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Q9UIF8

- BAZ2B_HUMAN

UniProt

Q9UIF8 - BAZ2B_HUMAN

Protein

Bromodomain adjacent to zinc finger domain protein 2B

Gene

BAZ2B

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 3 (05 May 2009)
      Previous versions | rss
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    Functioni

    May play a role in transcriptional regulation interacting with ISWI.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1931 – 198151PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: BHF-UCL
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: BHF-UCL
    2. transcription, DNA-templated Source: BHF-UCL

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bromodomain adjacent to zinc finger domain protein 2B
    Alternative name(s):
    hWALp4
    Gene namesi
    Name:BAZ2B
    Synonyms:KIAA1476
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:963. BAZ2B.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25273.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21682168Bromodomain adjacent to zinc finger domain protein 2BPRO_0000211174Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1462 – 14621N6-acetyllysine1 Publication
    Cross-linki1538 – 1538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei1680 – 16801Phosphoserine1 Publication
    Modified residuei2014 – 20141Phosphothreonine1 Publication
    Modified residuei2019 – 20191Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UIF8.
    PaxDbiQ9UIF8.
    PRIDEiQ9UIF8.

    PTM databases

    PhosphoSiteiQ9UIF8.

    Expressioni

    Tissue specificityi

    Expressed at varying levels in several tissues, whereas a smaller transcript was expressed specifically in testis.

    Gene expression databases

    ArrayExpressiQ9UIF8.
    BgeeiQ9UIF8.
    CleanExiHS_BAZ2B.
    GenevestigatoriQ9UIF8.

    Organism-specific databases

    HPAiHPA019819.

    Interactioni

    Subunit structurei

    Interacts with acetylated lysine residues on histone H1.4, H2A, H2B, H3 and H4 (in vitro).1 Publication

    Protein-protein interaction databases

    BioGridi119019. 5 interactions.
    IntActiQ9UIF8. 4 interactions.
    MINTiMINT-1483920.
    STRINGi9606.ENSP00000376534.

    Structurei

    Secondary structure

    1
    2168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2063 – 207715
    Helixi2080 – 20823
    Helixi2083 – 20853
    Turni2091 – 20933
    Beta strandi2094 – 20963
    Helixi2097 – 21004
    Helixi2107 – 21159
    Helixi2122 – 213918
    Beta strandi2142 – 21443
    Helixi2145 – 216521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E7ONMR-A2062-2166[»]
    3G0LX-ray2.03A2054-2168[»]
    3Q2FX-ray2.06A2054-2168[»]
    4CUPX-ray1.88A2054-2168[»]
    4CUQX-ray2.11A2054-2168[»]
    4CURX-ray1.84A2054-2168[»]
    4CUSX-ray1.78A2054-2168[»]
    4CUTX-ray1.84A2054-2168[»]
    4CUUX-ray1.80A2054-2168[»]
    4IR3X-ray2.00A2054-2168[»]
    4IR4X-ray2.05A2054-2168[»]
    4IR5X-ray1.70A2054-2168[»]
    4IR6X-ray1.80A2054-2168[»]
    4NR9X-ray1.98A2054-2168[»]
    4NRAX-ray1.85A2054-2168[»]
    4NRBX-ray2.08A2054-2168[»]
    4NRCX-ray1.86A2054-2168[»]
    4QC1X-ray1.99A/B2062-2166[»]
    4QC3X-ray1.60A/B2062-2166[»]
    ProteinModelPortaliQ9UIF8.
    SMRiQ9UIF8. Positions 748-806, 1929-2167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIF8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini739 – 81072MBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini1087 – 115266DDTPROSITE-ProRule annotationAdd
    BLAST
    Domaini2077 – 214771BromoPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili883 – 1061179Sequence AnalysisAdd
    BLAST
    Coiled coili1334 – 137542Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi149 – 265117Ser-richAdd
    BLAST
    Compositional biasi269 – 2757Poly-Glu
    Compositional biasi595 – 66672Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi837 – 86832Arg-richAdd
    BLAST
    Compositional biasi902 – 1061160Lys-richAdd
    BLAST
    Compositional biasi1296 – 133944Asp-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WAL family.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 fingeri1931 – 198151PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000231981.
    HOVERGENiHBG050670.
    InParanoidiQ9UIF8.
    OMAiDSDDQAD.
    OrthoDBiEOG783MTG.
    PhylomeDBiQ9UIF8.
    TreeFamiTF329083.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    3.30.890.10. 1 hit.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR004022. DDT_dom.
    IPR018500. DDT_dom_subgr.
    IPR018501. DDT_dom_superfamily.
    IPR016177. DNA-bd_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF01429. MBD. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. 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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9UIF8-1) [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

    MESGERLPSS AASSTTPTSS STPSVASVVS KGGLSTGVAS LSSTINPCGH     50
    LFRTAGDQPF NLSTVSSAFP MVSHPVFGLH SASSGHSEFG GLGTLGTPTA 100
    LAAHPQLASF PGAEWWRTTD AHTRTGATFF PPLLGIPPLF APPAQNHDSS 150
    SFHSRTSGKS NRNGPEKGVN GSINGSNTSS VIGINTSVLS TTASSSMGQT 200
    KSTSSGGGNR KCNQEQSKNQ PLDARVDKIK DKKPRKKAME SSSNSDSDSG 250
    TSSDTSSEGI SSSDSDDLEE DEEEEDQSIE ESEDDDSDSE SEAQHKSNNQ 300
    VLLHGISDPK ADGQKATEKA QEKRIHQPLP LASESQTHSF QSQQKQPQVL 350
    SQQLPFIFQS SQAKEESVNK HTSVIQSTGL VSNVKPLSLV NQAKKETYMK 400
    LIVPSPDVLK AGNKNTSEES SLLTSELRSK REQYKQAFPS QLKKQESSKS 450
    LKKVIAALSN PKATSSSPAH PKQTLENNHP NPFLTNALLG NHQPNGVIQS 500
    VIQEAPLALT TKTKMQSKIN ENIAAASSTP FSSPVNLSTS GRRTPGNQTP 550
    VMPSASPILH SQGKEKAVSN NVNPVKTQHH SHPAKSLVEQ FRGTDSDIPS 600
    SKDSEDSNED EEEDDEEEDE EDDEDDESDD SQSESDSNSE SDTEGSEEED 650
    DDDKDQDESD SDTEGEKTSM KLNKTTSSVK SPSMSLTGHS TPRNLHIAKA 700
    PGSAPAALCS ESQSPAFLGT SSSTLTSSPH SGTSKRRRVT DERELRIPLE 750
    YGWQRETRIR NFGGRLQGEV AYYAPCGKKL RQYPEVIKYL SRNGIMDISR 800
    DNFSFSAKIR VGDFYEARDG PQGMQWCLLK EEDVIPRIRA MEGRRGRPPN 850
    PDRQRAREES RMRRRKGRPP NVGNAEFLDN ADAKLLRKLQ AQEIARQAAQ 900
    IKLLRKLQKQ EQARVAKEAK KQQAIMAAEE KRKQKEQIKI MKQQEKIKRI 950
    QQIRMEKELR AQQILEAKKK KKEEAANAKL LEAEKRIKEK EMRRQQAVLL 1000
    KHQERERRRQ HMMLMKAMEA RKKAEEKERL KQEKRDEKRL NKERKLEQRR 1050
    LELEMAKELK KPNEDMCLAD QKPLPELPRI PGLVLSGSTF SDCLMVVQFL 1100
    RNFGKVLGFD VNIDVPNLSV LQEGLLNIGD SMGEVQDLLV RLLSAAVCDP 1150
    GLITGYKAKT ALGEHLLNVG VNRDNVSEIL QIFMEAHCGQ TELTESLKTK 1200
    AFQAHTPAQK ASVLAFLINE LACSKSVVSE IDKNIDYMSN LRRDKWVVEG 1250
    KLRKLRIIHA KKTGKRDTSG GIDLGEEQHP LGTPTPGRKR RRKGGDSDYD 1300
    DDDDDDSDDQ GDEDDEDEED KEDKKGKKTD ICEDEDEGDQ AASVEELEKQ 1350
    IEKLSKQQSQ YRRKLFDASH SLRSVMFGQD RYRRRYWILP QCGGIFVEGM 1400
    ESGEGLEEIA KEREKLKKAE SVQIKEEMFE TSGDSLNCSN TDHCEQKEDL 1450
    KEKDNTNLFL QKPGSFSKLS KLLEVAKMPP ESEVMTPKPN AGANGCTLSY 1500
    QNSGKHSLGS VQSTATQSNV EKADSNNLFN TGSSGPGKFY SPLPNDQLLK 1550
    TLTEKNRQWF SLLPRTPCDD TSLTHADMST ASLVTPQSQP PSKSPSPTPA 1600
    PLGSSAQNPV GLNPFALSPL QVKGGVSMMG LQFCGWPTGV VTSNIPFTSS 1650
    VPSLGSGLGL SEGNGNSFLT SNVASSKSES PVPQNEKATS AQPAAVEVAK 1700
    PVDFPSPKPI PEEMQFGWWR IIDPEDLKAL LKVLHLRGIR EKALQKQIQK 1750
    HLDYITQACL KNKDVAIIEL NENEENQVTR DIVENWSVEE QAMEMDLSVL 1800
    QQVEDLERRV ASASLQVKGW MCPEPASERE DLVYFEHKSF TKLCKEHDGE 1850
    FTGEDESSAH ALERKSDNPL DIAVTRLADL ERNIERRIEE DIAPGLRVWR 1900
    RALSEARSAA QVALCIQQLQ KSIAWEKSIM KVYCQICRKG DNEELLLLCD 1950
    GCDKGCHTYC HRPKITTIPD GDWFCPACIA KASGQTLKIK KLHVKGKKTN 2000
    ESKKGKKVTL TGDTEDEDSA STSSSLKRGN KDLKKRKMEE NTSINLSKQE 2050
    SFTSVKKPKR DDSKDLALCS MILTEMETHE DAWPFLLPVN LKLVPGYKKV 2100
    IKKPMDFSTI REKLSSGQYP NLETFALDVR LVFDNCETFN EDDSDIGRAG 2150
    HNMRKYFEKK WTDTFKVS 2168
    Length:2,168
    Mass (Da):240,459
    Last modified:May 5, 2009 - v3
    Checksum:iC64EEEE6243CF779
    GO
    Isoform 2 (identifier: Q9UIF8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         112-113: Missing.
         633-730: Missing.

