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P36583 (PCK2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein kinase C-like 2

EC=2.7.11.13
Gene names
Name:pck2
Synonyms:pkc1, sts6
ORF Names:SPBC12D12.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1016 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the control of the cell shape. Target of the inhibitor staurosporine.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with rho2. Ref.5

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

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

Contains 1 protein kinase domain.

Contains 2 REM (Hr1) repeats.

Ontologies

Keywords
   Biological processCell shape
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processactivation of bipolar cell growth

Inferred from mutant phenotype. Source: GeneDB_Spombe

intracellular signal transduction

Inferred by curator. Source: GeneDB_Spombe

positive regulation of calcium-mediated signaling

Inferred from mutant phenotype. Source: GeneDB_Spombe

regulation of alpha-glucan biosynthetic process

Inferred from mutant phenotype. Source: GeneDB_Spombe

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell wall (1->3)-beta-D-glucan biosynthetic process

Inferred from mutant phenotype. Source: GeneDB_Spombe

regulation of establishment or maintenance of cell polarity

Inferred from mutant phenotype. Source: GeneDB_Spombe

   Cellular componentcell division site

Inferred from direct assay. Source: GeneDB_Spombe

cell septum

Inferred from direct assay. Source: GeneDB_Spombe

cell tip

Inferred from direct assay. Source: GeneDB_Spombe

intracellular

Inferred by curator. Source: GOC

   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: GeneDB_Spombe

protein kinase C activity

Traceable author statement. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10161016Protein kinase C-like 2
PRO_0000055741

Regions

Repeat6 – 7974REM 1
Repeat123 – 19876REM 2
Domain683 – 942260Protein kinase
Domain943 – 101371AGC-kinase C-terminal
Zinc finger405 – 45349Phorbol-ester/DAG-type 1
Zinc finger473 – 52351Phorbol-ester/DAG-type 2
Nucleotide binding689 – 6979ATP By similarity
Compositional bias554 – 5607Poly-His

Sites

Active site8081Proton acceptor By similarity
Binding site7121ATP By similarity

Amino acid modifications

Modified residue9841Phosphothreonine Ref.6

Experimental info

Sequence conflict1521E → V in BAA03268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36583 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 060CDC4F718A0069

FASTA1,016116,005
        10         20         30         40         50         60 
MDMIDEAITE VVRKIERERS VIHGALSMKR LTQNQTVHQQ LHSNIEESKK SIIYLEERLE 

        70         80         90        100        110        120 
KLKLRKNGVR KSNSEKPSVG IEKNPSFSTT KSAKSFSSTS SNIDSNLDLL NYDTPLTISK 

       130        140        150        160        170        180 
ISFLLQQLEF KLSVEEQYRK GIEKMAKLYE REHDRRSIAE AEKKYVESAQ KITLLKQALK 

       190        200        210        220        230        240 
RYHDLHIEID EEDVPSTESR GNLNARRPQS GLLKITVGSL RNVTHSAGIS KQTEMIVAIR 

       250        260        270        280        290        300 
AEDLERARTR PSRTDRFNET FEIDLEKTNE VEIVVYEKKN EKLLLPVGLL WIRLSDLVEK 

       310        320        330        340        350        360 
QRRKKVEQEV SDKGWVSADK MINQRLSIFL PSALNNISKP ESTDRPNTAS GNQSVSAWFS 

       370        380        390        400        410        420 
LEPMGQINLT MNFTKHNTRK RPMDAGLGRQ GAIRQRKESV HEVYGHKFLQ HQFYQIMRCA 

       430        440        450        460        470        480 
LCGEFLKNAA GMQCIDCHYT CHKKCYPKVV TKCISKSSDS ASSEYEKINH RIPHHFESHT 

       490        500        510        520        530        540 
NIGANWCCHC GYILPLGRKT ARKCTECGIT AHAQCVHLVP DFCGMSMEMA NRVISEIRTT 

