SSK1_YEAST
ID SSK1_YEAST Reviewed; 712 AA.
AC Q07084; D6VY08; Q07909;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Osmolarity two-component system protein SSK1;
GN Name=SSK1; OrderedLocusNames=YLR006C;
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], AND MUTAGENESIS OF ASP-554.
RX PubMed=8183345; DOI=10.1038/369242a0;
RA Maeda T., Wurgler-Murphy S.M., Saito H.;
RT "A two-component system that regulates an osmosensing MAP kinase cascade in
RT yeast.";
RL Nature 369:242-245(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION, PHOSPHORYLATION AT ASP-554, AND INTERACTION WITH YPD1.
RX PubMed=8808622; DOI=10.1016/s0092-8674(00)80162-2;
RA Posas F., Wurgler-Murphy S.M., Maeda T., Witten E.A., Thai T.C., Saito H.;
RT "Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay
RT mechanism in the SLN1-YPD1-SSK1 two-component osmosensor.";
RL Cell 86:865-875(1996).
RN [5]
RP FUNCTION.
RX PubMed=11073911; DOI=10.1128/jb.182.23.6673-6678.2000;
RA Janiak-Spens F., Sparling D.P., West A.H.;
RT "Novel role for an HPt domain in stabilizing the phosphorylated state of a
RT response regulator domain.";
RL J. Bacteriol. 182:6673-6678(2000).
RN [6]
RP FUNCTION, AND DEGRADATION.
RX PubMed=12944490; DOI=10.1128/mcb.23.18.6662-6671.2003;
RA Sato N., Kawahara H., Toh-e A., Maeda T.;
RT "Phosphorelay-regulated degradation of the yeast Ssk1p response regulator
RT by the ubiquitin-proteasome system.";
RL Mol. Cell. Biol. 23:6662-6671(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14665464; DOI=10.1128/ec.2.6.1304-1314.2003;
RA Lu J.M.-Y., Deschenes R.J., Fassler J.S.;
RT "Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles
RT between the nucleus and cytoplasm for SLN1-dependent phosphorylation of
RT Ssk1p and Skn7p.";
RL Eukaryot. Cell 2:1304-1314(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-673, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-673 AND THR-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-327 AND SER-703, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-380; SER-703 AND
RP SER-706, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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: Final receptor of the SLN1-YPD1-SSK1 two-component regulatory
CC system, which controls activity of the HOG1 pathway in response to
CC changes in the osmolarity of the extracellular environment. Under
CC normal osmotic conditions, maintained in a phosphorylated and inactive
CC state by the phosphorelay intermediate protein YPD1. Under conditions
CC of high osmolarity, the histidine kinase SLN1 is no longer active and
CC the unphosphorylated form of SSK1 interacts with and activates SSK2 and
CC SSK22, two MAPKKKs that further stimulate the PBS2-HOG1 MAPKK-MAPK
CC cascade. Unphosphorylated SSK1 is subsequently degraded by the UBC7-
CC dependent ubiquitin-proteasome system to down-regulate the HOG1 pathway
CC after completion of the osmotic adaptation.
CC {ECO:0000269|PubMed:11073911, ECO:0000269|PubMed:12944490,
CC ECO:0000269|PubMed:8808622}.
CC -!- SUBUNIT: Interacts with SSK2, SSK22 and YPD1.
CC {ECO:0000269|PubMed:8808622}.
CC -!- INTERACTION:
CC Q07084; P53599: SSK2; NbExp=7; IntAct=EBI-18184, EBI-18191;
CC Q07084; P25390: SSK22; NbExp=5; IntAct=EBI-18184, EBI-18129;
CC Q07084; Q07688: YPD1; NbExp=3; IntAct=EBI-18184, EBI-34423;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14665464}.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to
CC 'His-64' (H2) of YPD1 and finally to Asp-554 (D2) of SSK1.
CC -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L26523; AAA35100.1; -; Genomic_DNA.
DR EMBL; Z73178; CAA97528.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09324.1; -; Genomic_DNA.
DR PIR; S64828; S64828.
DR RefSeq; NP_013106.1; NM_001181893.1.
