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Q9UIF9

- BAZ2A_HUMAN

UniProt

Q9UIF9 - BAZ2A_HUMAN

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Protein

Bromodomain adjacent to zinc finger domain protein 2A

Gene

BAZ2A

Organism
Homo sapiens (Human)
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 By similarity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi649 – 66113A.T hook 1Add
BLAST
DNA bindingi670 – 68213A.T hook 2Add
BLAST
DNA bindingi1186 – 119813A.T hook 3Add
BLAST
DNA bindingi1404 – 141613A.T hook 4Add
BLAST
Zinc fingeri1676 – 172651PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. ligand-dependent nuclear receptor binding Source: BHF-UCL
  3. lysine-acetylated histone binding Source: UniProtKB
  4. RNA binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin remodeling Source: UniProtKB
  2. chromatin silencing at rDNA Source: UniProtKB
  3. DNA methylation Source: UniProtKB
  4. heterochromatin assembly involved in chromatin silencing Source: Ensembl
  5. histone deacetylation Source: UniProtKB
  6. histone H3-K9 methylation Source: Ensembl
  7. histone H4 deacetylation Source: Ensembl
  8. histone H4-K20 methylation Source: Ensembl
  9. regulation of transcription, DNA-templated Source: UniProtKB
  10. 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

ReactomeiREACT_200856. 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
ProteomesiUP000005640: 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

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19051905Bromodomain adjacent to zinc finger domain protein 2APRO_0000211172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei509 – 5091Phosphoserine2 Publications
Modified residuei680 – 6801N6-acetyllysine; by KAT81 Publication
Modified residuei799 – 7991N6-acetyllysineBy similarity
Modified residuei1397 – 13971Phosphoserine3 Publications
Modified residuei1559 – 15591Phosphoserine1 Publication
Modified residuei1747 – 17471Phosphoserine1 Publication
Modified residuei1770 – 17701Phosphoserine2 Publications
Modified residuei1783 – 17831Phosphoserine4 Publications
Modified residuei1785 – 17851Phosphoserine1 Publication

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UIF9.
PaxDbiQ9UIF9.
PRIDEiQ9UIF9.

PTM databases

PhosphoSiteiQ9UIF9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9UIF9.
CleanExiHS_BAZ2A.
ExpressionAtlasiQ9UIF9. baseline and differential.
GenevestigatoriQ9UIF9.

Organism-specific databases

HPAiHPA005782.

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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-934890,EBI-389883

Protein-protein interaction databases

BioGridi116346. 11 interactions.
IntActiQ9UIF9. 7 interactions.
MINTiMINT-7240976.
STRINGi9606.ENSP00000368754.

Structurei

Secondary structure

1
1905
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1674 – 16763Combined sources
Turni1680 – 16823Combined sources
Helixi1688 – 16903Combined sources
Beta strandi1691 – 16933Combined sources
Beta strandi1695 – 16984Combined sources
Beta strandi1700 – 17023Combined sources
Turni1703 – 17053Combined sources
Helixi1721 – 17266Combined sources
Helixi1796 – 181116Combined sources
Helixi1813 – 18186Combined sources
Turni1824 – 18263Combined sources
Helixi1830 – 18334Combined sources
Helixi1840 – 18489Combined sources
Helixi1855 – 187218Combined sources
Helixi1878 – 189417Combined sources
Helixi1895 – 18984Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9UIF9.
SMRiQ9UIF9. Positions 1673-1899.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini546 – 61772MBDPROSITE-ProRule annotationAdd
BLAST
Domaini848 – 91366DDTPROSITE-ProRule annotationAdd
BLAST
Domaini1810 – 188071BromoPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili693 – 792100Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi660 – 799140Lys-richAdd
BLAST
Compositional biasi1212 – 127766Glu-richAdd
BLAST
Compositional biasi1290 – 1411122Pro-richAdd
BLAST
Compositional biasi1759 – 17624Poly-Arg

