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Q00772 (SLT2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Mitogen-activated protein kinase SLT2/MPK1

Short name=MAP kinase MPK1
EC=2.7.11.24
Gene names
Name:SLT2
Synonyms:MPK1
Ordered Locus Names:YHR030C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein kinase involved in a signal transduction pathway that play a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act the BCK1 kinase that then phosphorylates MKK1 and MKK2 which themselves phosphorylate the SLT2/MPK1 kinase which itself then phosphorylates and activates the transcription factor RLM1. Directly phosphorylates BCY1 upon TOR complex 1 (TORC1) inhibition. Ref.5 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by tyrosine and threonine phosphorylation by MKK1 and MKK2 Probable.

Subunit structure

Interacts with RLM1. Ref.5

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.

Miscellaneous

Present with 3230 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from sequence or structural similarity PubMed 8386319. Source: GOC

UFP-specific transcription factor mRNA processing involved in endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype PubMed 18971375. Source: SGD

barrier septum assembly

Inferred from genetic interaction PubMed 19633265. Source: SGD

endoplasmic reticulum unfolded protein response

Inferred from direct assay PubMed 16380504. Source: SGD

fungal-type cell wall biogenesis

Inferred from genetic interaction PubMed 16524906. Source: SGD

peroxisome degradation

Inferred from mutant phenotype PubMed 20385774. Source: SGD

protein phosphorylation

Inferred from mutant phenotype PubMed 14703512PubMed 20219973. Source: SGD

regulation of cell size

Inferred from mutant phenotype PubMed 17302939. Source: SGD

regulation of fungal-type cell wall organization

Inferred from mutant phenotype PubMed 8386319. Source: SGD

regulation of transcription factor import into nucleus

Inferred from mutant phenotype PubMed 20219973. Source: SGD

response to acid

Inferred from mutant phenotype PubMed 16087742. Source: SGD

signal transduction

Inferred from mutant phenotype PubMed 8386319. Source: SGD

   Cellular_componentcellular bud neck

Inferred from direct assay PubMed 12361575PubMed 23924898. Source: SGD

cellular bud tip

Inferred from direct assay PubMed 12361575PubMed 23924898. Source: SGD

mating projection tip

Inferred from direct assay PubMed 12361575. Source: SGD

nucleus

Inferred from direct assay PubMed 12361575PubMed 23924898. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from sequence or structural similarity PubMed 8386319. Source: SGD

protein binding

Inferred from physical interaction PubMed 10688190PubMed 15766533PubMed 15879519PubMed 20489023PubMed 21376235. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay PubMed 20823268PubMed 24554767. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Mitogen-activated protein kinase SLT2/MPK1
PRO_0000186338

Regions

Domain23 – 318296Protein kinase
Nucleotide binding29 – 379ATP By similarity
Motif190 – 1923TXY
Compositional bias370 – 39122Poly-Gln

Sites

Active site1531Proton acceptor By similarity
Binding site541ATP By similarity

Amino acid modifications

Modified residue1901Phosphothreonine Ref.8
Modified residue1921Phosphotyrosine Ref.7

Experimental info

Sequence conflict561V → L in CAA41954. Ref.1
Sequence conflict4671T → S in CAA41954. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q00772 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 559A3E0D3EBDE5F9

FASTA48455,636
        10         20         30         40         50         60 
MADKIERHTF KVFNQDFSVD KRFQLIKEIG HGAYGIVCSA RFAEAAEDTT VAIKKVTNVF 

        70         80         90        100        110        120 
SKTLLCKRSL RELKLLRHFR GHKNITCLYD MDIVFYPDGS INGLYLYEEL MECDMHQIIK 

       130        140        150        160        170        180 
SGQPLTDAHY QSFTYQILCG LKYIHSADVL HRDLKPGNLL VNADCQLKIC DFGLARGYSE 

       190        200        210        220        230        240 
NPVENSQFLT EYVATRWYRA PEIMLSYQGY TKAIDVWSAG CILAEFLGGK PIFKGKDYVN 

       250        260        270        280        290        300 
QLNQILQVLG TPPDETLRRI GSKNVQDYIH QLGFIPKVPF VNLYPNANSQ ALDLLEQMLA 

       310        320        330        340        350        360 
FDPQKRITVD EALEHPYLSI WHDPADEPVC SEKFEFSFES VNDMEDLKQM VIQEVQDFRL 

       370        380        390        400        410        420 
FVRQPLLEEQ RQLQLQQQQQ QQQQQQQQQQ QPSDVDNGNA AASEENYPKQ MATSNSVAPQ 

       430        440        450        460        470        480 
QESFGIHSQN LPRHDADFPP RPQESMMEMR PATGNTADIP PQNDNGTLLD LEKELEFGLD 


RKYF 

« Hide

References

« Hide 'large scale' references
[1]"A protein kinase gene complements the lytic phenotype of Saccharomyces cerevisiae lyt2 mutants."
Torres L., Martin H., Garcia-Saez M.I., Arroyo J., Molina M., Sanchez M., Nombela C.
Mol. Microbiol. 5:2845-2854(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204510 / AB320.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae."
Mazzoni C., Zarzov P., Rambourg A., Mann C.
J. Cell Biol. 123:1821-1833(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway."
Watanabe Y., Takaesu G., Hagiwara M., Irie K., Matsumoto K.
Mol. Cell. Biol. 17:2615-2623(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RLM1.
[6]"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].
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"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 THR-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates."
Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.
Mol. Biol. Cell 21:3475-3486(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59262 Genomic DNA. Translation: CAA41954.1.
U00062 Genomic DNA. Translation: AAB68912.1.
BK006934 Genomic DNA. Translation: DAA06721.1.
PIRS43737.
RefSeqNP_011895.1. NM_001179160.1.

3D structure databases

ProteinModelPortalQ00772.
SMRQ00772. Positions 12-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36461. 620 interactions.
DIPDIP-1448N.
IntActQ00772. 39 interactions.
MINTMINT-395773.
STRING4932.YHR030C.

Proteomic databases

MaxQBQ00772.
PaxDbQ00772.
PeptideAtlasQ00772.
PRIDEQ00772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR030C; YHR030C; YHR030C.
GeneID856425.
KEGGsce:YHR030C.

Organism-specific databases

CYGDYHR030c.
SGDS000001072. SLT2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000112267.
HOGENOMHOG000233024.
KOK04464.
OMAFMPKKPF.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-31090-MONOMER.
BRENDA2.7.11.24. 984.

Gene expression databases

GenevestigatorQ00772.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982003.

Entry information

Entry nameSLT2_YEAST
AccessionPrimary (citable) accession number: Q00772
Secondary accession number(s): D3DKX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 144 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 VIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families