    Show »
    Length:2,068
    Mass (Da):230,154
    Checksum:i324018D11EF97BAD
    GO
    Isoform 3 (identifier: Q9UIF8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         789-822: Missing.

    Show »
    Length:2,134
    Mass (Da):236,551
    Checksum:i6320F9BC6B744581
    GO
    Isoform 4 (identifier: Q9UIF8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-196: Missing.

    Show »
    Length:1,972
    Mass (Da):220,710
    Checksum:iB3BA3FD40027174C
    GO
    Isoform 5 (identifier: Q9UIF8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         112-113: Missing.
         789-822: Missing.

    Show »
    Length:2,132
    Mass (Da):236,423
    Checksum:i28286671FC56180F
    GO

    Sequence cautioni

    The sequence AAH12576.1 differs from that shown. Reason: contaminating sequence. Potential poly-A sequence.
    The sequence AAH12576.1 differs from that shown. Reason: Frameshift at position 927.
    The sequence BAA96000.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55231.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951L → G in AAH12576. (PubMed:15489334)Curated
    Sequence conflicti333 – 3331S → F in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti823 – 8231G → E in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti918 – 9181E → K in AAH12576. (PubMed:15489334)Curated
    Sequence conflicti986 – 9861R → Q in AAH12576. (PubMed:15489334)Curated
    Sequence conflicti1324 – 13241K → Q in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti1379 – 13791Q → P in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti1391 – 13911Q → R in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti1649 – 16491S → L in BAA89212. (PubMed:10662543)Curated
    Sequence conflicti2034 – 20341K → Q in BAA89212. (PubMed:10662543)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711M → T.1 Publication
    Corresponds to variant rs10202670 [ dbSNP | Ensembl ].
    VAR_055549
    Natural varianti422 – 4221L → S.2 Publications
    Corresponds to variant rs3213790 [ dbSNP | Ensembl ].
    VAR_055550
    Natural varianti530 – 5301P → L.
    Corresponds to variant rs3732287 [ dbSNP | Ensembl ].
    VAR_055551
    Natural varianti702 – 7021G → V.
    Corresponds to variant rs2302924 [ dbSNP | Ensembl ].
    VAR_055552
    Natural varianti2024 – 20241S → N.
    Corresponds to variant rs415793 [ dbSNP | Ensembl ].
    VAR_055553

