P32597 (STH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear protein STH1/NPS1
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase STH1
Chromatin structure-remodeling complex protein STH1
SNF2 homolog

Gene names

Name:	STH1
Synonyms:	NPS1
Ordered Locus Names:	YIL126W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts directly with SFH1, CSE4, histones H3, H4 and H2B, and via its N-terminus, with RSC8. Interacts with LDB7, NPL6 and RTT102. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Ref.6 Ref.7 Ref.8 Ref.16 Ref.18 Ref.20
Subcellular location	Nucleus. Note: Localizes to centromeric and flanking chromatin. Association of the RSC complex with these loci is dependent on this subunit. Ref.16
Miscellaneous	Present with 1990 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SNF2/RAD54 helicase family. Contains 1 bromo domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from direct assay Ref.10Ref.14. Source: UniProtKB G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.9. Source: UniProtKB chromatin remodeling at centromere Inferred from mutant phenotype Ref.16. Source: SGD chromosome segregation Inferred from genetic interaction Ref.16. Source: SGD cytoskeleton organization Inferred from genetic interaction Ref.15. Source: UniProtKB double-strand break repair Inferred from mutant phenotype PubMed 16024655. Source: SGD meiosis Inferred from mutant phenotype Ref.12. Source: UniProtKB nucleosome disassembly Inferred from direct assay PubMed 16492771. Source: SGD nucleosome positioning Inferred from mutant phenotype PubMed 21343911. Source: SGD regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB transcription elongation from RNA polymerase II promoter Inferred from direct assay PubMed 17081996. Source: SGD
Cellular_component	RSC complex Inferred from direct assay Ref.6. Source: UniProtKB chromosome, centromeric region Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA translocase activity Inferred from direct assay Ref.14. Source: SGD helicase activity Inferred from direct assay Ref.14. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay PubMed 20126658. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HHF2	P02309	4	EBI-18410,EBI-8113
HHT2	P61830	4	EBI-18410,EBI-8098
HTB1	P02293	3	EBI-18410,EBI-8088
HTL1	Q9URQ5	3	EBI-18410,EBI-8717
LDB7	P38210	2	EBI-18410,EBI-21189
NHP6A	P11632	3	EBI-18410,EBI-12019
RSC58	Q07979	6	EBI-18410,EBI-36549
RTT102	P53330	5	EBI-18410,EBI-23637

