| Tag | Content |
|---|
| CPLM ID | CPLM-015015 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bromodomain-containing protein 2 |
Protein Synonyms/Alias | Protein RING3 |
Gene Name | Brd2 |
Gene Synonyms/Alias | Ring3 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 30 | PEAAAPGKRIRKPSL | acetylation | [1] | | 723 | RKPVGKTKEELALEK | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly (By similarity). May play a role in spermatogenesis or folliculogenesis (By similarity). |
Sequence Annotation | DOMAIN 90 162 Bromo 1.
DOMAIN 363 435 Bromo 2.
DOMAIN 630 712 NET.
MOTIF 553 557 Nuclear localization signal (Potential).
MOD_RES 1 1 N-acetylmethionine (By similarity).
MOD_RES 6 6 Phosphothreonine (By similarity).
MOD_RES 36 36 Phosphoserine (By similarity).
MOD_RES 297 297 Phosphoserine (By similarity).
MOD_RES 300 300 Phosphoserine (By similarity).
MOD_RES 304 304 Phosphoserine (By similarity).
MOD_RES 631 631 Phosphoserine (By similarity). |
Keyword | Acetylation; Bromodomain; Chromatin regulator; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 798 AA |
Protein Sequence | MLQNVTPHKL PGEGNAGLLG LGPEAAAPGK RIRKPSLLYE GFESPTMASV PALQLAPANP 60
PPPEVSNPKK PGRVTNQLQY LHKVVMKALW KHQFAWPFRQ PVDAVKLGLP DYHKIIKQPM 120
DMGTIKRRLE NNYYWAASEC MQDFNTMFTN CYIYNKPTDD IVLMAQTLEK IFLQKVASMP 180
QEEQELVVTI PKNSHKKGAK LAALQGSITS AHQVPAVSSV SHTALYTPPP EIPTTVLNIP 240
HPSVISSPLL KSLHSAGPPL LAVSAAPPAQ PLAKKKGVKR KADTTTPTPT AILAPGSPAS 300
PPGSLEPKAA RLPPMRRESG RPIKPPRKDL PDSQQQHQSS KKGKLSEQLK HCNGILKELL 360
SKKHAAYAWP FYKPVDASAL GLHDYHDIIK HPMDLSTVKR KMENRDYRDA QEFAADVRLM 420
FSNCYKYNPP DHDVVAMARK LQDVFEFRYA KMPDEPLEPG PLPVSTALPP GLAKSSSESS 480
SEESSSESSS EEEEEEDEED EEEESESSDS EEERAHRLAE LQEQLRAVHE QLAALSQGPI 540
SKPKRKREKK EKKKKRKAEK HRGRIGIDED DKGPRAPRPL QPKKSKKAGG GGSNATTLSH 600
PGFGTSAGSS NKLPKKAQKT APPVLPTGYD SEEEEESRPM SYDEKRQLSL DINKLPGEKL 660
GRVVHIIQAR EPSLRDSNPE EIEIDFETLK PSTLRELERY VLSCLRKKPR KPYTIRKPVG 720
KTKEELALEK KRELEKRLQD VSGQLNSTKK PPKKASEKTE SSAQQVAVSR LSASSSSSDS 780
SSSSSSSSSS DTSDSDSG 798 |
Gene Ontology | GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0003682; F:chromatin binding; ISS:UniProtKB. GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0006334; P:nucleosome assembly; ISS:UniProtKB. GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
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PRINTS | |