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Q91YE5 (BAZ2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Baz2a
Synonyms:Kiaa0314, Tip5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1889 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.6

Subunit structure

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. Ref.2 Ref.4 Ref.5 Ref.6

Subcellular location

Nucleusnucleolus. Note: Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus. Ref.2 Ref.4 Ref.6 Ref.9 Ref.10

Domain

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. Ref.6 Ref.7

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. Ref.6 Ref.7

Post-translational modification

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. Ref.10

Sequence similarities

Belongs to the WAL family.

Contains 4 A.T hook DNA-binding domains.

Contains 1 bromo domain.

Contains 1 DDT domain.

Contains 1 MBD (methyl-CpG-binding) domain.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
Coiled coil
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
RNA-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from direct assay Ref.6Ref.10. Source: UniProtKB

chromatin remodeling

Inferred from genetic interaction Ref.2. Source: MGI

chromatin silencing at rDNA

Inferred from direct assay Ref.4Ref.6Ref.10. Source: UniProtKB

heterochromatin assembly involved in chromatin silencing

Inferred from direct assay Ref.7. Source: MGI

histone H3-K9 methylation

Inferred from direct assay Ref.7. Source: MGI

histone H4 deacetylation

Inferred from direct assay Ref.7. Source: MGI

histone H4-K20 methylation

Inferred from direct assay Ref.7. Source: MGI

histone deacetylation

Inferred from direct assay Ref.4. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin silencing complex

Inferred from direct assay Ref.6Ref.10. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.6Ref.9Ref.10. Source: UniProtKB

rDNA heterochromatin

Inferred from direct assay Ref.4Ref.10. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.2. Source: MGI

RNA binding

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

lysine-acetylated histone binding

Inferred from direct assay Ref.6Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.4Ref.6Ref.10. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91YE5-1)

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.
Isoform 2 (identifier: Q91YE5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1712-1712: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q91YE5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     305-305: L → LA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18891889Bromodomain adjacent to zinc finger domain protein 2A
PRO_0000211173

Regions

Domain538 – 60972MBD
Domain839 – 90466DDT
Domain1794 – 186471Bromo
DNA binding641 – 65313A.T hook 1
DNA binding662 – 67413A.T hook 2
DNA binding1176 – 118813A.T hook 3
DNA binding1390 – 140213A.T hook 4
Zinc finger1662 – 171251PHD-type
Coiled coil686 – 813128 Potential
Compositional bias652 – 777126Lys-rich
Compositional bias1045 – 10517Poly-Glu

Amino acid modifications

Modified residue1341Phosphoserine By similarity
Modified residue5011Phosphoserine By similarity
Modified residue6721N6-acetyllysine; by KAT8 Ref.10
Modified residue7901N6-acetyllysine Ref.11
Modified residue13831Phosphoserine By similarity
Modified residue15451Phosphoserine By similarity
Modified residue17331Phosphoserine By similarity
Modified residue17551Phosphoserine By similarity
Modified residue17671Phosphoserine By similarity

Natural variations

Alternative sequence3051L → LA in isoform 3.
VSP_037962
Alternative sequence17121Missing in isoform 2.
VSP_037963

Experimental info

Mutagenesis570 – 5712WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. Ref.7
Mutagenesis6721K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. Ref.7 Ref.10
Mutagenesis18141Y → F: Impairs binding to chromatin. Ref.4 Ref.7
Sequence conflict41 – 422NF → SL in CAC69992. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 14E7A817877EB114

FASTA1,889209,618
        10         20         30         40         50         60 
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST 

        70         80         90        100        110        120 
VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS ANPGNNLKDP PLLSQFPGGQ 

       130        140        150        160        170        180 
YPLNGILGGN RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP 

       190        200        210        220        230        240 
NGPPSFFTSP QTSPMLGSSI QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL 

       250        260        270        280        290        300 
EEEQPELKMC GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 

       310        320        330        340        350        360 
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA FSLLADDSQT 

       370        380        390        400        410        420 
SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ SSNFQRPLTE PAPDQPPSTQ 

       430        440        450        460        470        480 
LHPAVSPTAS PAASLTASAE ISPAVSPVAS SPVPPEVFVA VSPASSPALP AISLEASMTT 

       490        500        510        520        530        540 
PVTSPQGSPE PSPAAAFQTV SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT 

       550        560        570        580        590        600 
PEEVRLPLQH GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE 

       610        620        630        640        650        660 
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN EKAKNKEVPK 

       670        680        690        700        710        720 
VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA KMTKNKKKMR QKVQRGESQT 

       730        740        750        760        770        780 
PVQGQARNKR KQDTKSLKQK DTKKKLKAEK EKMKTKQEKL KEKVKREKKE KVKAKGKEGP 

       790        800        810        820        830        840 
RARPSCRADK TLATQKRLEE QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR 

       850        860        870        880        890        900 
AFSDCLTIVE FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH 

