Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9P2X0

- DPM3_HUMAN

UniProt

Q9P2X0 - DPM3_HUMAN

Protein

Dolichol-phosphate mannosyltransferase subunit 3

Gene

DPM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. C-terminal protein lipidation Source: Reactome
    4. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    5. GPI anchor biosynthetic process Source: UniProtKB
    6. post-translational protein modification Source: Reactome
    7. protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan Source: HGNC
    8. protein mannosylation Source: HGNC
    9. protein N-linked glycosylation via asparagine Source: Reactome
    10. protein O-linked mannosylation Source: HGNC
    11. regulation of protein stability Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_2032. Synthesis of dolichyl-phosphate mannose.
    UniPathwayiUPA00378.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dolichol-phosphate mannosyltransferase subunit 3
    Alternative name(s):
    Dolichol-phosphate mannose synthase subunit 3
    Short name:
    DPM synthase subunit 3
    Dolichyl-phosphate beta-D-mannosyltransferase subunit 3
    Mannose-P-dolichol synthase subunit 3
    Short name:
    MPD synthase subunit 3
    Prostin-1
    Gene namesi
    Name:DPM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3007. DPM3.

    Subcellular locationi

    GO - Cellular componenti

    1. dolichol-phosphate-mannose synthase complex Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: HGNC
    4. integral component of endoplasmic reticulum membrane Source: HGNC
    5. mannosyltransferase complex Source: HGNC
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1O (CDG1O) [MIM:612937]: 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. CDG1O patients have increased serum creatine kinase, dystrophic changes on muscle biopsy, and reduced O-mannosylation of 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 varianti85 – 851L → S in CDG1O; affects interaction with DPM1. 1 Publication
    VAR_062518

    Keywords - Diseasei

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

    Organism-specific databases

    MIMi612937. phenotype.
    Orphaneti263494. DPM3-CDG.
    PharmGKBiPA27465.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9292Dolichol-phosphate mannosyltransferase subunit 3PRO_0000195000Add
    BLAST

    Proteomic databases

    MaxQBiQ9P2X0.
    PaxDbiQ9P2X0.
    PRIDEiQ9P2X0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9P2X0.
    BgeeiQ9P2X0.
    CleanExiHS_DPM3.
    GenevestigatoriQ9P2X0.

    Organism-specific databases

    HPAiHPA014667.

    Interactioni

    Subunit structurei

    Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex associated with DPM1 via its C-terminal domain and with DPM2 via its N-terminal portion.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DPM1O607624EBI-9087337,EBI-719526
    Dpm2Q9Z3252EBI-9087337,EBI-9097185From a different organism.

    Protein-protein interaction databases

    BioGridi119935. 1 interaction.
    IntActiQ9P2X0. 4 interactions.
    STRINGi9606.ENSP00000357384.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2X0.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei37 – 5721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DPM3 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG145469.
    HOGENOMiHOG000038272.
    HOVERGENiHBG018968.
    InParanoidiQ9P2X0.
    KOiK09659.
    OMAiYREVAWP.
    OrthoDBiEOG73540R.
    PhylomeDBiQ9P2X0.
    TreeFamiTF300274.

    Family and domain databases

    InterProiIPR013174. DPM3.
    [Graphical view]
    PfamiPF08285. DPM3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P2X0-1) [UniParc]FASTAAdd to Basket

    Also known as: Short

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTKLAQWLWG LAILGSTWVA LTTGALGLEL PLSCQEVLWP LPAYLLVSAG   50
    CYALGTVGYR VATFHDCEDA ARELQSQIQE ARADLARRGL RF 92
    Length:92
    Mass (Da):10,094
    Last modified:February 6, 2007 - v2
    Checksum:iC350A6896842A877
    GO
    Isoform 2 (identifier: Q9P2X0-2) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLSVGGLRLSLVRFSFLLLRGALLPSLAVTM

    Show »
    Length:122
    Mass (Da):13,277
    Checksum:iDD8661D41C2AE5C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901L → V in BAA96291. (PubMed:10835346)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851L → S in CDG1O; affects interaction with DPM1. 1 Publication
    VAR_062518

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MLSVGGLRLSLVRFSFLLLR GALLPSLAVTM in isoform 2. 2 PublicationsVSP_001308

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028128 mRNA. Translation: BAA96291.1.
    AF312922 mRNA. Translation: AAK28487.1.
    AF312923 mRNA. Translation: AAK28486.1.
    AL691442 Genomic DNA. Translation: CAI15325.1.
    AL691442 Genomic DNA. Translation: CAI15326.1.
    CH471121 Genomic DNA. Translation: EAW53126.1.
    BC104202 mRNA. Translation: AAI04203.1.
    BC104203 mRNA. Translation: AAI04204.1.
    CCDSiCCDS1094.1. [Q9P2X0-2]
    CCDS1095.1. [Q9P2X0-1]
    RefSeqiNP_061846.2. NM_018973.3. [Q9P2X0-2]
    NP_714963.1. NM_153741.1. [Q9P2X0-1]
    UniGeneiHs.110477.

