqNP_003850.1. NM_003859.1.
UniGeneHs.654951.

3D structure databases

ProteinModelPortalO60762.
SMRO60762. Positions 24-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114340. 12 interactions.
IntActO60762. 9 interactions.
STRING9606.ENSP00000360644.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteO60762.

Proteomic databases

PaxDbO60762.
PRIDEO60762.

Protocols and materials databases

DNASU8813.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371588; ENSP00000360644; ENSG00000000419.
GeneID8813.
KEGGhsa:8813.
UCSCuc002xvw.1. human.

Organism-specific databases

CTD8813.
GeneCardsGC20M049551.
HGNCHGNC:3005. DPM1.
HPAHPA051818.
MIM603503. gene.
608799. phenotype.
neXtProtNX_O60762.
Orphanet79322. DPM1-CDG.
PharmGKBPA27463.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0463.
HOGENOMHOG000283250.
HOVERGENHBG018967.
KOK00721.
OrthoDBEOG7W41CN.
PhylomeDBO60762.
TreeFamTF105617.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO60762.
BgeeO60762.
CleanExHS_DPM1.
GenevestigatorO60762.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDPM1. human.
GeneWikiDPM1.
GenomeRNAi8813.
NextBio33058.
PROO60762.
SOURCESearch...

Entry information

Entry nameDPM1_HUMAN
AccessionPrimary (citable) accession number: O60762
Secondary accession number(s): O15157, Q6IB78, Q96HK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM