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UniProtKB - Q91YE5 (BAZ2A_MOUSE)

UniProt

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: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi641 – 65313A.T hook 1Add
BLAST
DNA bindingi662 – 67413A.T hook 2Add
BLAST
DNA bindingi1176 – 118813A.T hook 3Add
BLAST
DNA bindingi1390 – 140213A.T hook 4Add
BLAST
Zinc fingeri1662 – 171251PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: MGI
  • histone binding Source: MGI
  • lysine-acetylated histone binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase I CORE element sequence-specific DNA binding Source: MGI
  • zinc ion binding Source: InterPro

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 from RNA polymerase I promoter Source: CACAO
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-427413. NoRC negatively regulates rRNA expression.
R-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 › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2151152. Baz2a.

Subcellular locationi

GO - Cellular componenti

  • chromatin silencing complex Source: UniProtKB
  • cytoplasm Source: MGI
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: MGI
  • rDNA heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi570 – 5712WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. 2 Publications
Mutagenesisi672 – 6721K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. 1 Publication
Mutagenesisi1814 – 18141Y → F: Impairs binding to chromatin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18891889Bromodomain adjacent to zinc finger domain protein 2APRO_0000211173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei499 – 4991PhosphothreonineBy similarity
Modified residuei501 – 5011PhosphoserineBy similarity
Modified residuei540 – 5401PhosphothreonineBy similarity
Modified residuei605 – 6051PhosphoserineBy similarity
Modified residuei672 – 6721N6-acetyllysine; by KAT81 Publication
Modified residuei790 – 7901N6-acetyllysineCombined sources
Modified residuei1042 – 10421PhosphoserineCombined sources
Cross-linki1141 – 1141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1174 – 11741PhosphoserineCombined sources
Modified residuei1374 – 13741PhosphoserineCombined sources
Modified residuei1377 – 13771PhosphoserineCombined sources
Modified residuei1383 – 13831PhosphoserineCombined sources
Modified residuei1545 – 15451PhosphoserineBy similarity
Modified residuei1733 – 17331PhosphoserineBy similarity
Modified residuei1738 – 17381PhosphothreonineCombined sources
Modified residuei1755 – 17551PhosphoserineBy similarity
Modified residuei1767 – 17671PhosphoserineBy similarity

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

MaxQBiQ91YE5.
PaxDbiQ91YE5.
PRIDEiQ91YE5.

PTM databases

iPTMnetiQ91YE5.
PhosphoSiteiQ91YE5.

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

Protein-protein interaction databases

IntActiQ91YE5. 1 interaction.
STRINGi10090.ENSMUSP00000044359.

Structurei

3D structure databases

ProteinModelPortaliQ91YE5.
SMRiQ91YE5. Positions 535-642, 1659-1882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini538 – 60972MBDPROSITE-ProRule annotationAdd
BLAST
Domaini839 – 90466DDTPROSITE-ProRule annotationAdd
BLAST
Domaini1794 – 186471BromoPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili686 – 813128Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi652 – 777126Lys-richAdd
BLAST
Compositional biasi1045 – 10517Poly-Glu

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 recritment 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
Contains 4 A.T hook DNA-binding domains.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 DDT domain.PROSITE-ProRule annotation
Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1662 – 171251PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

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

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
3.30.890.10. 1 hit.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018501. DDT_dom.
IPR016177. DNA-bd_dom.
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.
[Graphical view]
PANTHERiPTHR22880:SF141. PTHR22880:SF141. 3 hits.
PfamiPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WSD. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00384. AT_hook. 4 hits.
SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00391. MBD. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF54171. SSF54171. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS50982. MBD. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 422NF → SL in CAC69992 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei305 – 3051L → LA in isoform 3. 1 PublicationVSP_037962
Alternative sequencei1712 – 17121Missing in isoform 2. 1 PublicationVSP_037963

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ91YE5.
SMRiQ91YE5. Positions 535-642, 1659-1882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91YE5. 1 interaction.
STRINGi10090.ENSMUSP00000044359.

PTM databases

iPTMnetiQ91YE5.
PhosphoSiteiQ91YE5.

Proteomic databases

MaxQBiQ91YE5.
PaxDbiQ91YE5.
PRIDEiQ91YE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:2151152. Baz2a.
RougeiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-573389. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiBaz2a. mouse.
PROiQ91YE5.
SOURCEiSearch...

Gene expression databases

CleanExiMM_BAZ2A.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
3.30.890.10. 1 hit.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018501. DDT_dom.
IPR016177. DNA-bd_dom.
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.
[Graphical view]
PANTHERiPTHR22880:SF141. PTHR22880:SF141. 3 hits.
PfamiPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WSD. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00384. AT_hook. 4 hits.
SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00391. MBD. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF54171. SSF54171. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS50982. MBD. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAZ2A_MOUSE
AccessioniPrimary (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: September 7, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.