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O70152

- DPM1_MOUSE

UniProt

O70152 - DPM1_MOUSE

Protein

Dolichol-phosphate mannosyltransferase subunit 1

Gene

Dpm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.

    Pathwayi

    GO - Molecular functioni

    1. dolichyl-phosphate beta-D-mannosyltransferase activity Source: HGNC
    2. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: HGNC

    GO - Biological processi

    1. GPI anchor biosynthetic process Source: HGNC
    2. protein mannosylation Source: HGNC
    3. protein O-linked mannosylation Source: HGNC

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT2. Glycosyltransferase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended 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
    Gene namesi
    Name:Dpm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1330239. Dpm1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: HGNC

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 260259Dolichol-phosphate mannosyltransferase subunit 1PRO_0000059171Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei9 – 91PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO70152.
    PaxDbiO70152.
    PRIDEiO70152.

    PTM databases

    PhosphoSiteiO70152.

    Expressioni

    Gene expression databases

    BgeeiO70152.
    CleanExiMM_DPM1.
    GenevestigatoriO70152.

    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.By similarity

    Protein-protein interaction databases

    IntActiO70152. 2 interactions.
    MINTiMINT-4093451.

    Structurei

    3D structure databases

    ProteinModelPortaliO70152.
    SMRiO70152. Positions 26-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0463.
    GeneTreeiENSGT00550000075000.
    HOVERGENiHBG018967.
    InParanoidiO70152.
    KOiK00721.
    OMAiHGIKHAT.
    OrthoDBiEOG7W41CN.
    PhylomeDBiO70152.
    TreeFamiTF105617.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O70152-1 [UniParc]FASTAAdd to Basket

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    MASTGASRSL AASPRPPQGR SSRQDKYSVL LPTYNERENL PLIVWLLVKS    50
    FSESAINYEI IIIDDGSPDG TREVAEQLAE IYGPDRILLR PREKKLGLGT 100
    AYIHGIKHAT GNYVIIMDAD LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG 150
    NGGVYGWDLK RKIISRGANF ITQILLRPGA SDLTGSFRLY RKEVLQKLIE 200
    KCVSKGYVFQ MEMIVRARQM NYTIGEVPIS FVDRVYGESK LGGNEIVSFL 250
    KGLLTLFATT 260
    Length:260
    Mass (Da):29,175
    Last modified:August 1, 1998 - v1
    Checksum:i8CB1BCDF1977EBA6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761E → G in BAB25735. (PubMed:16141072)Curated
    Sequence conflicti122 – 1221S → Y in BAB25735. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004789 mRNA. Translation: BAA25759.1.
    AK005268 mRNA. Translation: BAB23920.1.
    AK004834 mRNA. Translation: BAB23602.1.
    AK008548 mRNA. Translation: BAB25735.1.
    BC061151 mRNA. Translation: AAH61151.1.
    CCDSiCCDS17109.1.
    RefSeqiNP_034202.1. NM_010072.3.
    UniGeneiMm.422657.

    Genome annotation databases

    EnsembliENSMUST00000138667; ENSMUSP00000139070; ENSMUSG00000093752.
    ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
    GeneIDi13480.
    KEGGimmu:13480.
    UCSCiuc008oas.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004789 mRNA. Translation: BAA25759.1 .
    AK005268 mRNA. Translation: BAB23920.1 .
    AK004834 mRNA. Translation: BAB23602.1 .
    AK008548 mRNA. Translation: BAB25735.1 .
    BC061151 mRNA. Translation: AAH61151.1 .
    CCDSi CCDS17109.1.
    RefSeqi NP_034202.1. NM_010072.3.
    UniGenei Mm.422657.

    3D structure databases

    ProteinModelPortali O70152.
    SMRi O70152. Positions 26-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O70152. 2 interactions.
    MINTi MINT-4093451.

    Protein family/group databases

    CAZyi GT2. Glycosyltransferase Family 2.

    PTM databases

    PhosphoSitei O70152.

    Proteomic databases

    MaxQBi O70152.
    PaxDbi O70152.
    PRIDEi O70152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000138667 ; ENSMUSP00000139070 ; ENSMUSG00000093752 .
    ENSMUST00000154111 ; ENSMUSP00000118776 ; ENSMUSG00000078919 .
    GeneIDi 13480.
    KEGGi mmu:13480.
    UCSCi uc008oas.1. mouse.

    Organism-specific databases

    CTDi 8813.
    MGIi MGI:1330239. Dpm1.

    Phylogenomic databases

    eggNOGi COG0463.
    GeneTreei ENSGT00550000075000.
    HOVERGENi HBG018967.
    InParanoidi O70152.
    KOi K00721.
    OMAi HGIKHAT.
    OrthoDBi EOG7W41CN.
    PhylomeDBi O70152.
    TreeFami TF105617.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 283971.
    PROi O70152.
    SOURCEi Search...

    Gene expression databases

    Bgeei O70152.
    CleanExi MM_DPM1.
    Genevestigatori O70152.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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 [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum, Lung and Small intestine.
    3. "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: Liver.

    Entry informationi

    Entry nameiDPM1_MOUSE
    AccessioniPrimary (citable) accession number: O70152
    Secondary accession number(s): Q9D829
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3