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Protein

Dolichol-phosphate mannosyltransferase subunit 3

Gene

DPM3

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

Functioni

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

Pathwayi

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
Complete GO annotation...

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

Topology

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

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
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1O1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612937
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

BgeeiQ9P2X0.
CleanExiHS_DPM3.
ExpressionAtlasiQ9P2X0. baseline and differential.
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...

Family & Domainsi

Sequence similaritiesi

Belongs to the DPM3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145469.
GeneTreeiENSGT00390000008892.
HOGENOMiHOG000038272.
HOVERGENiHBG018968.
InParanoidiQ9P2X0.
KOiK09659.
OMAiPCREVLW.
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

        10         20         30         40         50
MTKLAQWLWG LAILGSTWVA LTTGALGLEL PLSCQEVLWP LPAYLLVSAG
60 70 80 90
CYALGTVGYR VATFHDCEDA ARELQSQIQE ARADLARRGL RF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9P2X0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Polymorphism databases

DMDMi125987822.

Proteomic databases

MaxQBiQ9P2X0.
PaxDbiQ9P2X0.
PRIDEiQ9P2X0.

Protocols and materials databases

DNASUi54344.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi54344.
GeneCardsiGC01M155112.
GeneReviewsiDPM3.
HGNCiHGNC:3007. DPM3.
HPAiHPA014667.
MIMi605951. gene.
612937. phenotype.
neXtProtiNX_Q9P2X0.
Orphaneti263494. DPM3-CDG.
PharmGKBiPA27465.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145469.
GeneTreeiENSGT00390000008892.
HOGENOMiHOG000038272.
HOVERGENiHBG018968.
InParanoidiQ9P2X0.
KOiK09659.
OMAiPCREVLW.
OrthoDBiEOG73540R.
PhylomeDBiQ9P2X0.
TreeFamiTF300274.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_2032. Synthesis of dolichyl-phosphate mannose.

Miscellaneous databases

GeneWikiiDPM3.
GenomeRNAii54344.
NextBioi56581.
PROiQ9P2X0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2X0.
CleanExiHS_DPM3.
ExpressionAtlasiQ9P2X0. baseline and differential.
GenevestigatoriQ9P2X0.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.