SA190_YEAST
ID SA190_YEAST Reviewed; 1033 AA.
AC P36123; D6VX93;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=SIT4-associating protein SAP190;
GN Name=SAP190; OrderedLocusNames=YKR028W;
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], IDENTIFICATION OF FRAMESHIFT,
RP INTERACTION WITH SIT4, AND PHOSPHORYLATION.
RC STRAIN=S288c / GRF88;
RX PubMed=8649382; DOI=10.1128/mcb.16.6.2744;
RA Luke M.M., della Seta F., di Como C.J., Sugimoto H., Kobayashi R.,
RA Arndt K.T.;
RT "The SAPs, a new family of proteins, associate and function positively with
RT the SIT4 phosphatase.";
RL Mol. Cell. Biol. 16:2744-2755(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 1009.
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.
RX PubMed=14718557; DOI=10.1091/mbc.e03-10-0750;
RA Jablonowski D., Fichtner L., Stark M.J.R., Schaffrath R.;
RT "The yeast elongator histone acetylase requires Sit4-dependent
RT dephosphorylation for toxin-target capacity.";
RL Mol. Biol. Cell 15:1459-1469(2004).
RN [5]
RP FUNCTION.
RX PubMed=15367655; DOI=10.1128/mcb.24.19.8332-8341.2004;
RA Rohde J.R., Campbell S., Zurita-Martinez S.A., Cutler N.S., Ashe M.,
RA Cardenas M.E.;
RT "TOR controls transcriptional and translational programs via Sap-Sit4
RT protein phosphatase signaling effectors.";
RL Mol. Cell. Biol. 24:8332-8341(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774 AND SER-857, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-857; SER-862;
RP SER-892; THR-990 AND SER-991, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Positive regulator of protein phosphatase SIT4. Involved in
CC the general amino acid control (GAAC) response regulated by TOR.
CC Involved in the dephosphorylation of the elongator complex subunit
CC IKI3. {ECO:0000269|PubMed:14718557, ECO:0000269|PubMed:15367655}.
CC -!- SUBUNIT: Associates with the SIT4 protein phosphatase catalytic subunit
CC in a cell-cycle-dependent manner.
CC -!- INTERACTION:
CC P36123; P20604: SIT4; NbExp=4; IntAct=EBI-16392, EBI-13707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Hyperphosphorylated in the absence of SIT4.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82100.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50561; AAC49304.1; -; Genomic_DNA.
DR EMBL; Z28253; CAA82100.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006944; DAA09183.2; -; Genomic_DNA.
DR PIR; S38100; S38100.
DR RefSeq; NP_012953.2; NM_001179818.2.
DR AlphaFoldDB; P36123; -.
DR BioGRID; 34161; 334.
DR ComplexPortal; CPX-1866; SIT4-SAP190 phosphatase complex.
DR DIP; DIP-4850N; -.
DR IntAct; P36123; 14.
DR MINT; P36123; -.
DR STRING; 4932.YKR028W; -.
DR iPTMnet; P36123; -.
DR MaxQB; P36123; -.
DR PaxDb; P36123; -.
DR PRIDE; P36123; -.
DR EnsemblFungi; YKR028W_mRNA; YKR028W; YKR028W.
DR GeneID; 853899; -.
DR KEGG; sce:YKR028W; -.
DR SGD; S000001736; SAP190.
DR VEuPathDB; FungiDB:YKR028W; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_003676_2_0_1; -.
DR InParanoid; P36123; -.
DR OMA; TYDPIYL; -.
DR BioCyc; YEAST:G3O-32004-MON; -.
DR PRO; PR:P36123; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36123; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IPI:ComplexPortal.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IGI:SGD.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1033
FT /note="SIT4-associating protein SAP190"
FT /id="PRO_0000046107"
FT REGION 32..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1018
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 990
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1033 AA; 117098 MW; 33E5575B58B73B1A CRC64;
MSGSFWKFGQ DYSIESPVSK ILNSAFIKIN KDQDDDVPTG TCEENIADDE DNSSHDYAAS
EDNVVNENEE KEEENTLPTT ESEYENYRPN LDVLDDLLDD DELYTELMCS NFKLLIFLKY
PDVLSKLIEY VTNEKILDEE TDSAKKPEII EGVNDHPILI ERDRKDKKED AEEGGDSEET
TNDSDHDSGD ERSVDSEETS ITLPPESEEQ VETRRARIAA EILSADVWPI SAAIMQNKDL
LGRLWSILDH PAPLPIPAST YFMKINERLL DMDITGMLEF ILSRDSLVAR FLTHVDNPSL
MDFLLKVIST DKPDSPTGVI KILKSQELIP KLLDHLNPEY GISTQSAAGD FIKAFVTLST
NSSNELASGI GPNELTRQLV SEEMIEKLIK IMLKGGTSLS NGVGIIIELI RKNNSDYDFI
QLVYTTLESH PPTDRDPIHL IHLVKLFAKH MPDFADMLDK TKLPLMEMPF GNIEPLGFER
FKICELIAEL LHCSNMTLLN EPNGEMIAQE RDIERAKELE TSTEKENITA IVDNKSSYYD
KDCVEKDITE NLGALQINNQ GSEEDELNDT GVSSVKLDVK SDAKVVEGLE NDASGVELYD
ETLSDTESVR ECLREKPLVG DRLKIALEDT KILISILDMF TEFPWNNFLH NVIFDIAQQI
FNGPLKTGYN RFLLKDYLVD AYLTKKIVDA DKACQDYEKK TGLRYGYMGH LTLVAEEISK
FKEYIDEMKL TFCNTAVSDR LEEPFWKEYS ETILADTREK YNTVLGDFGN DQESDDDVIR
NSDSEDIIGD TEGNENYGNG ENDELLSNGH DSGNMDLYYN FNNNENEENE EDYAEYSDVD
NKNYYNNVET NDDDYDSDDG KSKSAESEFT DKISEHRDGN SLYNEDNDEN GSDKWTSGTS
LFPPDHFPSR SQPSDPKLQD QNIFHHQFDF EGVGDDDDYM DPNDDGQSYA RPGNPLYTTP
KTPPRPKTIL FNSLSALDNN GEDEEVALGT SVDDRMDNEI SSDEEDSEDE DEENDMGNEE
GYSLYRSRSK EAF
