SSP1_SCHPO
ID SSP1_SCHPO Reviewed; 652 AA.
AC P50526; Q9UTZ4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase ssp1;
DE EC=2.7.11.1;
GN Name=ssp1; ORFNames=SPCC297.03;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7628434; DOI=10.1002/j.1460-2075.1995.tb07339.x;
RA Matsusaka T., Hirata D., Yanagida M., Toda T.;
RT "A novel protein kinase gene ssp1+ is required for alteration of growth
RT polarity and actin localization in fission yeast.";
RL EMBO J. 14:3325-3338(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 177-393.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-59 AND TYR-63, AND
RP IDENTIFICATION BY 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 -!- FUNCTION: Involved in actin localization and thus in polarized cell
CC growth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D45882; BAA08301.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB40783.1; -; Genomic_DNA.
DR EMBL; AB027913; BAA87217.1; -; Genomic_DNA.
DR PIR; S58666; S58666.
DR RefSeq; NP_588360.1; NM_001023351.2.
DR AlphaFoldDB; P50526; -.
DR SMR; P50526; -.
DR BioGRID; 275525; 25.
DR STRING; 4896.SPCC297.03.1; -.
DR iPTMnet; P50526; -.
DR MaxQB; P50526; -.
DR PaxDb; P50526; -.
DR PRIDE; P50526; -.
DR EnsemblFungi; SPCC297.03.1; SPCC297.03.1:pep; SPCC297.03.
DR GeneID; 2538951; -.
DR KEGG; spo:SPCC297.03; -.
DR PomBase; SPCC297.03; ssp1.
DR VEuPathDB; FungiDB:SPCC297.03; -.
DR eggNOG; KOG0585; Eukaryota.
DR HOGENOM; CLU_021055_0_0_1; -.
DR OMA; ELCWTDL; -.
DR PhylomeDB; P50526; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P50526; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0005516; F:calmodulin binding; ISS:PomBase.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0030042; P:actin filament depolymerization; IGI:PomBase.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IC:PomBase.
DR GO; GO:0051523; P:cell growth mode switching, monopolar to bipolar; IMP:PomBase.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:PomBase.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; EXP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:PomBase.
DR GO; GO:0140648; P:positive regulation of cell cycle switching, mitotic to meiotic cell cycle; EXP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..652
FT /note="Serine/threonine-protein kinase ssp1"
FT /id="PRO_0000086683"
FT DOMAIN 135..409
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 467..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 141..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 63
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 652 AA; 73992 MW; B1931E5EB75A85DA CRC64;
MGSVNNEEKT LIEPQRLLRK NTWHPEVDDS EVPPSVFPEY PVHKAIQKTS DSFRKRNYSA
GDYVIAPLGG EREGSSLTHS WTFQPGKHNQ RLYSDNFQEA QRQWKRLQEW GEVKETKKIR
KRFDRFSGRK YINHYEIIKE LGRGMHGKVK LGRDTVTREL LAIKIIPKTE RRPKLGRANA
SSQKEKVRRE IAILKKCVHP NVVRLREVID DPSSTKVYLV LEYMSGGEVP WTDCDSPVLS
ISEARQYFRD VVLGLEYLHY QGIIHRDIKP ANLLLNSSNC VKISDFGVSY IANAGLNEDN
DVELAKTVGT PAFFAPELCW TDLDRPRPKI SEAIDVWALG VTLFCLLFGR CPFNASMEYE
LFDKIVNERL NIPSTPDIGE EGRDLLKRLL CKDPEQRITL VEVKLHPWTL DGLKDPEKWL
QNTDPSTVSR VEVSTDEVAS AISLVGRLRR KLGKLFRFRR PKARVFDSSS SVPSDSSICR
PESSGNSSIG LSASELSDSF NRLAVNESQK DRERKQVHPV EMGRNSSEKK PRCDFGWDYE
AFPNDNQDAD DACSYNTGDS IPQVSKSING HFETYSRTSM DTDDVASFES PNAKHEESGM
PVVTFRNYEN YDANPSNFHP VVPGFVSSPN LHLAGGSDTP IYCIEHSFTP TN