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1676 – 172651PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000169644.
HOVERGENiHBG107494.
InParanoidiQ9UIF9.
KOiK15224.
OMAiNYSQYPS.
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.
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 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 AAB60864.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAG51228.1 differs from that shown. Reason: Erroneous termination at position 168. Translated as Tyr.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061N → S in CAH18232. (PubMed:17974005)Curated
Sequence conflicti148 – 1481E → K in BAA89211. (PubMed:10662543)Curated
Sequence conflicti155 – 1551Q → H in BAA89211. (PubMed:10662543)Curated
Sequence conflicti207 – 2071Q → P in CAH18232. (PubMed:17974005)Curated
Sequence conflicti210 – 2101G → C in BAA89211. (PubMed:10662543)Curated
Sequence conflicti236 – 2361G → C in BAA89211. (PubMed:10662543)Curated
Sequence conflicti503 – 5031A → T in CAH18232. (PubMed:17974005)Curated
Sequence conflicti601 – 6011V → L in BAA89211. (PubMed:10662543)Curated
Sequence conflicti727 – 7271Q → L in BAA89211. (PubMed:10662543)Curated
Sequence conflicti747 – 7471Q → H in BAA89211. (PubMed:10662543)Curated
Sequence conflicti812 – 8121R → K in BAA89211. (PubMed:10662543)Curated
Sequence conflicti978 – 9781L → P in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1032 – 10332EG → GR in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1190 – 11901G → S in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1193 – 11931R → L in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1199 – 11991S → F in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1205 – 12051L → F in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1229 – 12291A → V in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1274 – 12741S → N in CAH18232. (PubMed:17974005)Curated
Sequence conflicti1319 – 13191P → L in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1322 – 13221L → F in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1340 – 13401P → L in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1443 – 14431R → P in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1568 – 15681R → P in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1598 – 15981E → K in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1643 – 16431V → I in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1649 – 16491E → Q in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1656 – 16561Q → H in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1663 – 16631Q → H in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1766 – 17661R → K in BAA89211. (PubMed:10662543)Curated
Sequence conflicti1781 – 17811G → R in BAA89211. (PubMed:10662543)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti498 – 4981V → E.
Corresponds to variant rs2230579 [ dbSNP | Ensembl ].
VAR_055548

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei6 – 61N → NEAN in isoform 1. 1 PublicationVSP_037960
Alternative sequencei178 – 20730Missing in isoform 1. 1 PublicationVSP_019111Add
BLAST
Alternative sequencei1434 – 14374Missing in isoform 3. CuratedVSP_037961

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000549787; ENSP00000448760; ENSG00000076108.
ENST00000551812; ENSP00000446880; ENSG00000076108. [Q9UIF9-1]
GeneIDi11176.
KEGGihsa:11176.
UCSCiuc001slp.1. human. [Q9UIF9-1]

Polymorphism databases

DMDMi257051081.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS44924.1. [Q9UIF9-1 ]
RefSeqi NP_038477.2. NM_013449.3. [Q9UIF9-1 ]
UniGenei Hs.314263.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LZ2 X-ray 1.76 A 1796-1899 [» ]
4Q6F X-ray 1.91 A/B/C/D 1673-1728 [» ]
4QBM X-ray 1.65 A/B 1796-1899 [» ]
4QF2 X-ray 1.70 A/B/C/D 1673-1728 [» ]
ProteinModelPortali Q9UIF9.
SMRi Q9UIF9. Positions 1673-1899.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116346. 11 interactions.
IntActi Q9UIF9. 7 interactions.
MINTi MINT-7240976.
STRINGi 9606.ENSP00000368754.

Chemistry

ChEMBLi CHEMBL3108642.

PTM databases

PhosphoSitei Q9UIF9.

Polymorphism databases

DMDMi 257051081.

Proteomic databases

MaxQBi Q9UIF9.
PaxDbi Q9UIF9.
PRIDEi Q9UIF9.

Protocols and materials databases

DNASUi 11176.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000549787 ; ENSP00000448760 ; ENSG00000076108 .
ENST00000551812 ; ENSP00000446880 ; ENSG00000076108 . [Q9UIF9-1 ]
GeneIDi 11176.
KEGGi hsa:11176.
UCSCi uc001slp.1. human. [Q9UIF9-1 ]

Organism-specific databases

CTDi 11176.
GeneCardsi GC12M056954.
H-InvDB HIX0010736.
HGNCi HGNC:962. BAZ2A.
HPAi HPA005782.
MIMi 605682. gene.
neXtProti NX_Q9UIF9.
PharmGKBi PA25272.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119099.
HOGENOMi HOG000169644.
HOVERGENi HBG107494.
InParanoidi Q9UIF9.
KOi K15224.
OMAi NYSQYPS.
PhylomeDBi Q9UIF9.
TreeFami TF329083.

Enzyme and pathway databases

Reactomei REACT_200856. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSi BAZ2A. human.
GeneWikii BAZ2A.
GenomeRNAii 11176.
NextBioi 42525.
PROi Q9UIF9.
SOURCEi Search...

Gene expression databases

Bgeei Q9UIF9.
CleanExi HS_BAZ2A.
ExpressionAtlasi Q9UIF9. baseline and differential.
Genevestigatori Q9UIF9.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1905 (ISOFORM 2).
    Tissue: Brain.
  5. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-1905 (ISOFORMS 1/2).
    Tissue: Placenta.
  7. Jansa P., Grummt I.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 359-753.
    Tissue: Lung.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1905.
    Tissue: Lymph.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747; SER-1770 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-680.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1397 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-1397; SER-1770 AND SER-1783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-509; SER-1397; SER-1783 AND SER-1785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 142 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

External Data

Dasty 3