ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P24583


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KPC1_YEAST
Primary accession number P24583
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on October 1, 1994 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 90)
Name and origin of the protein
Protein name Protein kinase C-like 1
Synonyms PKC 1
EC 2.7.11.13
Gene name
Name: PKC1
Synonyms: HPO2, STT1
OrderedLocusNames: YBL105C
ORFNames: YBL0807
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 204278 / EG123 / SM1058;
DOI=10.1016/0092-8674(90)90360-Q; PubMed=2196995 [NCBI, ExPASy, EBI, Israel, Japan]
Levin D.E., Fields F.O., Kunisawa R., Bishop J.M., Thorner J.;
"A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle.";
Cell 62:213-224(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320111112; PubMed=7502586 [NCBI, ExPASy, EBI, Israel, Japan]
Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II.";
Yeast 11:1103-1112(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577 AND SER-761, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-577; THR-751; SER-761; THR-981; THR-983 AND THR-1125, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[6]
VARIANTS CLY5 AND CLY7.
DOI=10.1002/(SICI)1097-0061(19970330)13:4<305::AID-YEA91>3.3.CO;2-6; PubMed=9133734 [NCBI, ExPASy, EBI, Israel, Japan]
Baymiller J., McCullough J.E.;
"Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define temperature-sensitive alleles of PKC1, the gene encoding yeast protein kinase C.";
Yeast 13:305-312(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M32491; AAA34878.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X79489; CAA55990.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35866; CAA84932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45390; S45390.
RefSeq NP_009445.1; -.
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
ModBase P24583.
Protein-protein interaction databases
DIP DIP:1516N; -.
IntAct P24583; -.
Organism-specific databases
CYGD YBL105c; -.
SGD S000000201; PKC1.
Yeast-GFP YBL105C.
Gene expression databases
ArrayExpress P24583; -.
GermOnline YBL105C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0030427; Cellular component: site of polarized growth (inferred from direct assay from SGD).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019992; Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004697; Molecular function: protein kinase C activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007015; Biological process: actin filament organization (inferred from genetic interaction from SGD).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0007047; Biological process: cell wall organization (inferred from mutant phenotype from SGD).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007243; Biological process: protein kinase cascade (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR002219; DAG_PE_bd.
IPR000861; HR1-like_rho-bd.
IPR011072; HR1_rho-bd.
IPR015745; PKC.
IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22985:SF86; PKC; 1.
Pfam PF00130; C1_1; 2.
PF00168; C2; 1.
PF02185; HR1; 2.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00008; DAGPEDOMAIN.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00109; C1; 2.
SM00239; C2; 1.
SM00742; Hr1; 2.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; FALSE_NEG.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P24583.
ProtoNet P24583.
Proteomic databases
PeptideAtlas P24583; -.
Genome annotation databases
Ensembl YBL105C; Saccharomyces cerevisiae. [Contig view]
GeneID 852169; -.
GenomeReviews Y13134_GR; YBL105C.
KEGG sce:YBL105C; -.
NMPDR fig|4932.3.peg.130; -.
Phylogenomic databases
HOGENOM P24583; -.
Other
LinkHub P24583; -.
NextBio 970614; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Calcium; Cell cycle; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1151  1151     Protein kinase C-like 1. PRO_0000055738
REPEAT   5     77  73     REM 1. 
REPEAT   118    193  76     REM 2. 
DOMAIN   196    288  93     C2. 
DOMAIN   824   1083  260     Protein kinase. 
DOMAIN   1084   1151  68     AGC-kinase C-terminal. 
ZN_FING   414    461  48     Phorbol-ester/DAG-type 1. 
ZN_FING   481    531  51     Phorbol-ester/DAG-type 2. 
NP_BIND   830    838  9     ATP (By similarity). 
ACT_SITE   949    949        Proton acceptor (By similarity). 
BINDING   853    853        ATP (By similarity). 
MOD_RES   226    226        Phosphoserine. 
MOD_RES   577    577        Phosphoserine. 
MOD_RES   751    751        Phosphothreonine. 
MOD_RES   761    761        Phosphoserine. 
MOD_RES   981    981        Phosphothreonine. 
MOD_RES   983    983        Phosphothreonine. 
MOD_RES   1125   1125        Phosphothreonine. 
VARIANT   958    958  1     T -> I (in cly5; temperature-sensitive mutation that cause cell lysis at high temperature). 
VARIANT   1023   1023  1     P -> S (in cly7; temperature-sensitive mutation that cause cell lysis at high temperature). 
CONFLICT   81     81        F -> C (in Ref. 1; AAA34878). 
CONFLICT   244    244        T -> S (in Ref. 1; AAA34878). 
CONFLICT   606    606        G -> E (in Ref. 1; AAA34878). 
CONFLICT   623    623        S -> P (in Ref. 1; AAA34878). 
CONFLICT   789    789        P -> A (in Ref. 1; AAA34878). 
Sequence information
Length: 1151 AA [This is the length of the unprocessed precursor] Molecular weight: 131519 Da [This is the MW of the unprocessed precursor] CRC64: 3300E8D523C8587C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSFSQLEQNI KKKIAVEENI IRGASALKKK TSNVMVIQKC NTNIREARQN LEYLEDSLKK 

        70         80         90        100        110        120 
LRLKTAQQSQ GENGSEDNER FNSKEYGFLS 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 KISLQTHGRE 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 
SLAPTSTHPS 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 

P24583 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!