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O60762

- DPM1_HUMAN

UniProt

O60762 - DPM1_HUMAN

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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

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. C-terminal protein lipidation Source: Reactome
  2. GDP-mannose metabolic process Source: Ensembl
  3. GPI anchor biosynthetic process Source: UniProtKB
  4. cellular protein metabolic process Source: Reactome
  5. dolichol metabolic process Source: MGI
  6. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  7. post-translational protein modification Source: Reactome
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. protein O-linked mannosylation Source: HGNC
  10. protein mannosylation Source: HGNC
Complete GO annotation...

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: MGI
  5. nucleus Source: UniProt
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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 – 11Removed1 Publication
Chaini2 – 260259Dolichol-phosphate mannosyltransferase subunit 1
PRO_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.

Family & Domainsi

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91S → G in AAH08466. 1 Publication
Sequence conflicti15 – 151R → W in AAC98797. 1 Publication
Sequence conflicti135 – 1351Q → K in AAC98797. 1 Publication
Sequence conflicti143 – 1431V → A in AAC98797. 1 Publication
Sequence conflicti154 – 1541V → I in AAC98797. 1 Publication
Sequence conflicti177 – 1771R → T in AAC98797. 1 Publication
Sequence conflicti191 – 1911R → P in AAC98797. 1 Publication
Sequence conflicti220 – 2201L → M in AAH08466. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 138 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

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