P38781 (RSC30_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromatin structure-remodeling complex protein RSC30

Alternative name(s):
Remodel the structure of chromatin complex subunit 30

Gene names

Name:	RSC30
Ordered Locus Names:	YHR056C

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	883 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall. Together with HTL1, LDB7, NPL6, RSC3 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
Subunit structure	Forms a heteromer with RSC3. Interacts with NPL6. 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. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex. Ref.4 Ref.10 Ref.12
Subcellular location	Nucleus. Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. Ref.10
Sequence similarities	Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair via nonhomologous end joining Inferred from mutant phenotype PubMed 15870268. Source: SGD nucleosome disassembly Inferred from direct assay PubMed 16492771. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: GOC transcription elongation from RNA polymerase II promoter Inferred from direct assay PubMed 17081996. Source: SGD
Cellular_component	RSC complex Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	sequence-specific DNA binding Inferred from direct assay PubMed 19111667PubMed 19158363. Source: SGD sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RSC3	Q06639	5	EBI-24549,EBI-22058

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 883	883	Chromatin structure-remodeling complex protein RSC30		PRO_0000114974
Regions
	DNA binding	14 – 45	32	Zn(2)-C6 fungal-type
Amino acid modifications
	Modified residue	135	1	Phosphoserine Ref.13 Ref.14
	Modified residue	150	1	Phosphoserine Ref.14
	Modified residue	152	1	Phosphoserine Ref.14
Experimental info
	Mutagenesis	15	1	C → G: Complete inactivation. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P38781 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: E8542445950FAA93	FASTA	883	101,335
	10 20 30 40 50 60 MMDMQVRKVR KPPACTQCRK RKIGCDRAKP ICGNCVKYNK PDCFYPDGPG KMVAVPSASG 70 80 90 100 110 120 MSTHGNGQGS NHFSQGNGVN QKNVMIQTQY PIMQTSIEAF NFSFNPSVDT AMQWTKAASY 130 140 150 160 170 180 QNNNTNNNTA PRQNSSTVSS NVHGNTIVRS DSPDVPSMDQ IREYNTRLQL VNAQSFDYTD 190 200 210 220 230 240 NPYSFNVGIN QDSAVFDLMT SPFTQEEVLI KEIDFLKNKL LDLQSLQLKS LKEKSNLNAD 250 260 270 280 290 300 NTTANKINKT GENSKKGKVD GKRAGFDHQT SRTSQSSQKY FTALTITDVQ SLVQVKPLKD 310 320 330 340 350 360 TPNYLFTKNF IIFRDHYLFK FYNILHDICH INQFKVSPPN NKNHQQYMEV CKVNFPPKAI 370 380 390 400 410 420 IIETLNSESL NNLNIEEFLP IFDKTLLLEF VHNSFPNGDT CPSFSTVDLP LSQLTKLGEL 430 440 450 460 470 480 TVLLLLLNDS MTLFNKQAIN NHVSALMNNL RLIRSQITLI NLEYYDQETI KFIAITKFYE 490 500 510 520 530 540 SLYMHDDHKS SLDEDLSCLL SFQIKDFKLF HFLKKMYYSR HSLLGQSSFM VPAAENLSPI 550 560 570 580 590 600 PASIDTNDIP LIANDLKLLE TQAKLINILQ GVPFYLPVNL TKIESLLETL TMGVSNTVDL 610 620 630 640 650 660 YFHDNEVRKE WKDTLNFINT IVYTNFFLFV QNESSLSMAV QHSSNNNKTS NSERCAKDLM 670 680 690 700 710 720 KIISNMHIFY SITFNFIFPI KSIKSFSSGN NRFHSNGKEF LFANHFIEIL QNFIAITFAI 730 740 750 760 770 780 FQRCEVILYD EFYKNLSNEE INVQLLLIHD KILEILKKIE IIVSFLRDEM NSNGSFKSIK 790 800 810 820 830 840 GFNKVLNLIK YMLRFSKKKQ NFARNSDNNN VTDYSQSAKN KNVLLKFPVS ELNRIYLKFK 850 860 870 880 EISDFLMERE VVQRSIIIDK DLESDNLGIT TANFNDFYDA FYN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Fisk D., Cherry J.M. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A Rsc3/Rsc30 zinc cluster dimer reveals novel roles for the chromatin remodeler RSC in gene expression and cell cycle control." Angus-Hill M.L., Schlichter A., Roberts D., Erdjument-Bromage H., Tempst P., Cairns B.R. Mol. Cell 7:741-751(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-37, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF THE RSC COMPLEX, HETEROMERIC COMPLEX FORMATION WITH RSC3, MUTAGENESIS OF CYS-15.
[5]	"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: FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
[6]	"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.
[7]	"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.
[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]	"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.
[12]	"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: FUNCTION, INTERACTION WITH NPL6.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, MASS SPECTROMETRY.
[14]	"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-135; SER-150 AND SER-152, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00061 Genomic DNA. Translation: AAB68385.2. BK006934 Genomic DNA. Translation: DAA06749.1.
RefSeq	NP_011923.2. NM_001179186.2.
3D structure databases
ProteinModelPortal	P38781.
SMR	P38781. Positions 13-45.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4275N.
IntAct	P38781. 26 interactions.
MINT	MINT-510758.
STRING	4932.YHR056C.
Proteomic databases
PaxDb	P38781.
PeptideAtlas	P38781.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR056C; YHR056C; YHR056C.
GeneID	856453.
KEGG	sce:YHR056C.
Organism-specific databases
CYGD	YHR056c.
SGD	S000001098. RSC30.
Phylogenomic databases
eggNOG	NOG285310.
GeneTree	ENSGT00390000004801.
KO	K11758.
Gene expression databases
ArrayExpress	P38781.
Genevestigator	P38781.
GermOnline	YHR056C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	4.10.240.10. 1 hit.
InterPro	IPR001138. Zn2-C6_fun-type_DNA-bd. [Graphical view]
Pfam	PF00172. Zn_clus. 1 hit. [Graphical view]
SMART	SM00066. GAL4. 1 hit. [Graphical view]
SUPFAM	SSF57701. Fungi_TrN. 1 hit.
PROSITE	PS00463. ZN2_CY6_FUNGAL_1. 1 hit. PS50048. ZN2_CY6_FUNGAL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982084.

Entry information

Entry name

RSC30_YEAST

Accession

Primary (citable) accession number: P38781
Secondary accession number(s): D3DL05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program