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Protein

Chromatin structure-remodeling complex subunit SFH1

Gene

SFH1

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

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 essential for mitotic growth and required for cell cycle progression.7 Publications

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • chromatin remodeling at centromere Source: SGD
  • chromosome segregation Source: SGD
  • double-strand break repair Source: SGD
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • nucleosome disassembly Source: SGD
  • regulation of nuclear cell cycle DNA replication Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32405-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin structure-remodeling complex subunit SFH1
Alternative name(s):
RSC complex subunit SFH1
SNF5 homolog 1
Gene namesi
Name:SFH1
Ordered Locus Names:YLR321C
ORF Names:L8543.4
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR321C.
SGDiS000004313. SFH1.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.

GO - Cellular componenti

  • nuclear chromosome Source: InterPro
  • RSC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Chromatin structure-remodeling complex subunit SFH1PRO_0000205962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in the G1 phase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06168.
PeptideAtlasiQ06168.

PTM databases

iPTMnetiQ06168.

Interactioni

Subunit structurei

Interacts directly with STH1. 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
YLR345WQ061373EBI-35813,EBI-33827

Protein-protein interaction databases

BioGridi31585. 54 interactions.
DIPiDIP-1898N.
IntActiQ06168. 33 interactions.
MINTiMINT-398787.

Structurei

3D structure databases

ProteinModelPortaliQ06168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 24242Interaction with STH1Add
BLAST

Sequence similaritiesi

Belongs to the SNF5 family.Curated

Phylogenomic databases

HOGENOMiHOG000074513.
InParanoidiQ06168.
KOiK11770.
OMAiRNMRRLK.
OrthoDBiEOG7HHX3G.

Family and domain databases

InterProiIPR006939. SNF5.
IPR017393. SWI_SNF_chromatin_remodel_cplx.
[Graphical view]
PANTHERiPTHR10019. PTHR10019. 1 hit.
PfamiPF04855. SNF5. 2 hits.
[Graphical view]
PIRSFiPIRSF038126. SWI_SNF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q06168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHQNQLIPQ AYISNFHNRL TNEDDGIPIF TMAQQTRQHK RAKVVNYAEY
60 70 80 90 100
DNDLFDEFNM NGSNFNNADT HYKDNAVSHE NTPALTNGVT MDGSEYNVLE
110 120 130 140 150
NMNGADSIIS NNKYDAGSNM VVESLSGLNS NNNASNGPSN KAQAQDIGNA
160 170 180 190 200
VLPDLQDQHH NPFNILRYPK IRDTFINGKV VSPYRLNTDQ ETKANANSGE
210 220 230 240 250
AIMIPITLDI EHMGHTIKDQ FLWNYNDDSI SPEEFASIYC KDLDMTSATL
260 270 280 290 300
QTQIANIIKE QLKDLENIAA TEIMSDLHVI INLTCNLQDR FFEDNFQWNL
310 320 330 340 350
NDKSLTPERF ATSIVQDLGL TREFIPLISQ SLHETILKIK KDWVDGHLIQ
360 370 380 390 400
DHVPNDAAFG YLSGIRLDID ELGSNWCPRV EILTKEEIQK REIEKERNLR
410 420
RLKRETDRLS RRGRRRLDDL ETTMRM
Length:426
Mass (Da):48,777
Last modified:November 1, 1996 - v1
Checksum:iC8D6F151249E8479
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20618 Genomic DNA. Translation: AAB64513.1.
BK006945 Genomic DNA. Translation: DAA09630.1.
PIRiS53399.
RefSeqiNP_013425.1. NM_001182210.1.

Genome annotation databases

EnsemblFungiiYLR321C; YLR321C; YLR321C.
GeneIDi851032.
KEGGisce:YLR321C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20618 Genomic DNA. Translation: AAB64513.1.
BK006945 Genomic DNA. Translation: DAA09630.1.
PIRiS53399.
RefSeqiNP_013425.1. NM_001182210.1.

3D structure databases

ProteinModelPortaliQ06168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31585. 54 interactions.
DIPiDIP-1898N.
IntActiQ06168. 33 interactions.
MINTiMINT-398787.

PTM databases

iPTMnetiQ06168.

Proteomic databases

MaxQBiQ06168.
PeptideAtlasiQ06168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR321C; YLR321C; YLR321C.
GeneIDi851032.
KEGGisce:YLR321C.

Organism-specific databases

EuPathDBiFungiDB:YLR321C.
SGDiS000004313. SFH1.

Phylogenomic databases

HOGENOMiHOG000074513.
InParanoidiQ06168.
KOiK11770.
OMAiRNMRRLK.
OrthoDBiEOG7HHX3G.

Enzyme and pathway databases

BioCyciYEAST:G3O-32405-MONOMER.

Miscellaneous databases

PROiQ06168.

Family and domain databases

InterProiIPR006939. SNF5.
IPR017393. SWI_SNF_chromatin_remodel_cplx.
[Graphical view]
PANTHERiPTHR10019. PTHR10019. 1 hit.
PfamiPF04855. SNF5. 2 hits.
[Graphical view]
PIRSFiPIRSF038126. SWI_SNF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: FUNCTION OF THE RSC COMPLEX.
  4. "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: FUNCTION, IDENTIFICATION IN THE RSC COMPLEX, INTERACTION WITH STH1, PHOSPHORYLATION.
  5. "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.
  6. "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 OF THE RSC COMPLEX.
  7. "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.
  8. "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 OF THE RSC COMPLEX.
  9. "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.
  10. "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, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "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-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSFH1_YEAST
AccessioniPrimary (citable) accession number: Q06168
Secondary accession number(s): D6VYW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 129 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 3940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.