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1359	1359	Nuclear protein STH1/NPS1		PRO_0000074361
Regions
	Domain	307 – 383	77	HSA
	Domain	482 – 647	166	Helicase ATP-binding
	Domain	795 – 956	162	Helicase C-terminal
	Domain	1270 – 1340	71	Bromo
	Nucleotide binding	495 – 502	8	ATP Probable
	Motif	597 – 600	4	DEGH box
	Compositional bias	1198 – 1247	50	Lys-rich
Amino acid modifications
	Modified residue	38	1	Phosphoserine Ref.22
	Modified residue	51	1	Phosphoserine Ref.19 Ref.22
	Modified residue	52	1	Phosphoserine Ref.22
	Modified residue	964	1	Phosphoserine Ref.22
	Modified residue	1156	1	Phosphoserine Ref.22
	Modified residue	1166	1	Phosphothreonine Ref.22
	Modified residue	1187	1	Phosphoserine Ref.22
	Modified residue	1188	1	Phosphoserine Ref.22
	Modified residue	1232	1	Phosphoserine Ref.21
Experimental info
	Mutagenesis	505	1	S → F: Temperature-sensitive. Ref.9
	Mutagenesis	646	1	P → L: Temperature-sensitive. Ref.9
	Mutagenesis	763	1	C → Y: Temperature-sensitive. Reduced sporulation efficiency. Ref.12
	Mutagenesis	792	1	K → E: Complete inactivation.
	Mutagenesis	806	1	S → L: Temperature-sensitive; when associated with M-881. Altered cell cycle distribution. Ref.9
	Mutagenesis	881	1	T → M: Temperature-sensitive; when associated with L-806. Altered cell cycle distribution. Ref.9
	Sequence conflict	105 – 106	2	DK → NE in AAZ22501. Ref.3
	Sequence conflict	144	1	D → N in AAZ22501. Ref.3
	Sequence conflict	227	1	K → R in AAZ22501. Ref.3
	Sequence conflict	546	1	N → T in AAA35120. Ref.2
	Sequence conflict	566	1	V → I in AAZ22501. Ref.3
	Sequence conflict	1010	1	A → R in AAA35120. Ref.2
	Sequence conflict	1074 – 1080	7	Missing Ref.2
	Sequence conflict	1114	1	A → V in AAZ22501. Ref.3
	Sequence conflict	1157	1	I → V in AAZ22501. Ref.3
	Sequence conflict	1221	1	G → S in AAZ22501. Ref.3
	Sequence conflict	1246	1	S → P in AAZ22501. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P32597 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 269A91BD853C20D0	FASTA	1,359	156,743
	10 20 30 40 50 60 MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY 70 80 90 100 110 120 RYRAIQNHPK ENKLEIKAIE DTFRNISRDQ DIYETKLDTL RKSIDKGFQY DEDLLNKHLV 130 140 150 160 170 180 ALQLLEKDTD VPDYFLDLPD TKNDNTTAIE VDYSEKKPIK ISADFNAKAK SLGLESKFSN 190 200 210 220 230 240 ATKTALGDPD TEIRISARIS NRINELERLP ANLGTYSLDD CLEFITKDDL SSRMDTFKIK 250 260 270 280 290 300 ALVELKSLKL LTKQKSIRQK LINNVASQAH HNIPYLRDSP FTAAAQRSVQ IRSKVIVPQT 310 320 330 340 350 360 VRLAEELERQ QLLEKRKKER NLHLQKINSI IDFIKERQSE QWSRQERCFQ FGRLGASLHN 370 380 390 400 410 420 QMEKDEQKRI ERTAKQRLAA LKSNDEEAYL KLLDQTKDTR ITQLLRQTNS FLDSLSEAVR 430 440 450 460 470 480 AQQNEAKILH GEEVQPITDE EREKTDYYEV AHRIKEKIDK QPSILVGGTL KEYQLRGLEW 490 500 510 520 530 540 MVSLYNNHLN GILADEMGLG KTIQSISLIT YLYEVKKDIG PFLVIVPLST ITNWTLEFEK 550 560 570 580 590 600 WAPSLNTIIY KGTPNQRHSL QHQIRVGNFD VLLTTYEYII KDKSLLSKHD WAHMIIDEGH 610 620 630 640 650 660 RMKNAQSKLS FTISHYYRTR NRLILTGTPL QNNLPELWAL LNFVLPKIFN SAKTFEDWFN 670 680 690 700 710 720 TPFANTGTQE KLELTEEETL LIIRRLHKVL RPFLLRRLKK EVEKDLPDKV EKVIKCKLSG 730 740 750 760 770 780 LQQQLYQQML KHNALFVGAG TEGATKGGIK GLNNKIMQLR KICNHPFVFD EVEGVVNPSR 790 800 810 820 830 840 GNSDLLFRVA GKFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS 850 860 870 880 890 900 TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDWN PHQDLQAQDR 910 920 930 940 950 960 AHRIGQKNEV RILRLITTDS VEEVILERAM QKLDIDGKVI QAGKFDNKST AEEQEAFLRR 970 980 990 1000 1010 1020 LIESETNRDD DDKAELDDDE LNDTLARSAD EKILFDKIDK ERMNQERADA KAQGLRVPPP 1030 1040 1050 1060 1070 1080 RLIQLDELPK VFREDIEEHF KKEDSEPLGR IRQKKRVYYD DGLTEEQFLE AVEDDNMSLE 1090 1100 1110 1120 1130 1140 DAIKKRREAR ERRRLRQNGT KENEIETLEN TPEASETSLI ENNSFTAAVD EETNADKETT 1150 1160 1170 1180 1190 1200 ASRSKRRSSR KKRTISIVTA EDKENTQEES TSQENGGAKV EEEVKSSSVE IINGSESKKK 1210 1220 1230 1240 1250 1260 KPKLTVKIKL NKTTVLENND GKRAEEKPES KSPAKKTAAK KTKTKSKSLG IFPTVEKLVE 1270 1280 1290 1300 1310 1320 EMREQLDEVD SHPRTSIFEK LPSKRDYPDY FKVIEKPMAI DIILKNCKNG TYKTLEEVRQ 1330 1340 1350 ALQTMFENAR FYNEEGSWVY VDADKLNEFT DEWFKEHSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae NPS1 gene, a novel CDC gene which encodes a 160 kDa nuclear protein involved in G2 phase control." Tsuchiya E., Uno M., Kiguchi A., Masuoka K., Kanemori Y., Okabe S., Miyakawa T. EMBO J. 11:4017-4026(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family." Laurent B.C., Yang X., Carlson M. Mol. Cell. Biol. 12:1893-1902(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Quantitative trait loci mapped to single-nucleotide resolution in yeast." Deutschbauer A.M., Davis R.W. Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SK1.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"RSC, an essential, abundant chromatin-remodeling complex." Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D. Cell 87:1249-1260(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 961-987 AND 993-1002, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF THE RSC COMPLEX.