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 196196Missing in isoform 4. 1 PublicationVSP_037114Add
    BLAST
    Alternative sequencei112 – 1132Missing in isoform 2 and isoform 5. 2 PublicationsVSP_037115
    Alternative sequencei633 – 73098Missing in isoform 2. 1 PublicationVSP_000553Add
    BLAST
    Alternative sequencei789 – 82234Missing in isoform 3 and isoform 5. 2 PublicationsVSP_000554Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032255 mRNA. Translation: BAA89212.1.
    AB040909 mRNA. Translation: BAA96000.2. Different initiation.
    AL080173 mRNA. Translation: CAB45759.1.
    AL834381 mRNA. Translation: CAD39044.2.
    CH471058 Genomic DNA. Translation: EAX11404.1.
    CH471058 Genomic DNA. Translation: EAX11405.1.
    CH471058 Genomic DNA. Translation: EAX11407.1.
    BC012576 mRNA. Translation: AAH12576.1. Sequence problems.
    AK027612 mRNA. Translation: BAB55231.1. Different initiation.
    CCDSiCCDS2209.2. [Q9UIF8-1]
    PIRiT12495.
    RefSeqiNP_001276904.1. NM_001289975.1. [Q9UIF8-5]
    NP_038478.2. NM_013450.3. [Q9UIF8-1]
    UniGeneiHs.470369.
    Hs.731786.

    Genome annotation databases

    EnsembliENST00000343439; ENSP00000339670; ENSG00000123636. [Q9UIF8-2]
    ENST00000392782; ENSP00000376533; ENSG00000123636. [Q9UIF8-5]
    ENST00000392783; ENSP00000376534; ENSG00000123636. [Q9UIF8-1]
    GeneIDi29994.
    KEGGihsa:29994.
    UCSCiuc002uao.3. human. [Q9UIF8-1]
    uc002uap.3. human. [Q9UIF8-5]

    Polymorphism databases

    DMDMi229462995.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032255 mRNA. Translation: BAA89212.1 .
    AB040909 mRNA. Translation: BAA96000.2 . Different initiation.
    AL080173 mRNA. Translation: CAB45759.1 .
    AL834381 mRNA. Translation: CAD39044.2 .
    CH471058 Genomic DNA. Translation: EAX11404.1 .
    CH471058 Genomic DNA. Translation: EAX11405.1 .
    CH471058 Genomic DNA. Translation: EAX11407.1 .
    BC012576 mRNA. Translation: AAH12576.1 . Sequence problems.
    AK027612 mRNA. Translation: BAB55231.1 . Different initiation.
    CCDSi CCDS2209.2. [Q9UIF8-1 ]
    PIRi T12495.
    RefSeqi NP_001276904.1. NM_001289975.1. [Q9UIF8-5 ]
    NP_038478.2. NM_013450.3. [Q9UIF8-1 ]
    UniGenei Hs.470369.
    Hs.731786.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E7O NMR - A 2062-2166 [» ]
    3G0L X-ray 2.03 A 2054-2168 [» ]
    3Q2F X-ray 2.06 A 2054-2168 [» ]
    4CUP X-ray 1.88 A 2054-2168 [» ]
    4CUQ X-ray 2.11 A 2054-2168 [» ]
    4CUR X-ray 1.84 A 2054-2168 [» ]
    4CUS X-ray 1.78 A 2054-2168 [» ]
    4CUT X-ray 1.84 A 2054-2168 [» ]
    4CUU X-ray 1.80 A 2054-2168 [» ]
    4IR3 X-ray 2.00 A 2054-2168 [» ]
    4IR4 X-ray 2.05 A 2054-2168 [» ]
    4IR5 X-ray 1.70 A 2054-2168 [» ]
    4IR6 X-ray 1.80 A 2054-2168 [» ]
    4NR9 X-ray 1.98 A 2054-2168 [» ]
    4NRA X-ray 1.85 A 2054-2168 [» ]
    4NRB X-ray 2.08 A 2054-2168 [» ]
    4NRC X-ray 1.86 A 2054-2168 [» ]
    4QC1 X-ray 1.99 A/B 2062-2166 [» ]
    4QC3 X-ray 1.60 A/B 2062-2166 [» ]
    ProteinModelPortali Q9UIF8.
    SMRi Q9UIF8. Positions 748-806, 1929-2167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119019. 5 interactions.
    IntActi Q9UIF8. 4 interactions.
    MINTi MINT-1483920.
    STRINGi 9606.ENSP00000376534.

    Chemistry

    BindingDBi Q9UIF8.
    ChEMBLi CHEMBL1741220.

    PTM databases

    PhosphoSitei Q9UIF8.

    Polymorphism databases

    DMDMi 229462995.

    Proteomic databases

    MaxQBi Q9UIF8.
    PaxDbi Q9UIF8.
    PRIDEi Q9UIF8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343439 ; ENSP00000339670 ; ENSG00000123636 . [Q9UIF8-2 ]
    ENST00000392782 ; ENSP00000376533 ; ENSG00000123636 . [Q9UIF8-5 ]
    ENST00000392783 ; ENSP00000376534 ; ENSG00000123636 . [Q9UIF8-1 ]
    GeneIDi 29994.
    KEGGi hsa:29994.
    UCSCi uc002uao.3. human. [Q9UIF8-1 ]
    uc002uap.3. human. [Q9UIF8-5 ]

    Organism-specific databases

    CTDi 29994.
    GeneCardsi GC02M160139.
    H-InvDB HIX0002531.
    HGNCi HGNC:963. BAZ2B.
    HPAi HPA019819.
    MIMi 605683. gene.
    neXtProti NX_Q9UIF8.
    PharmGKBi PA25273.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000231981.
    HOVERGENi HBG050670.
    InParanoidi Q9UIF8.
    OMAi DSDDQAD.
    OrthoDBi EOG783MTG.
    PhylomeDBi Q9UIF8.
    TreeFami TF329083.

    Miscellaneous databases

    ChiTaRSi BAZ2B. human.
    EvolutionaryTracei Q9UIF8.
    GenomeRNAii 29994.
    NextBioi 52792.
    PROi Q9UIF8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UIF8.
    Bgeei Q9UIF8.
    CleanExi HS_BAZ2B.
    Genevestigatori Q9UIF8.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    3.30.890.10. 1 hit.
    InterProi 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.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF02791. DDT. 1 hit.
    PF01429. MBD. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi 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 4).
      Tissue: Testis.
    2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Brain.
    3. Ohara O., Nagase T., Kikuno R.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-967 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1720-2168 (ISOFORMS 1/2/3/4/5), VARIANTS THR-71 AND SER-422.
      Tissue: Melanoma and Testis.
    6. "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 95-986 (ISOFORM 2), VARIANT SER-422.
      Tissue: Skeletal muscle.
    7. "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 670-1411 (ISOFORM 3).
    8. "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.
    9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1538.
      Tissue: Mammary cancer.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-1680; THR-2014 AND SER-2019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of the bromodomain from human bromodomain adjacent to zinc finger domain 2B."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 2062-2166.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2054-2168, SUBUNIT.

    Entry informationi

    Entry nameiBAZ2B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIF8
    Secondary accession number(s): D3DPA8
    , Q96EA1, Q96SQ8, Q9P252, Q9Y4N8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 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 2
      Human chromosome 2: 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