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P24583 (KPC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. 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:
Protein kinase C-like 1

Short name=PKC 1
EC=2.7.11.13
Gene names
Name:PKC1
Synonyms:HPO2, STT1
Ordered Locus Names:YBL105C
ORF Names:YBL0807
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cell growth and for the G2->M transition of the cell division cycle. Mediates a protein kinase cascade; it activates BCK1 which itself activates MKK1/MKK2.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Contains 2 REM (Hr1) repeats.

Ontologies

Keywords
   Biological processCell cycle
   DomainRepeat
Zinc-finger
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactin filament organization

Inferred from genetic interaction. Source: SGD

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic mRNA processing body assembly

Inferred from mutant phenotype. Source: SGD

fungal-type cell wall organization

Inferred from mutant phenotype. Source: SGD

intracellular protein kinase cascade

Inferred from mutant phenotype. Source: SGD

peroxisome degradation

Inferred from mutant phenotype. Source: SGD

regulation of nuclear-transcribed mRNA poly(A) tail shortening

Inferred from mutant phenotype. Source: SGD

   Cellular componentcytoplasm

Inferred from direct assay. Source: SGD

cytoskeleton

Inferred from direct assay. Source: SGD

nucleus

Inferred from direct assay. Source: SGD

plasma membrane enriched fraction

Inferred from direct assay. Source: SGD

site of polarized growth

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

protein kinase C activity

Inferred from direct assay. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ENO1P009242EBI-9860,EBI-6468

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11511151Protein kinase C-like 1
PRO_0000055738

Regions

Repeat5 – 7773REM 1
Repeat118 – 19376REM 2
Domain196 – 28893C2
Domain824 – 1083260Protein kinase
Domain1084 – 115168AGC-kinase C-terminal
Zinc finger414 – 46148Phorbol-ester/DAG-type 1
Zinc finger481 – 53151Phorbol-ester/DAG-type 2
Nucleotide binding830 – 8389ATP By similarity

Sites

Active site9491Proton acceptor By similarity
Binding site8531ATP By similarity

Amino acid modifications

Modified residue2261Phosphoserine Ref.6
Modified residue5771Phosphoserine Ref.5 Ref.6
Modified residue7511Phosphothreonine Ref.6
Modified residue7611Phosphoserine Ref.5 Ref.6
Modified residue9811Phosphothreonine Ref.6
Modified residue9831Phosphothreonine Ref.6
Modified residue11251Phosphothreonine Ref.6

Natural variations

Natural variant9581T → I in cly5; temperature-sensitive mutation that cause cell lysis at high temperature.
Natural variant10231P → S in cly7; temperature-sensitive mutation that cause cell lysis at high temperature.

Experimental info

Sequence conflict811C → F in CAA55990. Ref.2
Sequence conflict811C → F in CAA84932. Ref.3
Sequence conflict2441T → S in AAA34878. Ref.1
Sequence conflict6061G → E in AAA34878. Ref.1
Sequence conflict6211R → K in AAA34878. Ref.1
Sequence conflict6211R → K in CAA55990. Ref.2
Sequence conflict6211R → K in CAA84932. Ref.3
Sequence conflict6231S → P in AAA34878. Ref.1
Sequence conflict7891A → P in CAA55990. Ref.2
Sequence conflict7891A → P in CAA84932. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P24583 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8200EC2A2C6E649E

FASTA1,151131,477
        10         20         30         40         50         60 
MSFSQLEQNI KKKIAVEENI IRGASALKKK TSNVMVIQKC NTNIREARQN LEYLEDSLKK 

        70         80         90        100        110        120 
LRLKTAQQSQ GENGSEDNER CNSKEYGFLS TKSPNEHIFS RLDLVKYDCP SLAQRIQYML 

       130        140        150        160        170        180 
QQLEFKLQVE KQYQEANTKL TKLYQIDGDQ RSSSAAEGGA MESKYRIQML NKALKKYQAI 

       190        200        210        220        230        240 
NVDFDQFKHQ PNDIMDNQQP KFRRKQLTGV LTIGITAARD VDHIQSPMFA RKPESYVTIK 

       250        260        270        280        290        300 
IDDTIKARTK PSRNDRWSED FQIPVEKGNE IEITVYDKVN DSLIPVAIMW LLLSDIAEEI 

       310        320        330        340        350        360 
RKKKAGQTNE QQGWVNASNI NGGSSLASEE GSTLTSTYSN SAIQSTSAKN VQGENTSTSQ 

       370        380        390        400        410        420 
ISTNSWFVLE PSGQILLTLG FHKSSQIERK QLMGGLHRHG AIINRKEEIF EQHGHHFVQK 

