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Protein

Protein kinase C-like 1

Gene

pck1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 sitei693 – 6931ATPPROSITE-ProRule annotation
Active sitei789 – 7891Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri413 – 46149Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 53051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi670 – 6789ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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 1 (EC:2.7.11.13)
Gene namesi
Name:pck1
ORF Names:SPAC17G8.14c, SPAC22H10.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.14c.
PomBaseiSPAC17G8.14c. pck1.

Subcellular locationi

GO - Cellular componenti

  • cell division site Source: PomBase
  • cell septum Source: UniProtKB-SubCell
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 988988Protein kinase C-like 1PRO_0000055740Add
BLAST

Proteomic databases

MaxQBiP36582.

Interactioni

Protein-protein interaction databases

BioGridi278761. 104 interactions.
MINTiMINT-4688688.

Structurei

3D structure databases

ProteinModelPortaliP36582.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati6 – 7873REM 1Add
BLAST
Repeati119 – 19274REM 2Add
BLAST
Domaini664 – 923260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini924 – 98865AGC-kinase C-terminalAdd
BLAST

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 fingeri413 – 46149Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 53051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000176156.
InParanoidiP36582.
KOiK02677.
OrthoDBiEOG092C0HH3.
PhylomeDBiP36582.

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.
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.

P36582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQLDDALQD AYKKVEREES LILGAKAMVA STKNPEVKRR LESNIAVSEN
60 70 80 90 100
NIKYLRERID ALKVESGSER ESQSDKDSSK KYSDSAKSTN SDDHLLSYNR
110 120 130 140 150
SAFDLFNSEK PLSPEKISTM LQHLQMRLSI EQQCVSGIEK IMSLYSKEQK
160 170 180 190 200
DKTDVIIKLK EGKQKVNLLK RSLKRYNELH IPFDISTPSS EEKQQASGLN
210 220 230 240 250
FRGLAKPISG TLKVTIHSLR NIEHTSFLQT HSFTMPSYAV LYVDDAQVAK
260 270 280 290 300
SRISQTDTWD ETFIFDVHRA KEFQIIIYEK KKDFDIPIAL ILIPTTIIAE
310 320 330 340 350
ELRRKRNIQE MSETSWKPSI AESASRSDEK GSKSDPINAP NSSSSISTNS
360 370 380 390 400
PLAPTAYYKL LSKSWLSLEP VGQICISLSF SKRTTKRQFP ETGLGRQGAI
410 420 430 440 450
RQKKEDVVAS QVGHQFVQRQ FYQIMRCAVC AELFSYSPGL QCENCSFVCH
460 470 480 490 500
KKCVTKVLAS CIAQSNSEKS DFGGLRYRIP HRFEPFNSLG AQWCAHCGFF
510 520 530 540 550
LPLRRKDCFK CVECGITCHG QCAHLIPDYC GMSNDLKHQL LTELEVSKRP
560 570 580 590 600
KKPELPNQEN KTTNEKVYRK PLSSQNTFDT LPTISQGLLA ATQPVTSVLN
610 620 630 640 650
TSPLPKTPEK DRSLNVTPSS STPTPASVLA PPSSASLSSS KDANRSVPES
660 670 680 690 700
PRREKKNRVT LDDFTFLAVL GKGNFGKVML AEYKVNKKFY AIKVLKKEAI
710 720 730 740 750
LKNEELESLK TEKHVFEVAN KEKHPFLLNL FASFQTSTRV YFVMEYILGG
760 770 780 790 800
DLMVHIQRQQ FSVKRARFYG AEVCLALKYF HENGIAYRDL KLDNILLCPD
810 820 830 840 850
GHIRIADYGL CKENMLLGNT TSTFCGTPEF MAPEILLEQQ YSKDVDWWAF
860 870 880 890 900
GVLMYQMLLG QSPFKGEDEE EIFDAILSDE PLFPINMPAD AVSLLRGLLT
910 920 930 940 950
RDPNQRLGSG PKDANEVMAH PFFASIVWDD LYNKLYEPSY KPLINDPRDL
960 970 980
NNFDEEFTSA CPTLTPVNTV LTRQQQECFR GFSSFATE
Length:988
Mass (Da):111,784
Last modified:October 1, 1996 - v2
Checksum:i0969BDEC1AB43C4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 359AMVASTKNP → SNGGFDGES (PubMed:8491190).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14337 Genomic DNA. Translation: BAA03267.1.
CU329670 Genomic DNA. Translation: CAA93697.1.
AB027982 Genomic DNA. Translation: BAA87286.1.
PIRiS35362.
RefSeqiNP_593737.2. NM_001019168.2.

Genome annotation databases

EnsemblFungiiSPAC17G8.14c.1; SPAC17G8.14c.1:pep; SPAC17G8.14c.
GeneIDi2542293.
KEGGispo:SPAC17G8.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14337 Genomic DNA. Translation: BAA03267.1.
CU329670 Genomic DNA. Translation: CAA93697.1.
AB027982 Genomic DNA. Translation: BAA87286.1.
PIRiS35362.
RefSeqiNP_593737.2. NM_001019168.2.

3D structure databases

ProteinModelPortaliP36582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278761. 104 interactions.
MINTiMINT-4688688.

Proteomic databases

MaxQBiP36582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17G8.14c.1; SPAC17G8.14c.1:pep; SPAC17G8.14c.
GeneIDi2542293.
KEGGispo:SPAC17G8.14c.

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.14c.
PomBaseiSPAC17G8.14c. pck1.

Phylogenomic databases

HOGENOMiHOG000176156.
InParanoidiP36582.
KOiK02677.
OrthoDBiEOG092C0HH3.
PhylomeDBiP36582.

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

PROiP36582.

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.
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...

Entry informationi

Entry nameiPCK1_SCHPO
AccessioniPrimary (citable) accession number: P36582
Secondary accession number(s): Q9UTU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 153 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.