       910        920        930        940        950        960 
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR TQPFQAQPPQ 

       970        980        990       1000       1010       1020 
QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV EGRLRRLKTA LAKRTGRPEV 

      1030       1040       1050       1060       1070       1080 
MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE ENTTAVHGRR GRKEGEIDVA ASSIPELERH 

      1090       1100       1110       1120       1130       1140 
IEKLSKRQLF FRKKLLHSSQ MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI 

      1150       1160       1170       1180       1190       1200 
KQETESLMEV VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR 

      1210       1220       1230       1240       1250       1260 
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL SQSAFLSWLS 

      1270       1280       1290       1300       1310       1320 
QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ SCPGPQGPWF NFSAQIPCDA 

      1330       1340       1350       1360       1370       1380 
APTPPPAVSE DQPTPSLQLL ASSKPMNTPG AANPCSPVQL SSTHLPGGTP KRLSGDSEEM 

      1390       1400       1410       1420       1430       1440 
SQSPTGLGQP KRRGRPPSKF FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA 

      1450       1460       1470       1480       1490       1500 
LHPRGIREKA LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD 

      1510       1520       1530       1540       1550       1560 
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP WRGRGREGTV 

      1570       1580       1590       1600       1610       1620 
PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV EKALLSTPNG APDGTSTEIS 

      1630       1640       1650       1660       1670       1680 
YEITPRVRVW RQTLERCRSA AQVCLCMGQL ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC 

      1690       1700       1710       1720       1730       1740 
DGCDRGCHIY CHRPKMEAVP EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP 

      1750       1760       1770       1780       1790       1800 
EGDSRRRMLS RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW 

      1810       1820       1830       1840       1850       1860 
PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF DNCQTFNEDD 

      1870       1880 
SEVGKAGHVM RRFFESRWEE FYQGKQANL 

« Hide

Isoform 2 [UniParc].

Checksum: 1D218D87B4861FBB
Show »

FASTA1,888209,490
Isoform 3 [UniParc].

Checksum: 0A2259C4955FFFBB
Show »

FASTA1,890209,689

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-703 (ISOFORM 3).
Strain: NOD.
[2]"NoRC -- a novel member of mammalian ISWI-containing chromatin remodeling machines."
Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R., Laengst G., Grummt I.
EMBO J. 20:4892-4900(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-1889 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA5 AND TTF1.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1889 (ISOFORM 2).
Tissue: Brain.
[4]"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
Zhou Y., Santoro R., Grummt I.
EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND SIN3A, MUTAGENESIS OF TYR-1814.
[5]"The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo."
Nemeth A., Strohner R., Grummt I., Laengst G.
Nucleic Acids Res. 32:4091-4099(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTF1.
[6]"The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
Zhou Y., Grummt I.
Curr. Biol. 15:1434-1438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BROMO AND PHD-TYPE ZINC-FINGER, INTERACTION WITH DNMT1; DNM3B; HDAC1 AND SMARCA5.
[7]"Intergenic transcripts regulate the epigenetic state of rRNA genes."
Mayer C., Schmitz K.-M., Li J., Grummt I., Santoro R.
Mol. Cell 22:351-361(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, DOMAIN MBD, MUTAGENESIS OF 570-TRP-TYR-571.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The structure of NoRC-associated RNA is crucial for targeting the chromatin remodelling complex NoRC to the nucleolus."
Mayer C., Neubert M., Grummt I.
EMBO Rep. 9:774-780(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
[10]"Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing."
Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.
Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK155523 mRNA. Translation: BAE33307.1.
AJ309544 mRNA. Translation: CAC69992.1.
AK122243 mRNA. Translation: BAC65525.1.
UniGeneMm.252213.

3D structure databases

ProteinModelPortalQ91YE5.
SMRQ91YE5. Positions 547-606, 1659-1882.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ91YE5.

Proteomic databases

PaxDbQ91YE5.
PRIDEQ91YE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2151152. Baz2a.
RougeSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000169644.
HOVERGENHBG107494.
InParanoidQ80U42.
PhylomeDBQ91YE5.

Enzyme and pathway databases

ReactomeREACT_200794. Mus musculus biological processes.

Gene expression databases

CleanExMM_BAZ2A.
GenevestigatorQ91YE5.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
3.30.890.10. 1 hit.
InterProIPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR028940. TIP5.
IPR028942. WHIM1_dom.
IPR028935. WHIM3_domain.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR22880:SF141. PTHR22880:SF141. 1 hit.
PfamPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00384. AT_hook. 4 hits.
SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00391. MBD. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF54171. SSF54171. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. 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]
ProtoNetSearch...

Other

ChiTaRSBAZ2A. mouse.
PROQ91YE5.
SOURCESearch...

Entry information

Entry nameBAZ2A_MOUSE
AccessionPrimary (citable) accession number: Q91YE5
Secondary accession number(s): Q3U235, Q80U42
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot