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UniProtKB - Q91YE5 (BAZ2A_MOUSE)

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Protein

Bromodomain adjacent to zinc finger domain protein 2A

Gene

Baz2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi641 – 653A.T hook 1Add BLAST13
DNA bindingi662 – 674A.T hook 2Add BLAST13
DNA bindingi1176 – 1188A.T hook 3Add BLAST13
DNA bindingi1390 – 1402A.T hook 4Add BLAST13
Zinc fingeri1662 – 1712PHD-typePROSITE-ProRule annotationAdd BLAST51

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
View the complete GO annotation on QuickGO ...

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
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Repressor, RNA-binding
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-573389. NoRC negatively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain adjacent to zinc finger domain protein 2A
Alternative 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2151152. Baz2a.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi570 – 571WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. 2 Publications2
Mutagenesisi672K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. 1 Publication1
Mutagenesisi1814Y → F: Impairs binding to chromatin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002111731 – 1889Bromodomain adjacent to zinc finger domain protein 2AAdd BLAST1889

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei499PhosphothreonineBy similarity1
Modified residuei501PhosphoserineBy similarity1
Modified residuei540PhosphothreonineBy similarity1
Modified residuei605PhosphoserineBy similarity1
Modified residuei672N6-acetyllysine; by KAT81 Publication1
Modified residuei790N6-acetyllysineCombined sources1
Cross-linki857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1042PhosphoserineCombined sources1
Cross-linki1141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1174PhosphoserineCombined sources1
Modified residuei1374PhosphoserineCombined sources1
Modified residuei1377PhosphoserineCombined sources1
Modified residuei1383PhosphoserineCombined sources1
Modified residuei1545PhosphoserineBy similarity1
Cross-linki1662Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1695Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1733PhosphoserineBy similarity1
Modified residuei1738PhosphothreonineCombined sources1
Modified residuei1755PhosphoserineBy similarity1
Modified residuei1767PhosphoserineBy similarity1

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 conjugation

Proteomic databases

PaxDbiQ91YE5.
PRIDEiQ91YE5.

PTM databases

iPTMnetiQ91YE5.
PhosphoSitePlusiQ91YE5.

Expressioni

Gene expression databases

CleanExiMM_BAZ2A.

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
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

CORUMiQ91YE5.
IntActiQ91YE5. 1 interactor.
STRINGi10090.ENSMUSP00000044359.

Structurei

3D structure databases

ProteinModelPortaliQ91YE5.
SMRiQ91YE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini538 – 609MBDPROSITE-ProRule annotationAdd BLAST72
Domaini839 – 904DDTPROSITE-ProRule annotationAdd BLAST66
Domaini1794 – 1864BromoPROSITE-ProRule annotationAdd BLAST71

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili686 – 813Sequence analysisAdd BLAST128

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi652 – 777Lys-richAdd BLAST126
Compositional biasi1045 – 1051Poly-Glu7

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 keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1662 – 1712PHD-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1245. Eukaryota.
COG5076. LUCA.
HOGENOMiHOG000169644.
HOVERGENiHBG107494.
InParanoidiQ91YE5.
PhylomeDBiQ91YE5.

Family and domain databases

CDDicd05503. Bromo_BAZ2A_B_like. 1 hit.
Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiView 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.
PANTHERiPTHR22880:SF141. PTHR22880:SF141. 1 hit.
PfamiView 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.
PRINTSiPR00503. BROMODOMAIN.
SMARTiView protein in SMART
SM00384. AT_hook. 4 hits.
SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00391. MBD. 1 hit.
SM00249. PHD. 1 hit.
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF54171. SSF54171. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiView 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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative 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.

« Hide

        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
Length:1,889
Mass (Da):209,618
Last modified:September 1, 2009 - v2
Checksum:i14E7A817877EB114
GO
Isoform 2 (identifier: Q91YE5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1712-1712: Missing.

Note: No experimental confirmation available.
Show »
Length:1,888
Mass (Da):209,490
Checksum:i1D218D87B4861FBB
GO
Isoform 3 (identifier: Q91YE5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     305-305: L → LA

Note: No experimental confirmation available.
Show »
Length:1,890
Mass (Da):209,689
Checksum:i0A2259C4955FFFBB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41 – 42NF → SL in CAC69992 (PubMed:16141072).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_037962305L → LA in isoform 3. 1 Publication1
Alternative sequenceiVSP_0379631712Missing in isoform 2. 1 Publication1

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.
UniGeneiMm.252213.

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiBAZ2A_MOUSE
AccessioniPrimary (citable) accession number: Q91YE5
Secondary accession number(s): Q3U235, Q80U42
Entry historyiIntegrated 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome