Q9Z277 (BAZ1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1479 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
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 process	DNA damage Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from electronic annotation. Source: Compara DNA replication-dependent nucleosome disassembly Inferred from electronic annotation. Source: Compara chromatin assembly or disassembly 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	WINAC complex Inferred from electronic annotation. Source: Compara 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: Compara nucleus Inferred from direct assay PubMed 11980720. Source: MGI
Molecular_function	ATP 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 kinase activity Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: 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
Smarca5	Q91ZW3	2	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1479	1479	Tyrosine-protein kinase BAZ1B		PRO_0000211171
Regions
	Domain	20 – 126	107	WAC
	Domain	605 – 669	65	DDT
	Domain	1352 – 1422	71	Bromo
	Zinc finger	1184 – 1234	51	PHD-type
	Region	1 – 345	345	Mediates the tyrosine-protein kinase activity By similarity
	Coiled coil	537 – 587	51	Potential
	Coiled coil	774 – 809	36	Potential
	Coiled coil	854 – 890	37	Potential
	Coiled coil	1257 – 1284	28	Potential
	Motif	207 – 213	7	C motif
	Compositional bias	306 – 579	274	Lys-rich
Amino acid modifications
	Modified residue	161	1	Phosphoserine Ref.7
	Modified residue	266	1	Phosphothreonine By similarity
	Modified residue	283	1	Phosphoserine Ref.9
	Modified residue	330	1	Phosphoserine By similarity
	Modified residue	345	1	Phosphoserine By similarity
	Modified residue	361	1	Phosphoserine By similarity
	Modified residue	374	1	Phosphoserine By similarity
	Modified residue	706	1	Phosphoserine By similarity
	Modified residue	709	1	Phosphoserine By similarity
	Modified residue	717	1	Phosphoserine By similarity
	Modified residue	1315	1	Phosphoserine By similarity
	Modified residue	1338	1	Phosphoserine Ref.8 Ref.9
	Modified residue	1464	1	Phosphoserine Ref.7 Ref.9
	Modified residue	1466	1	Phosphoserine Ref.7
	Modified residue	1468	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	1 – 298	298	Missing in isoform 2.		VSP_037470
Experimental info
	Sequence conflict	957	1	S → R in AAD08676. Ref.1
	Sequence conflict	1017	1	L → F in AAD08676. Ref.1
	Sequence conflict	1031 – 1034	4	SIYL → CNYM in AAD08676. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 6EFBF3913EA93AF0	FASTA	1,479	170,651
	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
	Isoform 2 [UniParc]. Checksum: A5A6A30F20BA9091	FASTA	1,181	135,988
	10 20 30 40 50 60 MTLNPSTKRR NTGSPDRKPS KKPKRDSSSL SSPLNPKLWC HVHLEKSLNG PPLKVKNSKN 70 80 90 100 110 120 SKSPEEHLEG VMKIMSPNNN KLHSFHIPKK GPAAKKPGKH SDKPLKAKGR GKGILNGQKS 130 140 150 160 170 180 TGNSKSPSKC VKTPKTKMKQ MTLLDMAKGT QKMTRTPRSS GGVPRSSGKP HKHLPPAALH 190 200 210 220 230 240 LIAYYKENKD KEDKKSALSC VISKTARLLS NEDRARLPEE LRALVQKRYE LLEHKKRWAS 250 260 270 280 290 300 MSEEQRKEYL KKKRQELKER LREKAKERRE REMLERLEKQ KRFEDQELGG RNLPAFRLVD 310 320 330 340 350 360 TPEGLPNTLF GDVALVVEFL SCYSGLLLPD AQYPITAVSL MEALSADKGG FLYLNRVLVI 370 380 390 400 410 420 LLQTLLQDEI AEDYGELGMK LSEIPLTLHS VSELVRLCLR RCDVQEDSEG SETDDNKDST 430 440 450 460 470 480 PFEDNEVQDE FLEKLETSEF FELTSEEKLR ILTALCHRIL MTYSVQDHME TRQQVSAELW 490 500 510 520 530 540 KERLAVLKEE NDKKRAEKQK RKEMEARNKE NGKEENVLGK VDRKKEIVKI EQQVEVEADD 550 560 570 580 590 600 MISAVKSRRL LSMQAKRKRE IQERETKVRL EREAEEERMR KHKAAAEKAF QEGIAKAKLV 610 620 630 640 650 660 LRRTPIGTDR NHNRYWLFSN EVPGLFIEKG WVHNSIDYRF KHHRKDHSNL PDDDYCPRSK 670 680 690 700 710 720 KANLGKNASV NAHHGPALEA VETTVPKQGQ NLWFLCDSQK ELDELLSCLH PQGIRESQLK 730 740 750 760 770 780 ERLEKRYQEI THSIYLARKP NLGLKSCDGN QELLNFLRSD LIEVATRLQK GGLGYMEGTS 790 800 810 820 830 840 EFEARVISLE KLKDFGECVI ALQASVIKKF LQGFMAPKQK KRKLQSEDST KSEEVDEEKK 850 860 870 880 890 900 MVEEAKVASA LEKWKTAIRE AQTFSRMHVL LGMLDACIKW DMSAENARCK VCRKKGEDDK 910 920 930 940 950 960 LILCDECNKA FHLFCLRPAL YEVPDGEWQC PACQPPTARR NSRGRNYTEE STSEGSEGDE 970 980 990 1000 1010 1020 SGEEEEEEEE EEEEEEDYEV AGLRLRPRKT IRGKQSVIPA ARPGRPPGKK SHPARRSRPK 1030 1040 1050 1060 1070 1080 DDPEVDDLVL QTKRISRRQS LELQKCEDIL HKLVKYRFSW PFREPVTRDE AEDYYDVIEH 1090 1100 1110 1120 1130 1140 PMDFQTIQNK CSCGNYRSVQ EFLTDMKQVF ANAELYNCRG SHVLSCMEKT EQCLLALLQK 1150 1160 1170 1180 HLPGHPYVRR KRRKFPDRLA DDEGDSDSES VGQSRGRRQK K

