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O94777 (DPM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichol phosphate-mannose biosynthesis regulatory protein
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 2
Short name=DPM synthase subunit 2
Gene names
Name:DPM2
ORF Names:My026
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length84 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. When associated with the GPI-GlcNAc transferase (GPI-GnT) complex enhances but is not essential for its activity. Ref.9

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. Associates with the GPI-GlcNAc transferase (GPI-GnT) complex. Ref.8

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

Congenital disorder of glycosylation 1U (CDG1U) [MIM:615042]: 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 CDG1U patients have dystrophic changes seen on muscle biopsy and reduced O-mannosyl glycans on alpha-dystroglycan.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the DPM2 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCongenital disorder of glycosylation
Congenital muscular dystrophy
Disease mutation
Dystroglycanopathy
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

GPI anchor biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

dolichol metabolic process

Inferred from electronic annotation. Source: Ensembl

dolichol-linked oligosaccharide biosynthetic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

preassembly of GPI anchor in ER membrane

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein O-linked mannosylation

Traceable author statement PubMed 16280320. Source: HGNC

regulation of protein stability

Inferred from physical interaction Ref.8. Source: UniProtKB

   Cellular_componentdolichol-phosphate-mannose synthase complex

Inferred from direct assay Ref.8. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement PubMed 16280320. Source: HGNC

glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex

Traceable author statement PubMed 16280320. Source: HGNC

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondolichyl-phosphate beta-D-mannosyltransferase activity

Inferred from electronic annotation. Source: Ensembl

enzyme regulator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.8. Source: HGNC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 8483Dolichol phosphate-mannose biosynthesis regulatory protein
PRO_0000220873

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane49 – 6921Helical; Potential

Natural variations

Natural variant231Y → C in CDG1U. Ref.10
VAR_069745
Natural variant761T → S. Ref.4 Ref.6 Ref.7
Corresponds to variant rs7997 [ dbSNP | Ensembl ].
VAR_033895

Sequences

Sequence LengthMass (Da)Tools
O94777 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0247A0843A711EE9

FASTA849,312
        10         20         30         40         50         60 
MATGTDQVVG LGLVAVSLII FTYYTAWVIL LPFIDSQHVI HKYFLPRAYA VAIPLAAGLL 

        70         80 
LLLFVGLFIS YVMLKTKRVT KKAQ 

« Hide

References

« Hide 'large scale' references
[1]"DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate."
Maeda Y., Tomita S., Watanabe R., Ohishi K., Kinoshita T.
EMBO J. 17:4920-4929(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mao Y.M., Xie Y., Ying K.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal brain.
[3]"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].
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-76.
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-76.
[7]"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], VARIANT SER-76.
Tissue: Pancreas.
[8]"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: PROTEIN SEQUENCE OF 2-31, SUBUNIT.
[9]"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2."
Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J., Kangawa K., Julius M., Kinoshita T.
EMBO J. 19:4402-4411(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE GPI-GNT COMPLEX.
[10]"DPM2-CDG: a muscular dystrophy-dystroglycanopathy syndrome with severe epilepsy."
Barone R., Aiello C., Race V., Morava E., Foulquier F., Riemersma M., Passarelli C., Concolino D., Carella M., Santorelli F., Vleugels W., Mercuri E., Garozzo D., Sturiale L., Messina S., Jaeken J., Fiumara A., Wevers R.A. expand/collapse author list , Bertini E., Matthijs G., Lefeber D.J.
Ann. Neurol. 72:550-558(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1U CYS-23.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013361 mRNA. Translation: BAA33974.1.
AF061729 mRNA. Translation: AAG43140.1.
CR542134 mRNA. Translation: CAG46931.1.
AB451329 mRNA. Translation: BAG70143.1.
AB451473 mRNA. Translation: BAG70287.1.
AL157935 Genomic DNA. Translation: CAI12615.1.
CH471090 Genomic DNA. Translation: EAW87730.1.
BC015233 mRNA. Translation: AAH15233.1.
BC107863 mRNA. Translation: AAI07864.1.
CCDSCCDS6886.1.
RefSeqNP_003854.1. NM_003863.3.
UniGeneHs.108973.

3D structure databases

ProteinModelPortalO94777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114345. 3 interactions.
IntActO94777. 2 interactions.
STRING9606.ENSP00000322181.

Proteomic databases

PRIDEO94777.

Protocols and materials databases

DNASU8818.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314392; ENSP00000322181; ENSG00000136908.
GeneID8818.
KEGGhsa:8818.
UCSCuc004bsv.2. human.

Organism-specific databases

CTD8818.
GeneCardsGC09M130697.
GeneReviewsDPM2.
HGNCHGNC:3006. DPM2.
MIM603564. gene.
615042. phenotype.
neXtProtNX_O94777.
Orphanet329178. Congenital muscular dystrophy with intellectual disability and severe epilepsy.
PharmGKBPA27464.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273053.
HOGENOMHOG000212369.
KOK09658.
OMAENAYANS.
OrthoDBEOG7NCV64.
PhylomeDBO94777.
TreeFamTF300257.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO94777.
BgeeO94777.
CleanExHS_DPM2.
GenevestigatorO94777.

Family and domain databases

InterProIPR009914. DPM2.
[Graphical view]
PfamPF07297. DPM2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDPM2.
GenomeRNAi8818.
NextBio33078.
PROO94777.
SOURCESearch...

Entry information

Entry nameDPM2_HUMAN
AccessionPrimary (citable) accession number: O94777
Secondary accession number(s): Q5XKK9, Q6FGH3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 3 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 9

Human chromosome 9: entries, gene names and cross-references to MIM