ID STH1_YEAST Reviewed; 1359 AA.
AC P32597; D6VVG1; Q45U09;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 27-MAR-2024, entry version 228.
DE RecName: Full=Nuclear protein STH1/NPS1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase STH1;
DE AltName: Full=Chromatin structure-remodeling complex protein STH1;
DE AltName: Full=SNF2 homolog;
GN Name=STH1; Synonyms=NPS1; OrderedLocusNames=YIL126W;
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=1396591; DOI=10.1002/j.1460-2075.1992.tb05495.x;
RA Tsuchiya E., Uno M., Kiguchi A., Masuoka K., Kanemori Y., Okabe S.,
RA Miyakawa T.;
RT "The Saccharomyces cerevisiae NPS1 gene, a novel CDC gene which encodes a
RT 160 kDa nuclear protein involved in G2 phase control.";
RL EMBO J. 11:4017-4026(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1549132; DOI=10.1128/mcb.12.4.1893-1902.1992;
RA Laurent B.C., Yang X., Carlson M.;
RT "An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a
RT helicase-related protein in a new family.";
RL Mol. Cell. Biol. 12:1893-1902(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 961-987 AND 993-1002, IDENTIFICATION IN THE RSC
RP COMPLEX, AND FUNCTION OF THE RSC COMPLEX.
RX PubMed=8980231; DOI=10.1016/s0092-8674(00)81820-6;
RA Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H.,
RA Tempst P., Du J., Laurent B.C., Kornberg R.D.;
RT "RSC, an essential, abundant chromatin-remodeling complex.";
RL Cell 87:1249-1260(1996).
RN [7]
RP INTERACTION WITH RSC8.
RX PubMed=9121424; DOI=10.1128/mcb.17.4.1768;
RA Treich I., Carlson M.;
RT "Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-
RT related complex with an essential function in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:1768-1775(1997).
RN [8]
RP INTERACTION WITH SFH1.
RX PubMed=9154831; DOI=10.1128/mcb.17.6.3323;
RA Cao Y., Cairns B.R., Kornberg R.D., Laurent B.C.;
RT "Sfh1p, a component of a novel chromatin-remodeling complex, is required
RT for cell cycle progression.";
RL Mol. Cell. Biol. 17:3323-3334(1997).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF SER-505; PRO-646; SER-806 AND THR-881.
RX PubMed=9799253; DOI=10.1093/genetics/150.3.987;
RA Du J., Nasir I., Benton B.K., Kladde M.P., Laurent B.C.;
RT "Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential
RT ATPase in RSC and differs from Snf/Swi in its interactions with histones
RT and chromatin-associated proteins.";
RL Genetics 150:987-1005(1998).
RN [10]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=10025404; DOI=10.1016/s0092-8674(00)80551-6;
RA Lorch Y., Zhang M., Kornberg R.D.;
RT "Histone octamer transfer by a chromatin-remodeling complex.";
RL Cell 96:389-392(1999).
RN [11]
RP FUNCTION.
RX PubMed=10329629; DOI=10.1093/emboj/18.10.2836;
RA Moreira J.M.A., Holmberg S.;
RT "Transcriptional repression of the yeast CHA1 gene requires the chromatin-
RT remodeling complex RSC.";
RL EMBO J. 18:2836-2844(1999).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF CYS-763.
RX PubMed=10320476; DOI=10.1046/j.1365-2443.1999.00242.x;
RA Yukawa M., Katoh S., Miyakawa T., Tsuchiya E.;
RT "Nps1/Sth1p, a component of an essential chromatin-remodeling complex of
RT Saccharomyces cerevisiae, is required for the maximal expression of early
RT meiotic genes.";
RL Genes Cells 4:99-110(1999).
RN [13]
RP COMPOSITION OF THE RSC COMPLEX.
RX PubMed=10619019; DOI=10.1016/s1097-2765(00)80382-2;
RA Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D.,
RA Winston F.;
RT "Two functionally distinct forms of the RSC nucleosome-remodeling complex,
RT containing essential AT hook, BAH, and bromodomains.";
RL Mol. Cell 4:715-723(1999).
RN [14]
RP FUNCTION.
RX PubMed=12183366; DOI=10.1101/gad.995002;
RA Saha A., Wittmeyer J., Cairns B.R.;
RT "Chromatin remodeling by RSC involves ATP-dependent DNA translocation.";
RL Genes Dev. 16:2120-2134(2002).
