Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear protein STH1/NPS1

Gene

STH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi495 – 502ATPCurated8

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • DNA-dependent ATPase activity Source: SGD
  • DNA translocase activity Source: SGD
  • helicase activity Source: UniProtKB
  • lysine-acetylated histone binding Source: SGD

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • base-excision repair Source: SGD
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling at centromere Source: SGD
  • chromosome segregation Source: SGD
  • cytoskeleton organization Source: UniProtKB
  • double-strand break repair Source: SGD
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • meiotic nuclear division Source: UniProtKB
  • nucleosome disassembly Source: SGD
  • nucleosome positioning Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transfer RNA gene-mediated silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31377-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:STH1
Synonyms:NPS1
Ordered Locus Names:YIL126W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL126W.
SGDiS000001388. STH1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

  • Note: Localizes to centromeric and flanking chromatin. Association of the RSC complex with these loci is dependent on this subunit.

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • nucleus Source: SGD
  • RSC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi505S → F: Temperature-sensitive. 1 Publication1
Mutagenesisi646P → L: Temperature-sensitive. 1 Publication1
Mutagenesisi763C → Y: Temperature-sensitive. Reduced sporulation efficiency. 1 Publication1
Mutagenesisi792K → E: Complete inactivation. 1
Mutagenesisi806S → L: Temperature-sensitive; when associated with M-881. Altered cell cycle distribution. 1 Publication1
Mutagenesisi881T → M: Temperature-sensitive; when associated with L-806. Altered cell cycle distribution. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000743611 – 1359Nuclear protein STH1/NPS1Add BLAST1359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32597.
PRIDEiP32597.

PTM databases

iPTMnetiP32597.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023094EBI-18410,EBI-8113
HHT2P618304EBI-18410,EBI-8098
HTB1P022933EBI-18410,EBI-8088
HTL1Q9URQ53EBI-18410,EBI-8717
LDB7P382102EBI-18410,EBI-21189
NHP6AP116323EBI-18410,EBI-12019
NUP170P381813EBI-18410,EBI-11756
RSC58Q079796EBI-18410,EBI-36549
RTT102P533305EBI-18410,EBI-23637

GO - Molecular functioni

  • lysine-acetylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi34865. 170 interactors.
DIPiDIP-5889N.
IntActiP32597. 66 interactors.
MINTiMINT-615490.

Structurei

3D structure databases

ProteinModelPortaliP32597.
SMRiP32597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini307 – 383HSAPROSITE-ProRule annotationAdd BLAST77
Domaini482 – 647Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST166
Domaini795 – 956Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162
Domaini1270 – 1340BromoPROSITE-ProRule annotationAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi597 – 600DEGH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1198 – 1247Lys-richAdd BLAST50

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HSA domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172362.
InParanoidiP32597.
KOiK11786.
OMAiFTISHYY.
OrthoDBiEOG092C1YH4.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM01314. SnAC. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00633. 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]

Sequencei

Sequence statusi: Complete.

P32597-1 [UniParc]FASTAAdd to basket

« Hide

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

DEWFKEHSS
Length:1,359
Mass (Da):156,743
Last modified:October 1, 1993 - v1
Checksum:i269A91BD853C20D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti105 – 106DK → NE in AAZ22501 (PubMed:16273108).Curated2
Sequence conflicti144D → N in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti227K → R in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti546N → T in AAA35120 (PubMed:1549132).Curated1
Sequence conflicti566V → I in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti1010A → R in AAA35120 (PubMed:1549132).Curated1
Sequence conflicti1074 – 1080Missing (PubMed:1549132).Curated7
Sequence conflicti1114A → V in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti1157I → V in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti1221G → S in AAZ22501 (PubMed:16273108).Curated1
Sequence conflicti1246S → P in AAZ22501 (PubMed:16273108).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS49883.
RefSeqiNP_012140.1. NM_001179474.1.

Genome annotation databases

EnsemblFungiiYIL126W; YIL126W; YIL126W.
GeneIDi854680.
KEGGisce:YIL126W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS49883.
RefSeqiNP_012140.1. NM_001179474.1.

3D structure databases

ProteinModelPortaliP32597.
SMRiP32597.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34865. 170 interactors.
DIPiDIP-5889N.
IntActiP32597. 66 interactors.
MINTiMINT-615490.

PTM databases

iPTMnetiP32597.

Proteomic databases

MaxQBiP32597.
PRIDEiP32597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL126W; YIL126W; YIL126W.
GeneIDi854680.
KEGGisce:YIL126W.

Organism-specific databases

EuPathDBiFungiDB:YIL126W.
SGDiS000001388. STH1.

Phylogenomic databases

GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172362.
InParanoidiP32597.
KOiK11786.
OMAiFTISHYY.
OrthoDBiEOG092C1YH4.

Enzyme and pathway databases

BioCyciYEAST:G3O-31377-MONOMER.

Miscellaneous databases

PROiP32597.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM01314. SnAC. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00633. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiSTH1_YEAST
AccessioniPrimary (citable) accession number: P32597
Secondary accession number(s): D6VVG1, Q45U09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 2, 2016
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1990 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.