Q91YE5 (BAZ2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Baz2a
Synonyms:	Kiaa0314, Tip5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1889 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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_component	chromatin 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_function	DNA binding Inferred from direct assay Ref.2. Source: MGI RNA binding Inferred from direct assay Ref.9Ref.10. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay Ref.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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1889	1889	Bromodomain adjacent to zinc finger domain protein 2A		PRO_0000211173
Regions
	Domain	538 – 609	72	MBD
	Domain	839 – 904	66	DDT
	Domain	1794 – 1864	71	Bromo
	DNA binding	641 – 653	13	A.T hook 1
	DNA binding	662 – 674	13	A.T hook 2
	DNA binding	1176 – 1188	13	A.T hook 3
	DNA binding	1390 – 1402	13	A.T hook 4
	Zinc finger	1662 – 1712	51	PHD-type
	Coiled coil	686 – 813	128	Potential
	Compositional bias	652 – 777	126	Lys-rich
	Compositional bias	1045 – 1051	7	Poly-Glu
Amino acid modifications
	Modified residue	134	1	Phosphoserine By similarity
	Modified residue	501	1	Phosphoserine By similarity
	Modified residue	672	1	N6-acetyllysine; by KAT8 Ref.10
	Modified residue	790	1	N6-acetyllysine Ref.11
	Modified residue	1383	1	Phosphoserine By similarity
	Modified residue	1545	1	Phosphoserine By similarity
	Modified residue	1733	1	Phosphoserine By similarity
	Modified residue	1755	1	Phosphoserine By similarity
	Modified residue	1767	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	305	1	L → LA in isoform 3.		VSP_037962
	Alternative sequence	1712	1	Missing in isoform 2.		VSP_037963
Experimental info
	Mutagenesis	570 – 571	2	WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. Ref.7
	Mutagenesis	672	1	K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. Ref.7 Ref.10
	Mutagenesis	1814	1	Y → F: Impairs binding to chromatin. Ref.4 Ref.7
	Sequence conflict	41 – 42	2	NF → SL in CAC69992. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 1, 2009. Version 2. Checksum: 14E7A817877EB114	FASTA	1,889	209,618
	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
	Isoform 2 [UniParc]. Checksum: 1D218D87B4861FBB	FASTA	1,888	209,490
	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 SQVEEEYTQR PGFPKRGQKR KSSFPLTFPE 1750 1760 1770 1780 1790 1800 GDSRRRMLSR SRDSPAVPRY PEDGLSPPKR RRHSMRSHHS DLTFCEIILM EMESHDAAWP 1810 1820 1830 1840 1850 1860 FLEPVNPRLV SGYRRVIKNP MDFSTMRERL LRGGYTSSEE FAADALLVFD NCQTFNEDDS 1870 1880 EVGKAGHVMR RFFESRWEEF YQGKQANL
	Isoform 3 [UniParc]. Checksum: 0A2259C4955FFFBB	FASTA	1,890	209,689
	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 PFDSLAAAEP VSGSLYGIDD AELMGAEDKL PLEGNPVISA LDCPALSNAN AFSLLADDSQ 370 380 390 400 410 420 TSASIFVSPT SPPVLGESVL QDNSFGLNSC SDSEQEEIET QSSNFQRPLT EPAPDQPPST 430 440 450 460 470 480 QLHPAVSPTA SPAASLTASA EISPAVSPVA SSPVPPEVFV AVSPASSPAL PAISLEASMT 490 500 510 520 530 540 TPVTSPQGSP EPSPAAAFQT VSPARKNVSS APKARADREE TTGGAVAVSG SGDVLKRRIA 550 560 570 580 590 600 TPEEVRLPLQ HGWRREVRIK KGSHRWQGET WYYGPCGKRM KQFPEVIKYL SRNVVHSVRR 610 620 630 640 650 660 EHFSFSPRMP VGDFFEERDT PEGLQWVQLS AEEIPSRIQA ITGKRGRPRN NEKAKNKEVP 670 680 690 700 710 720 KVKRGRGRPP KIKMPELLNK TDNRLPKKLE TQEILSEDDK AKMTKNKKKM RQKVQRGESQ 730 740 750 760 770 780 TPVQGQARNK RKQDTKSLKQ KDTKKKLKAE KEKMKTKQEK LKEKVKREKK EKVKAKGKEG 790 800 810 820 830 840 PRARPSCRAD KTLATQKRLE EQQRQQAILE EMKKPTEGMC LSDHQPLPDF TRIPGLTLSS 850 860 870 880 890 900 RAFSDCLTIV EFLHSFGKVL GFDLTKDVPS LGVLQEGLLC QGDSLDKVQD LLVRLLKAAL 910 920 930 940 950 960 HDPGLPPYCQ SLKILGEKMS EIPLTRDNVS EILRCFLMAY RVEPPFCDSL RTQPFQAQPP 970 980 990 1000 1010 1020 QQKAAILAFL VHELNSSTII INEIDKTLES VSSCRKNKWI VEGRLRRLKT ALAKRTGRPE 1030 1040 1050 1060 1070 1080 VMMEGAEDGL GRRRSSRIME ETSGIEEEEE EENTTAVHGR RGRKEGEIDV AASSIPELER 1090 1100 1110 1120 1130 1140 HIEKLSKRQL FFRKKLLHSS QMLRAVSLGQ DRYRRHYWVL PYLAGIFVEG SEGSTVTEDE 1150 1160 1170 1180 1190 1200 IKQETESLME VVTSTPSSAR ASVKRELTGS NASTSPARSR GRPRKPKPGS LQPQHLQSTI 1210 1220 1230 1240 1250 1260 RECDSEQAQT QVHPEPQPQL QAPTQPHLQP SSGFLEPEGS PFSLGQSQHD LSQSAFLSWL 1270 1280 1290 1300 1310 1320 SQTQSHNSLL SSSVLTPDSS PGKLDSAPSQ SLEEPEPDEA QSCPGPQGPW FNFSAQIPCD 1330 1340 1350 1360 1370 1380 AAPTPPPAVS EDQPTPSLQL LASSKPMNTP GAANPCSPVQ LSSTHLPGGT PKRLSGDSEE 1390 1400 1410 1420 1430 1440 MSQSPTGLGQ PKRRGRPPSK FFKQVEQHYL TQLTAQPIPP EMCSGWWWIR DPETLDVLLK 1450 1460 1470 1480 1490 1500 ALHPRGIREK ALHKHLSKHK DFLQEVCLQP LTDPIFEPNE LPALEEGVMS WSPKEKTYET 1510 1520 1530 1540 1550 1560 DLAVLQWVEE LEQRVVLSDL QIRGWTCPTP DSTREDLTYC EHLPDSPEDI PWRGRGREGT 1570 1580 1590 1600 1610 1620 VPQRQNNNPL DLAVMRLAVL EQNVERRYLR EPLWAAHEVV VEKALLSTPN GAPDGTSTEI 1630 1640 1650 1660 1670 1680 SYEITPRVRV WRQTLERCRS AAQVCLCMGQ LERSIAWEKS VNKVTCLVCR KGDNDEFLLL 1690 1700 1710 1720 1730 1740 CDGCDRGCHI YCHRPKMEAV PEGDWFCAVC LSQQVEEEYT QRPGFPKRGQ KRKSSFPLTF 1750 1760 1770 1780 1790 1800 PEGDSRRRML SRSRDSPAVP RYPEDGLSPP KRRRHSMRSH HSDLTFCEII LMEMESHDAA 1810 1820 1830 1840 1850 1860 WPFLEPVNPR LVSGYRRVIK NPMDFSTMRE RLLRGGYTSS EEFAADALLV FDNCQTFNED 1870 1880 1890 DSEVGKAGHV MRRFFESRWE EFYQGKQANL