References

	« Hide 'large scale' referencesShow '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. , 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; SER-1464; SER-1466 AND SER-1468, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1338, MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"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-283; SER-1338 AND SER-1464, MASS SPECTROMETRY. Tissue: Macrophage.
[10]	"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.
+	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.
IPI	IPI00923656. IPI00930843.
PIR	T17401.
RefSeq	NP_035844.2. NM_011714.2.
UniGene	Mm.40331.
3D structure databases
ProteinModelPortal	Q9Z277.
SMR	Q9Z277. Positions 1185-1235, 1327-1444.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36072N.
IntAct	Q9Z277. 1 interaction.
PTM databases
PhosphoSite	Q9Z277.
Proteomic databases
PaxDb	Q9Z277.
PRIDE	Q9Z277.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748.
GeneID	22385.
KEGG	mmu:22385.
UCSC	uc008zxz.2. mouse.
Organism-specific databases
CTD	9031.
MGI	MGI:1353499. Baz1b.
Phylogenomic databases
eggNOG	COG5076.
GeneTree	ENSGT00660000095335.
HOVERGEN	HBG050668.
InParanoid	Q3USR7.
KO	K11658.
OMA	CNKAFHL.
OrthoDB	EOG4MKNFK.
Gene expression databases
Bgee	Q9Z277.
CleanEx	MM_BAZ1B.
Genevestigator	Q9Z277.
GermOnline	ENSMUSG00000002748. Mus musculus.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR018500. DDT_dom_subgr. IPR018501. DDT_dom_superfamily. 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]
Pfam	PF00439. Bromodomain. 1 hit. PF00628. PHD. 1 hit. PF10537. WAC_Acf1_DNA_bd. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00571. DDT. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF47370. Bromodomain. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS00633. 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]
ProtoNet	Search...
Other
ChiTaRS	BAZ1B. mouse.
NextBio	302753.
SOURCE	Search...

Entry information

Entry name

BAZ1B_MOUSE

Accession

Primary (citable) accession number: Q9Z277
Secondary accession number(s): B9EJ99 , Q3URP5, Q3USR7, Q3UVM2, Q8CAU9, Q9CU68

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program