RN [15]
RP FUNCTION OF THE RSC COMPLEX.
RX PubMed=12072455; DOI=10.1093/genetics/161.2.575;
RA Chai B., Hsu J.-M., Du J., Laurent B.C.;
RT "Yeast RSC function is required for organization of the cellular
RT cytoskeleton via an alternative PKC1 pathway.";
RL Genetics 161:575-584(2002).
RN [16]
RP FUNCTION OF THE RSC COMPLEX, INTERACTION WITH CSE4 AND HISTONES H3; H4 AND
RP H2B, AND SUBCELLULAR LOCATION.
RX PubMed=12697820; DOI=10.1128/mcb.23.9.3202-3215.2003;
RA Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.;
RT "The yeast RSC chromatin-remodeling complex is required for kinetochore
RT function in chromosome segregation.";
RL Mol. Cell. Biol. 23:3202-3215(2003).
RN [17]
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 [18]
RP INTERACTION WITH RTT102.
RX PubMed=15506919; DOI=10.1042/bst0320899;
RA Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P.,
RA Workman J.L.;
RT "Proteomic analysis of chromatin-modifying complexes in Saccharomyces
RT cerevisiae identifies novel subunits.";
RL Biochem. Soc. Trans. 32:899-903(2004).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [20]
RP INTERACTION WITH LDB7 AND NPL6.
RX PubMed=16204215; DOI=10.1534/genetics.105.047589;
RA Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.;
RT "The RSC chromatin remodeling complex bears an essential fungal-specific
RT protein module with broad functional roles.";
RL Genetics 172:795-809(2006).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [23]
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).
CC -!- FUNCTION: Catalytic component of the chromatin structure-remodeling
CC complex (RSC), which is involved in transcription regulation and
CC nucleosome positioning. RSC is responsible for the transfer of a
CC histone octamer from a nucleosome core particle to naked DNA. The
CC reaction requires ATP and involves an activated RSC-nucleosome
CC intermediate. Remodeling reaction also involves DNA translocation, DNA
CC twist and conformational change. As a reconfigurer of centromeric and
CC flanking nucleosomes, RSC complex is required both for proper
CC kinetochore function in chromosome segregation and, via a PKC1-
CC dependent signaling pathway, for organization of the cellular
CC cytoskeleton. This subunit is the essential ATPase of the complex. It
CC is a DNA translocase capable of nucleosome remodeling. Required for
CC full expression of early meiotic genes. Essential for mitotic growth
CC and repression of CHA1 expression. Also involved in G2 phase control.
CC {ECO:0000269|PubMed:10025404, ECO:0000269|PubMed:10320476,
CC ECO:0000269|PubMed:10329629, ECO:0000269|PubMed:12072455,
CC ECO:0000269|PubMed:12183366, ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:8980231, ECO:0000269|PubMed:9799253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts directly with SFH1, CSE4, histones H3, H4 and H2B,
CC and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and
CC RTT102. Component of the two forms of the RSC complex composed of at
CC least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30,
CC RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102.
CC The complexes interact with histone and histone variant components of
CC centromeric chromatin. {ECO:0000269|PubMed:12697820,
CC ECO:0000269|PubMed:15506919, ECO:0000269|PubMed:16204215,
CC ECO:0000269|PubMed:8980231, ECO:0000269|PubMed:9121424,
CC ECO:0000269|PubMed:9154831}.
CC -!- INTERACTION:
CC P32597; P02309: HHF2; NbExp=4; IntAct=EBI-18410, EBI-8113;
CC P32597; P61830: HHT2; NbExp=4; IntAct=EBI-18410, EBI-8098;
CC P32597; P02293: HTB1; NbExp=3; IntAct=EBI-18410, EBI-8088;
CC P32597; Q9URQ5: HTL1; NbExp=3; IntAct=EBI-18410, EBI-8717;
CC P32597; P38210: LDB7; NbExp=2; IntAct=EBI-18410, EBI-21189;
CC P32597; P11632: NHP6A; NbExp=3; IntAct=EBI-18410, EBI-12019;
CC P32597; P38181: NUP170; NbExp=3; IntAct=EBI-18410, EBI-11756;
CC P32597; Q07979: RSC58; NbExp=6; IntAct=EBI-18410, EBI-36549;
CC P32597; P53330: RTT102; NbExp=5; IntAct=EBI-18410, EBI-23637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and
CC flanking chromatin. Association of the RSC complex with these loci is
CC dependent on this subunit.
CC -!- MISCELLANEOUS: Present with 1990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; D10595; BAA01446.1; -; Genomic_DNA.
DR EMBL; M83755; AAA35120.1; -; Genomic_DNA.
DR EMBL; DQ115392; AAZ22501.1; -; Genomic_DNA.
DR EMBL; Z46833; CAA86866.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08427.1; -; Genomic_DNA.
DR PIR; S49883; S49883.
DR RefSeq; NP_012140.1; NM_001179474.1.
DR PDB; 6K15; EM; 3.40 A; J=1-1359.
DR PDB; 6KMB; X-ray; 2.40 A; A/B/C/D=1248-1359.
DR PDB; 6KMJ; X-ray; 1.40 A; A=1248-1359.
DR PDB; 6KW3; EM; 7.13 A; J/W/Y=1-1359.
DR PDB; 6KW4; EM; 7.55 A; J/V/Y=1-1359.
DR PDB; 6KW5; EM; 10.13 A; J/P/Q=1-1359.
DR PDB; 6LQZ; NMR; -; B=1183-1240.
DR PDB; 6MR4; X-ray; 2.71 A; A/B/C/D/E/F=1250-1359.
DR PDB; 6TDA; EM; 15.00 A; S=1-1359.
DR PDB; 6UY1; X-ray; 2.21 A; A/B/C/D/E/F/G/H=1250-1359.
DR PDB; 6V8O; EM; 3.07 A; R=1-1359.
DR PDB; 6V92; EM; 20.00 A; R=1-1359.
DR PDB; 6VZ4; EM; 3.90 A; K=301-1097.
DR PDB; 6VZG; EM; 4.20 A; K=301-1097.
DR PDB; 7F3S; X-ray; 1.40 A; A=1248-1359.
DR PDBsum; 6K15; -.
DR PDBsum; 6KMB; -.
DR PDBsum; 6KMJ; -.
DR PDBsum; 6KW3; -.
DR PDBsum; 6KW4; -.
DR PDBsum; 6KW5; -.
DR PDBsum; 6LQZ; -.
DR PDBsum; 6MR4; -.
DR PDBsum; 6TDA; -.
DR PDBsum; 6UY1; -.
DR PDBsum; 6V8O; -.
DR PDBsum; 6V92; -.
DR PDBsum; 6VZ4; -.
DR PDBsum; 6VZG; -.
DR PDBsum; 7F3S; -.
DR AlphaFoldDB; P32597; -.
DR EMDB; EMD-0777; -.
DR EMDB; EMD-0778; -.
DR EMDB; EMD-0779; -.
DR EMDB; EMD-10465; -.
DR EMDB; EMD-21107; -.
DR EMDB; EMD-21114; -.
DR EMDB; EMD-21484; -.
DR EMDB; EMD-21489; -.
DR EMDB; EMD-9905; -.
DR SMR; P32597; -.
DR BioGRID; 34865; 234.
DR ComplexPortal; CPX-1888; RSC chromatin remodelling complex, variant RSC2.
DR ComplexPortal; CPX-1889; RSC chromatin remodelling complex, variant RSC1.
DR DIP; DIP-5889N; -.
DR IntAct; P32597; 68.
DR MINT; P32597; -.
DR STRING; 4932.YIL126W; -.
DR iPTMnet; P32597; -.
DR MaxQB; P32597; -.
DR PaxDb; 4932-YIL126W; -.
DR PeptideAtlas; P32597; -.
DR EnsemblFungi; YIL126W_mRNA; YIL126W; YIL126W.
DR GeneID; 854680; -.
DR KEGG; sce:YIL126W; -.
DR AGR; SGD:S000001388; -.
DR SGD; S000001388; STH1.
DR VEuPathDB; FungiDB:YIL126W; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_3_1; -.
DR InParanoid; P32597; -.
DR OMA; VNYISHT; -.
DR OrthoDB; 5482994at2759; -.
DR BioCyc; YEAST:G3O-31377-MONOMER; -.
DR BioGRID-ORCS; 854680; 2 hits in 10 CRISPR screens.
DR PRO; PR:P32597; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32597; Protein.
DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016586; C:RSC-type complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0015616; F:DNA translocase activity; IDA:SGD.
DR GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0031055; P:chromatin remodeling at centromere; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IGI:SGD.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD.
DR CDD; cd04369; Bromodomain; 1.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd22568; EBM_STH1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF1012; NUCLEAR PROTEIN STH1_NPS1; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Bromodomain; Cell cycle; Chromatin regulator;
KW Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1359
FT /note="Nuclear protein STH1/NPS1"
FT /id="PRO_0000074361"
FT DOMAIN 307..383
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 482..647
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 795..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1270..1340
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1090..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..600
FT /note="DEGH box"
FT COMPBIAS 1090..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 505
FT /note="S->F: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:9799253"
FT MUTAGEN 646
FT /note="P->L: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:9799253"
FT MUTAGEN 763
FT /note="C->Y: Temperature-sensitive. Reduced sporulation
FT efficiency."
FT /evidence="ECO:0000269|PubMed:10320476"
FT MUTAGEN 792
FT /note="K->E: Complete inactivation."
FT MUTAGEN 806
FT /note="S->L: Temperature-sensitive; when associated with M-
FT 881. Altered cell cycle distribution."
FT /evidence="ECO:0000269|PubMed:9799253"
FT MUTAGEN 881
FT /note="T->M: Temperature-sensitive; when associated with L-
FT 806. Altered cell cycle distribution."
FT /evidence="ECO:0000269|PubMed:9799253"
FT CONFLICT 105..106
FT /note="DK -> NE (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="D -> N (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> R (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="N -> T (in Ref. 2; AAA35120)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="V -> I (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="A -> R (in Ref. 2; AAA35120)"
FT /evidence="ECO:0000305"
FT CONFLICT 1074..1080
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1114
FT /note="A -> V (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 1157
FT /note="I -> V (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 1221
FT /note="G -> S (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="S -> P (in Ref. 3; AAZ22501)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:6K15"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6K15"
FT TURN 26..33
FT /evidence="ECO:0007829|PDB:6K15"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 75..101
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6V8O"
FT TURN 220..224
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 251..266
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:6V8O"
FT HELIX 299..317
FT /evidence="ECO:0007829|PDB:6V8O"
FT STRAND 1205..1209
FT /evidence="ECO:0007829|PDB:6LQZ"
FT STRAND 1213..1215
FT /evidence="ECO:0007829|PDB:6LQZ"
FT HELIX 1252..1263
FT /evidence="ECO:0007829|PDB:6KMJ"
FT TURN 1268..1270
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 1276..1278
FT /evidence="ECO:0007829|PDB:6KMJ"
FT TURN 1284..1286
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 1290..1293
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 1300..1308
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 1315..1332
FT /evidence="ECO:0007829|PDB:6KMJ"
FT HELIX 1338..1356
FT /evidence="ECO:0007829|PDB:6KMJ"
SQ SEQUENCE 1359 AA; 156743 MW; 269A91BD853C20D0 CRC64;
MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY
RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL RKSIDKGFQY DEDLLNKHLV
ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE VDYSEKKPIK ISADFNAKAK SLGLESKFSN
ATKTALGDPD TEIRISARIS NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK
ALVELKSLKL LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT
VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ FGRLGASLHN
QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR ITQLLRQTNS FLDSLSEAVR
AQQNEAKILH GEEVQPITDE EREKTDYYEV AHRIKEKIDK QPSILVGGTL KEYQLRGLEW
MVSLYNNHLN GILADEMGLG KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK
WAPSLNTIIY KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH
RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN SAKTFEDWFN
TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK EVEKDLPDKV EKVIKCKLSG
LQQQLYQQML KHNALFVGAG TEGATKGGIK GLNNKIMQLR KICNHPFVFD EVEGVVNPSR
GNSDLLFRVA GKFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS
TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR
AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST AEEQEAFLRR
LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK ERMNQERADA KAQGLRVPPP
RLIQLDELPK VFREDIEEHF KKEDSEPLGR IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE
DAIKKRREAR ERRRLRQNGT KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT
ASRSKRRSSR KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK
KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG IFPTVEKLVE
EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI DIILKNCKNG TYKTLEEVRQ
ALQTMFENAR FYNEEGSWVY VDADKLNEFT DEWFKEHSS
//
