| Tag | Content |
|---|
| CPLM ID | CPLM-018565 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bromodomain adjacent to zinc finger domain protein 2A |
Protein Synonyms/Alias | Transcription termination factor I-interacting protein 5; TTF-I-interacting protein 5; Tip5 |
Gene Name | Baz2a |
Gene Synonyms/Alias | Kiaa0314; Tip5 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 672 | RGRPPKIKMPELLNK | acetylation | [1] |
|
Reference | [1] Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing. Zhou Y, Schmitz KM, Mayer C, Yuan X, Akhtar A, Grummt I. Nat Cell Biol. 2009 Aug;11(8):1010-6. [ PMID: 19578370] |
Functional Description | Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys- 16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA- binding is required for heterochromatin formation and rDNA silencing. |
Sequence Annotation | DOMAIN 538 609 MBD.
DOMAIN 839 904 DDT.
DOMAIN 1794 1864 Bromo.
DNA_BIND 641 653 A.T hook 1.
DNA_BIND 662 674 A.T hook 2.
DNA_BIND 1176 1188 A.T hook 3.
DNA_BIND 1390 1402 A.T hook 4.
ZN_FING 1662 1712 PHD-type.
MOD_RES 134 134 Phosphoserine (By similarity).
MOD_RES 501 501 Phosphoserine (By similarity).
MOD_RES 672 672 N6-acetyllysine; by KAT8.
MOD_RES 1042 1042 Phosphoserine.
MOD_RES 1383 1383 Phosphoserine (By similarity).
MOD_RES 1545 1545 Phosphoserine (By similarity).
MOD_RES 1733 1733 Phosphoserine (By similarity).
MOD_RES 1755 1755 Phosphoserine (By similarity).
MOD_RES 1767 1767 Phosphoserine (By similarity). |
Keyword | Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Coiled coil; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1889 AA |
Protein Sequence | MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST 60
VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS ANPGNNLKDP PLLSQFPGGQ 120
YPLNGILGGN RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP 180
NGPPSFFTSP QTSPMLGSSI QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL 240
EEEQPELKMC GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 300
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA FSLLADDSQT 360
SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ SSNFQRPLTE PAPDQPPSTQ 420
LHPAVSPTAS PAASLTASAE ISPAVSPVAS SPVPPEVFVA VSPASSPALP AISLEASMTT 480
PVTSPQGSPE PSPAAAFQTV SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT 540
PEEVRLPLQH GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE 600
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN EKAKNKEVPK 660
VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA KMTKNKKKMR QKVQRGESQT 720
PVQGQARNKR KQDTKSLKQK DTKKKLKAEK EKMKTKQEKL KEKVKREKKE KVKAKGKEGP 780
RARPSCRADK TLATQKRLEE QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR 840
AFSDCLTIVE FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH 900
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR TQPFQAQPPQ 960
QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV EGRLRRLKTA LAKRTGRPEV 1020
MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE ENTTAVHGRR GRKEGEIDVA ASSIPELERH 1080
IEKLSKRQLF FRKKLLHSSQ MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI 1140
KQETESLMEV VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR 1200
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL SQSAFLSWLS 1260
QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ SCPGPQGPWF NFSAQIPCDA 1320
APTPPPAVSE DQPTPSLQLL ASSKPMNTPG AANPCSPVQL SSTHLPGGTP KRLSGDSEEM 1380
SQSPTGLGQP KRRGRPPSKF FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA 1440
LHPRGIREKA LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD 1500
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP WRGRGREGTV 1560
PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV EKALLSTPNG APDGTSTEIS 1620
YEITPRVRVW RQTLERCRSA AQVCLCMGQL ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC 1680
DGCDRGCHIY CHRPKMEAVP EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP 1740
EGDSRRRMLS RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW 1800
PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF DNCQTFNEDD 1860
SEVGKAGHVM RRFFESRWEE FYQGKQANL 1889 |
Gene Ontology | GO:0005677; C:chromatin silencing complex; IDA:UniProtKB. GO:0005730; C:nucleolus; IDA:UniProtKB. GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB. GO:0003677; F:DNA binding; IDA:MGI. GO:0070577; F:histone acetyl-lysine binding; IDA:UniProtKB. GO:0003723; F:RNA binding; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB. GO:0006306; P:DNA methylation; IDA:UniProtKB. GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IDA:MGI. GO:0051567; P:histone H3-K9 methylation; IDA:MGI. GO:0070933; P:histone H4 deacetylation; IDA:MGI. GO:0034770; P:histone H4-K20 methylation; IDA:MGI. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |