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Q9Z277

- BAZ1B_MOUSE

UniProt

Q9Z277 - BAZ1B_MOUSE

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Protein

Tyrosine-protein kinase BAZ1B

Gene

Baz1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. histone binding Source: UniProtKB
  4. histone kinase activity Source: UniProtKB
  5. lysine-acetylated histone binding Source: UniProtKB
  6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  7. protein tyrosine kinase activity Source: UniProtKB
  8. vitamin D receptor activator activity Source: BHF-UCL
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. chromatin assembly or disassembly Source: MGI
  3. chromatin-mediated maintenance of transcription Source: BHF-UCL
  4. chromatin remodeling Source: MGI
  5. double-strand break repair Source: BHF-UCL
  6. heart morphogenesis Source: BHF-UCL
  7. histone phosphorylation Source: UniProtKB
  8. peptidyl-tyrosine phosphorylation Source: GOC
  9. positive regulation of receptor activity Source: GOC
  10. regulation of transcription, DNA-templated Source: BHF-UCL
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Baz1b
Synonyms:Wbscr9, Wstf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1353499. Baz1b.

Subcellular locationi

Nucleus PROSITE-ProRule annotation
Note: Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase via its association with PCNA (By similarity).By similarity

GO - Cellular componenti

  1. condensed chromosome Source: MGI
  2. nuclear replication fork Source: Ensembl
  3. nucleus Source: MGI
  4. pericentric heterochromatin Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14791479Tyrosine-protein kinase BAZ1BPRO_0000211171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei266 – 2661PhosphothreonineBy similarity
Modified residuei330 – 3301PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei374 – 3741PhosphoserineBy similarity
Modified residuei706 – 7061PhosphoserineBy similarity
Modified residuei709 – 7091PhosphoserineBy similarity
Modified residuei717 – 7171PhosphoserineBy similarity
Modified residuei1315 – 13151PhosphoserineBy similarity
Modified residuei1331 – 13311N6-acetyllysine1 Publication
Modified residuei1338 – 13381PhosphoserineBy similarity
Modified residuei1464 – 14641Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Z277.
PaxDbiQ9Z277.
PRIDEiQ9Z277.

PTM databases

PhosphoSiteiQ9Z277.

Expressioni

Tissue specificityi

Expressed in all tissues examined including heart, brain, spleen, lung, skeletal muscle, kidney and testis.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ9Z277.
CleanExiMM_BAZ1B.
GenevestigatoriQ9Z277.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Smarca5Q91ZW32EBI-927576,EBI-927547

Protein-protein interaction databases

BioGridi204552. 3 interactions.
DIPiDIP-36072N.
IntActiQ9Z277. 2 interactions.
MINTiMINT-4089121.

Structurei

3D structure databases

ProteinModelPortaliQ9Z277.
SMRiQ9Z277. Positions 1185-1235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 126107WACPROSITE-ProRule annotationAdd
BLAST
Domaini605 – 66965DDTPROSITE-ProRule annotationAdd
BLAST
Domaini1352 – 142271BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 345345Mediates the tyrosine-protein kinase activityBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili537 – 58751Sequence AnalysisAdd
BLAST
Coiled coili774 – 80936Sequence AnalysisAdd
BLAST
Coiled coili854 – 89037Sequence AnalysisAdd
BLAST
Coiled coili1257 – 128428Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2137C motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi306 – 579274Lys-richAdd
BLAST

