UniProtKB - Q91YE5 (BAZ2A_MOUSE)
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Protein
Bromodomain adjacent to zinc finger domain protein 2A
Gene
Baz2a
Organism
Mus musculus (Mouse)
Status
Functioni
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.3 Publications
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 641 – 653 | A.T hook 1Add BLAST | 13 | |
DNA bindingi | 662 – 674 | A.T hook 2Add BLAST | 13 | |
DNA bindingi | 1176 – 1188 | A.T hook 3Add BLAST | 13 | |
DNA bindingi | 1390 – 1402 | A.T hook 4Add BLAST | 13 | |
Zinc fingeri | 1662 – 1712 | PHD-typePROSITE-ProRule annotationAdd BLAST | 51 |
GO - Molecular functioni
- DNA binding Source: MGI
- histone binding Source: MGI
- lysine-acetylated histone binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- RNA binding Source: UniProtKB
- RNA polymerase I CORE element sequence-specific DNA binding Source: MGI
GO - Biological processi
- chromatin remodeling Source: MGI
- chromatin silencing at rDNA Source: UniProtKB
- DNA methylation Source: UniProtKB
- heterochromatin assembly involved in chromatin silencing Source: MGI
- histone deacetylation Source: UniProtKB
- histone H3-K9 methylation Source: MGI
- histone H4 deacetylation Source: MGI
- histone H4-K20 methylation Source: MGI
- negative regulation of transcription by RNA polymerase I Source: CACAO
Keywordsi
Molecular function | Chromatin regulator, DNA-binding, Repressor, RNA-binding |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-573389. NoRC negatively regulates rRNA expression. |
Names & Taxonomyi
Protein namesi | Recommended name: Bromodomain adjacent to zinc finger domain protein 2AAlternative name(s): Transcription termination factor I-interacting protein 5 Short name: TTF-I-interacting protein 5 Short name: Tip5 |
Gene namesi | Name:Baz2a Synonyms:Kiaa0314, Tip5 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2151152. Baz2a. |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 570 – 571 | WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. 2 Publications | 2 | |
Mutagenesisi | 672 | K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. 1 Publication | 1 | |
Mutagenesisi | 1814 | Y → F: Impairs binding to chromatin. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000211173 | 1 – 1889 | Bromodomain adjacent to zinc finger domain protein 2AAdd BLAST | 1889 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 499 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 501 | PhosphoserineBy similarity | 1 | |
Modified residuei | 540 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 605 | PhosphoserineBy similarity | 1 | |
Modified residuei | 672 | N6-acetyllysine; by KAT81 Publication | 1 | |
Modified residuei | 790 | N6-acetyllysineCombined sources | 1 | |
Cross-linki | 857 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 1042 | PhosphoserineCombined sources | 1 | |
Cross-linki | 1141 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 1163 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 1174 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1374 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1377 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1383 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1545 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1662 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 1695 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 1733 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1738 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1755 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1767 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Ubiquitinated. Deubiquitinated by USP21 leading to its stabilization.By similarity
Acetylation at Lys-672 by KAT8/MOF promotes its dissociation from pRNA, affecting heterochromatin formation, nucleosome positioning and rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-binding, allowing de novo DNA methylation and heterochromatin formation. Acetylation is high during S phase and declines to background levels in late S phase when the silent copies of rRNA genes are replicated.1 Publication
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q91YE5. |
PRIDEi | Q91YE5. |
PTM databases
iPTMneti | Q91YE5. |
PhosphoSitePlusi | Q91YE5. |
Interactioni
Subunit structurei
Component of the NoRC complex, at least composed of SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for recruitment of the NoRC complex to rDNA. Interacts with DNMT1, DNM3B, HDAC1 and SIN3A. Interacts with BEND3 and USP21 (By similarity).By similarity4 Publications
GO - Molecular functioni
- histone binding Source: MGI
- lysine-acetylated histone binding Source: UniProtKB
Protein-protein interaction databases
CORUMi | Q91YE5. |
IntActi | Q91YE5. 1 interactor. |
STRINGi | 10090.ENSMUSP00000044359. |
Structurei
3D structure databases
ProteinModelPortali | Q91YE5. |
SMRi | Q91YE5. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 538 – 609 | MBDPROSITE-ProRule annotationAdd BLAST | 72 | |
Domaini | 839 – 904 | DDTPROSITE-ProRule annotationAdd BLAST | 66 | |
Domaini | 1794 – 1864 | BromoPROSITE-ProRule annotationAdd BLAST | 71 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 686 – 813 | Sequence analysisAdd BLAST | 128 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 652 – 777 | Lys-richAdd BLAST | 126 | |
Compositional biasi | 1045 – 1051 | Poly-Glu | 7 |
Domaini
The bromo domain and the PHD-type zinc finger recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2 domains play a central role in the recruitment of chromatin silencing proteins such as DNMT1, DNMT3B and HDAC1.
The MBD (methyl-CpG-binding) domain, also named TAM domain, specifically recognizes and binds a conserved stem-loop structure the association within pRNA. Binding to pRNA induces a conformational change of BAZ2A/TIP5 and is essential for targeting the NoRC complex to the nucleolus.
Sequence similaritiesi
Belongs to the WAL family.Curated
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1662 – 1712 | PHD-typePROSITE-ProRule annotationAdd BLAST | 51 |
Keywords - Domaini
Bromodomain, Coiled coil, Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1245. Eukaryota. COG5076. LUCA. |
HOGENOMi | HOG000169644. |
HOVERGENi | HBG107494. |
InParanoidi | Q91YE5. |
PhylomeDBi | Q91YE5. |
Family and domain databases
CDDi | cd05503. Bromo_BAZ2A_B_like. 1 hit. |
Gene3Di | 1.20.920.10. 1 hit. 3.30.40.10. 1 hit. |
InterProi | View protein in InterPro IPR017956. AT_hook_DNA-bd_motif. IPR037374. BAZ2A/B_Bromo. IPR001487. Bromodomain. IPR036427. Bromodomain-like_sf. IPR018359. Bromodomain_CS. IPR018501. DDT_dom. IPR016177. DNA-bd_dom_sf. IPR001739. Methyl_CpG_DNA-bd. IPR028940. TIP5. IPR028942. WHIM1_dom. IPR028941. WHIM2_dom. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. |
PANTHERi | PTHR22880:SF141. PTHR22880:SF141. 1 hit. |
Pfami | View protein in Pfam PF00439. Bromodomain. 1 hit. PF02791. DDT. 1 hit. PF01429. MBD. 1 hit. PF00628. PHD. 1 hit. PF15612. WHIM1. 1 hit. PF15613. WSD. 1 hit. |
PRINTSi | PR00503. BROMODOMAIN. |
SMARTi | View protein in SMART SM00384. AT_hook. 4 hits. SM00297. BROMO. 1 hit. SM00571. DDT. 1 hit. SM00391. MBD. 1 hit. SM00249. PHD. 1 hit. |
SUPFAMi | SSF47370. SSF47370. 1 hit. SSF54171. SSF54171. 1 hit. SSF57903. SSF57903. 1 hit. |
PROSITEi | View protein in PROSITE PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS50827. DDT. 1 hit. PS50982. MBD. 1 hit. PS50016. ZF_PHD_2. 1 hit. |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q91YE5-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN
60 70 80 90 100
GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS
110 120 130 140 150
ANPGNNLKDP PLLSQFPGGQ YPLNGILGGN RQPSSPSHNT NLRAGSQEFW
160 170 180 190 200
ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI
210 220 230 240 250
QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL EEEQPELKMC
260 270 280 290 300
GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE
310 320 330 340 350
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA
360 370 380 390 400
FSLLADDSQT SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ
410 420 430 440 450
SSNFQRPLTE PAPDQPPSTQ LHPAVSPTAS PAASLTASAE ISPAVSPVAS
460 470 480 490 500
SPVPPEVFVA VSPASSPALP AISLEASMTT PVTSPQGSPE PSPAAAFQTV
510 520 530 540 550
SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT PEEVRLPLQH
560 570 580 590 600
GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE
610 620 630 640 650
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN
660 670 680 690 700
EKAKNKEVPK VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA
710 720 730 740 750
KMTKNKKKMR QKVQRGESQT PVQGQARNKR KQDTKSLKQK DTKKKLKAEK
760 770 780 790 800
EKMKTKQEKL KEKVKREKKE KVKAKGKEGP RARPSCRADK TLATQKRLEE
810 820 830 840 850
QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR AFSDCLTIVE
860 870 880 890 900
FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH
910 920 930 940 950
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR
960 970 980 990 1000
TQPFQAQPPQ QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV
1010 1020 1030 1040 1050
EGRLRRLKTA LAKRTGRPEV MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE
1060 1070 1080 1090 1100
ENTTAVHGRR GRKEGEIDVA ASSIPELERH IEKLSKRQLF FRKKLLHSSQ
1110 1120 1130 1140 1150
MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI KQETESLMEV
1160 1170 1180 1190 1200
VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR
1210 1220 1230 1240 1250
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL
1260 1270 1280 1290 1300
SQSAFLSWLS QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ
1310 1320 1330 1340 1350
SCPGPQGPWF NFSAQIPCDA APTPPPAVSE DQPTPSLQLL ASSKPMNTPG
1360 1370 1380 1390 1400
AANPCSPVQL SSTHLPGGTP KRLSGDSEEM SQSPTGLGQP KRRGRPPSKF
1410 1420 1430 1440 1450
FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA LHPRGIREKA
1460 1470 1480 1490 1500
LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD
1510 1520 1530 1540 1550
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP
1560 1570 1580 1590 1600
WRGRGREGTV PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV
1610 1620 1630 1640 1650
EKALLSTPNG APDGTSTEIS YEITPRVRVW RQTLERCRSA AQVCLCMGQL
1660 1670 1680 1690 1700
ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC DGCDRGCHIY CHRPKMEAVP
1710 1720 1730 1740 1750
EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP EGDSRRRMLS
1760 1770 1780 1790 1800
RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW
1810 1820 1830 1840 1850
PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF
1860 1870 1880
DNCQTFNEDD SEVGKAGHVM RRFFESRWEE FYQGKQANL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 41 – 42 | NF → SL in CAC69992 (PubMed:16141072).Curated | 2 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_037962 | 305 | L → LA in isoform 3. 1 Publication | 1 | |
Alternative sequenceiVSP_037963 | 1712 | Missing in isoform 2. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK155523 mRNA. Translation: BAE33307.1. AJ309544 mRNA. Translation: CAC69992.1. AK122243 mRNA. Translation: BAC65525.1. |
UniGenei | Mm.252213. |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | BAZ2A_MOUSE | |
Accessioni | Q91YE5Primary (citable) accession number: Q91YE5 Secondary accession number(s): Q3U235, Q80U42 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 30, 2002 |
Last sequence update: | September 1, 2009 | |
Last modified: | March 28, 2018 | |
This is version 146 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |