| Tag | Content |
|---|
| CPLM ID | CPLM-001640 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bromodomain-containing protein 1 |
Protein Synonyms/Alias | BR140-like protein; Bromodomain and PHD finger-containing protein 2 |
Gene Name | BRD1 |
Gene Synonyms/Alias | BRL; BRPF2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 368 | YMKMEPVKELTGGGT | ubiquitination | [1, 2] | | 523 | KAAKEKLKYWQRLRH | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] |
Functional Description | Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. |
Sequence Annotation | DOMAIN 579 649 Bromo.
DOMAIN 929 1012 PWWP.
ZN_FING 214 264 PHD-type.
MOD_RES 128 128 Phosphoserine.
MOD_RES 368 368 N6-acetyllysine.
MOD_RES 516 516 N6-acetyllysine.
MOD_RES 519 519 N6-acetyllysine.
MOD_RES 903 903 N6-acetyllysine.
MOD_RES 1052 1052 Phosphoserine.
MOD_RES 1055 1055 Phosphoserine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1058 AA |
Protein Sequence | MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII 60
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSAHGT PASASALPEP 120
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA 180
VSQSMFEFLM DRFEKESHCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA 240
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 300
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL 360
YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV 420
RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW 480
LLKRLSRNGA PLLRRLQSSL QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE 540
LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL 600
DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR AAVRLRDQGG 660
VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV DRLLDPANRA HLGLEEQLRE 720
LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPLPTGPGLE GFEEDGAALG 780
PEAGEEGDKS PPKLEPSDAL PLPSNSETNS EPPTLKPVEL NPEQSKLFKR VTFDNESHSA 840
CTQSALVSGR PPEPTRASSG DVPAAAASAV AEPASDVNRR TSVLFCKSKS VSPPKSAKNT 900
ETQPTSPQLG TKTFLSVVLP RLETLLQPRK RSRSTCGDSE VEEESPGKRL DAGLTNGFGG 960
ARSEQEPGGG LGRKATPRRR CASESSISSS NSPLCDSSFN APKCGRGKPA LVRRHTLEDR 1020
SELISCIENG NYAKAARIAA EVGQSSMWIS TDAAASVLEP LKVVWAKCSG YPSYPALIID 1080
PKMPRVPGHH NGVTIPAPPL DVLKIGEHMQ TKSDEKLFLV LFFDNKRSWQ WLPKSKMVPL 1140
GIDETIDKLK MMEGRNSSIR KAVRIAFDRA MNHLSRVHGE PTSDLSDID 1189 |
Gene Ontology | GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB. GO:0042393; F:histone binding; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0043966; P:histone H3 acetylation; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |