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Protein

Protein kinase C-like 2

Gene

pck2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei712 – 7121ATPPROSITE-ProRule annotation
Active sitei808 – 8081Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri405 – 45349Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri473 – 52351Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi689 – 6979ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • fungal-type cell wall biogenesis Source: PomBase
  • intracellular signal transduction Source: PomBase
  • negative regulation of peptidyl-tyrosine phosphorylation Source: PomBase
  • protein phosphorylation Source: PomBase
  • regulation of alpha-glucan biosynthetic process Source: PomBase
  • regulation of cell wall (1->3)-beta-D-glucan biosynthetic process Source: PomBase
  • regulation of establishment or maintenance of cell polarity regulating cell shape Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell shape

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.11.13. 5613.
ReactomeiR-SPO-114508. Effects of PIP2 hydrolysis.
R-SPO-114516. Disinhibition of SNARE formation.
R-SPO-114604. GPVI-mediated activation cascade.
R-SPO-1169091. Activation of NF-kappaB in B cells.
R-SPO-1257604. PIP3 activates AKT signaling.
R-SPO-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-SPO-1489509. DAG and IP3 signaling.
R-SPO-165158. Activation of AKT2.
R-SPO-198693. AKT phosphorylates targets in the nucleus.
R-SPO-199418. Negative regulation of the PI3K/AKT network.
R-SPO-202424. Downstream TCR signaling.
R-SPO-2029485. Role of phospholipids in phagocytosis.
R-SPO-2179392. EGFR Transactivation by Gastrin.
R-SPO-2871837. FCERI mediated NF-kB activation.
R-SPO-389357. CD28 dependent PI3K/Akt signaling.
R-SPO-389513. CTLA4 inhibitory signaling.
R-SPO-392451. G beta:gamma signalling through PI3Kgamma.
R-SPO-399997. Acetylcholine regulates insulin secretion.
R-SPO-4419969. Depolymerisation of the Nuclear Lamina.
R-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-SPO-5218920. VEGFR2 mediated vascular permeability.
R-SPO-5218921. VEGFR2 mediated cell proliferation.
R-SPO-5607764. CLEC7A (Dectin-1) signaling.
R-SPO-5625740. RHO GTPases activate PKNs.
R-SPO-6804758. Regulation of TP53 Activity through Acetylation.
R-SPO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-SPO-76005. Response to elevated platelet cytosolic Ca2+.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C-like 2 (EC:2.7.11.13)
Gene namesi
Name:pck2
Synonyms:pkc1, sts6
ORF Names:SPBC12D12.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12D12.04c.
PomBaseiSPBC12D12.04c. pck2.

Subcellular locationi

GO - Cellular componenti

  • barrier septum Source: PomBase
  • cell division site Source: PomBase
  • cell tip Source: PomBase
  • intracellular Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10161016Protein kinase C-like 2PRO_0000055741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei984 – 9841Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36583.

PTM databases

iPTMnetiP36583.

Interactioni

Subunit structurei

Interacts with rho2.1 Publication

Protein-protein interaction databases

BioGridi276204. 27 interactions.
MINTiMINT-4688713.

Structurei

3D structure databases

ProteinModelPortaliP36583.
SMRiP36583. Positions 680-1007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati6 – 7974REM 1Add
BLAST
Repeati123 – 19876REM 2Add
BLAST
Domaini683 – 942260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini943 – 101371AGC-kinase C-terminalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi554 – 5607Poly-His

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal 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 fingeri405 – 45349Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri473 – 52351Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000176156.
InParanoidiP36583.
KOiK18050.
OMAiEEVHEMY.
OrthoDBiEOG7R2BT5.
PhylomeDBiP36583.

Family and domain databases

Gene3Di1.10.287.160. 1 hit.
2.60.40.150. 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.
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.

