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Protein

Bromodomain adjacent to zinc finger domain protein 2A

Gene

BAZ2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi649 – 661A.T hook 1Add BLAST13
DNA bindingi670 – 682A.T hook 2Add BLAST13
DNA bindingi1186 – 1198A.T hook 3Add BLAST13
DNA bindingi1404 – 1416A.T hook 4Add BLAST13
Zinc fingeri1676 – 1726PHD-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: BHF-UCL
  • lysine-acetylated histone binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase I CORE element sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • chromatin remodeling Source: UniProtKB
  • chromatin silencing at rDNA Source: UniProtKB
  • DNA methylation Source: UniProtKB
  • histone deacetylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB
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

BioCyciZFISH:ENSG00000076108-MONOMER.
ReactomeiR-HSA-427413. 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
hWALp3
Gene namesi
Name:BAZ2A
Synonyms:KIAA0314, TIP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:962. BAZ2A.

Subcellular locationi

  • Nucleusnucleolus By similarity

  • Note: Colocalizes with the basal RNA polymerase I transcription factor UBF in the nucleolus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi11176.
OpenTargetsiENSG00000076108.
PharmGKBiPA25272.

Chemistry databases

ChEMBLiCHEMBL3108642.
GuidetoPHARMACOLOGYi2721.

Polymorphism and mutation databases

BioMutaiBAZ2A.
DMDMi257051081.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002111721 – 1905Bromodomain adjacent to zinc finger domain protein 2AAdd BLAST1905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei507PhosphothreonineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Modified residuei548PhosphothreonineCombined sources1
Modified residuei613PhosphoserineCombined sources1
Modified residuei680N6-acetyllysine; by KAT81 Publication1
Modified residuei799N6-acetyllysineBy similarity1
Modified residuei1051PhosphoserineBy similarity1
Cross-linki1150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1184PhosphoserineBy similarity1
Modified residuei1397PhosphoserineCombined sources1
Modified residuei1559PhosphoserineCombined sources1
Modified residuei1747PhosphoserineCombined sources1
Modified residuei1770PhosphoserineCombined sources1
Modified residuei1783PhosphoserineCombined sources1
Modified residuei1785PhosphoserineCombined sources1

Post-translational modificationi

Acetylation at Lys-680 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 (By similarity).By similarity
Ubiquitinated. Deubiquitinated by USP21 leading to its stabilization.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UIF9.
PaxDbiQ9UIF9.
PeptideAtlasiQ9UIF9.
PRIDEiQ9UIF9.

PTM databases

iPTMnetiQ9UIF9.
PhosphoSitePlusiQ9UIF9.

Expressioni

Tissue specificityi

Expressed at moderate levels in most tissues analyzed, including heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiENSG00000076108.
CleanExiHS_BAZ2A.
ExpressionAtlasiQ9UIF9. baseline and differential.
GenevisibleiQ9UIF9. HS.

Organism-specific databases

HPAiHPA005782.
HPA063806.

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 (By similarity). Interacts with BEND3 and USP21.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-934890,EBI-389883
Ttf1Q621873EBI-934890,EBI-11705418From a different organism.

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: BHF-UCL
  • lysine-acetylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116346. 17 interactors.
IntActiQ9UIF9. 9 interactors.
MINTiMINT-7240976.
STRINGi9606.ENSP00000446880.

Chemistry databases

BindingDBiQ9UIF9.

Structurei

Secondary structure

11905
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi549 – 558Combined sources10
Beta strandi561 – 568Combined sources8
Beta strandi570 – 580Combined sources11
Beta strandi582 – 584Combined sources3
Helixi590 – 599Combined sources10
Helixi607 – 609Combined sources3
Beta strandi618 – 627Combined sources10
Beta strandi630 – 636Combined sources7
Turni638 – 640Combined sources3
Helixi641 – 648Combined sources8
Helixi1674 – 1676Combined sources3
Turni1680 – 1682Combined sources3
Helixi1688 – 1690Combined sources3
Beta strandi1691 – 1693Combined sources3
Beta strandi1695 – 1698Combined sources4
Beta strandi1700 – 1702Combined sources3
Turni1703 – 1705Combined sources3
Helixi1721 – 1724Combined sources4
Helixi1796 – 1811Combined sources16
Helixi1813 – 1818Combined sources6
Turni1824 – 1826Combined sources3
Helixi1830 – 1833Combined sources4
Helixi1840 – 1848Combined sources9
Helixi1855 – 1872Combined sources18
Helixi1878 – 1894Combined sources17
Helixi1895 – 1898Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LZ2X-ray1.76A1796-1899[»]
4Q6FX-ray1.91A/B/C/D1673-1728[»]
4QBMX-ray1.65A/B1796-1899[»]
4QF2X-ray1.70A/B/C/D1673-1728[»]
5AGQNMR-A543-650[»]
ProteinModelPortaliQ9UIF9.
SMRiQ9UIF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini546 – 617MBDPROSITE-ProRule annotationAdd BLAST72
Domaini848 – 913DDTPROSITE-ProRule annotationAdd BLAST66
Domaini1810 – 1880BromoPROSITE-ProRule annotationAdd BLAST71

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili693 – 792Sequence analysisAdd BLAST100

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi660 – 799Lys-richAdd BLAST140
Compositional biasi1212 – 1277Glu-richAdd BLAST66
Compositional biasi1290 – 1411Pro-richAdd BLAST122
Compositional biasi1759 – 1762Poly-Arg4

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 (By similarity).By similarity

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)DescriptionActionsGraphical viewLength
Zinc fingeri1676 – 1726PHD-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1245. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000169644.
HOVERGENiHBG107494.
InParanoidiQ9UIF9.
KOiK15224.
OMAiQKRKSGY.
OrthoDBiEOG091G00WO.
PhylomeDBiQ9UIF9.
TreeFamiTF329083.

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.
IPR018501. DDT_dom.
IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR028940. TIP5.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22880:SF141. PTHR22880:SF141. 3 hits.
PfamiPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WSD. 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. AlignAdd to basket

Isoform 2 (identifier: Q9UIF9-1) [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 HLHHPSVAYD CLWNYSQYPS
110 120 130 140 150
ANPGSNLKDP PLLSQFSGGQ YPLNGILGGS RQPSSPSHNT NLRAGSQEFW
160 170 180 190 200
ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI
210 220 230 240 250
QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL EEEQPELKMC
260 270 280 290 300
GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE
310 320 330 340 350
PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA
360 370 380 390 400
FSLLADDSQT STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ
410 420 430 440 450
SSDFPPSLTQ PAPDQSSTIQ LHPATSPAVS PTTSPAVSLV VSPAASPEIS
460 470 480 490 500
PEVCPAASTV VSPAVFSVVS PASSAVLPAV SLEVPLTASV TSPKASPVTS
510 520 530 540 550
PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD VMRRRIATPE
560 570 580 590 600
EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN
610 620 630 640 650
VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG
660 670 680 690 700
KRGRPRNTEK AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE
710 720 730 740 750
TLNEEDKAKI AKSKKKMRQK VQRGECQTTI QGQARNKRKQ ETKSLKQKEA
760 770 780 790 800
KKKSKAEKEK GKTKQEKLKE KVKREKKEKV KMKEKEEVTK AKPACKADKT
810 820 830 840 850
LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR VPGLTLPSGA
860 870 880 890 900
FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL
910 920 930 940 950
VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV
960 970 980 990 1000
EPALCDRLRT QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS
1010 1020 1030 1040 1050
SYRKNKWIVE GRLRRLKTVL AKRTGRSEVE MEGPEECLGR RRSSRIMEET
1060 1070 1080 1090 1100
SGMEEEEEEE SIAAVPGRRG RRDGEVDATA SSIPELERQI EKLSKRQLFF
1110 1120 1130 1140 1150
RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE GNLVPEEVIK
1160 1170 1180 1190 1200
KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM
1210 1220 1230 1240 1250
QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ
1260 1270 1280 1290 1300
EGSPLSLGQS QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA
1310 1320 1330 1340 1350
PSQPPEEPEP DEAESSPDPQ ALWFNISAQM PCNAAPTPPP AVSEDQPTPS
1360 1370 1380 1390 1400
PQQLASSKPM NRPSAANPCS PVQFSSTPLA GLAPKRRAGD PGEMPQSPTG
1410 1420 1430 1440 1450
LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW WIRDPEMLDA
1460 1470 1480 1490 1500
MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG
1510 1520 1530 1540 1550
IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL
1560 1570 1580 1590 1600
AYCEHLSDSQ EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR
1610 1620 1630 1640 1650
YLREPLWPTH EVVLEKALLS TPNGAPEGTT TEISYEITPR IRVWRQTLER
1660 1670 1680 1690 1700
CRSAAQVCLC LGQLERSIAW EKSVNKVTCL VCRKGDNDEF LLLCDGCDRG
1710 1720 1730 1740 1750
CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK RGQKRKSGYS
1760 1770 1780 1790 1800
LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT
1810 1820 1830 1840 1850
FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG
1860 1870 1880 1890 1900
GYTSSEEFAA DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG

KQANL
Length:1,905
Mass (Da):211,198
Last modified:September 1, 2009 - v4
Checksum:iF364E2AC4BF89EA2
GO
Isoform 1 (identifier: Q9UIF9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     6-6: N → NEAN
     178-207: Missing.

Note: No experimental confirmation available.
Show »
Length:1,878
Mass (Da):208,390
Checksum:i8F197C2BE4F4EB4A
GO
Isoform 3 (identifier: Q9UIF9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1434-1437: Missing.

Note: No experimental confirmation available.
Show »
Length:1,901
Mass (Da):210,747
Checksum:i00A922530275504E
GO

Sequence cautioni

The sequence AAB60864 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAG51228 differs from that shown. Reason: Erroneous termination at position 168. Translated as Tyr.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106N → S in CAH18232 (PubMed:17974005).Curated1
Sequence conflicti148E → K in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti155Q → H in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti207Q → P in CAH18232 (PubMed:17974005).Curated1
Sequence conflicti210G → C in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti236G → C in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti503A → T in CAH18232 (PubMed:17974005).Curated1
Sequence conflicti601V → L in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti727Q → L in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti747Q → H in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti812R → K in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti978L → P in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1032 – 1033EG → GR in BAA89211 (PubMed:10662543).Curated2
Sequence conflicti1190G → S in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1193R → L in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1199S → F in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1205L → F in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1229A → V in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1274S → N in CAH18232 (PubMed:17974005).Curated1
Sequence conflicti1319P → L in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1322L → F in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1340P → L in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1443R → P in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1568R → P in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1598E → K in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1643V → I in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1649E → Q in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1656Q → H in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1663Q → H in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1766R → K in BAA89211 (PubMed:10662543).Curated1
Sequence conflicti1781G → R in BAA89211 (PubMed:10662543).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055548498V → E.Corresponds to variant rs2230579dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0379606N → NEAN in isoform 1. 1 Publication1
Alternative sequenceiVSP_019111178 – 207Missing in isoform 1. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_0379611434 – 1437Missing in isoform 3. Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032254 mRNA. Translation: BAA89211.1.
CR749379 mRNA. Translation: CAH18232.1.
AC090681 Genomic DNA. No translation available.
AB002312 mRNA. Translation: BAA20773.2.
AK023830 mRNA. Translation: BAG51228.1. Sequence problems.
AF000422 mRNA. Translation: AAB60864.1. Sequence problems.
BC008965 mRNA. Translation: AAH08965.2.
CCDSiCCDS44924.1. [Q9UIF9-1]
RefSeqiNP_038477.2. NM_013449.3. [Q9UIF9-1]
UniGeneiHs.314263.