       550        560        570        580        590        600 
KIYKAQQHKQ KSSHHKHHHH KKSKSSSSKH KENDKASVSI TTTTTPSITP ADPVPTSPKP 

       610        620        630        640        650        660 
LAIEPVKRKP VHAGNLEVTS VSDNKLGATV QVVEQKVDDK ADALTKPPSL DAVKEPIPVP 

       670        680        690        700        710        720 
SVETSVVAQD LTHKAKRIGL EDFTFLSVLG KGNFGKVMLA ELKSEKQLYA IKVLKKEFIL 

       730        740        750        760        770        780 
ENDEVESTKS EKRVFLVANR ERHPFLVNLH SCFQTETRIY FVMDFVSGGD LMLHIQQEQF 

       790        800        810        820        830        840 
SRRRAQFYAA EVCLALKYFH DNGIIYRDLK LDNILLSPDG HVKVADYGLC KEDMWHDNTT 

       850        860        870        880        890        900 
ATFCGTPEFM APEILLEQQY TRSVDWWAFG VLIYQMLLGQ SPFRGEDEEE IFDAILSDEP 

       910        920        930        940        950        960 
LYPIHMPRDS VSILQQLLTR DPKKRLGSGP NDAEDVMTHP FFSNINWDDI YHKRTQPPYI 

       970        980        990       1000       1010 
PSLNSPTDTK YFDEEFTREL PVLTPVNSIL TKEMQQHFEG FSYSCEDDKP STTDNA 

« Hide

References

« Hide 'large scale' references
[1]"Two novel protein kinase C-related genes of fission yeast are essential for cell viability and implicated in cell shape control."
Toda T., Shimanuki M., Yanagida M.
EMBO J. 12:1987-1995(1993) [PubMed: 8491190] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A Ca(2+)-independent protein kinase C from fission yeast."
Mazzei G.J., Schmid E.M., Knowles J.K., Payton M.A., Maundrell K.G.
J. Biol. Chem. 268:7401-7406(1993) [PubMed: 8463273] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[4]"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
Genes Cells 5:169-190(2000) [PubMed: 10759889] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 755-928.
Strain: ATCC 38364 / 968.
[5]"Schizosaccharomyces pombe rho2p GTPase regulates cell wall alpha-glucan biosynthesis through the protein kinase pck2p."
Calonge T.M., Nakano K., Arellano M., Arai R., Katayama S., Toda T., Mabuchi I., Perez P.
Mol. Biol. Cell 11:4393-4401(2000) [PubMed: 11102532] [Abstract]
Cited for: INTERACTION WITH RHO2.
[6]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-984, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14338 Genomic DNA. Translation: BAA03268.1.
L07637 Genomic DNA. Translation: AAA35323.1.
CU329671 Genomic DNA. Translation: CAA22678.1.
AB027824 Genomic DNA. Translation: BAA87128.1.
PIRA46079.
RefSeqNP_595950.1. NM_001021859.1.

3D structure databases

ProteinModelPortalP36583.
SMRP36583. Positions 680-1007.
ModBaseSearch...

Protein-protein interaction databases

STRINGP36583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC12D12.04c.1; SPBC12D12.04c.1:pep; SPBC12D12.04c.
GeneID2539649.
GenomeReviewsGene locus pck2 in contig CU329671_GR.
KEGGspo:SPBC12D12.04c.
NMPDRfig|4896.1.peg.1816.

Organism-specific databases

GeneDB_SpombeSPBC12D12.04c.

Phylogenomic databases

eggNOGfuNOG05723.
GeneTreeEFGT00070000008712.
HOGENOMHBG396709.
OMAWCCHCGY.
OrthoDBEOG4CRQ75.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004014-MONOMER.
BRENDA2.7.11.13. 5615.

Gene expression databases

ArrayExpressP36583.

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.
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.
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...

Entry information

Entry namePCK2_SCHPO
AccessionPrimary (citable) accession number: P36583
Secondary accession number(s): Q9UU42
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families