ID M3WHD2_FELCA Unreviewed; 1482 AA.
AC M3WHD2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 1B {ECO:0000313|Ensembl:ENSFCAP00000011750.5};
GN Name=BAZ1B {ECO:0000313|Ensembl:ENSFCAP00000011750.5,
GN ECO:0000313|VGNC:VGNC:69152};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000011750.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000011750.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011750.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000011750.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011750.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000011750.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011750.5};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; AANG04004562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000011750; -.
DR PaxDb; 9685-ENSFCAP00000011750; -.
DR Ensembl; ENSFCAT00000012675.6; ENSFCAP00000011750.5; ENSFCAG00000012672.6.
DR VGNC; VGNC:69152; BAZ1B.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000156831; -.
DR HOGENOM; CLU_004410_0_0_1; -.
DR InParanoid; M3WHD2; -.
DR OMA; RFNHRKD; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000012672; Expressed in embryonic head and 10 other cell types or tissues.
DR GO; GO:0110016; C:B-WICH complex; IEA:Ensembl.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0090535; C:WICH complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:Ensembl.
DR GO; GO:0035173; F:histone kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR CDD; cd05505; Bromo_WSTF_like; 1.
DR CDD; cd15628; PHD_BAZ1B; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047174; BAZ1B.
DR InterPro; IPR037375; BAZ1B_Bromo.
DR InterPro; IPR047256; BAZ1B_PHD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 20..126
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 604..668
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1183..1233
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1186..1231
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1355..1425
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 144..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 537..583
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 170786 MW; 63DC4786D5D41054 CRC64;
MAPLLGRKPF PLVKPLPGEE PLFTIAHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL
THKEAWEEEQ EVAELLKEEF PAWYEKLVLE MVHHNTASLE KLVDTAWLEI MTKYAVGEEC
DFEVGKEKML KVRIVKIHPL EKVDEEATEK KSDGACDSPS SDKENSSQIA QDHQKKEPIV
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS
LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
LNPSTKRKNT GSPDRKPSKK SKTDNSSLSS PLNPKLWCHV HLKKSLNGSP LKVKNSKNSK
SPEEHLEEVM KMMSPNKLHA NFHIPKKGPP AKKSGKHSDK PLKVKGRSKG ILNGQKSTGN
SKSPKKGLKT PKTKMKQMTL LDMAKGTQKM TRAPRNSGGT PRSSSKPHKH LPPAALHLIA
YYKENKDRED KKSALSCVIS KTARLLSSED RARLPEELRS IVQKRFELLE HKKRWASMSE
EQRKEYLKKK REELKEKLKE KAKERREKEM LEKLEKQKRY EDQELTGKSL PAFRLVDTPE
GLPNTLFGDV AMVVEFLSCY SGLLLPDAQY PITAVSLMEA LSAEKGGFLY LNRVLVILLQ
TLLQDEIAED YGELGMKLSE IPLTLHSVSE LVRLCLRKSD VQEESEGSDT DDNKDSAPFE
DNEVQDEFLE KLETSEFFEL TSEEKLQILT ALCHRILMTY SVQDHMETRQ QMSAELWKER
LAVLKEENDK KRAEKQKRKE MEARNKENGK EENGLGKTDR KKEVVKFEPQ VDVGAEDMIS
AVKSRRLLAI QAKKEREIQE REMKVKLERE AEEERIRKHK AAAEKAFQEG IAKAKLVMRR
TPIGTDRNHN RYWLFSDEVP GLFIEKGWVH DSIDYRFNHR KDRADSPDED YCPRSKKANL
GKNVSMNVQP GPSAEVAVET TIPKQGQNLW FLCDSQKELD ELLNCLHPQG IRESQLKERL
EKRYQDIIHS IHLARKPNLG LKSCDGNQEL LNFLRSDLIE VATRLQKGGL GYVEETSEFE
ARVISLEKLK DFGECVIALQ ASVIKKFLQG FMAPKQKRRK LQSEDSAKTE EVDEEKKMAE
EAKVASALEK WKTAIREAQT FSRMHVLLGM LDACIKWDMS AENARCKVCR KKGEDDKLIL
CDECNKAFHL FCLRPALYEV PDGEWQCPAC QPATARRNSR GRNYTEESAS EDSEDDESNE
EEEEEEEEEE EEDYEVAGLR LRPRKTVRGK HGVIPPAARP GRRPGKKPHP ARKSRPKVPP
VDDAEVEELV LQTKRSSRRQ SLELQKCEEI LHKIVKYRFS WPFREPVTRD EAEDYYDVIT
HPMDFQTMQN KCSCGSYRSV QEFLTDMKQV FTNAELYNCR GSHVLNCMVK TEQCLVALLH
KHLPGHPYVR RKRKKFPDRL AEDEGDSESE PIGQSRGRRQ KK
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