[7]	"Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae." Treich I., Carlson M. Mol. Cell. Biol. 17:1768-1775(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RSC8.
[8]	"Sfh1p, a component of a novel chromatin-remodeling complex, is required for cell cycle progression." Cao Y., Cairns B.R., Kornberg R.D., Laurent B.C. Mol. Cell. Biol. 17:3323-3334(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SFH1.
[9]	"Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins." Du J., Nasir I., Benton B.K., Kladde M.P., Laurent B.C. Genetics 150:987-1005(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-505; PRO-646; SER-806 AND THR-881.
[10]	"Histone octamer transfer by a chromatin-remodeling complex." Lorch Y., Zhang M., Kornberg R.D. Cell 96:389-392(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[11]	"Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC." Moreira J.M.A., Holmberg S. EMBO J. 18:2836-2844(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Nps1/Sth1p, a component of an essential chromatin-remodeling complex of Saccharomyces cerevisiae, is required for the maximal expression of early meiotic genes." Yukawa M., Katoh S., Miyakawa T., Tsuchiya E. Genes Cells 4:99-110(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-763.
[13]	"Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains." Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., Winston F. Mol. Cell 4:715-723(1999) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE RSC COMPLEX.
[14]	"Chromatin remodeling by RSC involves ATP-dependent DNA translocation." Saha A., Wittmeyer J., Cairns B.R. Genes Dev. 16:2120-2134(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway." Chai B., Hsu J.-M., Du J., Laurent B.C. Genetics 161:575-584(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX.
[16]	"The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation." Hsu J.-M., Huang J., Meluh P.B., Laurent B.C. Mol. Cell. Biol. 23:3202-3215(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE RSC COMPLEX, INTERACTION WITH CSE4 AND HISTONES H3; H4 AND H2B, SUBCELLULAR LOCATION.
[17]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]	"Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits." Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L. Biochem. Soc. Trans. 32:899-903(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RTT102.
[19]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Strain: YAL6B.
[20]	"The RSC chromatin remodeling complex bears an essential fungal-specific protein module with broad functional roles." Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R. Genetics 172:795-809(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LDB7 AND NPL6.
[21]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, MASS SPECTROMETRY.
[22]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-51; SER-52; SER-964; SER-1156; THR-1166; SER-1187 AND SER-1188, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D10595 Genomic DNA. Translation: BAA01446.1. M83755 Genomic DNA. Translation: AAA35120.1. DQ115392 Genomic DNA. Translation: AAZ22501.1. Z46833 Genomic DNA. Translation: CAA86866.1. BK006942 Genomic DNA. Translation: DAA08427.1.
PIR	S49883.
RefSeq	NP_012140.1. NM_001179474.1.
3D structure databases
ProteinModelPortal	P32597.
SMR	P32597. Positions 456-990, 1259-1356.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5889N.
IntAct	P32597. 62 interactions.
MINT	MINT-615490.
STRING	4932.YIL126W.
Proteomic databases
PaxDb	P32597.
PeptideAtlas	P32597.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL126W; YIL126W; YIL126W.
GeneID	854680.
KEGG	sce:YIL126W.
Organism-specific databases
CYGD	YIL126w.
SGD	S000001388. STH1.
Phylogenomic databases
eggNOG	COG0553.
GeneTree	ENSGT00670000098110.
HOGENOM	HOG000172362.
KO	K11786.
OMA	MEDFLRM.
OrthoDB	EOG4D565R.
Gene expression databases
Genevestigator	P32597.
GermOnline	YIL126W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.920.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR014012. Helicase/SANT-assoc_DNA-bd. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. [Graphical view]
Pfam	PF00439. Bromodomain. 1 hit. PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51204. HSA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977286.

Entry information

Entry name

STH1_YEAST

Accession

Primary (citable) accession number: P32597
Secondary accession number(s): D6VVG1, Q45U09

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program