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P31382 (PMT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2

EC=2.4.1.109
Gene names
Name:PMT2
Ordered Locus Names:YAL023C
ORF Names:FUN25
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to be active on chitinase.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Miscellaneous

Present with 6510 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PMT1P337752EBI-13573,EBI-13567

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 759758Dolichyl-phosphate-mannose--protein mannosyltransferase 2
PRO_0000121492

Regions

Topological domain2 – 6463Cytoplasmic Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 16782Lumenal Potential
Transmembrane168 – 18821Helical; Potential
Topological domain189 – 19810Cytoplasmic Potential
Transmembrane199 – 21921Helical; Potential
Topological domain220 – 25132Lumenal Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 28917Cytoplasmic Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 609299Lumenal Potential
Transmembrane610 – 63021Helical; Potential
Topological domain631 – 64717Cytoplasmic Potential
Transmembrane648 – 66821Helical; Potential
Topological domain669 – 6768Lumenal Potential
Transmembrane677 – 69721Helical; Potential
Topological domain698 – 71013Cytoplasmic Potential
Transmembrane711 – 73121Helical; Potential
Topological domain732 – 75928Lumenal Potential
Domain339 – 39456MIR 1
Domain407 – 46357MIR 2
Domain471 – 52959MIR 3

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue321Phosphoserine Ref.11
Modified residue381Phosphoserine Ref.11
Modified residue391Phosphoserine Ref.11
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P31382 [UniParc].

Last modified June 16, 2003. Version 2.
Checksum: B1E1480C2E04BE3D

FASTA75986,870
        10         20         30         40         50         60 
MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK EKPAAQSSLL 

        70         80         90        100        110        120 
RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG SYYLRHEFYH DVHPPLGKML 

       130        140        150        160        170        180 
VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK MRLFNASFSA LCVPLAYFTA KAIGFSLPTV 

       190        200        210        220        230        240 
WLMTVLVLFE NSYSTLGRFI LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG 

       250        260        270        280        290        300 
ISLGCTISVK MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI 

       310        320        330        340        350        360 
FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS IKNQALGGSL 

       370        380        390        400        410        420 
LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW SENETDIEYL KPGTSYRLVH 

       430        440        450        460        470        480 
KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV VGDNKDNWVI EIMDQRGDED PEKLHTLTTS 

       490        500        510        520        530        540 
FRIKNLEMGC YLAQTGNSLP EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED 

       550        560        570        580        590        600 
FQYPKTNFLK DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP 

       610        620        630        640        650        660 
KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM GGFYPLLAWG 

       670        680        690        700        710        720 
LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW SRSKCGRIMR FVLYAGFMAL 

       730        740        750 
VIGCFWYFSP ISFGMEGPSS NFRYLNWFST WDIADKQEA 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Dolinski K.J., Cherry J.M.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 137-139.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity."
Lussier M., Gentzsch M., Sdicu A.-M., Bussey H., Tanner W.
J. Biol. Chem. 270:2770-2775(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital."
Gaentzsch M., Tanner W.
EMBO J. 15:5752-5759(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-38 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05146 Genomic DNA. Translation: AAC04934.2.
BK006935 Genomic DNA. Translation: DAA06965.1.
PIRS36711.
RefSeqNP_009379.2. NM_001178168.1.

3D structure databases

ProteinModelPortalP31382.
SMRP31382. Positions 358-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31743. 169 interactions.
DIPDIP-6720N.
IntActP31382. 3 interactions.
MINTMINT-655858.
STRING4932.YAL023C.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbP31382.
PeptideAtlasP31382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL023C; YAL023C; YAL023C.
GeneID851210.
KEGGsce:YAL023C.

Organism-specific databases

CYGDYAL023c.
SGDS000000021. PMT2.

Phylogenomic databases

eggNOGCOG1928.
GeneTreeENSGT00740000115531.
HOGENOMHOG000157526.
KOK00728.
OMAWLCISRF.
OrthoDBEOG7BP89X.

Enzyme and pathway databases

BioCycYEAST:YAL023C-MONOMER.
BRENDA2.4.1.109. 984.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorP31382.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio968085.

Entry information

Entry namePMT2_YEAST
AccessionPrimary (citable) accession number: P31382
Secondary accession number(s): D6VPJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 16, 2003
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways