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O13898

- PMT1_SCHPO

UniProt

O13898 - PMT1_SCHPO

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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

ogm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1.2 Publications

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: PomBase

GO - Biological processi

  1. cell wall mannoprotein biosynthetic process Source: PomBase
  2. chain elongation of O-linked mannose residue Source: PomBase
  3. protein O-linked mannosylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.109. 5615.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC:2.4.1.109)
Gene namesi
Name:ogm1
Synonyms:oma1
ORF Names:SPAC22A12.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC22A12.07c.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Nucleus membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921HelicalSequence AnalysisAdd
BLAST
Transmembranei77 – 9721HelicalSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence AnalysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Transmembranei224 – 24421HelicalSequence AnalysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Transmembranei573 – 59321HelicalSequence AnalysisAdd
BLAST
Transmembranei610 – 63021HelicalSequence AnalysisAdd
BLAST
Transmembranei643 – 66321HelicalSequence AnalysisAdd
BLAST
Transmembranei671 – 69121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase complex Source: PomBase
  2. endomembrane system Source: PomBase
  3. endoplasmic reticulum membrane Source: PomBase
  4. integral component of membrane Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Dolichyl-phosphate-mannose--protein mannosyltransferase 1PRO_0000121499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
Modified residuei451 – 4511Phosphothreonine1 Publication
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO13898.

Interactioni

Protein-protein interaction databases

BioGridi277924. 4 interactions.
STRINGi4896.SPAC22A12.07c-1.

Structurei

3D structure databases

ProteinModelPortaliO13898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini310 – 36455MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini374 – 43360MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini443 – 49957MIR 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 39 family.Curated
Contains 3 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
InParanoidiO13898.
KOiK00728.
OMAiFANCELM.
OrthoDBiEOG7BP89X.
PhylomeDBiO13898.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13898-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKQSTFQDP KEKHRIQRDV KLSRPRKRFS FLDYVVVIFL TVVAFCVRAQ
60 70 80 90 100
RLMNPAKVVF EELRYYNYAV DYVNNKLLMD VYPPLGKLLF SLVAALTGNK
110 120 130 140 150
YELNTLDEPG QQYPFTDVAY SMRLFTCLLG SLLVPLMYGT VYFPTKSKTA
160 170 180 190 200
ASLAALFVIF DNGLITMSRY IMIEIPALYF MSLTAFYWSV YEAQQKRPFS
210 220 230 240 250
LRWHTSLLST GVALGLALST KLSAMFTFGW LLILAAFHLW NLLGDLSVPM
260 270 280 290 300
YRIVKHLFSY IFYLIGVPIT VYLAVFAVHS HIAYKASVAD AFLPPEHRHA
310 320 330 340 350
LAGNRFDDQF ADVAYGSLVT IRNAIPEHGY LHSSELLYPE GTEQQIISLV
360 370 380 390 400
DEPNQNALWI IEHEHSQDNN RSNIELLKDG SVVRLRHVMT GRALHSHEHK
410 420 430 440 450
PIVSNNDWQL EASAYGGFGF EGDANDLFRI QILEKKSKHA TSNGTVETLN
460 470 480 490 500
TKFRLIHVFA NCELMSSHRR FPDWGDYQRE VTCCRNCVER STTWFIESNY
510 520 530 540 550
HDGLPSDSRK ITYRKPGFLE SFVEHNKLMW LKDRKMGDGH VYESSALTWP
560 570 580 590 600
LLLGPLRFFY EQHLQVFFMG NPFVWYSVIS LVAFFVIVQI FCLARWNLGY
610 620 630 640 650
NDFGPSAFHY NYNIGKFVVA WLLHWAPYIL ETDRVFLYHY LPALYFGIAA
660 670 680 690 700
LGVSWSFLGN AVFGNRTAYK ALSVIIMALM FLVYRLYSPF TYMTTLTKSS
710 720 730 740 750
CRALELKGSW NFHCNTYLDN LSDYKFSSDA GETYFEKAAP HPFVYSEDTA
760 770 780 790 800
KKSEGDTPLN KNLNDYYPSW DQRVEAGYKL AAQQKAEQEA REAAEKAASE
810 820 830 840 850
AAERSSSEAA ASSSSESVAA ASVEAERLAM EADEFNGASE TVDGASVEAE
860 870 880 890
RSAMEAAALN NAAESTEVVG SSPESVASEQ EENVAESAQA RVE
Length:893
Mass (Da):101,335
Last modified:January 1, 1998 - v1
Checksum:i67047E4D896A3568
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16577.1.
PIRiT38147.
RefSeqiNP_593237.1. NM_001018634.2.

Genome annotation databases

EnsemblFungiiSPAC22A12.07c.1; SPAC22A12.07c.1:pep; SPAC22A12.07c.
GeneIDi2541418.
KEGGispo:SPAC22A12.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16577.1 .
PIRi T38147.
RefSeqi NP_593237.1. NM_001018634.2.

3D structure databases

ProteinModelPortali O13898.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277924. 4 interactions.
STRINGi 4896.SPAC22A12.07c-1.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi O13898.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC22A12.07c.1 ; SPAC22A12.07c.1:pep ; SPAC22A12.07c .
GeneIDi 2541418.
KEGGi spo:SPAC22A12.07c.

Organism-specific databases

PomBasei SPAC22A12.07c.

Phylogenomic databases

eggNOGi COG1928.
InParanoidi O13898.
KOi K00728.
OMAi FANCELM.
OrthoDBi EOG7BP89X.
PhylomeDBi O13898.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.109. 5615.

Miscellaneous databases

NextBioi 20802522.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
Pfami PF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view ]
SMARTi SM00472. MIR. 3 hits.
[Graphical view ]
SUPFAMi SSF82109. SSF82109. 1 hit.
PROSITEi PS50919. MIR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe."
    Tanaka N., Fujita Y., Suzuki S., Morishita M., Giga-Hama Y., Shimoda C., Takegawa K.
    Biochem. Biophys. Res. Commun. 330:813-820(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  3. "Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast."
    Willer T., Brandl M., Sipiczki M., Strahl S.
    Mol. Microbiol. 57:156-170(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPMT1_SCHPO
AccessioniPrimary (citable) accession number: O13898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3