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Protein

Serine/threonine-protein kinase PRR2

Gene

PRR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase that functions as regulator in the pheromone-induced mating pathway downstream of mitogen-activated protein kinase (MAPK) FUS3. Diminishes transcriptional induction of genes in response to pheromone signaling.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei390 – 3901ATPPROSITE-ProRule annotation
Active sitei484 – 4841Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi367 – 3759ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • negative regulation of conjugation with cellular fusion Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter by pheromones Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Pheromone response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29596-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PRR2 (EC:2.7.11.1)
Alternative name(s):
Pheromone response regulator 2
Gene namesi
Name:PRR2
Ordered Locus Names:YDL214C
ORF Names:D1014
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL214C.
SGDiS000002373. PRR2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi390 – 3901K → R: Abolishes kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Serine/threonine-protein kinase PRR2PRO_0000262752Add
BLAST

PTM databases

iPTMnetiQ12310.

Expressioni

Inductioni

By the macrolide rapamycin in a TOR-dependent manner.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi31831. 66 interactions.
DIPiDIP-1640N.
IntActiQ12310. 5 interactions.
MINTiMINT-387579.

Structurei

3D structure databases

ProteinModelPortaliQ12310.
SMRiQ12310. Positions 351-652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 653293Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000075309.
HOGENOMiHOG000093332.
InParanoidiQ12310.
OrthoDBiEOG7008J9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSRILRYN QRNNKTTASL TAEHAYSDNW AYSVSLGDPT SVGVNMAAKT
60 70 80 90 100
GEALNKSYDS VFSSLPVADS VPRTDFTASS RDDENTDVQK LTTSWMEKID
110 120 130 140 150
TKMPENISKI DSNIISSPMV SKVEARFIVP KGRLRKNSTD FTSSFSNSLS
160 170 180 190 200
LPKSYGKLIF FTSKKNSSST KKNLANDISD NKHNNNSSNT IGHNIPVTTA
210 220 230 240 250
TATCDEIACT STEHEYNVYE EERMFTTRVY SLEDSVSSLS TNPLDDTYSE
260 270 280 290 300
AVQVNTRHIE DTESTAHIRK HSYTTSLSSI KRLFKITSFS NNNSNSCDHQ
310 320 330 340 350
ESTVADDCAI SSSLKETTSS PVSTGSFSLM IENEDSDRDQ IIQALYSNIE
360 370 380 390 400
ASTDLVSRKY RDLDVVLGEG SGGKVKLVQR VLDNKVFALK EYRSKKKRES
410 420 430 440 450
ERKYIKNIIS EYCIASTLKN PNICETLEIL YEKGKIFQIL EYCEYDLFSL
460 470 480 490 500
VMSEKMHYEE ICCLFKQLIN GVKYLHDIGL SHRDLKLDNC VVTRRGILKL
510 520 530 540 550
IDFGASSVFH YPLSSQMIEA NGIVGSDPYL SPEVFYFNEY DPRALDVWSV
560 570 580 590 600
GIIFFCMITR RFPWKYPKVK DVQFKAFCSG RGVSSFKDLV TRPATDDSNN
610 620 630 640 650
YDNDGYEEGV IDMGPNFILH RLPEETHKIM RRILEVSPFR RITINGILQD
660 670 680 690
GWIKEIETCQ VVGAASPNEA SLRIINKGNH IHTNIDQRYA HIGGLHQRT
Length:699
Mass (Da):78,939
Last modified:November 1, 1996 - v1
Checksum:iBB178BCE735D6086
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99000 Genomic DNA. Translation: CAA67476.1.
Z74262 Genomic DNA. Translation: CAA98792.1.
BK006938 Genomic DNA. Translation: DAA11650.1.
PIRiS67773.
RefSeqiNP_010067.1. NM_001180274.1.

Genome annotation databases

EnsemblFungiiYDL214C; YDL214C; YDL214C.
GeneIDi851312.
KEGGisce:YDL214C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99000 Genomic DNA. Translation: CAA67476.1.
Z74262 Genomic DNA. Translation: CAA98792.1.
BK006938 Genomic DNA. Translation: DAA11650.1.
PIRiS67773.
RefSeqiNP_010067.1. NM_001180274.1.

3D structure databases

ProteinModelPortaliQ12310.
SMRiQ12310. Positions 351-652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31831. 66 interactions.
DIPiDIP-1640N.
IntActiQ12310. 5 interactions.
MINTiMINT-387579.

PTM databases

iPTMnetiQ12310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL214C; YDL214C; YDL214C.
GeneIDi851312.
KEGGisce:YDL214C.

Organism-specific databases

EuPathDBiFungiDB:YDL214C.
SGDiS000002373. PRR2.

Phylogenomic databases

GeneTreeiENSGT00550000075309.
HOGENOMiHOG000093332.
InParanoidiQ12310.
OrthoDBiEOG7008J9.

Enzyme and pathway databases

BioCyciYEAST:G3O-29596-MONOMER.

Miscellaneous databases

PROiQ12310.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new open reading frames, nine known genes and one gene for Gly-tRNA."
    Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U., Schmidt E.R.
    Yeast 13:163-169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases."
    Bertram P.G., Choi J.H., Carvalho J., Ai W., Zeng C., Chan T.-F., Zheng X.F.S.
    J. Biol. Chem. 275:35727-35733(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: CATALYTIC ACTIVITY.
  6. "Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast."
    Burchett S.A., Scott A., Errede B., Dohlman H.G.
    J. Biol. Chem. 276:26472-26478(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-390.
  7. Cited for: CATALYTIC ACTIVITY.

Entry informationi

Entry nameiPRR2_YEAST
AccessioniPrimary (citable) accession number: Q12310
Secondary accession number(s): D6VRE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 117 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.