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O60762

- DPM1_HUMAN

UniProt

O60762 - DPM1_HUMAN

Protein

Dolichol-phosphate mannosyltransferase subunit 1

Gene

DPM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (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.

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. alcohol binding Source: Ensembl
    2. dolichyl-phosphate beta-D-mannosyltransferase activity Source: UniProtKB
    3. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: HGNC
    4. mannose binding Source: Ensembl
    5. protein binding Source: UniProtKB

    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: MGI
    5. GDP-mannose metabolic process Source: Ensembl
    6. GPI anchor biosynthetic process Source: UniProtKB
    7. post-translational protein modification Source: Reactome
    8. protein mannosylation Source: HGNC
    9. protein N-linked glycosylation via asparagine Source: Reactome
    10. protein O-linked mannosylation Source: HGNC

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_2032. Synthesis of dolichyl-phosphate mannose.
    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 subunit 1
    Gene namesi
    Name:DPM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:3005. DPM1.

    Subcellular locationi

    GO - Cellular componenti

    1. dolichol-phosphate-mannose synthase complex Source: UniProtKB
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum membrane Source: HGNC
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1E (CDG1E) [MIM:608799]: 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 CDG1E patients have features consistent with a dystroglycanopathy and congenital muscular dystrophy, including O-mannosylation defect, camptodactyly, elevated creatine kinase, motor delay and dystrophic changes on muscel biopsy.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921R → G in CDG1E. 2 Publications
    VAR_012341
    Natural varianti152 – 1521G → V in CDG1E; abolishes interaction with DPM3. 1 Publication
    VAR_070592
    Natural varianti248 – 2481S → P in CDG1E. 1 Publication
    VAR_019841

    Keywords - Diseasei

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

    Organism-specific databases

    MIMi608799. phenotype.
    Orphaneti79322. DPM1-CDG.
    PharmGKBiPA27463.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 260259Dolichol-phosphate mannosyltransferase subunit 1PRO_0000059170Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei9 – 91Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60762.
    PaxDbiO60762.
    PRIDEiO60762.

    PTM databases

    PhosphoSiteiO60762.

    Expressioni

    Gene expression databases

    ArrayExpressiO60762.
    BgeeiO60762.
    CleanExiHS_DPM1.
    GenevestigatoriO60762.

    Organism-specific databases

    HPAiHPA051818.

    Interactioni

    Subunit structurei

    Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DPM3Q9P2X04EBI-719526,EBI-9087337

    Protein-protein interaction databases

    BioGridi114340. 11 interactions.
    IntActiO60762. 9 interactions.
    STRINGi9606.ENSP00000360644.

    Structurei

    3D structure databases

    ProteinModelPortaliO60762.
    SMRiO60762. Positions 26-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0463.
    HOGENOMiHOG000283250.
    HOVERGENiHBG018967.
    KOiK00721.
    OrthoDBiEOG7W41CN.
    PhylomeDBiO60762.
    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.

    O60762-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLEVSRSP RRSRRELEVR SPRQNKYSVL LPTYNERENL PLIVWLLVKS    50
    FSESGINYEI IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT 100
    AYIHGMKHAT GNYIIIMDAD LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG 150
    NGGVYGWDLK RKIISRGANF LTQILLRPGA SDLTGSFRLY RKEVLEKLIE 200
    KCVSKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK LGGNEIVSFL 250
    KGLLTLFATT 260
    Length:260
    Mass (Da):29,634
    Last modified:August 1, 1998 - v1
    Checksum:i9792145BFC8F0514
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91S → G in AAH08466. (PubMed:15489334)Curated
    Sequence conflicti15 – 151R → W in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti135 – 1351Q → K in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti143 – 1431V → A in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti154 – 1541V → I in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti177 – 1771R → T in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti191 – 1911R → P in AAC98797. (PubMed:9223280)Curated
    Sequence conflicti220 – 2201L → M in AAH08466. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921R → G in CDG1E. 2 Publications
    VAR_012341
    Natural varianti152 – 1521G → V in CDG1E; abolishes interaction with DPM3. 1 Publication
    VAR_070592
    Natural varianti248 – 2481S → P in CDG1E. 1 Publication
    VAR_019841

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86198 mRNA. Translation: BAA25646.1.
    D86202 Genomic DNA. Translation: BAA25647.1.
    CR456926 mRNA. Translation: CAG33207.1.
    AK289569 mRNA. Translation: BAF82258.1.
    AL034553 Genomic DNA. Translation: CAB53749.1.
    BC007073 mRNA. Translation: AAH07073.1.
    BC008466 mRNA. Translation: AAH08466.1.
    BC016322 mRNA. Translation: AAH16322.1.
    AF007875 mRNA. Translation: AAC98797.1.
    CCDSiCCDS13434.1.
    RefSeqiNP_003850.1. NM_003859.1.
    UniGeneiHs.654951.