P36583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMIDEAITE VVRKIERERS VIHGALSMKR LTQNQTVHQQ LHSNIEESKK
60 70 80 90 100
SIIYLEERLE KLKLRKNGVR KSNSEKPSVG IEKNPSFSTT KSAKSFSSTS
110 120 130 140 150
SNIDSNLDLL NYDTPLTISK ISFLLQQLEF KLSVEEQYRK GIEKMAKLYE
160 170 180 190 200
REHDRRSIAE AEKKYVESAQ KITLLKQALK RYHDLHIEID EEDVPSTESR
210 220 230 240 250
GNLNARRPQS GLLKITVGSL RNVTHSAGIS KQTEMIVAIR AEDLERARTR
260 270 280 290 300
PSRTDRFNET FEIDLEKTNE VEIVVYEKKN EKLLLPVGLL WIRLSDLVEK
310 320 330 340 350
QRRKKVEQEV SDKGWVSADK MINQRLSIFL PSALNNISKP ESTDRPNTAS
360 370 380 390 400
GNQSVSAWFS LEPMGQINLT MNFTKHNTRK RPMDAGLGRQ GAIRQRKESV
410 420 430 440 450
HEVYGHKFLQ HQFYQIMRCA LCGEFLKNAA GMQCIDCHYT CHKKCYPKVV
460 470 480 490 500
TKCISKSSDS ASSEYEKINH RIPHHFESHT NIGANWCCHC GYILPLGRKT
510 520 530 540 550
ARKCTECGIT AHAQCVHLVP DFCGMSMEMA NRVISEIRTT KIYKAQQHKQ
560 570 580 590 600
KSSHHKHHHH KKSKSSSSKH KENDKASVSI TTTTTPSITP ADPVPTSPKP
610 620 630 640 650
LAIEPVKRKP VHAGNLEVTS VSDNKLGATV QVVEQKVDDK ADALTKPPSL
660 670 680 690 700
DAVKEPIPVP SVETSVVAQD LTHKAKRIGL EDFTFLSVLG KGNFGKVMLA
710 720 730 740 750
ELKSEKQLYA IKVLKKEFIL ENDEVESTKS EKRVFLVANR ERHPFLVNLH
760 770 780 790 800
SCFQTETRIY FVMDFVSGGD LMLHIQQEQF SRRRAQFYAA EVCLALKYFH
810 820 830 840 850
DNGIIYRDLK LDNILLSPDG HVKVADYGLC KEDMWHDNTT ATFCGTPEFM
860 870 880 890 900
APEILLEQQY TRSVDWWAFG VLIYQMLLGQ SPFRGEDEEE IFDAILSDEP
910 920 930 940 950
LYPIHMPRDS VSILQQLLTR DPKKRLGSGP NDAEDVMTHP FFSNINWDDI
960 970 980 990 1000
YHKRTQPPYI PSLNSPTDTK YFDEEFTREL PVLTPVNSIL TKEMQQHFEG
1010
FSYSCEDDKP STTDNA
Length:1,016
Mass (Da):116,005
Last modified:May 30, 2000 - v2
Checksum:i060CDC4F718A0069
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521E → V in BAA03268 (PubMed:8491190).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14338 Genomic DNA. Translation: BAA03268.1.
L07637 Genomic DNA. Translation: AAA35323.1.
CU329671 Genomic DNA. Translation: CAA22678.1.
AB027824 Genomic DNA. Translation: BAA87128.1.
PIRiA46079.
RefSeqiNP_595950.1. NM_001021859.2.

Genome annotation databases

EnsemblFungiiSPBC12D12.04c.1; SPBC12D12.04c.1:pep; SPBC12D12.04c.
GeneIDi2539649.
KEGGispo:SPBC12D12.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14338 Genomic DNA. Translation: BAA03268.1.
L07637 Genomic DNA. Translation: AAA35323.1.
CU329671 Genomic DNA. Translation: CAA22678.1.
AB027824 Genomic DNA. Translation: BAA87128.1.
PIRiA46079.
RefSeqiNP_595950.1. NM_001021859.2.

3D structure databases

ProteinModelPortaliP36583.
SMRiP36583. Positions 680-1007.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276204. 27 interactions.
MINTiMINT-4688713.

PTM databases

iPTMnetiP36583.

Proteomic databases

MaxQBiP36583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC12D12.04c.1; SPBC12D12.04c.1:pep; SPBC12D12.04c.
GeneIDi2539649.
KEGGispo:SPBC12D12.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC12D12.04c.
PomBaseiSPBC12D12.04c. pck2.

Phylogenomic databases

HOGENOMiHOG000176156.
InParanoidiP36583.
KOiK18050.
OMAiEEVHEMY.
OrthoDBiEOG7R2BT5.
PhylomeDBiP36583.

Enzyme and pathway databases

BRENDAi2.7.11.13. 5613.
ReactomeiR-SPO-114508. Effects of PIP2 hydrolysis.
R-SPO-114516. Disinhibition of SNARE formation.
R-SPO-114604. GPVI-mediated activation cascade.
R-SPO-1169091. Activation of NF-kappaB in B cells.
R-SPO-1257604. PIP3 activates AKT signaling.
R-SPO-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-SPO-1489509. DAG and IP3 signaling.
R-SPO-165158. Activation of AKT2.
R-SPO-198693. AKT phosphorylates targets in the nucleus.
R-SPO-199418. Negative regulation of the PI3K/AKT network.
R-SPO-202424. Downstream TCR signaling.
R-SPO-2029485. Role of phospholipids in phagocytosis.
R-SPO-2179392. EGFR Transactivation by Gastrin.
R-SPO-2871837. FCERI mediated NF-kB activation.
R-SPO-389357. CD28 dependent PI3K/Akt signaling.
R-SPO-389513. CTLA4 inhibitory signaling.
R-SPO-392451. G beta:gamma signalling through PI3Kgamma.
R-SPO-399997. Acetylcholine regulates insulin secretion.
R-SPO-4419969. Depolymerisation of the Nuclear Lamina.
R-SPO-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-SPO-5218920. VEGFR2 mediated vascular permeability.
R-SPO-5218921. VEGFR2 mediated cell proliferation.
R-SPO-5607764. CLEC7A (Dectin-1) signaling.
R-SPO-5625740. RHO GTPases activate PKNs.
R-SPO-6804758. Regulation of TP53 Activity through Acetylation.
R-SPO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-SPO-76005. Response to elevated platelet cytosolic Ca2+.

Miscellaneous databases

PROiP36583.

Family and domain databases

Gene3Di1.10.287.160. 1 hit.
2.60.40.150. 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.
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. "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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHO2.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-984, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPCK2_SCHPO
AccessioniPrimary (citable) accession number: P36583
Secondary accession number(s): Q9UU42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 30, 2000
Last modified: June 8, 2016
This is version 158 of the entry and version 2 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.