SAN1_YEAST
ID SAN1_YEAST Reviewed; 610 AA.
AC P22470; D6VSC6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein SAN1;
GN Name=SAN1; OrderedLocusNames=YDR143C; ORFNames=YD2943.02C;
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=2471670; DOI=10.1093/genetics/122.1.29;
RA Schnell R., D'Ari L., Foss M., Goodman D., Rine J.;
RT "Genetic and molecular characterization of suppressors of SIR4 mutations in
RT Saccharomyces cerevisiae.";
RL Genetics 122:29-46(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP IDENTIFICATION BY 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).
RN [6]
RP IDENTIFICATION BY MASS 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: Plays a specific role in mating-type regulation of yeast, by
CC acting post-translationally to control the stability or activity of the
CC SIR4 proteins.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X90585; CAA62213.1; -; Genomic_DNA.
DR EMBL; Z54139; CAA90812.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11986.1; -; Genomic_DNA.
DR PIR; S05807; S05807.
DR RefSeq; NP_010427.3; NM_001180450.3.
DR AlphaFoldDB; P22470; -.
DR SMR; P22470; -.
DR BioGRID; 32197; 201.
DR DIP; DIP-6517N; -.
DR IntAct; P22470; 24.
DR MINT; P22470; -.
DR STRING; 4932.YDR143C; -.
DR TCDB; 3.A.16.1.6; the endoplasmic reticular retrotranslocon (er-rt) family.
DR CarbonylDB; P22470; -.
DR iPTMnet; P22470; -.
DR MaxQB; P22470; -.
DR PaxDb; P22470; -.
DR PRIDE; P22470; -.
DR EnsemblFungi; YDR143C_mRNA; YDR143C; YDR143C.
DR GeneID; 851721; -.
DR KEGG; sce:YDR143C; -.
DR SGD; S000002550; SAN1.
DR VEuPathDB; FungiDB:YDR143C; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_020039_0_0_1; -.
DR InParanoid; P22470; -.
DR OMA; HIFGREC; -.
DR BioCyc; YEAST:G3O-29740-MON; -.
DR PRO; PR:P22470; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P22470; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0051788; P:response to misfolded protein; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR DisProt; DP01136; -.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..610
FT /note="Protein SAN1"
FT /id="PRO_0000056162"
FT ZN_FING 240..280
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 65618 MW; 15D9B5B1A8E3594E CRC64;
MSESGQEQNR GTNTSPNNAE NNNNSNAASG PLNGGAEQTR NITVSIQYSY FTPERLAHLS
NISNNDNNEN NSAASGSTIA NGTGPSFGIG NGGHQPDGAL VLSFRDVPAS TPQDRLNSFI
SVAAQLAMER FNRLLNRPKG ISKDEFDKLP VLQVSDLPKA EGPLCSICYD EYEDEVDSTK
AKRKRDSENE EESEGTKKRK DNEGAPLRTT ADNDSNPSIT NATVVEPPSI PLTEQQRTLN
DEETNPSYKH SPIKLPCGHI FGRECIYKWS RLENSCPLCR QKISESVGVQ RAAQQDTDEV
AANEAAFERI RRVLYDPTAV NSTNENSSAP SENTSNTTVP TIGNASSGEQ MLSRTGFFLV
PQNGQPLHNP VRLPPNDSDR NGVNGPSSTT QNPPSNSGGS NNNQSPRWVP IPLTLFQFHS
PNPNPSASDS SASPSAANGP NSNNTSSDAT DPHHNRLRAV LDHIFNVAQR GTSDTSATTA
PGAQTVHNQG RNDSSSSDTT QGSSFLENIS RLTGHFTNGS RDNNNDNNHS NDQQRGGSTG
ENNRNNLFSS GVASYRNQNG DVTTVELRNN NSAAFPPTDE NPSQGQGSSS SDTTIHNDVP
NDNNEQRSSQ
