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Protein

Serine/threonine-protein kinase ppk21

Gene

ppk21

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841ATPBy similarity
Binding sitei140 – 1401ATPBy similarity
Active sitei179 – 1791Proton acceptorPROSITE-ProRule annotation
Binding sitei183 – 1831ATP; via carbonyl oxygenBy similarity
Binding sitei197 – 1971ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 673ATPBy similarity
Nucleotide bindingi134 – 1363ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: PomBase

GO - Biological processi

  • mitotic cytokinesis Source: PomBase
  • protein phosphorylation 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

ReactomeiREACT_271751. Downstream TCR signaling.
REACT_276356. CD28 dependent PI3K/Akt signaling.
REACT_309750. VEGFR2 mediated vascular permeability.
REACT_314876. PIP3 activates AKT signaling.
REACT_328151. Activation of PKB.
REACT_352237. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_358773. RHO GTPases activate PKNs.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase ppk21 (EC:2.7.11.1)
Gene namesi
Name:ppk21
ORF Names:SPBC1778.10c, SPBC4C3.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1778.10c.
PomBaseiSPBC1778.10c. ppk21.

Subcellular locationi

GO - Cellular componenti

  • cell division site Source: PomBase
  • cell tip Source: PomBase
  • cytosol Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Serine/threonine-protein kinase ppk21PRO_0000086157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201Phosphoserine; by autocatalysisBy similarity
Modified residuei538 – 5381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y7J6.

Interactioni

Protein-protein interaction databases

BioGridi276357. 51 interactions.
MINTiMINT-4716341.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7J6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 315261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 13146PIF-pocketBy similarityAdd
BLAST

Domaini

The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiQ9Y7J6.
OMAiTHATRAS.
OrthoDBiEOG7354B2.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y7J6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMDLEHKRIS RSTLPDYADP DYFEARGERN PVKPQSSNVV PGTSHIGSIK
60 70 80 90 100
SPADYVFGDI IGDGSFSKVR RATDKKSWKE YAIKVLDKKY IVKENKVKYV
110 120 130 140 150
NIERDSMMRL NGFPGISRLF HTFQDDLKLY YVLELAPNGE LLQYIKKYRF
160 170 180 190 200
LDENCVRFYA AEILSSIEYM HSCGIIHRDL KPENILFDGN MHVKITDFGT
210 220 230 240 250
AKILPPKYVN SPDYTTFPSS FVGTAEYVAP ELLSRQVVSK SSDLWAFACV
260 270 280 290 300
VYQMIVGSPP FHGSNPNNIF KKIMSLEYEL PKLLPPDIVP LFSHLFRIQP
310 320 330 340 350
SDRSTTQQIK QFPFFATITW DNLWTQDPPP MQSFRPNYNI AIPNAPAYYR
360 370 380 390 400
SNVTAAAAAN AAAAFASASI VKHQETARRQ ELPTVNRFTA PTAHYGYASL
410 420 430 440 450
RSHQMPVDRL YYKLVPSSES IIESTSVFVS PIPSVPEGNK FPSGLSKMFL
460 470 480 490 500
KRKQRVMLLT DVGRCAFVCK GKHERLFIEM EVNLKDSSVV VIFDENSSKR
510 520 530 540 550
FLIEDKVQSW IIEDSSGDVT KYKDKILKFA DVASSHQSRS SEENVEENEE

E
Length:551
Mass (Da):62,716
Last modified:July 11, 2012 - v3
Checksum:iC591925366133DCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB39805.3.
PIRiT40486.
RefSeqiXP_001713142.2. XM_001713090.2.

Genome annotation databases

EnsemblFungiiSPBC1778.10c.1; SPBC1778.10c.1:pep; SPBC1778.10c.
GeneIDi2539807.
KEGGispo:SPBC1778.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB39805.3.
PIRiT40486.
RefSeqiXP_001713142.2. XM_001713090.2.

3D structure databases

ProteinModelPortaliQ9Y7J6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276357. 51 interactions.
MINTiMINT-4716341.

Proteomic databases

MaxQBiQ9Y7J6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1778.10c.1; SPBC1778.10c.1:pep; SPBC1778.10c.
GeneIDi2539807.
KEGGispo:SPBC1778.10c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1778.10c.
PomBaseiSPBC1778.10c. ppk21.

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiQ9Y7J6.
OMAiTHATRAS.
OrthoDBiEOG7354B2.

Enzyme and pathway databases

ReactomeiREACT_271751. Downstream TCR signaling.
REACT_276356. CD28 dependent PI3K/Akt signaling.
REACT_309750. VEGFR2 mediated vascular permeability.
REACT_314876. PIP3 activates AKT signaling.
REACT_328151. Activation of PKB.
REACT_352237. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_358773. RHO GTPases activate PKNs.

Miscellaneous databases

NextBioi20800956.
PROiQ9Y7J6.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR011009. Kinase-like_dom.
IPR011993. PH-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. Cited for: IDENTIFICATION.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPPK21_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7J6
Secondary accession number(s): O43064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 11, 2012
Last modified: July 22, 2015
This is version 112 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

External Data

Dasty 3

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 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.