Domaini

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 similaritiesi

Belongs to the WAL family. BAZ1B subfamily.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 DDT domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 WAC domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1184 – 123451PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOVERGENiHBG050668.
InParanoidiQ9Z277.
KOiK11658.
OMAiDEDYCPR.
OrthoDBiEOG72G17K.
PhylomeDBiQ9Z277.
TreeFamiTF106397.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001487. 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]
PfamiPF00439. 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]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Z277-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW
60 70 80 90 100
TCKSTGSSQL THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE
110 120 130 140 150
KLVDSAWLEI MTKYAVGEEC DFEVGKEKML KVKIVKIHPL EKVDEEAVEK
160 170 180 190 200
KSDGACDSPS SDKENSSQMA QDLQKKETVV KEDEGRRESI NDRARRSPRK
210 220 230 240 250
LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS LIRTERPPNK
260 270 280 290 300
EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
310 320 330 340 350
LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP
360 370 380 390 400
LKVKNSKNSK SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD
410 420 430 440 450
KPLKAKGRGK GILNGQKSTG NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK
460 470 480 490 500
MTRTPRSSGG VPRSSGKPHK HLPPAALHLI AYYKENKDKE DKKSALSCVI
510 520 530 540 550
SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS EEQRKEYLKK
560 570 580 590 600
KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP
610 620 630 640 650
EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL
660 670 680 690 700
YLNRVLVILL QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC
710 720 730 740 750
DVQEDSEGSE TDDNKDSTPF EDNEVQDEFL EKLETSEFFE LTSEEKLRIL
760 770 780 790 800
TALCHRILMT YSVQDHMETR QQVSAELWKE RLAVLKEEND KKRAEKQKRK
810 820 830 840 850
EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI SAVKSRRLLS
860 870 880 890 900
MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR
910 920 930 940 950
RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD
960 970 980 990 1000
DDYCPRSKKA NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL
1010 1020 1030 1040 1050
DELLSCLHPQ GIRESQLKER LEKRYQEITH SIYLARKPNL GLKSCDGNQE
1060 1070 1080 1090 1100
LLNFLRSDLI EVATRLQKGG LGYMEGTSEF EARVISLEKL KDFGECVIAL
1110 1120 1130 1140 1150
QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV EEAKVASALE
1160 1170 1180 1190 1200
KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI
1210 1220 1230 1240 1250
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST
1260 1270 1280 1290 1300
SEGSEGDESG EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR
1310 1320 1330 1340 1350
PGRPPGKKSH PARRSRPKDD PEVDDLVLQT KRISRRQSLE LQKCEDILHK
1360 1370 1380 1390 1400
LVKYRFSWPF REPVTRDEAE DYYDVIEHPM DFQTIQNKCS CGNYRSVQEF
1410 1420 1430 1440 1450
LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL PGHPYVRRKR
1460 1470
RKFPDRLADD EGDSDSESVG QSRGRRQKK
Length:1,479
Mass (Da):170,651
Last modified:June 16, 2009 - v2
Checksum:i6EFBF3913EA93AF0
GO
Isoform 2 (identifier: Q9Z277-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-298: Missing.

Note: No experimental confirmation available.

Show »
Length:1,181
Mass (Da):135,988
Checksum:iA5A6A30F20BA9091
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti957 – 9571S → R in AAD08676. (PubMed:9858827)Curated
Sequence conflicti1017 – 10171L → F in AAD08676. (PubMed:9858827)Curated
Sequence conflicti1031 – 10344SIYL → CNYM in AAD08676. (PubMed:9858827)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 298298Missing in isoform 2. 1 PublicationVSP_037470Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19736.1. [Q9Z277-1]
PIRiT17401.
RefSeqiNP_035844.2. NM_011714.2. [Q9Z277-1]
UniGeneiMm.40331.

Genome annotation databases

EnsembliENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748. [Q9Z277-1]
GeneIDi22385.
KEGGimmu:22385.
UCSCiuc008zxz.2. mouse. [Q9Z277-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS19736.1. [Q9Z277-1 ]
PIRi T17401.
RefSeqi NP_035844.2. NM_011714.2. [Q9Z277-1 ]
UniGenei Mm.40331.

3D structure databases

ProteinModelPortali Q9Z277.
SMRi Q9Z277. Positions 1185-1235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204552. 3 interactions.
DIPi DIP-36072N.
IntActi Q9Z277. 2 interactions.
MINTi MINT-4089121.

PTM databases

PhosphoSitei Q9Z277.

Proteomic databases

MaxQBi Q9Z277.
PaxDbi Q9Z277.
PRIDEi Q9Z277.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002825 ; ENSMUSP00000002825 ; ENSMUSG00000002748 . [Q9Z277-1 ]
GeneIDi 22385.
KEGGi mmu:22385.
UCSCi uc008zxz.2. mouse. [Q9Z277-1 ]

Organism-specific databases

CTDi 9031.
MGIi MGI:1353499. Baz1b.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119099.
HOVERGENi HBG050668.
InParanoidi Q9Z277.
KOi K11658.
OMAi DEDYCPR.
OrthoDBi EOG72G17K.
PhylomeDBi Q9Z277.
TreeFami TF106397.

Miscellaneous databases

ChiTaRSi Baz1b. mouse.
NextBioi 302753.
PROi Q9Z277.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z277.
CleanExi MM_BAZ1B.
Genevestigatori Q9Z277.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR001487. 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 ]
Pfami PF00439. 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 ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00571. DDT. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiBAZ1B_MOUSE
AccessioniPrimary (citable) accession number: Q9Z277
Secondary accession number(s): B9EJ99
, Q3URP5, Q3USR7, Q3UVM2, Q8CAU9, Q9CU68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 16, 2009
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3