ID H9GEW9_ANOCA Unreviewed; 1200 AA.
AC H9GEW9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Bromodomain containing 1 {ECO:0000313|Ensembl:ENSACAP00000009005.4};
GN Name=BRD1 {ECO:0000313|Ensembl:ENSACAP00000009005.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000009005.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000009005.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009005.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000009005.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; H9GEW9; -.
DR STRING; 28377.ENSACAP00000009005; -.
DR Ensembl; ENSACAT00000009198.4; ENSACAP00000009005.4; ENSACAG00000009136.4.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157236; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; H9GEW9; -.
DR OrthoDB; 163389at2759; -.
DR TreeFam; TF316118; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000009136; Expressed in embryonic post-anal tail and 13 other cell types or tissues.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0140566; F:histone reader activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15702; ePHD_BRPF2; 1.
DR CDD; cd15572; PHD_BRPF; 1.
DR CDD; cd20157; PWWP_BRPF2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR042004; BRPF2_ePHD.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
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; PTHR13793:SF17; BROMODOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 224..274
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 278..399
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 588..658
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1071..1154
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 787..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 136401 MW; BABF7821132E8155 CRC64;
MTLILGNPFQ MRRKGRCHRV PSTRHSSSPC SIKHSPTRET LTYAQAQRMV EIEIEGRLHR
ISIFEPLEII LEDDLTAQEL SECNSNKENS ERPPIFLRTK RHRNNKVKKK NEILPSSHGI
PSTASTLPEP KVHVVDYSPP SAPRRPPSYY KFIEKSSEEL DNEVEYDMDE EDYAWLEIIN
EKRKSDGISV VSQNMFEFLM DRFEKESYCE TQKQGEHQSL IDEDAVCCIC MDGECQNSNV
ILFCDMCNLA VHQECYGVPY IPEGQWLCRQ CLQSRSRPVD CVLCPNKGGA FKKTDDDRWG
HVVCALWIPE VGFANTVFIE PIDGVKNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF
HVTCAQKAGL YMKMEPVKEL TGSGTTFSVK KTAYCDVHTP PGSIRRPLNI YGEPELKNGL
CRKEGVAKTR SATRIRKKAK KSKKSPTEPC TAMPAVCAPC IPPQRLNKIM NRVAIQRKKQ
FVERVHSYWL LKRLSRNGVP LLRRLQSSLQ SQRNTQQRED DEETQALKEK LKYWQRLRHD
LERARLLIEL IRKREKLKRE QIKVEQVAME LQLTPFTVLL RSVLDQLQEK DSARIFAQPV
NLKEVPDYLD HIKHPMDFST MRERLDGQGY KNLSEFEEDF NFIIDNCMKY NAKDTIFYRA
AVRLRDQGGV VLRQARRDAE AIGYNNETGM HLPERPKLES PPPFTWEDVD RLLNPANRVH
MSLEEQLREL LEKLDLTCAM KSSGSRSKRA KLLKKEINLI RSKISQQQHQ LPQIESGIGS
FEEENAVLEQ EGEEEGDKSP PKLEPSDALP LPSNSETNSE PPTLKPVELN PEQNKHYKRV
KFDNELYSTS IQKEINGHTP ENLLDNNLSE STVSAVAESS TDVNRRTSIL FCKSKSVSPP
KSAKNTETQP TSPQLGTKTF LSVVLPRLET LLQPRKRSRS ACGDSEVDDE SPVKRLDTGL
SNGFGDGGKE SETDDTPGRK VEPRRRCASE SSISSSNSLL CSSRSRICSF SLPKCGKGKP
ALIRRHTLED RSELISCIEN GNYAKAARIA AEVGHSSMWI STDASNSVLE PLKVVWAKCS
GYPSYPALII DPKMPRVAGH HNGVTIPVPP LDVLKIGEQM QTKSDEKLFL VLFFDNKRSW
QWLPKSKMIP LGIDETIDKL KMMEGRNSSI RKAVRVAFDR AMNHLSRVHG EPVSDFSDID
//
