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Q9Z277 (BAZ1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase BAZ1B

EC=2.7.10.2
Alternative name(s):
Bromodomain adjacent to zinc finger domain protein 1B
Williams syndrome transcription factor homolog
Williams-Beuren syndrome chromosomal region 9 protein homolog
Gene names
Name:Baz1b
Synonyms:Wbscr9, Wstf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. In the complex, it mediates the recruitment of the WICH complex to replication foci during DNA replication. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. In the WINAC complex, plays an essential role by targeting the complex to acetylated histones, an essential step for VDR-promoter association By similarity. Ref.6

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Manganese By similarity.

Subunit structure

Interacts with MYO1C By similarity. Interacts with CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and forms the WICH complex. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with VDR; in a ligand-dependent manner. Interacts with PCNA; the interaction is direct By similarity. Ref.6 Ref.9

Subcellular location

Nucleus By similarity. Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA By similarity.

Tissue specificity

Expressed in all tissues examined including heart, brain, spleen, lung, skeletal muscle, kidney and testis. Ref.5

Developmental stage

Expressed as early as day 7 and in equal amounts during gestation.

Domain

The N-terminal part, including the WAC domain and the C motif, mediates the tyrosine-protein kinase activity By similarity.

The bromo domain mediates the specific interaction with acetylated histones By similarity.

Sequence similarities

Belongs to the WAL family. BAZ1B subfamily.

Contains 1 bromo domain.

Contains 1 DDT domain.

Contains 1 PHD-type zinc finger.

Contains 1 WAC domain.

Ontologies

Keywords
   Biological processDNA damage
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
Coiled coil
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

DNA replication-dependent nucleosome disassembly

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin assembly or disassembly

Inferred from direct assay PubMed 11980720. Source: MGI

chromatin remodeling

Inferred from direct assay PubMed 11980720. Source: MGI

chromatin-mediated maintenance of transcription

Inferred from mutant phenotype PubMed 19470456. Source: BHF-UCL

double-strand break repair

Inferred from mutant phenotype PubMed 19470456. Source: BHF-UCL

heart morphogenesis

Inferred from mutant phenotype PubMed 19470456. Source: BHF-UCL

histone phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

positive regulation of receptor activity

Inferred from mutant phenotype PubMed 19470456. Source: GOC

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19470456. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentWINAC complex

Inferred from electronic annotation. Source: Ensembl

centromeric heterochromatin

Inferred from direct assay PubMed 11980720. Source: MGI

condensed chromosome

Inferred from direct assay PubMed 11980720. Source: MGI

nuclear replication fork

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 11980720. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyl-lysine binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from physical interaction Ref.9. Source: UniProtKB

histone kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

vitamin D receptor activator activity

Inferred from mutant phenotype PubMed 19470456. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Smarca5Q91ZW32EBI-927576,EBI-927547

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z277-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Z277-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-298: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14791479Tyrosine-protein kinase BAZ1B
PRO_0000211171

Regions

Domain20 – 126107WAC
Domain605 – 66965DDT
Domain1352 – 142271Bromo
Zinc finger1184 – 123451PHD-type
Region1 – 345345Mediates the tyrosine-protein kinase activity By similarity
Coiled coil537 – 58751 Potential
Coiled coil774 – 80936 Potential
Coiled coil854 – 89037 Potential
Coiled coil1257 – 128428 Potential
Motif207 – 2137C motif
Compositional bias306 – 579274Lys-rich

Amino acid modifications

Modified residue1611Phosphoserine Ref.7
Modified residue2661Phosphothreonine By similarity
Modified residue3301Phosphoserine By similarity
Modified residue3451Phosphoserine By similarity
Modified residue3611Phosphoserine Ref.8
Modified residue3741Phosphoserine By similarity
Modified residue7061Phosphoserine By similarity
Modified residue7091Phosphoserine By similarity
Modified residue7171Phosphoserine By similarity
Modified residue13151Phosphoserine By similarity
Modified residue13311N6-acetyllysine Ref.10
Modified residue13381Phosphoserine By similarity
Modified residue14641Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 298298Missing in isoform 2.
VSP_037470

Experimental info

Sequence conflict9571S → R in AAD08676. Ref.1
Sequence conflict10171L → F in AAD08676. Ref.1
Sequence conflict1031 – 10344SIYL → CNYM in AAD08676. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 6EFBF3913EA93AF0

FASTA1,479170,651
        10         20         30         40         50         60 
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL 

        70         80         90        100        110        120 
THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE KLVDSAWLEI MTKYAVGEEC 

       130        140        150        160        170        180 
DFEVGKEKML KVKIVKIHPL EKVDEEAVEK KSDGACDSPS SDKENSSQMA QDLQKKETVV 

       190        200        210        220        230        240 
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS 

       250        260        270        280        290        300 
LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT 

       310        320        330        340        350        360 
LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP LKVKNSKNSK 

       370        380        390        400        410        420 
SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD KPLKAKGRGK GILNGQKSTG 

       430        440        450        460        470        480 
NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK MTRTPRSSGG VPRSSGKPHK HLPPAALHLI 

       490        500        510        520        530        540 
AYYKENKDKE DKKSALSCVI SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS 

       550        560        570        580        590        600 
EEQRKEYLKK KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP 

       610        620        630        640        650        660 
EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL YLNRVLVILL 

       670        680        690        700        710        720 
QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC DVQEDSEGSE TDDNKDSTPF 

       730        740        750        760        770        780 
EDNEVQDEFL EKLETSEFFE LTSEEKLRIL TALCHRILMT YSVQDHMETR QQVSAELWKE 

       790        800        810        820        830        840 
RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI 

       850        860        870        880        890        900 
SAVKSRRLLS MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR 

       910        920        930        940        950        960 
RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD DDYCPRSKKA 

       970        980        990       1000       1010       1020 
NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL DELLSCLHPQ GIRESQLKER 

      1030       1040       1050       1060       1070       1080 
LEKRYQEITH SIYLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYMEGTSEF 

      1090       1100       1110       1120       1130       1140 
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV 

      1150       1160       1170       1180       1190       1200 
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI 

      1210       1220       1230       1240       1250       1260 
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST SEGSEGDESG 

      1270       1280       1290       1300       1310       1320 
EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR PGRPPGKKSH PARRSRPKDD 

      1330       1340       1350       1360       1370       1380 
PEVDDLVLQT KRISRRQSLE LQKCEDILHK LVKYRFSWPF REPVTRDEAE DYYDVIEHPM 

      1390       1400       1410       1420       1430       1440 
DFQTIQNKCS CGNYRSVQEF LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL 

      1450       1460       1470 
PGHPYVRRKR RKFPDRLADD EGDSDSESVG QSRGRRQKK 

« Hide

Isoform 2 [UniParc].

Checksum: A5A6A30F20BA9091
Show »

FASTA1,181135,988

References

« Hide 'large scale' references
[1]"Identification of the WBSCR9 gene, encoding a novel transcriptional regulator, in the Williams-Beuren syndrome deletion at 7q11.23."
Peoples R.J., Cisco M.J., Kaplan P., Francke U.
Cytogenet. Cell Genet. 82:238-246(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-810 AND 823-1799 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Thymus and Urinary bladder.
[5]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription."
Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.
EMBO Rep. 7:525-530(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYO1C.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-1464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity."
Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., Elledge S.J., Allis C.D.
Nature 457:57-62(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SMARCA5.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084480 mRNA. Translation: AAD08676.1.
CH466529 Genomic DNA. Translation: EDL19376.1.
BC141399 mRNA. Translation: AAI41400.1.
AK017894 mRNA. Translation: BAB30992.1.
AK037737 mRNA. Translation: BAC29862.1.
AK137139 mRNA. Translation: BAE23247.1.
AK140172 mRNA. Translation: BAE24264.1.
AK141305 mRNA. Translation: BAE24643.1.
PIRT17401.
RefSeqNP_035844.2. NM_011714.2.
UniGeneMm.40331.

3D structure databases

ProteinModelPortalQ9Z277.
SMRQ9Z277. Positions 1185-1235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204552. 2 interactions.
DIPDIP-36072N.
IntActQ9Z277. 2 interactions.
MINTMINT-4089121.

PTM databases

PhosphoSiteQ9Z277.

Proteomic databases

PaxDbQ9Z277.
PRIDEQ9Z277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748. [Q9Z277-1]
GeneID22385.
KEGGmmu:22385.
UCSCuc008zxz.2. mouse. [Q9Z277-1]

Organism-specific databases

CTD9031.
MGIMGI:1353499. Baz1b.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00740000115051.
HOVERGENHBG050668.
InParanoidQ3USR7.
KOK11658.
OMADEDYCPR.
OrthoDBEOG72G17K.
PhylomeDBQ9Z277.
TreeFamTF106397.

Gene expression databases

BgeeQ9Z277.
CleanExMM_BAZ1B.
GenevestigatorQ9Z277.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028942. WHIM1_dom.
IPR028941. WHIM2_dom.
IPR028935. WHIM3_domain.
IPR013136. WSTF_Acf1_Cbp146.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF00628. PHD. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15612. WHIM1. 1 hit.
PF15613. WHIM2. 1 hit.
PF15614. WHIM3. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAZ1B. mouse.
NextBio302753.
PROQ9Z277.
SOURCESearch...

Entry information

Entry nameBAZ1B_MOUSE
AccessionPrimary (citable) accession number: Q9Z277
Secondary accession number(s): B9EJ99 expand/collapse secondary AC list , Q3URP5, Q3USR7, Q3UVM2, Q8CAU9, Q9CU68
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot