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Protein

Protein kinase C-like 1

Gene

PKC1

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

Functioni

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 activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei853 – 8531ATPPROSITE-ProRule annotation
Active sitei949 – 9491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri414 – 46148Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri481 – 53151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi830 – 8389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein kinase C activity Source: SGD

GO - Biological processi

  • actin filament organization Source: SGD
  • cellular bud neck septin ring organization Source: SGD
  • cytoplasmic mRNA processing body assembly Source: SGD
  • intracellular signal transduction Source: SGD
  • peptidyl-serine phosphorylation Source: GO_Central
  • pexophagy Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of fungal-type cell wall organization Source: SGD
  • regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • signal transduction Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-28989-MONOMER.
BRENDAi2.7.11.13. 984.
ReactomeiR-SCE-114508. Effects of PIP2 hydrolysis.
R-SCE-114516. Disinhibition of SNARE formation.
R-SCE-1169091. Activation of NF-kappaB in B cells.
R-SCE-1489509. DAG and IP3 signaling.
R-SCE-202424. Downstream TCR signaling.
R-SCE-2029485. Role of phospholipids in phagocytosis.
R-SCE-2179392. EGFR Transactivation by Gastrin.
R-SCE-2871837. FCERI mediated NF-kB activation.
R-SCE-399997. Acetylcholine regulates insulin secretion.
R-SCE-4419969. Depolymerisation of the Nuclear Lamina.
R-SCE-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5607764. CLEC7A (Dectin-1) signaling.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-76005. Response to elevated platelet cytosolic Ca2+.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C-like 1 (EC:2.7.11.13)
Short name:
PKC 1
Gene namesi
Name:PKC1
Synonyms:HPO2, STT1
Ordered Locus Names:YBL105C
ORF Names:YBL0807
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL105C.
SGDiS000000201. PKC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoskeleton Source: SGD
  • nucleus Source: SGD
  • site of polarized growth Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511151Protein kinase C-like 1PRO_0000055738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei761 – 7611PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24583.
PRIDEiP24583.

PTM databases

iPTMnetiP24583.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ENO1P009242EBI-9860,EBI-6468
TOP2P067862EBI-9860,EBI-19352

Protein-protein interaction databases

BioGridi32598. 323 interactions.
DIPiDIP-1516N.
IntActiP24583. 17 interactions.
MINTiMINT-411118.

Structurei

3D structure databases

ProteinModelPortaliP24583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati5 – 7773REM 1Add
BLAST
Repeati118 – 19376REM 2Add
BLAST
Domaini196 – 28893C2Add
BLAST
Domaini824 – 1083260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 115168AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 2 REM (Hr1) repeats.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri414 – 46148Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri481 – 53151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00820000126964.
HOGENOMiHOG000176156.
InParanoidiP24583.
KOiK02677.
OMAiEEVHEMY.
OrthoDBiEOG7R2BT5.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF02185. HR1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00742. Hr1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

P24583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFSQLEQNI KKKIAVEENI IRGASALKKK TSNVMVIQKC NTNIREARQN
60 70 80 90 100
LEYLEDSLKK LRLKTAQQSQ GENGSEDNER CNSKEYGFLS TKSPNEHIFS
110 120 130 140 150
RLDLVKYDCP SLAQRIQYML QQLEFKLQVE KQYQEANTKL TKLYQIDGDQ
160 170 180 190 200
RSSSAAEGGA MESKYRIQML NKALKKYQAI NVDFDQFKHQ PNDIMDNQQP
210 220 230 240 250
KFRRKQLTGV LTIGITAARD VDHIQSPMFA RKPESYVTIK IDDTIKARTK
260 270 280 290 300
PSRNDRWSED FQIPVEKGNE IEITVYDKVN DSLIPVAIMW LLLSDIAEEI
310 320 330 340 350
RKKKAGQTNE QQGWVNASNI NGGSSLASEE GSTLTSTYSN SAIQSTSAKN
360 370 380 390 400
VQGENTSTSQ ISTNSWFVLE PSGQILLTLG FHKSSQIERK QLMGGLHRHG
410 420 430 440 450
AIINRKEEIF EQHGHHFVQK SFYNIMCCAY CGDFLRYTGF QCQDCKFLCH
460 470 480 490 500
KKCYTNVVTK CIAKTSTDTD PDEAKLNHRI PHRFLPTSNR GTKWCCHCGY
510 520 530 540 550
ILPWGRHKVR KCSECGIMCH AQCAHLVPDF CGMSMEMANK ILKTIQDTKR
560 570 580 590 600
NQEKKKRTVP SAQLGSSIGT ANGSDLSPSK LAERANAPLP PQPRKHDKTP
610 620 630 640 650
SPQKVGRDSP TKQHDPIIDK RISLQTHGRE KLNKFIDENE AYLNFTEGAQ
660 670 680 690 700
QTAEFSSPEK TLDPTSNRRS LGLTDLSIEH SQTWESKDDL MRDELELWKA
710 720 730 740 750
QREEMELEIK QDSGEIQEDL EVDHIDLETK QKLDWENKND FREADLTIDS
760 770 780 790 800
THTNPFRDMN SETFQIEQDH ASKEVLQETV SLAPTSTHAS RTTDQQSPQK
810 820 830 840 850
SQTSTSAKHK KRAAKRRKVS LDNFVLLKVL GKGNFGKVIL SKSKNTDRLC
860 870 880 890 900
AIKVLKKDNI IQNHDIESAR AEKKVFLLAT KTKHPFLTNL YCSFQTENRI
910 920 930 940 950
YFAMEFIGGG DLMWHVQNQR LSVRRAKFYA AEVLLALKYF HDNGVIYRDL
960 970 980 990 1000
KLENILLTPE GHIKIADYGL CKDEMWYGNR TSTFCGTPEF MAPEILKEQE
1010 1020 1030 1040 1050
YTKAVDWWAF GVLLYQMLLC QSPFSGDDED EVFNAILTDE PLYPIDMAGE
1060 1070 1080 1090 1100
IVQIFQGLLT KDPEKRLGAG PRDADEVMEE PFFRNINFDD ILNLRVKPPY
1110 1120 1130 1140 1150
IPEIKSPEDT SYFEQEFTSA PPTLTPLPSV LTTSQQEEFR GFSFMPDDLD

L
Length:1,151
Mass (Da):131,477
Last modified:July 27, 2011 - v3
Checksum:i8200EC2A2C6E649E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811C → F in CAA55990 (PubMed:7502586).Curated
Sequence conflicti81 – 811C → F in CAA84932 (PubMed:7813418).Curated
Sequence conflicti244 – 2441T → S in AAA34878 (PubMed:2196995).Curated
Sequence conflicti606 – 6061G → E in AAA34878 (PubMed:2196995).Curated
Sequence conflicti621 – 6211R → K in AAA34878 (PubMed:2196995).Curated
Sequence conflicti621 – 6211R → K in CAA55990 (PubMed:7502586).Curated
Sequence conflicti621 – 6211R → K in CAA84932 (PubMed:7813418).Curated
Sequence conflicti623 – 6231S → P in AAA34878 (PubMed:2196995).Curated
Sequence conflicti789 – 7891A → P in CAA55990 (PubMed:7502586).Curated
Sequence conflicti789 – 7891A → P in CAA84932 (PubMed:7813418).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti958 – 9581T → I in cly5; temperature-sensitive mutation that cause cell lysis at high temperature.
Natural varianti1023 – 10231P → S in cly7; temperature-sensitive mutation that cause cell lysis at high temperature.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32491 mRNA. Translation: AAA34878.1.
X79489 Genomic DNA. Translation: CAA55990.1.
Z35866 Genomic DNA. Translation: CAA84932.1.
BK006936 Genomic DNA. Translation: DAA07018.2.
PIRiS45390.
RefSeqiNP_009445.2. NM_001178345.2.

Genome annotation databases

EnsemblFungiiYBL105C; YBL105C; YBL105C.
GeneIDi852169.
KEGGisce:YBL105C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32491 mRNA. Translation: AAA34878.1.
X79489 Genomic DNA. Translation: CAA55990.1.
Z35866 Genomic DNA. Translation: CAA84932.1.
BK006936 Genomic DNA. Translation: DAA07018.2.
PIRiS45390.
RefSeqiNP_009445.2. NM_001178345.2.

3D structure databases

ProteinModelPortaliP24583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32598. 323 interactions.
DIPiDIP-1516N.
IntActiP24583. 17 interactions.
MINTiMINT-411118.

PTM databases

iPTMnetiP24583.

Proteomic databases

MaxQBiP24583.
PRIDEiP24583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL105C; YBL105C; YBL105C.
GeneIDi852169.
KEGGisce:YBL105C.

Organism-specific databases

EuPathDBiFungiDB:YBL105C.
SGDiS000000201. PKC1.

Phylogenomic databases

GeneTreeiENSGT00820000126964.
HOGENOMiHOG000176156.
InParanoidiP24583.
KOiK02677.
OMAiEEVHEMY.
OrthoDBiEOG7R2BT5.

Enzyme and pathway databases

BioCyciYEAST:G3O-28989-MONOMER.
BRENDAi2.7.11.13. 984.
ReactomeiR-SCE-114508. Effects of PIP2 hydrolysis.
R-SCE-114516. Disinhibition of SNARE formation.
R-SCE-1169091. Activation of NF-kappaB in B cells.
R-SCE-1489509. DAG and IP3 signaling.
R-SCE-202424. Downstream TCR signaling.
R-SCE-2029485. Role of phospholipids in phagocytosis.
R-SCE-2179392. EGFR Transactivation by Gastrin.
R-SCE-2871837. FCERI mediated NF-kB activation.
R-SCE-399997. Acetylcholine regulates insulin secretion.
R-SCE-4419969. Depolymerisation of the Nuclear Lamina.
R-SCE-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5607764. CLEC7A (Dectin-1) signaling.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-76005. Response to elevated platelet cytosolic Ca2+.

Miscellaneous databases

PROiP24583.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF02185. HR1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00742. Hr1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 81; 621 AND 789.
    Strain: ATCC 204508 / S288c.
  5. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: VARIANTS CLY5 AND CLY7.

Entry informationi

Entry nameiKPC1_YEAST
AccessioniPrimary (citable) accession number: P24583
Secondary accession number(s): D6VPP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 169 of the entry and version 3 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.