| Tag | Content |
|---|
| CPLM ID | CPLM-011411 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chromatin structure-remodeling complex subunit RSC2 |
Protein Synonyms/Alias | RSC complex subunit RSC2; Remodel the structure of chromatin complex subunit 2 |
Gene Name | RSC2 |
Gene Synonyms/Alias | YLR357W; L9638.1 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 651 | KTGYSSSKLSSLRYN | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | 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 involved in meiotic sporulation through regulating IME2 expression, and is also essential for 2-micron plasmid maintenance and for normal REP1 protein localization. |
Sequence Annotation | DOMAIN 35 103 Bromo 1.
DOMAIN 295 365 Bromo 2.
DOMAIN 408 526 BAH.
MOD_RES 612 612 Phosphotyrosine.
MOD_RES 682 682 Phosphoserine. |
Keyword | Bromodomain; Chromatin regulator; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Sporulation; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 889 AA |
Protein Sequence | MMPDDNSNSS TQNSSALYKD LRKEYESLFT LKEDSGLEIS PIFNVLPPKK DYPDYYAVIK 60
NPVSFNTLKK RIPHYTDAQQ FMNDVVQIPW NAKTYNTRDS GIYKYALVLE KYLKDTIYPN 120
LKEKYPQLVY PDLGPLPDEP GYEEFQQKLR EKAEEVARAN AARAESSSSM NSTEAARRLR 180
KTRTSVKRES EPGTDTNNDE DYEATDMDID NPKDADFPDL IRKPLININP YTRKPLRDNR 240
STTPSHSGTP QPLGPRHRQV SRTQVKRGRP PIIDLPYIQR MKNVMKVLKK EVLDSGIGLT 300
DLFERLPDRH RDANYYIMIA NPISLQDINK KVKTRRYKTF QEFQNDFNLM LTNFRISHRG 360
DPESIKISNI LEKTFTSLAR FELSKPDRSF IPEGELRYPL DEVIVNNISY HVGDWALLRN 420
QNDPQKPIVG QIFRLWKTPD GKQWLNACWY YRPEQTVHRV DRLFYKNEVM KTGQYRDHLV 480
SNLVGKCYVI HFTRYQRGNP DMKLEGPLFV CEFRYNESDK IFNKIRTWKA CLPEEIRDLD 540
EATIPVNGRK FFKYPSPIRH LLPANATPHD RVPEPTMGSP DAPPLVGAVY MRPKMQRDDL 600
GEYATSDDCP RYIIRPNDSP EEGQVDIETG TITTNTPTAN ALPKTGYSSS KLSSLRYNRS 660
SMSLENQNAI GQQQIPLSRV GSPGAGGPLT VQGLKQHQLQ RLQQQQHQYQ QQKRSQASRY 720
NIPTIIDDLT SQASRGNLGN IMIDAASSFV LPISITKNVD VLQRTDLHSQ TKRSGREEMF 780
PWKKTKGEIL WFRGPSVIVN ERIINSGDPH LSLPLNRWFT TNKKRKLEYE EVEETMEDVT 840
GKDKDDDGLE PDVENEKESL PGPFVLGLRP SAKFTAHRLS MLRPPSSSS 889 |
Gene Ontology | GO:0016586; C:RSC complex; IDA:UniProtKB. GO:0003677; F:DNA binding; IEA:InterPro. GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB. GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD. GO:0006303; P:double-strand break repair via nonhomologous end joining; IPI:SGD. GO:0006337; P:nucleosome disassembly; IDA:SGD. GO:0006276; P:plasmid maintenance; IMP:UniProtKB. GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IMP:UniProtKB. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0007062; P:sister chromatid cohesion; IMP:SGD. GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD. |
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Pfam | |
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PRINTS | |