    Genome annotation databases

    EnsembliENST00000341298; ENSP00000344338; ENSG00000179085. [Q9P2X0-1]
    ENST00000368399; ENSP00000357384; ENSG00000179085. [Q9P2X0-2]
    ENST00000368400; ENSP00000357385; ENSG00000179085. [Q9P2X0-1]
    GeneIDi54344.
    KEGGihsa:54344.
    UCSCiuc001fhm.3. human. [Q9P2X0-2]
    uc001fhn.3. human. [Q9P2X0-1]

    Polymorphism databases

    DMDMi125987822.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028128 mRNA. Translation: BAA96291.1 .
    AF312922 mRNA. Translation: AAK28487.1 .
    AF312923 mRNA. Translation: AAK28486.1 .
    AL691442 Genomic DNA. Translation: CAI15325.1 .
    AL691442 Genomic DNA. Translation: CAI15326.1 .
    CH471121 Genomic DNA. Translation: EAW53126.1 .
    BC104202 mRNA. Translation: AAI04203.1 .
    BC104203 mRNA. Translation: AAI04204.1 .
    CCDSi CCDS1094.1. [Q9P2X0-2 ]
    CCDS1095.1. [Q9P2X0-1 ]
    RefSeqi NP_061846.2. NM_018973.3. [Q9P2X0-2 ]
    NP_714963.1. NM_153741.1. [Q9P2X0-1 ]
    UniGenei Hs.110477.

    3D structure databases

    ProteinModelPortali Q9P2X0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119935. 1 interaction.
    IntActi Q9P2X0. 4 interactions.
    STRINGi 9606.ENSP00000357384.

    Polymorphism databases

    DMDMi 125987822.

    Proteomic databases

    MaxQBi Q9P2X0.
    PaxDbi Q9P2X0.
    PRIDEi Q9P2X0.

    Protocols and materials databases

    DNASUi 54344.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341298 ; ENSP00000344338 ; ENSG00000179085 . [Q9P2X0-1 ]
    ENST00000368399 ; ENSP00000357384 ; ENSG00000179085 . [Q9P2X0-2 ]
    ENST00000368400 ; ENSP00000357385 ; ENSG00000179085 . [Q9P2X0-1 ]
    GeneIDi 54344.
    KEGGi hsa:54344.
    UCSCi uc001fhm.3. human. [Q9P2X0-2 ]
    uc001fhn.3. human. [Q9P2X0-1 ]

    Organism-specific databases

    CTDi 54344.
    GeneCardsi GC01M155112.
    GeneReviewsi DPM3.
    HGNCi HGNC:3007. DPM3.
    HPAi HPA014667.
    MIMi 605951. gene.
    612937. phenotype.
    neXtProti NX_Q9P2X0.
    Orphaneti 263494. DPM3-CDG.
    PharmGKBi PA27465.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145469.
    HOGENOMi HOG000038272.
    HOVERGENi HBG018968.
    InParanoidi Q9P2X0.
    KOi K09659.
    OMAi YREVAWP.
    OrthoDBi EOG73540R.
    PhylomeDBi Q9P2X0.
    TreeFami TF300274.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_2032. Synthesis of dolichyl-phosphate mannose.

    Miscellaneous databases

    GeneWikii DPM3.
    GenomeRNAii 54344.
    NextBioi 56581.
    PROi Q9P2X0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2X0.
    Bgeei Q9P2X0.
    CleanExi HS_DPM3.
    Genevestigatori Q9P2X0.

    Family and domain databases

    InterProi IPR013174. DPM3.
    [Graphical view ]
    Pfami PF08285. DPM3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-13, FUNCTION, SUBUNIT.
    2. "Dolichol-phosphate-mannose-3 (DPM3)/prostin-1 is a novel phospholipase C-gamma regulated gene negatively associated with prostate tumor invasion."
      Manos E.J., Kim M.L., Kassis J., Chang P.Y., Wells A., Jones D.A.
      Oncogene 20:2781-2790(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 2).
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: VARIANT CDG1O SER-85, CHARACTERIZATION OF VARIANT CDG1O SER-85.

    Entry informationi

    Entry nameiDPM3_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2X0
    Secondary accession number(s): Q5SR62
    , Q5SR63, Q9BXN4, Q9BXN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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 1
      Human chromosome 1: 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