PPK2_SCHPO
ID PPK2_SCHPO Reviewed; 665 AA.
AC Q10447;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein kinase domain-containing protein ppk2;
GN Name=ppk2; ORFNames=SPAC12B10.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION.
RX PubMed=15821139; DOI=10.1128/ec.4.4.799-813.2005;
RA Bimbo A., Jia Y., Poh S.L., Karuturi R.K.M., den Elzen N., Peng X.,
RA Zheng L., O'Connell M., Liu E.T., Balasubramanian M.K., Liu J.;
RT "Systematic deletion analysis of fission yeast protein kinases.";
RL Eukaryot. Cell 4:799-813(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Located at the cell tip.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- CAUTION: Lacks the active site aspartate. {ECO:0000305}.
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DR EMBL; CU329670; CAA94704.2; -; Genomic_DNA.
DR PIR; T37581; T37581.
DR RefSeq; NP_594646.1; NM_001020074.2.
DR AlphaFoldDB; Q10447; -.
DR SMR; Q10447; -.
DR BioGRID; 279532; 29.
DR STRING; 4896.SPAC12B10.14c.1; -.
DR iPTMnet; Q10447; -.
DR MaxQB; Q10447; -.
DR PaxDb; Q10447; -.
DR PRIDE; Q10447; -.
DR EnsemblFungi; SPAC12B10.14c.1; SPAC12B10.14c.1:pep; SPAC12B10.14c.
DR GeneID; 2543100; -.
DR KEGG; spo:SPAC12B10.14c; -.
DR PomBase; SPAC12B10.14c; -.
DR VEuPathDB; FungiDB:SPAC12B10.14c; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_412864_0_0_1; -.
DR InParanoid; Q10447; -.
DR Reactome; R-SPO-75153; Apoptotic execution phase.
DR PRO; PR:Q10447; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..665
FT /note="Protein kinase domain-containing protein ppk2"
FT /id="PRO_0000086829"
FT DOMAIN 388..637
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 665 AA; 74526 MW; EF24B8BCD2D56B61 CRC64;
MLSNSTFHEH HAKSHFHNNA CQSNASSSAC RASEDHLVSS FPNDSIIDLQ PSRPAPEPPK
KKFGYYARRL SGHFLSLIHG SGNSTRSPPF HLQNQKSNGQ SEVWHSSDDS GSPKRLNRSR
SSKEDMYRRR SLHGLPSLSR RNSKKSSTLS RSISLHLRSE SAPISLPIHL YKSYSYNHSP
SSLPTVLNSQ ALSSPPVPTT PDEVSTNRLS SSTSSMNCRN LVPDNFNISI RPNTTNYRSS
IQENSNGNRD SISPSAYDAP LLHNVDTQSI DGFVSVASHF SSASTAESLD DGHSATTIQQ
GDVSSYPLSR SVSTPVPMSP ISISPAKPSP QSPKLSQSAV GHPSSSIPAA AMHKVSYSDD
LMRFVAREKY YLQIVDCLCT QKDPLFFYTD FTKICQQDTV GTYVARQTLD KEVVVIKRFD
ISAVTHRRLL LEELQRLSGL SHKNLIRYNE SFWYLNNIWS VFEYKDPSTK LSALIPKYFF
SELNIASICY EISSGLAFLH NSGIAHHNLT TECIYLTKSS CLKIGNYAFS SPYIERQTNR
GAVSHVPDWL IEKNYKEGFM KDVKSLGLVA LEIFQGQPNF FRKSIQSIQL TPNANVLVNR
VRGLISQEFK EFLLQTLQAE TLQGPNINML LETSSFLEKR QTLNFEICLN NLNLRERKAS
RYSYL
