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O94777

- DPM2_HUMAN

UniProt

O94777 - DPM2_HUMAN

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Protein
Dolichol phosphate-mannose biosynthesis regulatory protein
Gene
DPM2, My026
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate beta-D-mannosyltransferase activity Source: Ensembl
  2. enzyme regulator activity Source: Ensembl
  3. protein binding Source: HGNC

GO - Biological processi

  1. C-terminal protein lipidation Source: Reactome
  2. GPI anchor biosynthetic process Source: UniProtKB
  3. cellular protein metabolic process Source: Reactome
  4. dolichol metabolic process Source: Ensembl
  5. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  6. post-translational protein modification Source: Reactome
  7. preassembly of GPI anchor in ER membrane Source: Reactome
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. protein O-linked mannosylation Source: HGNC
  10. regulation of protein stability Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_2032. Synthesis of dolichyl-phosphate mannose.
REACT_952. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichol phosphate-mannose biosynthesis regulatory protein
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 2
Short name:
DPM synthase subunit 2
Gene namesi
Name:DPM2
ORF Names:My026
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:3006. DPM2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Reviewed prediction
Add
BLAST
Transmembranei49 – 6921Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. dolichol-phosphate-mannose synthase complex Source: UniProtKB
  2. endoplasmic reticulum membrane Source: HGNC
  3. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Source: HGNC
  4. integral component of endoplasmic reticulum membrane Source: InterPro
  5. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231Y → C in CDG1U. 1 Publication
VAR_069745

Keywords - Diseasei

Congenital disorder of glycosylation, Congenital muscular dystrophy, Disease mutation, Dystroglycanopathy

Organism-specific databases

MIMi615042. phenotype.
Orphaneti329178. Congenital muscular dystrophy with intellectual disability and severe epilepsy.
PharmGKBiPA27464.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 8483Dolichol phosphate-mannose biosynthesis regulatory protein
PRO_0000220873Add
BLAST

Proteomic databases

PRIDEiO94777.

Expressioni

Gene expression databases

ArrayExpressiO94777.
BgeeiO94777.
CleanExiHS_DPM2.
GenevestigatoriO94777.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi114345. 3 interactions.
IntActiO94777. 2 interactions.
STRINGi9606.ENSP00000322181.

Structurei

3D structure databases

ProteinModelPortaliO94777.

Family & Domainsi

Sequence similaritiesi

Belongs to the DPM2 family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG273053.
HOGENOMiHOG000212369.
KOiK09658.
OMAiENAYANS.
OrthoDBiEOG7NCV64.
PhylomeDBiO94777.
TreeFamiTF300257.

Family and domain databases

InterProiIPR009914. DPM2.
[Graphical view]
PfamiPF07297. DPM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O94777-1 [UniParc]FASTAAdd to Basket

« Hide

MATGTDQVVG LGLVAVSLII FTYYTAWVIL LPFIDSQHVI HKYFLPRAYA   50
VAIPLAAGLL LLLFVGLFIS YVMLKTKRVT KKAQ 84
Length:84
Mass (Da):9,312
Last modified:January 23, 2007 - v3
Checksum:i0247A0843A711EE9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231Y → C in CDG1U. 1 Publication
VAR_069745
Natural varianti76 – 761T → S.3 Publications
Corresponds to variant rs7997 [ dbSNP | Ensembl ].
VAR_033895

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6886.1.
RefSeqiNP_003854.1. NM_003863.3.
UniGeneiHs.108973.

Genome annotation databases

EnsembliENST00000314392; ENSP00000322181; ENSG00000136908.
GeneIDi8818.
KEGGihsa:8818.
UCSCiuc004bsv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6886.1.
RefSeqi NP_003854.1. NM_003863.3.
UniGenei Hs.108973.

3D structure databases

ProteinModelPortali O94777.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114345. 3 interactions.
IntActi O94777. 2 interactions.
STRINGi 9606.ENSP00000322181.

Proteomic databases

PRIDEi O94777.

Protocols and materials databases

DNASUi 8818.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314392 ; ENSP00000322181 ; ENSG00000136908 .
GeneIDi 8818.
KEGGi hsa:8818.
UCSCi uc004bsv.2. human.

Organism-specific databases

CTDi 8818.
GeneCardsi GC09M130697.
GeneReviewsi DPM2.
HGNCi HGNC:3006. DPM2.
MIMi 603564. gene.
615042. phenotype.
neXtProti NX_O94777.
Orphaneti 329178. Congenital muscular dystrophy with intellectual disability and severe epilepsy.
PharmGKBi PA27464.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG273053.
HOGENOMi HOG000212369.
KOi K09658.
OMAi ENAYANS.
OrthoDBi EOG7NCV64.
PhylomeDBi O94777.
TreeFami TF300257.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_2032. Synthesis of dolichyl-phosphate mannose.
REACT_952. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

GeneWikii DPM2.
GenomeRNAii 8818.
NextBioi 33078.
PROi O94777.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94777.
Bgeei O94777.
CleanExi HS_DPM2.
Genevestigatori O94777.

Family and domain databases

InterProi IPR009914. DPM2.
[Graphical view ]
Pfami PF07297. DPM2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: VARIANT CDG1U CYS-23.

Entry informationi

Entry nameiDPM2_HUMAN
AccessioniPrimary (citable) accession number: O94777
Secondary accession number(s): Q5XKK9, Q6FGH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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