SSK2_YEAST
ID SSK2_YEAST Reviewed; 1579 AA.
AC P53599; D6W1K5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=MAP kinase kinase kinase SSK2;
DE EC=2.7.11.25;
DE AltName: Full=Suppressor of sensor kinase 2;
GN Name=SSK2; OrderedLocusNames=YNR031C; ORFNames=N3276;
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 [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-62; SER-78; SER-118
RP AND SER-1424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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=2.7.11.25;
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=2.7.11.25;
CC -!- SUBUNIT: Interacts with by SSK1.
CC -!- INTERACTION:
CC P53599; Q00772: SLT2; NbExp=2; IntAct=EBI-18191, EBI-17372;
CC P53599; Q07084: SSK1; NbExp=7; IntAct=EBI-18191, EBI-18184;
CC -!- MISCELLANEOUS: Present with 217 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; L41927; AAC41665.1; -; Genomic_DNA.
DR EMBL; Z71646; CAA96311.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10571.1; -; Genomic_DNA.
DR PIR; S59801; S59801.
DR RefSeq; NP_014428.1; NM_001183208.1.
DR AlphaFoldDB; P53599; -.
DR SMR; P53599; -.
DR BioGRID; 35855; 249.
DR DIP; DIP-2436N; -.
DR IntAct; P53599; 37.
DR MINT; P53599; -.
DR STRING; 4932.YNR031C; -.
DR iPTMnet; P53599; -.
DR MaxQB; P53599; -.
DR PaxDb; P53599; -.
DR PRIDE; P53599; -.
DR TopDownProteomics; P53599; -.
DR EnsemblFungi; YNR031C_mRNA; YNR031C; YNR031C.
DR GeneID; 855765; -.
DR KEGG; sce:YNR031C; -.
DR SGD; S000005314; SSK2.
DR VEuPathDB; FungiDB:YNR031C; -.
DR eggNOG; KOG4645; Eukaryota.
DR GeneTree; ENSGT00940000176701; -.
DR HOGENOM; CLU_001999_2_0_1; -.
DR InParanoid; P53599; -.
DR OMA; MIHFERE; -.
DR BioCyc; YEAST:G3O-33342-MON; -.
DR BRENDA; 2.7.11.25; 984.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR PRO; PR:P53599; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53599; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0071474; P:cellular hyperosmotic response; IMP:SGD.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IMP:SGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IGI:SGD.
DR GO; GO:0038066; P:p38MAPK cascade; IBA:GO_Central.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1579
FT /note="MAP kinase kinase kinase SSK2"
FT /id="PRO_0000086682"
FT DOMAIN 1266..1558
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1390
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1272..1280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1579 AA; 180528 MW; 91A07A195CB3772E CRC64;
MSHSDYFNYK PYGDSTEKPS SSKMRQSSSS SSSRLRSESL GRNSNTTQAR VASSPISPGL
HSTQYFRSPN AVYSPGESPL NTVQLFNRLP GIPQGQFFHQ NAISGSSSSS ARSSRRPSNI
GLPLPKNPQQ SLPKLSTQPV PVHKKVEASK TESEIIKKPA PVNSNQDPLL TTPTLVISPE
LASLNTTNTS IMSTPQNITN QTSNKHIPTR SQPNGSTSSS TLQDIVTTNS SQRSVGHHGG
STTSLRTYKK QYVLNEQLYL RKMRNRANDD YYTRGIVASS NFEDDEENFS NKGEDDLELE
MDDLLKVEGE DKDNDFNFGY NFITSSTKNN ENVVSMSLNY LKGKLDWLRD VNNDQPCEIE
DEEWHSILGS EDLLSKLLQN PMVNNRFEWQ TMLSKVLKGD IVRNEKTKIA NQGKGPGFNT
QFSDDIWIEL KAWMNGRTVE DQNKSLRIFR DSTDSVFQEI MAFKLEDNMS ADEAAETIKS
LVDKYYRVLN LWPNIKRMHA EKPITKTEAF RNRIDTLNSW LNFKFNFDTN IAYLKKWIVG
NKELESTTEV DNTTVNLDDP AVFATNCKRF AEQIMKEKDI ELIFQKKIFF PLAPWILKAK
FFFLKYQKTW NELNLSYLDQ DLEFLLMFPM RLVKDIILIR LSYAKKIQNP TLMMIDQMMD
DFSTYIKLAV QMKFTVASYC NDWFFKVKID PEFDHTVVEG LEYFFSILEL RILYSGKNSF
KTSKEPDLLL KYWEMFRNVG YYIDDAGELI AAEFTKLTLR LVHRLHAYLL RQQNTPPKLE
NEAAAEKWLV QIFEILGSMK RKLNRFTNIL TKAFQNFVRY KIEDHNYLLK QLKETGHFLI
YTGGYLEQNG TYLIGSPELL GCKDDDILRI IKNSDIGCDL VPKLEINNSL TIYNALDDNW
NSNSSLGSDI SNDGTPFYYI KNDLTTQPRS YNGNRVNREP DFENSRSTEE EFYELETRLN
SLGYVLVLTP QEPLLWEGEM YNLSDNKTIK PEGLNLKVIP NSIDLMCQGS SYALEYQCDR
FQQISGSSVS FLEKKSSSET VKNNLQRINK AYFRCTYSVL KNYTKIVTTF KKVSPVNDLL
NNIFLFGRDF GLNFLRINVA NNEKRSIIIL LMMRLSIGWL KFLAEDCDPT DQRVFRWCVT
SMEFAMHMVS GWNILALDEC QFSSLKQKIS ECMSLLISHF DIIGARSIEV EKINQQARSN
LDLEDVFDDD MMLQVNSEFR VQSIMELEER IKRNPHQTGK VIDDSDKGNK YLVSLASSIS
NVSMRWQKRN FIGGGTFGRV YSAVDLDNGE ILAVKEINIQ DSKSMQKIFP LIKEEMSVLE
ILNHPNIVSY YGVEVHRDKV NIFMEYCEGG SLAALLEHGR IEDEMVTQVY TLQLLEGLAY
LHESGIVHRD VKPENILLDF NGVIKYVDFG AAKKIANNGT RLASMNKIEN ADGEHEDVTH
VSDSKAVKNN ENALLDMMGT PMYMAPESIT GSTTKGKLGA DDVWSLGCVV LEMITGRRPW
ANLDNEWAIM YHVAAGHTPQ FPTKDEVSSA GMKFLERCLI QNPSKRASAV ELLMDPWIVQ
IREIAFGDDS SSTDTEERE
