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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

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-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. lysine-acetylated histone binding Source: UniProtKB
  3. RNA binding Source: UniProtKB
  4. 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 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
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 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

MaxQBiQ91YE5.
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 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.
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.
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

        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 .
UniGenei Mm.252213.

3D structure databases

ProteinModelPortali Q91YE5.
SMRi Q91YE5. Positions 1659-1882.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q91YE5.

Proteomic databases

MaxQBi Q91YE5.
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 Q91YE5.
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: November 26, 2014
This is version 117 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