SSK22_YEAST
ID SSK22_YEAST Reviewed; 1331 AA.
AC P25390; D6VR75;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase SSK22;
DE EC=2.7.11.1;
DE AltName: Full=MAP kinase kinase kinase SSK22;
DE AltName: Full=Suppressor of sensor kinase 22;
GN Name=SSK22; OrderedLocusNames=YCR073C; ORFNames=YCR73C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7624781; DOI=10.1126/science.7624781;
RA Maeda T., Takekawa M., Saito H.;
RT "Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-
RT containing osmosensor.";
RL Science 269:554-558(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Kinase involved in a signal transduction pathway that is
CC activated by changes in the osmolarity of the extracellular
CC environment. Activates the PBS2 MAP kinase kinase by phosphorylation.
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 -!- SUBUNIT: Interacts with by SSK1.
CC -!- INTERACTION:
CC P25390; Q07084: SSK1; NbExp=5; IntAct=EBI-18129, EBI-18184;
CC -!- MISCELLANEOUS: Present with 56 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; X59720; CAA42271.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07544.1; -; Genomic_DNA.
DR PIR; S19488; S19488.
DR RefSeq; NP_009998.2; NM_001178783.1.
DR AlphaFoldDB; P25390; -.
DR SMR; P25390; -.
DR BioGRID; 31048; 94.
DR DIP; DIP-5989N; -.
DR IntAct; P25390; 12.
DR MINT; P25390; -.
DR STRING; 4932.YCR073C; -.
DR iPTMnet; P25390; -.
DR PaxDb; P25390; -.
DR PRIDE; P25390; -.
DR EnsemblFungi; YCR073C_mRNA; YCR073C; YCR073C.
DR GeneID; 850436; -.
DR KEGG; sce:YCR073C; -.
DR SGD; S000000669; SSK22.
DR VEuPathDB; FungiDB:YCR073C; -.
DR eggNOG; KOG4645; Eukaryota.
DR GeneTree; ENSGT00940000176701; -.
DR HOGENOM; CLU_001999_2_0_1; -.
DR InParanoid; P25390; -.
DR OMA; ELIQNCY; -.
DR BioCyc; YEAST:G3O-29373-MON; -.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SCE-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5676590; NIK-->noncanonical NF-kB signaling.
DR PRO; PR:P25390; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25390; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IMP:SGD.
DR GO; GO:0038066; P:p38MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017240; MAPKKK_Ssk2/Ssk22.
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 PIRSF; PIRSF037579; MAPKKK_SSK22; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1331
FT /note="Serine/threonine-protein kinase SSK22"
FT /id="PRO_0000086681"
FT DOMAIN 1034..1310
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1040..1048
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1063
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1331 AA; 152718 MW; 2C3CE7C4FF4463B2 CRC64;
MMMDILNTQQ QKAAEGGRVL APHTISSKLV KRLSSHSSHK LSRSDLKALG GSETISDGPS
QLTFKDRYVF NESLYLKKLK KTALDDYYTR GIKLTNRYEE DDGDDEIIRL SNGDRIDEDL
HSGVKFFSTT PYCRKMRSDS DELAWNEIAT ERFKWQSMLA RVLKGDIVKG EKTRIANQVK
KPGLNKELSD EIWLELKAWL NGRTMQEMEQ SLTYLRDSSD SVFEEIMKFQ IPQGKILSLD
ALEAILQDLM NRYHSVVSYW PNLKKMYKDK PITNTAEFTA RIDVMNSWLN FKTNLTLRRQ
ELDDWINRFS PISSSDNCQE DFDGVPQWNC KMKILAEQLM KEKNIESIFQ KKIFYPLSPW
MFKLKLHFIV YRETLTKMNI KYPYERLRSL LAFPVYLIKE VILTRLSYAR KLKNPTMMMI
DQMIDDFNAF IRLSVQLKYT LTKYCSNLPF DVDFDPTFEN TVIEAIRYLF FLLNLKLIDS
SKQNFKAPDL LLKYWDHLKN TGHYINGAET VIPNEFLKLT LRLVHKLQFY LLKQQNFPPT
FANASEAEKW LSSIFENLGA MKRKLNRFSN ILVKAFQNSA VYQINHNAQL VKKLKDAHYF
LVYSGNTFES SGVYMFAAPE LLGCDNDTIL RILRNKSIGC DLVPKLDIGN NLNVYDITTK
ETDLNILVSK GEDSKGIPYY RVVANSSSDL DRHAHQSKKK NFSTDPFDQH LDEKNNEVFE
LEVALSSLGA LVVLYPGEPV VWDGPVYKLP GNNLFASNEM DLGKIGNPNT LILLNQGSNY
ALTYQIDKFN QTVGDSVSFI EKRCSLNSIE SSLQKINKAY YKLTYTVLNN YKGILGSFMK
QCPGNELLNS IFMFGRDFGR SFLKYNAFSS KRKYVIIFLM VKLGMNWLKF LVEECDPTDQ
RTFRWCVLAM DFAMQMTSGY NILALNVKQF QELKERVSVC MSLLISHFDV MGARATEAEN
GMQQARLNID TEENIDEEAT LEINSRLRLE AIKTLEKTMK RNPRQMGKVL DATDQGNKYL
LSLASSLSNV SMRWQKRSFI GGGTFGQVYS AINLENGEIL AVKEIKIHDT TTMKKIFPLI
KEEMTVLEML NHPNIVQYYG VEVHRDKVNI FMEYCEGGSL ASLLDHGRIE DEMVTQVYTF
ELLEGLAYLH QSGVVHRDIK PENILLDFNG IIKYVDFGTA RTVVGSRTRT VRNAAVQDFG
VETKSLNEMM GTPMYMAPET ISGSAVKGKL GADDVWALGC VVLEMATGRR PWSNLDNEWA
IMYHVAAGRI PQLPNRDEMT AAGRAFLERC LVQDPTMRAT AVELLIDPWM IQIREIAFGN
SEKDQVPILS S
