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   27-MAR-2024, entry version 172.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 341.
DR   ComplexPortal; CPX-1866; SIT4-SAP190 phosphatase complex.
DR   DIP; DIP-4850N; -.
DR   IntAct; P36123; 14.
DR   MINT; P36123; -.
DR   STRING; 4932.YKR028W; -.
DR   GlyGen; P36123; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P36123; -.
DR   MaxQB; P36123; -.
DR   PaxDb; 4932-YKR028W; -.
DR   PeptideAtlas; P36123; -.
DR   EnsemblFungi; YKR028W_mRNA; YKR028W; YKR028W.
DR   GeneID; 853899; -.
DR   KEGG; sce:YKR028W; -.
DR   AGR; SGD:S000001736; -.
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; HAYIACE; -.
DR   OrthoDB; 5491840at2759; -.
DR   BioCyc; YEAST:G3O-32004-MONOMER; -.
DR   Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR   BioGRID-ORCS; 853899; 0 hits in 10 CRISPR screens.
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:0031929; P:TOR signaling; IMP:SGD.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IGI:SGD.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR12634:SF8; FIERY MOUNTAIN, ISOFORM D; 1.
DR   PANTHER; PTHR12634; SIT4 YEAST -ASSOCIATING PROTEIN-RELATED; 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
//