O60762 (DPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dolichol-phosphate mannosyltransferase
EC=2.4.1.83

Alternative name(s):
Dolichol-phosphate mannose synthase
Short name=DPM synthase
Dolichyl-phosphate beta-D-mannosyltransferase
Mannose-P-dolichol synthase
Short name=MPD synthase

Gene names

Name:

DPM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Disease	Congenital disorder of glycosylation Disease mutation
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-terminal protein lipidation Traceable author statement. Source: Reactome GDP-mannose metabolic process Inferred from electronic annotation. Source: Compara GPI anchor biosynthetic process Inferred from direct assay PubMed 10835346. Source: UniProtKB dolichol metabolic process Inferred from direct assay Ref.1PubMed 9724629. Source: MGI dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome protein O-linked mannosylation Inferred from direct assay Ref.1. Source: HGNC
Cellular_component	dolichol-phosphate-mannose synthase complex Inferred from direct assay PubMed 10835346. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay PubMed 9724629. Source: HGNC
Molecular_function	alcohol binding Inferred from electronic annotation. Source: Compara dolichyl-phosphate beta-D-mannosyltransferase activity Inferred from direct assay PubMed 10835346. Source: UniProtKB dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from direct assay Ref.1. Source: HGNC mannose binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 260	259	Dolichol-phosphate mannosyltransferase		PRO_0000059170
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9 Ref.11
	Modified residue	9	1	Phosphoserine Ref.9 Ref.11
Natural variations
	Natural variant	92	1	R → G in CDG1E. Ref.12 Ref.13		VAR_012341
	Natural variant	248	1	S → P in CDG1E. Ref.14		VAR_019841
Experimental info
	Sequence conflict	15	1	R → W in AAC98797. Ref.6
	Sequence conflict	135	1	Q → K in AAC98797. Ref.6
	Sequence conflict	143	1	V → A in AAC98797. Ref.6
	Sequence conflict	154	1	V → I in AAC98797. Ref.6
	Sequence conflict	177	1	R → T in AAC98797. Ref.6
	Sequence conflict	191	1	R → P in AAC98797. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O60762 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 9792145BFC8F0514	FASTA	260	29,634
	10 20 30 40 50 60 MASLEVSRSP RRSRRELEVR SPRQNKYSVL LPTYNERENL PLIVWLLVKS FSESGINYEI 70 80 90 100 110 120 IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT AYIHGMKHAT GNYIIIMDAD 130 140 150 160 170 180 LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG NGGVYGWDLK RKIISRGANF LTQILLRPGA 190 200 210 220 230 240 SDLTGSFRLY RKEVLEKLIE KCVSKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK 250 260 LGGNEIVSFL KGLLTLFATT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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.
[8]	"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.
[9]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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, MASS SPECTROMETRY.
[12]	"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.
[13]	"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.
[14]	"Congenital disorder of glycosylation (CDG) type Ie. A new patient." Garcia-Silva M.T., Matthijs G., Schollen E., Cabrera J.C., Sanchez Del Pozo J., Herreros M.M., Simon R., Maties M., Hernandez E.M., Hennet T., Briones P. J. Inherit. Metab. Dis. 27:591-600(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1E PRO-248.
+	Additional computationally mapped references.

Web resources

GeneReviews

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. BC016322 mRNA. Translation: AAH16322.1. AF007875 mRNA. Translation: AAC98797.1.
IPI	IPI00022018.
RefSeq	NP_003850.1. NM_003859.1.
UniGene	Hs.654951.
3D structure databases
ProteinModelPortal	O60762.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60762. 7 interactions.
STRING	9606.ENSP00000360644.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
PTM databases
PhosphoSite	O60762.
Proteomic databases
PaxDb	O60762.
PRIDE	O60762.
Protocols and materials databases
DNASU	8813.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371588; ENSP00000360644; ENSG00000000419.
GeneID	8813.
KEGG	hsa:8813.
UCSC	uc002xvw.1. human.
Organism-specific databases
CTD	8813.
GeneCards	GC20M049551.
HGNC	HGNC:3005. DPM1.
HPA	HPA051818.
MIM	603503. gene. 608799. phenotype.
neXtProt	NX_O60762.
Orphanet	79322. CDG syndrome type Ie.
PharmGKB	PA27463.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0463.
HOGENOM	HOG000283250.
HOVERGEN	HBG018967.
KO	K00721.
OrthoDB	EOG4NP748.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	O60762.
Bgee	O60762.
CleanEx	HS_DPM1.
Genevestigator	O60762.
GermOnline	ENSG00000000419. Homo sapiens.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2572.
ChiTaRS	DPM1. human.
GenomeRNAi	8813.
NextBio	33058.
SOURCE	Search...

Entry information

Entry name

DPM1_HUMAN

Accession

Primary (citable) accession number: O60762
Secondary accession number(s): O15157, Q6IB78

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.