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O94777

- DPM2_HUMAN

UniProt

O94777 - DPM2_HUMAN

Protein

Dolichol phosphate-mannose biosynthesis regulatory protein

Gene

DPM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. cellular protein metabolic process Source: Reactome
    2. C-terminal protein lipidation Source: Reactome
    3. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    4. dolichol metabolic process Source: Ensembl
    5. GPI anchor biosynthetic process Source: UniProtKB
    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

    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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 proteinPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei49 – 6921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DPM2 family.Curated

    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

    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: October 1, 2014
    This is version 109 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