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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

ogm2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.1 Publication

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  • dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: PomBase

GO - Biological processi

  • protein O-linked mannosylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.109. 5613.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2 (EC:2.4.1.109)
Gene namesi
Name:ogm2
Synonyms:oma2
ORF Names:SPAPB1E7.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB1E7.09.
PomBaseiSPAPB1E7.09.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 7421HelicalSequence AnalysisAdd
BLAST
Transmembranei146 – 16621HelicalSequence AnalysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Transmembranei229 – 24921HelicalSequence AnalysisAdd
BLAST
Transmembranei285 – 30521HelicalSequence AnalysisAdd
BLAST
Transmembranei602 – 62221HelicalSequence AnalysisAdd
BLAST
Transmembranei639 – 65921HelicalSequence AnalysisAdd
BLAST
Transmembranei692 – 71221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endomembrane system Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Dolichyl-phosphate-mannose--protein mannosyltransferase 2PRO_0000237686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9C100.

Interactioni

Protein-protein interaction databases

BioGridi280071. 1 interaction.
MINTiMINT-4702145.
STRINGi4896.SPAPB1E7.09-1.

Structurei

3D structure databases

ProteinModelPortaliQ9C100.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini332 – 38655MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 45557MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini463 – 52159MIR 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.
HOGENOMiHOG000157526.
InParanoidiQ9C100.
KOiK00728.
OMAiTIEDLWE.
OrthoDBiEOG7BP89X.
PhylomeDBiQ9C100.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 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.

Q9C100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYEQLHAQS GQLRQRFPSK HSEIEDEVAN EKEELKDATK SALGEVKTNK
60 70 80 90 100
KYYILGYFLV PLLLTVIAGF VRVWKIADSN VVIWDEAHFG KFASYYLKHE
110 120 130 140 150
FYFDVHPPLG KMLNAVAGKL VGYDGSFDFS SGATYPEDLN YKFMRLWNAA
160 170 180 190 200
FGTLCIPLVY FTALNFNYSF LAATLCTLMV ALDNHLATIS RFILLDSMLL
210 220 230 240 250
FFIISTFFCL SRYHVYHKAP FTFYWFKWLF LTGVCIGCVC SVKLVGLFIT
260 270 280 290 300
AVVGLYTVDE LWCLLNDKRV TWKAYAGHWI ARVCLLIFLP ILIYAFTFWI
310 320 330 340 350
QFAVLYRSGP GDAQMPSLFQ ARLEGSPLTK NPIDLMYGSK FTLKSRNPTG
360 370 380 390 400
ALLHSHVQTY PEGSEQQQVT GYHHKDGNNE WMFVPTHGVA YNYEENDPMN
410 420 430 440 450
PILNGSVVRL IHPFTNRNLH THKIPAPLNK RMYEVSGYGL GDVGDEKDYW
460 470 480 490 500
IVNILYDTAH RDAYNVRSLS TVFQLYNPVV GCYLSSSSSS LPSWGFGQIE
510 520 530 540 550
MYCDPDPDPS NTDTQWNVEE HINPRLPEGS INDYPSSFWS DFLHLNRAML
560 570 580 590 600
RANNGLIPDE DKLDALRSEA YQWPFLLATL RMCGWGDNQI KYLLVGNPVA
610 620 630 640 650
YWFATSSLIV FALFVVGAVL AWRRRVLRWS QEACDTFHYA GIYPFLGWFF
660 670 680 690 700
NYLPYYIMGR VLYVHHYEPS YALSTFTAAF VVDWFTKKMP KIVRVVVFIS
710 720 730
LYAIIAGVFI YFKDVTFGMH GPASDFHRLR WLNSWNVHD
Length:739
Mass (Da):85,037
Last modified:June 1, 2001 - v1
Checksum:iF0F0BBD35D889252
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36926.1.
RefSeqiNP_594135.1. NM_001019559.2.

Genome annotation databases

EnsemblFungiiSPAPB1E7.09.1; SPAPB1E7.09.1:pep; SPAPB1E7.09.
GeneIDi2543657.
KEGGispo:SPAPB1E7.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC36926.1.
RefSeqiNP_594135.1. NM_001019559.2.

3D structure databases

ProteinModelPortaliQ9C100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280071. 1 interaction.
MINTiMINT-4702145.
STRINGi4896.SPAPB1E7.09-1.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiQ9C100.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB1E7.09.1; SPAPB1E7.09.1:pep; SPAPB1E7.09.
GeneIDi2543657.
KEGGispo:SPAPB1E7.09.

Organism-specific databases

EuPathDBiFungiDB:SPAPB1E7.09.
PomBaseiSPAPB1E7.09.

Phylogenomic databases

eggNOGiCOG1928.
HOGENOMiHOG000157526.
InParanoidiQ9C100.
KOiK00728.
OMAiTIEDLWE.
OrthoDBiEOG7BP89X.
PhylomeDBiQ9C100.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.109. 5613.

Miscellaneous databases

NextBioi20804663.
PROiQ9C100.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 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]
ProtoNetiSearch...

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.

Entry informationi

Entry nameiPMT2_SCHPO
AccessioniPrimary (citable) accession number: Q9C100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: May 27, 2015
This is version 94 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

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.