Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dolichol-phosphate mannosyltransferase subunit 1

Gene

Dpm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_317373. 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
Gene namesi
Name:Dpm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1330239. Dpm1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 260259Dolichol-phosphate mannosyltransferase subunit 1PRO_0000059171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO70152.
PaxDbiO70152.
PRIDEiO70152.

PTM databases

PhosphoSiteiO70152.

Expressioni

Gene expression databases

BgeeiO70152.
CleanExiMM_DPM1.
ExpressionAtlasiO70152. baseline and differential.
GenevisibleiO70152. MM.

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.By similarity

Protein-protein interaction databases

IntActiO70152. 2 interactions.
MINTiMINT-4093451.
STRINGi10090.ENSMUSP00000118776.

Structurei

3D structure databases

ProteinModelPortaliO70152.
SMRiO70152. Positions 26-120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiCOG0463.
GeneTreeiENSGT00550000075000.
HOVERGENiHBG018967.
InParanoidiO70152.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W41CN.
PhylomeDBiO70152.
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.

O70152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTGASRSL AASPRPPQGR SSRQDKYSVL LPTYNERENL PLIVWLLVKS
60 70 80 90 100
FSESAINYEI IIIDDGSPDG TREVAEQLAE IYGPDRILLR PREKKLGLGT
110 120 130 140 150
AYIHGIKHAT GNYVIIMDAD LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG
160 170 180 190 200
NGGVYGWDLK RKIISRGANF ITQILLRPGA SDLTGSFRLY RKEVLQKLIE
210 220 230 240 250
KCVSKGYVFQ MEMIVRARQM NYTIGEVPIS FVDRVYGESK LGGNEIVSFL
260
KGLLTLFATT
Length:260
Mass (Da):29,175
Last modified:August 1, 1998 - v1
Checksum:i8CB1BCDF1977EBA6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761E → G in BAB25735 (PubMed:16141072).Curated
Sequence conflicti122 – 1221S → Y in BAB25735 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004789 mRNA. Translation: BAA25759.1.
AK005268 mRNA. Translation: BAB23920.1.
AK004834 mRNA. Translation: BAB23602.1.
AK008548 mRNA. Translation: BAB25735.1.
BC061151 mRNA. Translation: AAH61151.1.
CCDSiCCDS17109.1.
RefSeqiNP_034202.1. NM_010072.3.
UniGeneiMm.422657.

Genome annotation databases

EnsembliENSMUST00000138667; ENSMUSP00000139070; ENSMUSG00000093752.
ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
GeneIDi13480.
KEGGimmu:13480.
UCSCiuc008oas.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004789 mRNA. Translation: BAA25759.1.
AK005268 mRNA. Translation: BAB23920.1.
AK004834 mRNA. Translation: BAB23602.1.
AK008548 mRNA. Translation: BAB25735.1.
BC061151 mRNA. Translation: AAH61151.1.
CCDSiCCDS17109.1.
RefSeqiNP_034202.1. NM_010072.3.
UniGeneiMm.422657.

3D structure databases

ProteinModelPortaliO70152.
SMRiO70152. Positions 26-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70152. 2 interactions.
MINTiMINT-4093451.
STRINGi10090.ENSMUSP00000118776.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteiO70152.

Proteomic databases

MaxQBiO70152.
PaxDbiO70152.
PRIDEiO70152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000138667; ENSMUSP00000139070; ENSMUSG00000093752.
ENSMUST00000154111; ENSMUSP00000118776; ENSMUSG00000078919.
GeneIDi13480.
KEGGimmu:13480.
UCSCiuc008oas.1. mouse.

Organism-specific databases

CTDi8813.
MGIiMGI:1330239. Dpm1.

Phylogenomic databases

eggNOGiCOG0463.
GeneTreeiENSGT00550000075000.
HOVERGENiHBG018967.
InParanoidiO70152.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W41CN.
PhylomeDBiO70152.
TreeFamiTF105617.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_317373. Synthesis of dolichyl-phosphate mannose.

Miscellaneous databases

NextBioi283971.
PROiO70152.
SOURCEiSearch...

Gene expression databases

BgeeiO70152.
CleanExiMM_DPM1.
ExpressionAtlasiO70152. baseline and differential.
GenevisibleiO70152. MM.

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.
ProtoNetiSearch...

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 [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Lung and Small intestine.
  3. "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: Liver.

Entry informationi

Entry nameiDPM1_MOUSE
AccessioniPrimary (citable) accession number: O70152
Secondary accession number(s): Q9D829
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.