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Q9P2X0 (DPM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DPM3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length92 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Pathway

Protein modification; protein glycosylation.

Subunit structure

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. Ref.1

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the DPM3 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseCongenital disorder of glycosylation
Congenital muscular dystrophy
Disease mutation
Dystroglycanopathy
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

GPI anchor biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

carbohydrate metabolic process

Non-traceable author statement Ref.1. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

dolichol-linked oligosaccharide biosynthetic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan

Traceable author statement PubMed 16280320. Source: HGNC

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein O-linked mannosylation

Traceable author statement PubMed 16280320. Source: HGNC

protein mannosylation

Traceable author statement PubMed 16280320. Source: HGNC

regulation of protein stability

Inferred from physical interaction Ref.1. Source: UniProtKB

   Cellular_componentdolichol-phosphate-mannose synthase complex

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement PubMed 16280320. Source: HGNC

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.1. Source: HGNC

mannosyltransferase complex

Traceable author statement PubMed 16280320. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DPM1O607624EBI-9087337,EBI-719526
Dpm2Q9Z3252EBI-9087337,EBI-9097185From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P2X0-1)

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.
Isoform 2 (identifier: Q9P2X0-2)

Also known as: Long;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9292Dolichol-phosphate mannosyltransferase subunit 3
PRO_0000195000

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane37 – 5721Helical; Potential

Natural variations

Alternative sequence11M → MLSVGGLRLSLVRFSFLLLR GALLPSLAVTM in isoform 2.
VSP_001308
Natural variant851L → S in CDG1O; affects interaction with DPM1. Ref.7
VAR_062518

Experimental info

Sequence conflict901L → V in BAA96291. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Short) [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: C350A6896842A877

FASTA9210,094
        10         20         30         40         50         60 
MTKLAQWLWG LAILGSTWVA LTTGALGLEL PLSCQEVLWP LPAYLLVSAG CYALGTVGYR 

        70         80         90 
VATFHDCEDA ARELQSQIQE ARADLARRGL RF 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: DD8661D41C2AE5C0
Show »

FASTA12213,277

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Deficiency of Dol-P-Man synthase subunit DPM3 bridges the congenital disorders of glycosylation with the dystroglycanopathies."
Lefeber D.J., Schonberger J., Morava E., Guillard M., Huyben K.M., Verrijp K., Grafakou O., Evangeliou A., Preijers F.W., Manta P., Yildiz J., Grunewald S., Spilioti M., van den Elzen C., Klein D., Hess D., Ashida H., Hofsteenge J. expand/collapse author list , Maeda Y., van den Heuvel L., Lammens M., Lehle L., Wevers R.A.
Am. J. Hum. Genet. 85:76-86(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDG1O SER-85, CHARACTERIZATION OF VARIANT CDG1O SER-85.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_061846.2. NM_018973.3.
NP_714963.1. NM_153741.1.
UniGeneHs.110477.

3D structure databases

ProteinModelPortalQ9P2X0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119935. 1 interaction.
IntActQ9P2X0. 3 interactions.
STRING9606.ENSP00000357384.

Polymorphism databases

DMDM125987822.

Proteomic databases

PaxDbQ9P2X0.
PRIDEQ9P2X0.

Protocols and materials databases

DNASU54344.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341298; ENSP00000344338; ENSG00000179085. [Q9P2X0-1]
ENST00000368399; ENSP00000357384; ENSG00000179085. [Q9P2X0-2]
ENST00000368400; ENSP00000357385; ENSG00000179085. [Q9P2X0-1]
GeneID54344.
KEGGhsa:54344.
UCSCuc001fhm.3. human. [Q9P2X0-2]
uc001fhn.3. human. [Q9P2X0-1]

Organism-specific databases

CTD54344.
GeneCardsGC01M155112.
HGNCHGNC:3007. DPM3.
HPAHPA014667.
MIM605951. gene.
612937. phenotype.
neXtProtNX_Q9P2X0.
Orphanet263494. DPM3-CDG.
PharmGKBPA27465.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145469.
HOGENOMHOG000038272.
HOVERGENHBG018968.
InParanoidQ9P2X0.
KOK09659.
OMAFGCYSLA.
OrthoDBEOG73540R.
PhylomeDBQ9P2X0.
TreeFamTF300274.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9P2X0.
BgeeQ9P2X0.
CleanExHS_DPM3.
GenevestigatorQ9P2X0.

Family and domain databases

InterProIPR013174. DPM3.
[Graphical view]
PfamPF08285. DPM3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDPM3.
GenomeRNAi54344.
NextBio56581.
PROQ9P2X0.
SOURCESearch...

Entry information

Entry nameDPM3_HUMAN
AccessionPrimary (citable) accession number: Q9P2X0
Secondary accession number(s): Q5SR62 expand/collapse secondary AC list , Q5SR63, Q9BXN4, Q9BXN5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM