| Tag | Content |
|---|
| CPLM ID | CPLM-011241 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcriptional regulatory protein RCO1 |
Protein Synonyms/Alias | |
Gene Name | RCO1 |
Gene Synonyms/Alias | YMR075W; YM9916.14 |
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 |
|---|
| 49 | QNVNYDLKRRKIITS | acetylation | [1] | | 157 | KRFTQVPKNFQDLNR | acetylation | [1] | | 227 | TNATYDSKSKLFGQN | acetylation | [1] | | 245 | STSNASEKIFRDKNN | acetylation | [1] | | 378 | QYSDENDKIPLTDRQ | 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 | Catalytic component of the RPD3C(S) histone deacetylase complex responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. |
Sequence Annotation | ZN_FING 260 309 PHD-type 1.
ZN_FING 414 472 PHD-type 2; atypical.
MOD_RES 68 68 Phosphoserine.
MOD_RES 683 683 Phosphoserine. |
Keyword | Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 684 AA |
Protein Sequence | MDTSKKDTTR SPSHSNSSSP SSSSLSSSSS KEKKRPKRLS SQNVNYDLKR RKIITSEGIE 60
RSFKNEHSNL AVEDNIPEEE PKELLEKDSK GNIIKLNEPS TISEDSKVSV TGLPLNKGPS 120
EKIKRESLWN YRKNLGGQSN NSEMTLVPSK RFTQVPKNFQ DLNRNDLKTF LTENMTEESN 180
IRSTIGWNGD IINRTRDREP ESDRDNKKLS NIRTKIILST NATYDSKSKL FGQNSIKSTS 240
NASEKIFRDK NNSTIDFENE DFCSACNQSG SFLCCDTCPK SFHFLCLDPP IDPNNLPKGD 300
WHCNECKFKI FINNSMATLK KIESNFIKQN NNVKIFAKLL FNIDSHNPKQ FQLPNYIKET 360
FPAVKTGSRG QYSDENDKIP LTDRQLFNTS YGQSITKLDS YNPDTHIDSN SGKFLICYKC 420
NQTRLGSWSH PENSRLIMTC DYCQTPWHLD CVPRASFKNL GSKWKCPLHS PTKVYKKIHH 480
CQEDNSVNYK VWKKQRLINK KNQLYYEPLQ KIGYQNNGNI QIIPTTSHTD YDFNQDFKIT 540
QIDENSIKYD FFDKIYKSKM VQKRKLFQFQ ESLIDKLVSN GSQNGNSEDN MVKDIASLIY 600
FQVSNNDKSS NNKSASKSNN LRKLWDLKEL TNVVVPNELD SIQFNDFSSD EIKHLLYLKK 660
IIESKPKEEL LKFLNIENPE NQSE 684 |
Gene Ontology | GO:0033698; C:Rpd3L complex; IDA:SGD. GO:0032221; C:Rpd3S complex; IDA:SGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0016575; P:histone deacetylation; IMP:SGD. GO:0060195; P:negative regulation of antisense RNA transcription; IMP:SGD. GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IMP:SGD. GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |