Skip Header

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

O70152

- DPM1_MOUSE

UniProt

O70152 - DPM1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dolichol-phosphate mannosyltransferase subunit 1

Gene

Dpm1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate beta-D-mannosyltransferase activity Source: HGNC
  2. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: HGNC

GO - Biological processi

  1. GPI anchor biosynthetic process Source: HGNC
  2. protein mannosylation Source: HGNC
  3. protein O-linked mannosylation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_251842. 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: Chromosome 2

Organism-specific databases

MGIiMGI:1330239. Dpm1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: HGNC
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.
GenevestigatoriO70152.

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.

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.
OMAiHGIKHAT.
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 .
CCDSi CCDS17109.1.
RefSeqi NP_034202.1. NM_010072.3.
UniGenei Mm.422657.

3D structure databases

ProteinModelPortali O70152.
SMRi O70152. Positions 26-120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O70152. 2 interactions.
MINTi MINT-4093451.

Protein family/group databases

CAZyi GT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSitei O70152.

Proteomic databases

MaxQBi O70152.
PaxDbi O70152.
PRIDEi O70152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000138667 ; ENSMUSP00000139070 ; ENSMUSG00000093752 .
ENSMUST00000154111 ; ENSMUSP00000118776 ; ENSMUSG00000078919 .
GeneIDi 13480.
KEGGi mmu:13480.
UCSCi uc008oas.1. mouse.

Organism-specific databases

CTDi 8813.
MGIi MGI:1330239. Dpm1.

Phylogenomic databases

eggNOGi COG0463.
GeneTreei ENSGT00550000075000.
HOVERGENi HBG018967.
InParanoidi O70152.
KOi K00721.
OMAi HGIKHAT.
OrthoDBi EOG7W41CN.
PhylomeDBi O70152.
TreeFami TF105617.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_251842. Synthesis of dolichyl-phosphate mannose.

Miscellaneous databases

NextBioi 283971.
PROi O70152.
SOURCEi Search...

Gene expression databases

Bgeei O70152.
CleanExi MM_DPM1.
ExpressionAtlasi O70152. baseline and differential.
Genevestigatori O70152.

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 [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: November 26, 2014
This is version 109 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