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Q91YE5

- BAZ2A_MOUSE

UniProt

Q91YE5 - BAZ2A_MOUSE

Protein

Bromodomain adjacent to zinc finger domain protein 2A

Gene

Baz2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 Sep 2009)
      Previous versions | rss
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    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

    1. DNA binding Source: MGI
    2. lysine-acetylated histone binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin remodeling Source: MGI
    2. chromatin silencing at rDNA Source: UniProtKB
    3. DNA methylation Source: UniProtKB
    4. heterochromatin assembly involved in chromatin silencing Source: MGI
    5. histone deacetylation Source: UniProtKB
    6. histone H3-K9 methylation Source: MGI
    7. histone H4 deacetylation Source: MGI
    8. histone H4-K20 methylation Source: MGI
    9. transcription, DNA-templated Source: UniProtKB-KW

    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

    ReactomeiREACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2151152. Baz2a.

    Subcellular locationi

    Nucleusnucleolus 5 Publications
    Note: Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus.

    GO - Cellular componenti

    1. chromatin silencing complex Source: UniProtKB
    2. nucleolus Source: UniProtKB
    3. rDNA heterochromatin Source: UniProtKB

    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. 1 Publication
    Mutagenesisi672 – 6721K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. 2 Publications
    Mutagenesisi1814 – 18141Y → F: Impairs binding to chromatin. 2 Publications

    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 residuei134 – 1341PhosphoserineBy similarity
    Modified residuei501 – 5011PhosphoserineBy similarity
    Modified residuei672 – 6721N6-acetyllysine; by KAT81 Publication
    Modified residuei790 – 7901N6-acetyllysine1 Publication
    Modified residuei1383 – 13831PhosphoserineBy similarity
    Modified residuei1545 – 15451PhosphoserineBy similarity
    Modified residuei1733 – 17331PhosphoserineBy similarity
    Modified residuei1755 – 17551PhosphoserineBy similarity
    Modified residuei1767 – 17671PhosphoserineBy similarity

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ91YE5.
    PRIDEiQ91YE5.

    PTM databases

    PhosphoSiteiQ91YE5.

    Expressioni

    Gene expression databases

    CleanExiMM_BAZ2A.
    GenevestigatoriQ91YE5.

    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.4 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YE5.
    SMRiQ91YE5. Positions 547-606, 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

    eggNOGiCOG5076.
    HOGENOMiHOG000169644.
    HOVERGENiHBG107494.
    InParanoidiQ80U42.
    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.
    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]
    PANTHERiPTHR22880:SF141. PTHR22880:SF141. 1 hit.
    PfamiPF00439. 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]
    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. Align

    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

    MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN     50
    GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS 100
    ANPGNNLKDP PLLSQFPGGQ YPLNGILGGN RQPSSPSHNT NLRAGSQEFW 150
    ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI 200
    QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL EEEQPELKMC 250
    GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 300
    PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA 350
    FSLLADDSQT SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ 400
    SSNFQRPLTE PAPDQPPSTQ LHPAVSPTAS PAASLTASAE ISPAVSPVAS 450
    SPVPPEVFVA VSPASSPALP AISLEASMTT PVTSPQGSPE PSPAAAFQTV 500
    SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT PEEVRLPLQH 550
    GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE 600
    HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN 650
    EKAKNKEVPK VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA 700
    KMTKNKKKMR QKVQRGESQT PVQGQARNKR KQDTKSLKQK DTKKKLKAEK 750
    EKMKTKQEKL KEKVKREKKE KVKAKGKEGP RARPSCRADK TLATQKRLEE 800
    QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR AFSDCLTIVE 850
    FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH 900
    DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR 950
    TQPFQAQPPQ QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV 1000
    EGRLRRLKTA LAKRTGRPEV MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE 1050
    ENTTAVHGRR GRKEGEIDVA ASSIPELERH IEKLSKRQLF FRKKLLHSSQ 1100
    MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI KQETESLMEV 1150
    VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR 1200
    ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL 1250
    SQSAFLSWLS QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ 1300
    SCPGPQGPWF NFSAQIPCDA APTPPPAVSE DQPTPSLQLL ASSKPMNTPG 1350
    AANPCSPVQL SSTHLPGGTP KRLSGDSEEM SQSPTGLGQP KRRGRPPSKF 1400
    FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA LHPRGIREKA 1450
    LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD 1500
    LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP 1550
    WRGRGREGTV PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV 1600
    EKALLSTPNG APDGTSTEIS YEITPRVRVW RQTLERCRSA AQVCLCMGQL 1650
    ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC DGCDRGCHIY CHRPKMEAVP 1700
    EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP EGDSRRRMLS 1750
    RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW 1800
    PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF 1850
    DNCQTFNEDD SEVGKAGHVM RRFFESRWEE FYQGKQANL 1889
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK155523 mRNA. Translation: BAE33307.1 .
    AJ309544 mRNA. Translation: CAC69992.1 .
    AK122243 mRNA. Translation: BAC65525.1 .
    UniGenei Mm.252213.

    3D structure databases

    ProteinModelPortali Q91YE5.
    SMRi Q91YE5. Positions 547-606, 1659-1882.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q91YE5.

    Proteomic databases

    PaxDbi Q91YE5.
    PRIDEi Q91YE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:2151152. Baz2a.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000169644.
    HOVERGENi HBG107494.
    InParanoidi Q80U42.
    PhylomeDBi Q91YE5.

    Enzyme and pathway databases

    Reactomei REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

    ChiTaRSi BAZ2A. mouse.
    PROi Q91YE5.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_BAZ2A.
    Genevestigatori Q91YE5.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    3.30.890.10. 1 hit.
    InterProi IPR017956. 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 ]
    PANTHERi PTHR22880:SF141. PTHR22880:SF141. 1 hit.
    Pfami PF00439. 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 ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00384. AT_hook. 4 hits.
    SM00297. BROMO. 1 hit.
    SM00571. DDT. 1 hit.
    SM00391. MBD. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF54171. SSF54171. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS00633. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    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: October 1, 2014
    This is version 115 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

    External Data

    Dasty 3