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Q9UIF9

- BAZ2A_HUMAN

UniProt

Q9UIF9 - BAZ2A_HUMAN

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. RNA binding Source: UniProtKB
    6. 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

    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

    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

    ArrayExpressiQ9UIF9.
    BgeeiQ9UIF9.
    CleanExiHS_BAZ2A.
    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 – 16763
    Turni1680 – 16823
    Helixi1688 – 16903
    Beta strandi1691 – 16933
    Beta strandi1695 – 16984
    Beta strandi1700 – 17023
    Turni1703 – 17053
    Helixi1721 – 17266
    Helixi1796 – 181116
    Helixi1813 – 18186
    Turni1824 – 18263
    Helixi1830 – 18334
    Helixi1840 – 18489
    Helixi1855 – 187218
    Helixi1878 – 189417
    Helixi1895 – 18984

    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[»]
    ProteinModelPortaliQ9UIF9.
    SMRiQ9UIF9. Positions 554-614, 1673-1898.
    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.
    HOGENOMiHOG000169644.
    HOVERGENiHBG107494.
    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

    MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN     50
    GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPSVAYD CLWNYSQYPS 100
    ANPGSNLKDP PLLSQFSGGQ YPLNGILGGS RQPSSPSHNT NLRAGSQEFW 150
    ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI 200
    QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL EEEQPELKMC 250
    GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 300
    PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA 350
    FSLLADDSQT STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ 400
    SSDFPPSLTQ PAPDQSSTIQ LHPATSPAVS PTTSPAVSLV VSPAASPEIS 450
    PEVCPAASTV VSPAVFSVVS PASSAVLPAV SLEVPLTASV TSPKASPVTS 500
    PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD VMRRRIATPE 550
    EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN 600
    VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG 650
    KRGRPRNTEK AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE 700
    TLNEEDKAKI AKSKKKMRQK VQRGECQTTI QGQARNKRKQ ETKSLKQKEA 750
    KKKSKAEKEK GKTKQEKLKE KVKREKKEKV KMKEKEEVTK AKPACKADKT 800
    LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR VPGLTLPSGA 850
    FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL 900
    VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV 950
    EPALCDRLRT QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS 1000
    SYRKNKWIVE GRLRRLKTVL AKRTGRSEVE MEGPEECLGR RRSSRIMEET 1050
    SGMEEEEEEE SIAAVPGRRG RRDGEVDATA SSIPELERQI EKLSKRQLFF 1100
    RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE GNLVPEEVIK 1150
    KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM 1200
    QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ 1250
    EGSPLSLGQS QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA 1300
    PSQPPEEPEP DEAESSPDPQ ALWFNISAQM PCNAAPTPPP AVSEDQPTPS 1350
    PQQLASSKPM NRPSAANPCS PVQFSSTPLA GLAPKRRAGD PGEMPQSPTG 1400
    LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW WIRDPEMLDA 1450
    MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG 1500
    IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL 1550
    AYCEHLSDSQ EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR 1600
    YLREPLWPTH EVVLEKALLS TPNGAPEGTT TEISYEITPR IRVWRQTLER 1650
    CRSAAQVCLC LGQLERSIAW EKSVNKVTCL VCRKGDNDEF LLLCDGCDRG 1700
    CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK RGQKRKSGYS 1750
    LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT 1800
    FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG 1850
    GYTSSEEFAA DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG 1900
    KQANL 1905
    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 [» ]
    ProteinModelPortali Q9UIF9.
    SMRi Q9UIF9. Positions 554-614, 1673-1898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

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

    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.
    HOGENOMi HOG000169644.
    HOVERGENi HBG107494.
    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

    ArrayExpressi Q9UIF9.
    Bgeei Q9UIF9.
    CleanExi HS_BAZ2A.
    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

    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 1, 2014
    This is version 141 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