DR PDB; 5KBX; X-ray; 2.80 A; B=495-712.
DR PDBsum; 5KBX; -.
DR AlphaFoldDB; Q07084; -.
DR SMR; Q07084; -.
DR BioGRID; 31279; 137.
DR DIP; DIP-2437N; -.
DR IntAct; Q07084; 42.
DR MINT; Q07084; -.
DR STRING; 4932.YLR006C; -.
DR iPTMnet; Q07084; -.
DR MaxQB; Q07084; -.
DR PaxDb; Q07084; -.
DR PRIDE; Q07084; -.
DR EnsemblFungi; YLR006C_mRNA; YLR006C; YLR006C.
DR GeneID; 850692; -.
DR KEGG; sce:YLR006C; -.
DR SGD; S000003996; SSK1.
DR VEuPathDB; FungiDB:YLR006C; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_008307_3_0_1; -.
DR InParanoid; Q07084; -.
DR OMA; NEDTITH; -.
DR BioCyc; YEAST:G3O-32167-MON; -.
DR PRO; PR:Q07084; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07084; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:1990315; C:Mcs4 RR-MAPKKK complex; IBA:GO_Central.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:SGD.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IMP:SGD.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IDA:SGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:SGD.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Two-component regulatory system.
FT CHAIN 1..712
FT /note="Osmolarity two-component system protein SSK1"
FT /id="PRO_0000081406"
FT DOMAIN 505..647
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 73..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 554
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:8808622"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 554
FT /note="D->N: Activates."
FT /evidence="ECO:0000269|PubMed:8183345"
FT CONFLICT 181
FT /note="P -> S (in Ref. 1; AAA35100)"
FT /evidence="ECO:0000305"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:5KBX"
FT HELIX 513..525
FT /evidence="ECO:0007829|PDB:5KBX"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:5KBX"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:5KBX"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:5KBX"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5KBX"
FT HELIX 562..575
FT /evidence="ECO:0007829|PDB:5KBX"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:5KBX"
FT HELIX 615..622
FT /evidence="ECO:0007829|PDB:5KBX"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:5KBX"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:5KBX"
FT HELIX 636..651
FT /evidence="ECO:0007829|PDB:5KBX"
SQ SEQUENCE 712 AA; 78529 MW; 33B2DBB4FCF2528A CRC64;
MLNSALLWKV WLRIDNSTDE VNQPIAVQFD EIDTVDDLKS RFFQKLSSTR WREINDNASI
AIGLYAPKFD NQADNTSSNN TNDNSCRSKS NGAGSGANLS VNSNTKSSVS PTAGSFGLSK
DLAKDRNVLQ HPKPTQKRGA LYDAFAAVPT VAATTNVDFP PNEAPMLSPQ RPYSTSPKQF
PATTKSPLLR FASVSPYPKF HSDNQIMASA GLTYVSPHNK NKYTRPLIRK GLNFTTESVN
DCTYKIIFEP DELAINIYKE LFGTMGSQPA SQPLLIFSNV NLRQDVPPLD ILNVVDYVPT
NEEISQQKTQ PTDHGAVGVF HLDDHISPGE QGLKQTIGDK ADLKGKDGNS SPQEFKLITD
EEQLRRASQE LKDEEKDAES PWQAILLLPK GYKGGVDFRN KPVAHTDSSF NNEDTITHSE
LEVNTGSPSQ ESGSLNEAGI GITQPMSEVQ RRKEDVTPAS PILTSSQTPH YSNSLYNAPF
AVSSPPDPLP NLFTTTSEKV FPKINVLIVE DNVINQAILG SFLRKHKISY KLAKNGQEAV
NIWKEGGLHL IFMDLQLPVL SGIEAAKQIR DFEKQNGIGI QKSLNNSHSN LEKGTSKRFS
QAPVIIVALT ASNSQMDKRK ALLSGCNDYL TKPVNLHWLS KKITEWGCMQ ALIDFDSWKQ
GESRMTDSVL VKSPQKPIAP SNPHSFKQAT SMTPTHSPVR KNSNLSPTQI EL
