SA185_YEAST
ID SA185_YEAST Reviewed; 1058 AA.
AC P40856; D6VW86;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=SIT4-associating protein SAP185;
GN Name=SAP185; OrderedLocusNames=YJL098W; ORFNames=J0840;
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].
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871887; DOI=10.1002/yea.320101112;
RA Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S.,
RA Zimmermann F.K.;
RT "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces
RT cerevisiae chromosome X including the BCK1 gene.";
RL Yeast 10:1481-1488(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-853.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [6]
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 [7]
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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Associates with the SIT4 phosphatase in a cell cycle
CC dependent manner. May be directly or indirectly involved in SIT4-
CC dependent functions in budding and in normal G1 cyclin expression.
CC -!- INTERACTION:
CC P40856; P20604: SIT4; NbExp=9; IntAct=EBI-16384, EBI-13707;
CC -!- PTM: Hyperphosphorylated in the absence of SIT4.
CC -!- MISCELLANEOUS: Present with 11200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
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DR EMBL; X77923; CAA54892.1; -; Genomic_DNA.
DR EMBL; X85021; CAA59396.1; -; Genomic_DNA.
DR EMBL; Z49373; CAA89392.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08702.1; -; Genomic_DNA.
DR PIR; S50295; S50295.
DR RefSeq; NP_012437.1; NM_001181531.1.
DR AlphaFoldDB; P40856; -.
DR BioGRID; 33659; 195.
DR ComplexPortal; CPX-1865; SIT4-SAP185 phosphatase complex.
DR DIP; DIP-5851N; -.
DR IntAct; P40856; 83.
DR MINT; P40856; -.
DR STRING; 4932.YJL098W; -.
DR iPTMnet; P40856; -.
DR MaxQB; P40856; -.
DR PaxDb; P40856; -.
DR PRIDE; P40856; -.
DR EnsemblFungi; YJL098W_mRNA; YJL098W; YJL098W.
DR GeneID; 853347; -.
DR KEGG; sce:YJL098W; -.
DR SGD; S000003634; SAP185.
DR VEuPathDB; FungiDB:YJL098W; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_003676_2_0_1; -.
DR InParanoid; P40856; -.
DR OMA; WDMDVQF; -.
DR BioCyc; YEAST:G3O-31553-MON; -.
DR PRO; PR:P40856; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40856; 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; IC:ComplexPortal.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Isopeptide bond; Reference proteome; Ubl conjugation.
FT CHAIN 1..1058
FT /note="SIT4-associating protein SAP185"
FT /id="PRO_0000046106"
FT REGION 34..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..833
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 1058 AA; 121403 MW; DD44DD53DDD87438 CRC64;
MSGSFWKFGQ DFGSQSPLAK LLNRAFIKID DKPTSTEAGK IDSNSTDESL ESNSFKSEDE
EEEYELPNRE EDYKAYKPNL SLLNDLLDDE ELYTELMCSN FKLLVYLKYP EVLSKLIDYV
RNSTILESNI DRVTSEDRDL VRGEDKDTTE DFENAKADKK NIDGTFEEKE RTRSGEEEEL
ENEENDSASE DTRVTLPHEL EEHDDTRRAR IAAEILSADV WPISSALIEN EGLLAKLWSI
LRLPSPLSIE ASTYFMKINE RLLDMNMDGI IEFILKKEHI VDDFLAHIDN PPLMDFLLKV
ISTDKPEISN GVIQLFKKQN LVPKLIHLLD PVFDSCTQSA AGDFLKALVT ISGNCPNEIT
SSIGPNELTR QLVSPNMMKQ LMDIMLKGGN SLNNGVGIII ELIRKNNSDY DTIQTNYTTI
ESHPPTDRDP IYLGYLVKMF SEHMADFNKI LTEKKIPLLQ TSYGTIEPLG FERFKICELI
AELLHCSNMT LLNEPSAYDI VRERDAERER IFNSQNYVDS NDRSELKENE DDNTGDADDE
VEDDTNQVES ANTSIDGEEV IDKLNSLQIE TNKVNQNMNN EEQHSLMPDF NNGDFKDEED
ENPFEPQYSD VILDSSDIEK NFRVSPNVGD QLKISLQDTR VIDTMLEMFF HFQWNNFLHN
VVYDVVQQIF NGPLKIGYNR FLLDDLLINI RLTDMIINGN NECIEYEKGH DTRLGYMGHL
TLIAEEVTKF TAYIEEMNIT FENTEVMSSL FESKWIAYTE DVLEDLKEKY NAILGDIAEE
GDMLQDEEED AVYDKGERTM GTVDDYINDI MQMDNVRCQE EEEDEGEGYV SFDEDEPQEY
RNGDSVRSKE SNSSEGKRDQ EQLYYEYVNE DGTKTRLNFN PDSDATEQVP GEVNRDHKIP
LKLKRSFTDA CKSETIPNNT VNAKEESVFQ FSNELSDGWE SSPSNSIPKR ASPSKNGMNS
PMFQHQFELH SPTDEFGGHK DEILSAEGHD YDIDEYDELS DDSDEEYDNC EDEDSLDYAD
SAAYALCRSK SKDKISWDEE EQARLMGVVK FNSEHYRD
