ULS1_YEAST
ID ULS1_YEAST Reviewed; 1619 AA.
AC Q08562; D6W2P7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=ATP-dependent helicase ULS1;
DE EC=3.6.4.-;
DE AltName: Full=Role in silencing protein 1;
DE AltName: Full=Ubiquitin ligase for SUMO conjugates protein 1;
GN Name=ULS1; Synonyms=DIS1, RIS1, TID4; OrderedLocusNames=YOR191W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP FUNCTION, AND INTERACTION WITH SIR4.
RX PubMed=9271422; DOI=10.1128/mcb.17.9.5461;
RA Zhang Z., Buchman A.R.;
RT "Identification of a member of a DNA-dependent ATPase family that causes
RT interference with silencing.";
RL Mol. Cell. Biol. 17:5461-5472(1997).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH UBC4 AND SMT3.
RX PubMed=17728242; DOI=10.1074/jbc.m706505200;
RA Uzunova K., Goettsche K., Miteva M., Weisshaar S.R., Glanemann C.,
RA Schnellhardt M., Niessen M., Scheel H., Hofmann K., Johnson E.S.,
RA Praefcke G.J.K., Dohmen R.J.;
RT "Ubiquitin-dependent proteolytic control of SUMO conjugates.";
RL J. Biol. Chem. 282:34167-34175(2007).
RN [6]
RP INTERACTION WITH EBP2; CDC3 AND CDC11, AND SUBCELLULAR LOCATION.
RX PubMed=18603780; DOI=10.1271/bbb.80131;
RA Shirai C., Mizuta K.;
RT "SUMO mediates interaction of Ebp2p, the yeast homolog of Epstein-Barr
RT virus nuclear antigen 1-binding protein 2, with a RING finger protein
RT Ris1p.";
RL Biosci. Biotechnol. Biochem. 72:1881-1886(2008).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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: ATP-dependent helicase involved mating type switching and in
CC silencing interference through its interaction with the silencing
CC regulator SIR4. Cooperates with UBC4 and UBC5 to mediate ubiquitination
CC of SUMO conjugates. {ECO:0000269|PubMed:17728242,
CC ECO:0000269|PubMed:9271422}.
CC -!- SUBUNIT: Interacts with CDC3, CDC11, EBP2, SIR4, UBC4 and SUMO/SMT3.
CC {ECO:0000269|PubMed:17728242, ECO:0000269|PubMed:18603780,
CC ECO:0000269|PubMed:9271422}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18603780}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; Z75099; CAA99400.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10963.1; -; Genomic_DNA.
DR PIR; S67083; S67083.
DR RefSeq; NP_014834.1; NM_001183610.1.
DR AlphaFoldDB; Q08562; -.
DR SMR; Q08562; -.
DR BioGRID; 34586; 202.
DR DIP; DIP-996N; -.
DR IntAct; Q08562; 8.
DR MINT; Q08562; -.
DR STRING; 4932.YOR191W; -.
DR iPTMnet; Q08562; -.
DR MaxQB; Q08562; -.
DR PaxDb; Q08562; -.
DR PRIDE; Q08562; -.
DR EnsemblFungi; YOR191W_mRNA; YOR191W; YOR191W.
DR GeneID; 854363; -.
DR KEGG; sce:YOR191W; -.
DR SGD; S000005717; ULS1.
DR VEuPathDB; FungiDB:YOR191W; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_34_1_1; -.
DR InParanoid; Q08562; -.
DR OMA; VHRLFIK; -.
DR BioCyc; YEAST:G3O-33700-MON; -.
