SDS22_YEAST
ID SDS22_YEAST Reviewed; 338 AA.
AC P36047; D6VX07;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein phosphatase 1 regulatory subunit SDS22;
GN Name=SDS22; Synonyms=EGP1; OrderedLocusNames=YKL193C;
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 200358 / YNN 295;
RX PubMed=7791785; DOI=10.1128/mcb.15.7.3777;
RA Mackelvie S.H., Andrews P.D., Stark M.J.R.;
RT "The Saccharomyces cerevisiae gene SDS22 encodes a potential regulator of
RT the mitotic function of yeast type 1 protein phosphatase.";
RL Mol. Cell. Biol. 15:3777-3785(1995).
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.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
RC STRAIN=S288c / GRF88;
RX PubMed=8394042; DOI=10.1002/yea.320090612;
RA Cheret G., Mattheakis L.C., Sor F.;
RT "DNA sequence analysis of the YCN2 region of chromosome XI in Saccharomyces
RT cerevisiae.";
RL Yeast 9:661-667(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH YPI1.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP 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: Regulator of the mitotic function of yeast type 1 protein
CC phosphatase. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with YPI1. {ECO:0000269|PubMed:14690591}.
CC -!- INTERACTION:
CC P36047; P32598: GLC7; NbExp=15; IntAct=EBI-16783, EBI-13715;
CC P36047; P32945: PPQ1; NbExp=3; IntAct=EBI-16783, EBI-13787;
CC P36047; P43587: YPI1; NbExp=10; IntAct=EBI-16783, EBI-22913;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDS22 family. {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; X83609; CAA58588.1; -; Genomic_DNA.
DR EMBL; Z28193; CAA82037.1; -; Genomic_DNA.
DR EMBL; AY558314; AAS56640.1; -; Genomic_DNA.
DR EMBL; X69765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006944; DAA08973.1; -; Genomic_DNA.
DR PIR; S38030; S38030.
DR RefSeq; NP_012728.1; NM_001179759.1.
DR AlphaFoldDB; P36047; -.
DR SMR; P36047; -.
DR BioGRID; 33928; 167.
DR ComplexPortal; CPX-1249; SDS22-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1260; SDS22-GLC7-YPI1 phosphatase complex.
DR DIP; DIP-2378N; -.
DR IntAct; P36047; 36.
DR MINT; P36047; -.
DR STRING; 4932.YKL193C; -.
DR iPTMnet; P36047; -.
DR MaxQB; P36047; -.
DR PaxDb; P36047; -.
DR PRIDE; P36047; -.
DR TopDownProteomics; P36047; -.
DR EnsemblFungi; YKL193C_mRNA; YKL193C; YKL193C.
DR GeneID; 853641; -.
DR KEGG; sce:YKL193C; -.
DR SGD; S000001676; SDS22.
DR VEuPathDB; FungiDB:YKL193C; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000162473; -.
DR HOGENOM; CLU_044236_0_0_1; -.
DR InParanoid; P36047; -.
DR OMA; YDNLIAH; -.
DR BioCyc; YEAST:G3O-31955-MON; -.
DR PRO; PR:P36047; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36047; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:SGD.
DR GO; GO:0072542; F:protein phosphatase activator activity; IGI:SGD.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IC:ComplexPortal.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:SGD.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:ComplexPortal.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Leucine-rich repeat; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..338
FT /note="Protein phosphatase 1 regulatory subunit SDS22"
FT /id="PRO_0000071447"
FT REPEAT 43..64
FT /note="LRR 1"
FT REPEAT 67..88
FT /note="LRR 2"
FT REPEAT 91..113
FT /note="LRR 3"
FT REPEAT 114..135
FT /note="LRR 4"
FT REPEAT 136..157
FT /note="LRR 5"
FT REPEAT 158..179
FT /note="LRR 6"
FT REPEAT 182..203
FT /note="LRR 7"
FT REPEAT 204..225
FT /note="LRR 8"
FT REPEAT 226..247
FT /note="LRR 9"
FT REPEAT 248..269
FT /note="LRR 10"
FT REPEAT 270..292
FT /note="LRR 11"
FT DOMAIN 306..338
FT /note="LRRCT"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 338 AA; 38887 MW; 1EF434C7276ABAEA CRC64;
MDKNSVNKDS EEKDERHKIE VVDDTNPDFI TADSELTQDL PDDVEVIDLV HLKIKSLEDL
NLYRFKNLKQ LCLRQNLIES ISEVEVLPHD KIVDLDFYDN KIKHISSNVN KLTKLTSLDL
SFNKIKHIKN LENLTDLENL YFVQNSISKI ENLSTLKSLK NLELGGNKVH SIEPDSFEGL
SNLEEIWLGK NSIPRLINLH PLKNLKILSI QSNKLKKIEN LEELTNLEEL YLSHNFITKI
EGLEKNLKLT TLDVTSNKIT SLENLNHLSN LTDIWASFNK IDQSFESLGE NLSALSRLET
IYLEGNPIQL ENKTSYRRKL TMNLPPSLQK IDATYIRG