Genome annotation databases

EnsembliENST00000551812; ENSP00000446880; ENSG00000076108. [Q9UIF9-1]
GeneIDi11176.
KEGGihsa:11176.
UCSCiuc001slq.2. human. [Q9UIF9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032254 mRNA. Translation: BAA89211.1.
CR749379 mRNA. Translation: CAH18232.1.
AC090681 Genomic DNA. No translation available.
AB002312 mRNA. Translation: BAA20773.2.
AK023830 mRNA. Translation: BAG51228.1. Sequence problems.
AF000422 mRNA. Translation: AAB60864.1. Sequence problems.
BC008965 mRNA. Translation: AAH08965.2.
CCDSiCCDS44924.1. [Q9UIF9-1]
RefSeqiNP_038477.2. NM_013449.3. [Q9UIF9-1]
UniGeneiHs.314263.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LZ2X-ray1.76A1796-1899[»]
4Q6FX-ray1.91A/B/C/D1673-1728[»]
4QBMX-ray1.65A/B1796-1899[»]
4QF2X-ray1.70A/B/C/D1673-1728[»]
5AGQNMR-A543-650[»]
ProteinModelPortaliQ9UIF9.
SMRiQ9UIF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116346. 17 interactors.
IntActiQ9UIF9. 9 interactors.
MINTiMINT-7240976.
STRINGi9606.ENSP00000446880.

Chemistry databases

BindingDBiQ9UIF9.
ChEMBLiCHEMBL3108642.
GuidetoPHARMACOLOGYi2721.

PTM databases

iPTMnetiQ9UIF9.
PhosphoSitePlusiQ9UIF9.

Polymorphism and mutation databases

BioMutaiBAZ2A.
DMDMi257051081.

Proteomic databases

EPDiQ9UIF9.
PaxDbiQ9UIF9.
PeptideAtlasiQ9UIF9.
PRIDEiQ9UIF9.

Protocols and materials databases

DNASUi11176.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000551812; ENSP00000446880; ENSG00000076108. [Q9UIF9-1]
GeneIDi11176.
KEGGihsa:11176.
UCSCiuc001slq.2. human. [Q9UIF9-1]

Organism-specific databases

CTDi11176.
DisGeNETi11176.
GeneCardsiBAZ2A.
H-InvDBHIX0010736.
HGNCiHGNC:962. BAZ2A.
HPAiHPA005782.
HPA063806.
MIMi605682. gene.
neXtProtiNX_Q9UIF9.
OpenTargetsiENSG00000076108.
PharmGKBiPA25272.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1245. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000169644.
HOVERGENiHBG107494.
InParanoidiQ9UIF9.
KOiK15224.
OMAiQKRKSGY.
OrthoDBiEOG091G00WO.
PhylomeDBiQ9UIF9.
TreeFamiTF329083.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000076108-MONOMER.
ReactomeiR-HSA-427413. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiBAZ2A. human.
GeneWikiiBAZ2A.
GenomeRNAii11176.
PROiQ9UIF9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000076108.
CleanExiHS_BAZ2A.
ExpressionAtlasiQ9UIF9. baseline and differential.
GenevisibleiQ9UIF9. HS.

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.
IPR018501. DDT_dom.
IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR028940. TIP5.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22880:SF141. PTHR22880:SF141. 3 hits.
PfamiPF00439. Bromodomain. 1 hit.
PF02791. DDT. 1 hit.
PF01429. MBD. 1 hit.
PF00628. PHD. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WSD. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiBAZ2A_HUMAN
AccessioniPrimary (citable) accession number: Q9UIF9
Secondary accession number(s): B3KN66
, O00536, O15030, Q68DI8, Q96H26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: September 1, 2009
Last modified: November 2, 2016
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.