       430        440        450        460        470        480 
SFYNIMCCAY CGDFLRYTGF QCQDCKFLCH KKCYTNVVTK CIAKTSTDTD PDEAKLNHRI 

       490        500        510        520        530        540 
PHRFLPTSNR GTKWCCHCGY ILPWGRHKVR KCSECGIMCH AQCAHLVPDF CGMSMEMANK 

       550        560        570        580        590        600 
ILKTIQDTKR NQEKKKRTVP SAQLGSSIGT ANGSDLSPSK LAERANAPLP PQPRKHDKTP 

       610        620        630        640        650        660 
SPQKVGRDSP TKQHDPIIDK RISLQTHGRE KLNKFIDENE AYLNFTEGAQ QTAEFSSPEK 

       670        680        690        700        710        720 
TLDPTSNRRS LGLTDLSIEH SQTWESKDDL MRDELELWKA QREEMELEIK QDSGEIQEDL 

       730        740        750        760        770        780 
EVDHIDLETK QKLDWENKND FREADLTIDS THTNPFRDMN SETFQIEQDH ASKEVLQETV 

       790        800        810        820        830        840 
SLAPTSTHAS RTTDQQSPQK SQTSTSAKHK KRAAKRRKVS LDNFVLLKVL GKGNFGKVIL 

       850        860        870        880        890        900 
SKSKNTDRLC AIKVLKKDNI IQNHDIESAR AEKKVFLLAT KTKHPFLTNL YCSFQTENRI 

       910        920        930        940        950        960 
YFAMEFIGGG DLMWHVQNQR LSVRRAKFYA AEVLLALKYF HDNGVIYRDL KLENILLTPE 

       970        980        990       1000       1010       1020 
GHIKIADYGL CKDEMWYGNR TSTFCGTPEF MAPEILKEQE YTKAVDWWAF GVLLYQMLLC 

      1030       1040       1050       1060       1070       1080 
QSPFSGDDED EVFNAILTDE PLYPIDMAGE IVQIFQGLLT KDPEKRLGAG PRDADEVMEE 

      1090       1100       1110       1120       1130       1140 
PFFRNINFDD ILNLRVKPPY IPEIKSPEDT SYFEQEFTSA PPTLTPLPSV LTTSQQEEFR 

      1150 
GFSFMPDDLD L 

« Hide

References

« Hide 'large scale' references
[1]"A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle."
Levin D.E., Fields F.O., Kunisawa R., Bishop J.M., Thorner J.
Cell 62:213-224(1990) [PubMed: 2196995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 204278 / EG123 / SM1058.
[2]"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 81; 621 AND 789.
Strain: ATCC 204508 / S288c.
[5]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577 AND SER-761, MASS SPECTROMETRY.
[6]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-577; THR-751; SER-761; THR-981; THR-983 AND THR-1125, MASS SPECTROMETRY.
[7]"Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define temperature-sensitive alleles of PKC1, the gene encoding yeast protein kinase C."
Baymiller J., McCullough J.E.
Yeast 13:305-312(1997) [PubMed: 9133734] [Abstract]
Cited for: VARIANTS CLY5 AND CLY7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32491 mRNA. Translation: AAA34878.1.
X79489 Genomic DNA. Translation: CAA55990.1.
Z35866 Genomic DNA. Translation: CAA84932.1.
BK006936 Genomic DNA. Translation: DAA07018.2.
PIRS45390.
RefSeqNP_009445.2. NM_001178345.2.

3D structure databases

ProteinModelPortalP24583.
SMRP24583. Positions 103-186, 207-279, 364-534, 818-1147.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1516N.
IntActP24583. 16 interactions.
MINTMINT-411118.
STRINGP24583.

Proteomic databases

PeptideAtlasP24583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID852169.
KEGGsce:YBL105C.
NMPDRfig|4932.3.peg.130.

Organism-specific databases

CYGDYBL105c.
SGDS000000201. PKC1.

Phylogenomic databases

eggNOGfuNOG05723.
GeneTreeEFGT00070000008712.
HOGENOMHBG396709.
OMAWCCHCGY.
OrthoDBEOG4CRQ75.

Enzyme and pathway databases

BRENDA2.7.11.13. 984.

Gene expression databases

ArrayExpressP24583.
GenevestigatorP24583.
GermOnlineYBL105C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
Gene3DG3DSA:1.10.287.160. HR1_rho-bd. 1 hit.
KOK02677.
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF02185. HR1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00742. Hr1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF46585. PKN_effector. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio970614.

Entry information

Entry nameKPC1_YEAST
AccessionPrimary (citable) accession number: P24583
Secondary accession number(s): D6VPP8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families