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Q91YE5

- BAZ2A_MOUSE

UniProt

Q91YE5 - BAZ2A_MOUSE

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Protein

Bromodomain adjacent to zinc finger domain protein 2A

Gene
Baz2a, Kiaa0314, Tip5
Organism
Mus musculus (Mouse)
Status
Reviewed - 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-typeAdd
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
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

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

GO - Cellular componenti

  1. chromatin silencing complex Source: UniProtKB
  2. nucleolus Source: UniProtKB
  3. 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. 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 – 1341Phosphoserine By similarity
Modified residuei501 – 5011Phosphoserine By similarity
Modified residuei672 – 6721N6-acetyllysine; by KAT81 Publication
Modified residuei790 – 7901N6-acetyllysine1 Publication
Modified residuei1383 – 13831Phosphoserine By similarity
Modified residuei1545 – 15451Phosphoserine By similarity
Modified residuei1733 – 17331Phosphoserine By similarity
Modified residuei1755 – 17551Phosphoserine By similarity
Modified residuei1767 – 17671Phosphoserine By 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.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini538 – 60972MBDAdd
BLAST
Domaini839 – 90466DDTAdd
BLAST
Domaini1794 – 186471BromoAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili686 – 813128 Reviewed predictionAdd
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 HDAC1.2 Publications
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.2 Publications

Sequence similaritiesi

Belongs to the WAL family.
Contains 1 bromo domain.
Contains 1 DDT domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1662 – 171251PHD-typeAdd
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei305 – 3051L → LA in isoform 3. VSP_037962
Alternative sequencei1712 – 17121Missing in isoform 2. VSP_037963

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 422NF → SL in CAC69992. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 114 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

Similar proteinsi