ASK10_YEAST
ID ASK10_YEAST Reviewed; 1146 AA.
AC P48361; D6VUM9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Activator of SKN7 protein 10;
DE AltName: Full=Regulator of the glycerol channel 2;
GN Name=ASK10; Synonyms=RGC2; OrderedLocusNames=YGR097W;
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].
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=8904339;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<267::aid-yea897>3.0.co;2-u;
RA Page N., Sheraton J., Brown J.L., Stewart R.S., Bussey H.;
RT "Identification of ASK10 as a multicopy activator of Skn7p-dependent
RT transcription of a HIS3 reporter gene.";
RL Yeast 12:267-272(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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, IDENTIFICATION IN THE RNA POLYMERASE II HOLOENZYME, INTERACTION
RP WITH RPO21 AND SSN8, AND PHOSPHORYLATION.
RX PubMed=14555478; DOI=10.1128/ec.2.5.962-970.2003;
RA Cohen T.J., Lee K., Rutkowski L.H., Strich R.;
RT "Ask10p mediates the oxidative stress-induced destruction of the
RT Saccharomyces cerevisiae C-type cyclin Ume3p/Srb11p.";
RL Eukaryot. Cell 2:962-970(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-793 AND THR-1017, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-1070, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-1070, 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=19956799; DOI=10.1371/journal.pgen.1000738;
RA Beese S.E., Negishi T., Levin D.E.;
RT "Identification of positive regulators of the yeast fps1 glycerol
RT channel.";
RL PLoS Genet. 5:E1000738-E1000738(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-969; SER-1070;
RP SER-1095 AND SER-1098, 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: Positive regulator of FPS1 glycerol channel required for the
CC glycerol efflux. As a component of the RNA polymerase II holoenzyme, is
CC required for SSN8 destruction in response to oxidative stress but not
CC heat shock. Required for cell survival in response to heat shock
CC independent of SSN8. {ECO:0000269|PubMed:14555478,
CC ECO:0000269|PubMed:19956799}.
CC -!- SUBUNIT: Component of the RNA polymerase II holoenzyme. Interacts with
CC RPO21 and SSN8. {ECO:0000269|PubMed:14555478}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19956799}. Note=Displays diffuse cytoplasmic
CC localization, but very rapidly aggregates into punctate spots that
CC appear near the cell surface in response to hypo-osmotic shock.
CC -!- PTM: Phosphorylated in response to various stresses. stress-induced
CC phosphorylation is partially dependent on HOG1.
CC {ECO:0000269|PubMed:14555478, ECO:0000269|PubMed:19956799}.
CC -!- SIMILARITY: Belongs to the RGC1 family. {ECO:0000305}.
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DR EMBL; U27209; AAA67368.1; -; Genomic_DNA.
DR EMBL; Z72882; CAA97100.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08190.1; -; Genomic_DNA.
DR PIR; S64402; S64402.
DR RefSeq; NP_011611.1; NM_001181226.1.
DR AlphaFoldDB; P48361; -.
DR BioGRID; 33340; 642.
DR DIP; DIP-1920N; -.
DR IntAct; P48361; 28.
DR MINT; P48361; -.
DR STRING; 4932.YGR097W; -.
DR iPTMnet; P48361; -.
DR MaxQB; P48361; -.
DR PaxDb; P48361; -.
DR PRIDE; P48361; -.
DR EnsemblFungi; YGR097W_mRNA; YGR097W; YGR097W.
DR GeneID; 852989; -.
DR KEGG; sce:YGR097W; -.
DR SGD; S000003329; ASK10.
DR VEuPathDB; FungiDB:YGR097W; -.
DR eggNOG; ENOG502QU0Q; Eukaryota.
DR GeneTree; ENSGT00940000176324; -.
DR HOGENOM; CLU_008754_0_0_1; -.
DR InParanoid; P48361; -.
DR OMA; GYFAIPV; -.
DR BioCyc; YEAST:G3O-30807-MON; -.
DR PRO; PR:P48361; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48361; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0016247; F:channel regulator activity; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0090372; P:positive regulation of glycerol transport; IMP:SGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR SMART; SM00233; PH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1146
FT /note="Activator of SKN7 protein 10"
FT /id="PRO_0000064699"
FT DOMAIN 482..606
FT /note="PH"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1017
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 57
FT /note="I -> T (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="T -> N (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="P -> R (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="V -> A (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="A -> V (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="L -> P (in Ref. 1; AAA67368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1146 AA; 126864 MW; 9E9EF22B0EE496EE CRC64;
MSDYFSSRPS QTLTPMGNKP SGGGGGDDAS SIHSKSSQYL MDILPDSMTL NESVSSIVAN
NQAKEFILPE TDERSPYFIN VPIPKAQPTS TTETKKPLAG DEAIDGQFVK EYPTDILVDR
FYKWKKILKG LVIYLREVAY AQEQFARINY QLKGSVKFPF LTDIDETTNT ITDPFTTAPR
GPKKAQPAQK KVGLTDSEQF QMQMQQEQQE NAVQAPTDES KMSLAPHEYK PVQTTESDNT
SAASGFVKFG SGSIQDIQVI LKKYHLSLAN QQFKISKEIT STVIPKLEEL RKDLRYKITE
IKDLHGDFKT NIGAHIQLTS QLLKKYIAAV KFMNAHGIGN DRASPTNKKP HKLDPKHDPY
LLKLQLDLQL KRQVAEETYL QEAFINLQSS GLQLEKIIYT KIQHALLRYS ALIDSEARLM
IKNMCQELQH GIISKPPAFE WDNFVTQHPS CLLNWKSNDP IPPPRKVSDV IYPHMKSPLA
KCIKAGYFLK KSELLPTYHQ GYFVLTSNYI HEFQSSDFYN LSSSTPNSTK SSAYSSSVSI
ADTYANANNA KANNHHRQAS DVHNSSTTTG GTAGANGIRG IRKKSYLAPI MSIPLNDCTL
KDASSTKFVL VGKPTLNENA DVRKSSSSTY LSGSSQASLP KYGHETAKIF SKAPFHKFLK
GSKPKNKNTK SSELDQFYAA AQKESNNYVT WTFKIVSPEP SEEELKHFKR WVQDLKNLTS
FNDTKDRIKF IEDRVMKSHR FKAGHMSRNS VNIGSHTPCL TDSTFTLQDG TTTSVNLKGR
AEKPQYIHIQ NNSLADFDGN GFRSKVNTPA IDDYGNLITV ERRPAQSPHQ YSDYMATSGN
TTPSYSSGSR PQSMYNGYNP AVSITSNGMM LQQSTANNNT NPTTNLRHQR NISQTSSLPG
FSYTSLSLPV NSPGSSNSES SSGGYFAIPL HGNNNNNNYT QRNSEGSSPC YNDDQIRQQQ
QPLQMQPLSR TSSSSVNVTA MRSTSAGNSI TANAPVVPKV MVNNQNVKTV AADQSATAPS
SPTMNSSVTT INRESPYQTL KKTNSTGNVP CLTAEKTHAH PAFYKRGNNS AQNLTTSSST
ASRVHPIRKH KKNVSFSSLN SLMFSKKGAN HGGNLMTNQF MSGGIQEDDG DSTNNDTIKL
NQSIYS
