ID F7EJB8_CALJA Unreviewed; 1521 AA.
AC F7EJB8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 1A {ECO:0000313|Ensembl:ENSCJAP00000012119.3};
GN Name=BAZ1A {ECO:0000313|Ensembl:ENSCJAP00000012119.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000012119.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000012119.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000012119.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR Ensembl; ENSCJAT00000012780.3; ENSCJAP00000012119.3; ENSCJAG00000006421.4.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000158135; -.
DR HOGENOM; CLU_002479_1_0_1; -.
DR TreeFam; TF316326; -.
DR Proteomes; UP000008225; Chromosome 10.
DR Bgee; ENSCJAG00000006421; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR CDD; cd15627; PHD_BAZ1A; 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; IPR037325; Acf1_Bromo.
DR InterPro; IPR047171; BAZ1A.
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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 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.
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:UP000008225};
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:PRU00146}.
FT DOMAIN 22..128
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 422..487
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1114..1164
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1411..1481
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 630..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 317..394
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 630..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 175235 MW; 4050F4B978138437 CRC64;
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP
GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTNLTHRSR LHEICDDIFA YVKDRYFVEE
TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK
KKEAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHIFS RDKLKLFLKQ HCEPQDGVIK
IKESSLSMYK LAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIPINLEDN IGNKQILASY
RNKTTKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER
LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL
PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA
IFQAIAEEEE EVAKEQLTDA DTKGCSLKSL DLDSCTLSEI LRLHILASGA DVTSANAKYR
YQKRGGFDAT DDACMELRLS NPSLLKKLSS TSVYDLTPGE KMKILHALCG KLLTLVSTRD
FIEDYVDILR QAKQEFRELK AEQHRKEREE AAARIRKKKE EKLKEQEQKM KEKQEKLKED
EQRNSTADIS IGEEEREDFD TSTESKDTEQ KELDQDMVTE DEDDPGSHKR GRKGKRGQNG
FKEFTRQEEI NCVTRDPLTA DEEEALKQEH QRKEKELLEK IQSAIACTNI FPLGRDRMYR
RYWIFPSIPG LFIEEDYSGL TEDMLLPRPS SFQNNVQSQD PQVSTGEPLT SESTSNIDQG
PCDHSVQLPK PVHKPNRWCF YSSCEQLDQL IEALNSRGHR ESALKETLLQ EKSRICAQLA
RFSEEKFHFS DKPQPDSKPT YSRGRSSSTY DPSQMSAEKQ LELRLRDFLL DIEDRIYQGT
LGAIKVTDRH IWRSALENGR YELLSEENKE NGIIKTVNED VEEMEIDEQT KVIVKDRLLG
IKTETPSTAS TNASTPQSVS SVVHYLAMAL FQIEQGIERR FLKAPLDASD SGRSYKTVLD
RWRESLLSSA SLSQVFLHLS TLDRSVMWSK SILNARCKIC RKKGDAENMV LCDGCDRGHH
TYCVRPKLKT VPEGDWFCPE CRPKQRSRRL SSRQRPSLES DEDVEDSMGG EDDEVGGDEE
EGQSEEEEYE IEQDEDDSQE EEEVSLPKRG RPQVRLPVKT RGRLCSFSSR GQQQEPGRYP
SRSQQSTLKT TVSSKTGRSL RKINSAAPTE TKSVRIASRS TRHNHSPLQA DVFVELLSPR
RKRRGRRSAN NTPENSPNFP NFRVIATKSS EQSRSLNVAS KLSLQENESK RRCRKRQSPE
SSPMTLSRRS SGRQGGVHEL SAFEQLVVEL VRHDDSWPFL KLVSKIQVPD YYDIIKKPIA
LNIIREKVNK CEYKLASEFI DDIELMFSNC FEYNPRNTSE AKAGTRLQAF FHIQAQKLGL
HVTPSNADQV STPPATKKSR I
//
