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Protein

Serine/threonine-protein kinase cek1

Gene

cek1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May facilitate the progression of anaphase through direct or indirect interaction with the cut8 protein.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei618 – 6181ATPPROSITE-ProRule annotation
Active sitei713 – 7131Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi595 – 6039ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • positive regulation of mitotic metaphase/anaphase transition Source: PomBase
  • signal transduction Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 5613.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase cek1 (EC:2.7.11.1)
Gene namesi
Name:cek1
ORF Names:SPCC1450.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1450.11c.
PomBaseiSPCC1450.11c. cek1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Serine/threonine-protein kinase cek1PRO_0000085847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei525 – 5251Phosphoserine1 Publication
Modified residuei748 – 7481Phosphoserine1 Publication
Modified residuei1211 – 12111Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38938.

PTM databases

iPTMnetiP38938.

Interactioni

Protein-protein interaction databases

BioGridi275778. 35 interactions.
IntActiP38938. 1 interaction.
MINTiMINT-4689362.

Structurei

3D structure databases

ProteinModelPortaliP38938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 9871PASPROSITE-ProRule annotationAdd
BLAST
Domaini589 – 958370Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini959 – 105799AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP38938.
KOiK12767.
OrthoDBiEOG7Z95VF.
PhylomeDBiP38938.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR011993. PH_dom-like.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50112. PAS. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHIKNEREE VFLEDDQAQH SQAELLSSKD ENLQPSIPLS PVAFELDFSG
60 70 80 90 100
NFQFISDNSS ELLDIPKDKI IGHSVAEVLG TDGYNAFMRA VNCLLKDDSH
110 120 130 140 150
SYHVRFQHSI NANHANQNYY TAKGDLPSDE KITKPFDAIG ILIRHPGSAI
160 170 180 190 200
PAHTMWVVNP ATNSLGSVSP LVTKLLDVIG FGASLLDKYL CDLRTSYHKH
210 220 230 240 250
NSLDALPLPT PEFCQICERE IQSWFFELHS KFCLSTSTYE SVVQAAQDSL
260 270 280 290 300
LYFRSTLLEI QEGMQKDSSL VPVYKNEPLI VDADDYFFTD ENKQTLSLCS
310 320 330 340 350
FLSQVMYYLE VAIDITIPPV KIIVNFDKVD SLRVQSPRSE KATIELDNYN
360 370 380 390 400
PSLENCSSAV IALWEDIKTA VDTKITGVLR LRNAIYYSER IRLEIDHHVQ
410 420 430 440 450
EIIDDVVSNL VTNHSSTSLG HLESKLAPSI TFPDACDALE AEECITRPGS
460 470 480 490 500
ATNTPQSDRS LDINDLSRSS SYSRHLSHVS LSNPDFAIGS PMSQDSSNYS
510 520 530 540 550
SPLHRRKASD SNFSDPRFDD LKYLSPNSSP RFVASDGPNR PASNGRSSLF
560 570 580 590 600
SRGRASNLGD VGLRLPSPSP RIHTIVPNSA PEHPSINDYK ILKPISKGAF
610 620 630 640 650
GSVYLAQKRT TGDYFAIKIL KKSNMIAKNQ VINVRAERAI LMSQGESPFV
660 670 680 690 700
AKLYYTFQSK DYLYLVMEYL NGGDCGSLLK TMGVLDLDWI RTYIAETVLC
710 720 730 740 750
LGDLHDRGII HRDIKPENLL ISQNGHLKLT DFGLSRVGYM KRHRRKQSSS
760 770 780 790 800
IPVLDLRDRS SAISDLSLST ASSVLEAQSL ITPERPKRPS LNEKLLSLDG
810 820 830 840 850
TSIRLAGQSF NYENSAEDSP TATNTPTSQV DESNIFRSTD SPRVQPFFEN
860 870 880 890 900
KDPSKRFIGT PDYIAPEVIL GNPGIKASDW WSLGCVVFEF LFGYPPFNAE
910 920 930 940 950
TPDQVFQNIL ARRINWPAEV FTAESSVALD LIDRLLCMNP ANRLGANGVE
960 970 980 990 1000
EIKAHPFFKS VNWDTILEED PPFVPKPFSP EDTVYFDSRG LKGFDFSEYY
1010 1020 1030 1040 1050
NQPTVTEAQK LEEERPASSI PQHVSGNRKG RLRSNTISTP EFGSFTYRNL
1060 1070 1080 1090 1100
DFLNKANRNT IQKLRKEHMA VKSAKTSVDD TFSQYMSRFK AKLSTSQSVG
1110 1120 1130 1140 1150
PVKSSRRASM ADYEASTTTR VQDITTDSID SIDDFDSLKE GRMLSFFDNL
1160 1170 1180 1190 1200
ALEDHKGVSS TMSASQSQSS MHTALPDVTE GTSSDEHTTI QKGRIDNLQA
1210 1220 1230 1240 1250
QSLTHKRNAI SYPGLFQLDR LQMIIPKDEI ELAEILKKIF PKLTLVLIDD
1260 1270 1280 1290 1300
PWSILKKLLQ NEQFNVVFLH FGNDKVSSSR LMYSVRTSAT INSRVPFVYI
1310 1320 1330
CEDETCIPTD LQSDGVLLKP ITCENIESCL RKLDVWHS
Length:1,338
Mass (Da):149,897
Last modified:January 11, 2001 - v3
Checksum:i755DD0A13D3D2762
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1297 – 133842FVYIC…DVWHS → VCIHLRGRDLHSD in BAA06551 (PubMed:8065367).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31773 Genomic DNA. Translation: BAA06551.1.
CU329672 Genomic DNA. Translation: CAB40178.1.
PIRiT40993.
RefSeqiNP_588310.1. NM_001023300.2.

Genome annotation databases

EnsemblFungiiSPCC1450.11c.1; SPCC1450.11c.1:pep; SPCC1450.11c.
GeneIDi2539208.
KEGGispo:SPCC1450.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31773 Genomic DNA. Translation: BAA06551.1.
CU329672 Genomic DNA. Translation: CAB40178.1.
PIRiT40993.
RefSeqiNP_588310.1. NM_001023300.2.

3D structure databases

ProteinModelPortaliP38938.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275778. 35 interactions.
IntActiP38938. 1 interaction.
MINTiMINT-4689362.

PTM databases

iPTMnetiP38938.

Proteomic databases

MaxQBiP38938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1450.11c.1; SPCC1450.11c.1:pep; SPCC1450.11c.
GeneIDi2539208.
KEGGispo:SPCC1450.11c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1450.11c.
PomBaseiSPCC1450.11c. cek1.

Phylogenomic databases

InParanoidiP38938.
KOiK12767.
OrthoDBiEOG7Z95VF.
PhylomeDBiP38938.

Enzyme and pathway databases

BRENDAi2.7.11.1. 5613.

Miscellaneous databases

PROiP38938.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR011993. PH_dom-like.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50112. PAS. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of cut8+ and cek1+, a novel protein kinase gene, which complement a fission yeast mutation that blocks anaphase."
    Samejima I., Yanagida M.
    Mol. Cell. Biol. 14:6361-6371(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Erratum
    Samejima I., Yanagida M.
    Mol. Cell. Biol. 14:7683-7683(1994)
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525; SER-748 AND SER-1211, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCEK1_SCHPO
AccessioniPrimary (citable) accession number: P38938
Secondary accession number(s): Q9Y7N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 11, 2001
Last modified: June 8, 2016
This is version 132 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. 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.