DR PRO; PR:Q08562; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08562; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032183; F:SUMO binding; IPI:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1619
FT /note="ATP-dependent helicase ULS1"
FT /id="PRO_0000268702"
FT DOMAIN 956..1157
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1447..1606
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 1330..1386
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 86..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..10
FT /note="SUMO interacting motif; type a 1"
FT MOTIF 371..378
FT /note="SUMO interacting motif; type b 1"
FT MOTIF 470..473
FT /note="SUMO interacting motif; type a 2"
FT MOTIF 543..550
FT /note="SUMO interacting motif; type b 2"
FT COMPBIAS 86..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 969..976
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1619 AA; 184406 MW; FCE20374085B0605 CRC64;
MAAVPTIDLT LADSDNEDIF HSFSSSTSVD KIDIRKENGK LRMAGLEVAQ SNDDAARQAF
HVFKTNISNN ETFDTILSKS KTITDSTFNN EKSSNEVKQQ QVLKEETMGS SNDEKKTQES
SPSAEMIKLF YENDDVPLSD SFKQKEEGKR INQDEQVKEN ICGISSSYVS KDYDGVEDDF
EPNTCQDSNL DFQEEKLNLN NKPSQQQFSD PETKDNSLKS ENKDQIKGVT TTSYRDLPIE
SSAFQDSETQ NNSKNTIPNI VNEKRTPALP SNLSSVESSL KNETAKVEGK TTVRLPGLQN
NVALLEQEQS ELFKHFSEQP VDISDFGRKI KRKHSGDFAD NKILKRPILP SKNMDHTTHN
SHDSEQKNSS IIILSDEDES GAGINDIESP LKVSEPNTAD ALRSSVPEVI SLLDLPNIDL
NNSVIKEASG SNSIPTSETD AQSSSSSVLQ GTIMTEQATQ SSQHECNSSL DTLKKNHQKL
LKDLNSRESE LRNALSCCKT NSEILRRKLS RREKEVSDAE KHWQLLLTSM ARGGRTISST
QQILVDEAEN QLNKLKEKRQ LTKSKLDSIN LKMYNYNEQW KSFVHSKNIN LQKSLAALER
SARDSKASAT VNKRNECLAE KEKLDQMLKE GTLSFSTYKQ LTGEIQQKLN DLKLGDQRTT
DINSVLPIVR QPLAKRDLFI KSIDTAKDLL AKNTSRTEMT KRILYRHLDN LVSYKNFFED
GRSLIDINRR HVAHESAQIL FTNGVKMPIV FETLQDYGIK FSNPAIVNPD RRAQYFKSIE
VARDLISKST RSEDAKRKIT RFLNIIEEFR KDIDTGFPPT PLKREGVGKA VVGLRQQGLK
MDRLYENLRR YKIPITSEEL LQQSYLFPVN ADQRPPSNWN IVENTEDTSS TANDLSMQDE
FHISNMHAAE DQEQIRALLE NVKQSESIID GEALTPEDMT VNLLKHQRLG LHWLLQVENS
AKKGGLLADD MGLGKTIQAI ALMLANRSEE SKCKTNLIVA PVSVLRVWKG ELETKVKKRA
KFTTFIFGGS GNGKVKHWRD LARYDAVLVS YQTLANEFKK HWPKKLDGEQ NQLPAVPHIQ
ALNRLKTSNE YYSPFFCNDS TFYRILLDEG QNIKNKNTRA SKACCTINGM YRWVLSGTPI
QNSMDELYSL IRFLRIPPYH KEQRFKLDIG RFFQRNKQYQ YDNEDRKNAL RKVRVLLNAI
MLRRSKADKI DGKPLLELPP KIVEVDESRL KGEELKFYTA LESKNQALAK KLLNNSTRGS
YSSVLTLLLR LRQACCHSEL VVMGEKKAEG TKVANGKSFE DDWLRLYYKI THMSGEAQAQ
VITSMNSMTC FWCMEQLEPE AMSVLTGCGH LICDTCIEPF IEESSMLPQA KKTKGGAFAI
PCKDCQRLTN EKDIVSHKLY DQVINQGFTE EDLHAEYLSE MEKQKIQQKN VYVPNFESLE
PSTKIEQCIQ VIQRVFDESA TEKIIIFSQF TTFFEILEHF LKNKLNFPYL KYIGSMNAQR
RSDVINEFYR DPEKRILLIS MKAGNSGLTL TCANHVVIVD PFWNPYVEEQ AQDRCYRISQ
TKKVQVHKLF IKDSVEDRIS ELQKRKKEMV DSAMDPGKIK EVNSLGRREL GFLFGLNAL