    Genome annotation databases

    EnsembliENST00000371588; ENSP00000360644; ENSG00000000419.
    GeneIDi8813.
    KEGGihsa:8813.
    UCSCiuc002xvw.1. human.

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86198 mRNA. Translation: BAA25646.1 .
    D86202 Genomic DNA. Translation: BAA25647.1 .
    CR456926 mRNA. Translation: CAG33207.1 .
    AK289569 mRNA. Translation: BAF82258.1 .
    AL034553 Genomic DNA. Translation: CAB53749.1 .
    BC007073 mRNA. Translation: AAH07073.1 .
    BC008466 mRNA. Translation: AAH08466.1 .
    BC016322 mRNA. Translation: AAH16322.1 .
    AF007875 mRNA. Translation: AAC98797.1 .
    CCDSi CCDS13434.1.
    RefSeqi NP_003850.1. NM_003859.1.
    UniGenei Hs.654951.

    3D structure databases

    ProteinModelPortali O60762.
    SMRi O60762. Positions 26-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114340. 11 interactions.
    IntActi O60762. 9 interactions.
    STRINGi 9606.ENSP00000360644.

    Protein family/group databases

    CAZyi GT2. Glycosyltransferase Family 2.

    PTM databases

    PhosphoSitei O60762.

    Proteomic databases

    MaxQBi O60762.
    PaxDbi O60762.
    PRIDEi O60762.

    Protocols and materials databases

    DNASUi 8813.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371588 ; ENSP00000360644 ; ENSG00000000419 .
    GeneIDi 8813.
    KEGGi hsa:8813.
    UCSCi uc002xvw.1. human.

    Organism-specific databases

    CTDi 8813.
    GeneCardsi GC20M049551.
    GeneReviewsi DPM1.
    HGNCi HGNC:3005. DPM1.
    HPAi HPA051818.
    MIMi 603503. gene.
    608799. phenotype.
    neXtProti NX_O60762.
    Orphaneti 79322. DPM1-CDG.
    PharmGKBi PA27463.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0463.
    HOGENOMi HOG000283250.
    HOVERGENi HBG018967.
    KOi K00721.
    OrthoDBi EOG7W41CN.
    PhylomeDBi O60762.
    TreeFami TF105617.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi DPM1. human.
    GeneWikii DPM1.
    GenomeRNAii 8813.
    NextBioi 33058.
    PROi O60762.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60762.
    Bgeei O60762.
    CleanExi HS_DPM1.
    Genevestigatori O60762.

    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 [GENOMIC DNA / MRNA].
      Tissue: Placenta.
    2. "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].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      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].
      Tissue: Brain and Urinary bladder.
    6. "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe."
      Colussi P.A., Taron C.H., Mack J.C., Orlean P.
      Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-260.
    7. "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: SUBUNIT.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3."
      Ashida H., Maeda Y., Kinoshita T.
      J. Biol. Chem. 281:896-904(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DPM3.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)."
      Kim S., Westphal V., Srikrishna G., Mehta D.P., Peterson S., Filiano J., Karnes P.S., Patterson M.C., Freeze H.H.
      J. Clin. Invest. 105:191-198(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDG1E GLY-92.
    16. "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie."
      Imbach T., Schenk B., Schollen E., Burda P., Stutz A., Gruenewald S., Bailie N.M., King M.D., Jaeken J., Matthijs G., Berger E.G., Aebi M., Hennet T.
      J. Clin. Invest. 105:233-239(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDG1E GLY-92.
    17. Cited for: VARIANT CDG1E PRO-248.
    18. "Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy."
      Yang A.C., Ng B.G., Moore S.A., Rush J., Waechter C.J., Raymond K.M., Willer T., Campbell K.P., Freeze H.H., Mehta L.
      Mol. Genet. Metab. 110:345-351(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDG1E VAL-152, CHARACTERIZATION OF VARIANT CDG1E VAL-152.

    Entry informationi

    Entry nameiDPM1_HUMAN
    AccessioniPrimary (citable) accession number: O60762
    Secondary accession number(s): O15157, Q6IB78, Q96HK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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