References

	« Hide 'large scale' referencesShow '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. , 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.
UniGene	Mm.252213.
3D structure databases
ProteinModelPortal	Q91YE5.
SMR	Q91YE5. Positions 547-606, 1659-1882.
ModBase	Search...
MobiDB	Search...
PTM databases
PhosphoSite	Q91YE5.
Proteomic databases
PaxDb	Q91YE5.
PRIDE	Q91YE5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:2151152. Baz2a.
Rouge	Search...
Phylogenomic databases
eggNOG	COG5076.
HOGENOM	HOG000169644.
HOVERGEN	HBG107494.
InParanoid	Q80U42.
PhylomeDB	Q91YE5.
Gene expression databases
CleanEx	MM_BAZ2A.
Genevestigator	Q91YE5.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 1 hit. 3.30.890.10. 1 hit.
InterPro	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]
PANTHER	PTHR22880:SF2. PTHR22880:SF2. 1 hit.
Pfam	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]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00384. AT_hook. 4 hits. SM00297. BROMO. 1 hit. SM00571. DDT. 1 hit. SM00391. MBD. 1 hit. SM00249. PHD. 1 hit. [Graphical view]
SUPFAM	SSF47370. SSF47370. 1 hit. SSF54171. SSF54171. 1 hit. SSF57903. SSF57903. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	BAZ2A. mouse.
PRO	Q91YE5.
SOURCE	Search...

Entry information

Entry name

BAZ2A_MOUSE

Accession

Primary (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:	April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program