ID F7CWE1_XENTR Unreviewed; 1208 AA.
AC F7CWE1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Bromodomain and PHD finger containing 1 {ECO:0000313|Ensembl:ENSXETP00000051065};
GN Name=brpf1 {ECO:0000313|Ensembl:ENSXETP00000051065};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000051065};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000051065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000051065};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000051065}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; F7CWE1; -.
DR STRING; 8364.ENSXETP00000051065; -.
DR PaxDb; 8364-ENSXETP00000038527; -.
DR Ensembl; ENSXETT00000051065; ENSXETP00000051065; ENSXETG00000023658.
DR AGR; Xenbase:XB-GENE-478798; -.
DR AGR; Xenbase:XB-GENE-995817; -.
DR Xenbase; XB-GENE-995817; brpf1.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_003589_1_0_1; -.
DR OrthoDB; 5403095at2759; -.
DR TreeFam; TF316118; -.
DR Bgee; ENSXETG00000023658; Expressed in 2-cell stage embryo and 14 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15701; ePHD_BRPF1; 1.
DR CDD; cd15676; PHD_BRPF1; 1.
DR CDD; cd20156; PWWP_BRPF1; 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; IPR042008; BRPF1_PHD.
DR InterPro; IPR049583; BRPF1_PWWP.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR042061; Peregrin_ePHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
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:SF85; PEREGRIN; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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 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 273..323
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 327..448
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 643..713
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1079..1162
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 46..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 137120 MW; FE24DC2F853BD0F6 CRC64;
MGVDFDVKTF CHNLRATKPP YECPVETCRK IYKSYSGIEY HLYHYDHDNP PLQQQTPIRK
SKKKGRHPRS ANKQSPTNSE VSQSPTREVM TYAQAQRLVE VELHGRVHRI SIFDNLDVVS
EDDDPPEETP ENGSNKENND TPATTPKSGK HKNKDKRKDS NHHHHHSATA GAATKLPEVV
YRELELDSPD APPRPSSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMND RRKNDGVNHI
PQEIFEYLMD RLEKESYFES HNKGDPNSLI DEDAVCCICN DGECQNSNVI LFCDMCNLAV
HQECYGVPYI PEGQWLCRRC LQSPSRAVDC ALCPNKGGAF KQTDDGRWAH VVCALWIPEV
CFANTVFLEP IDSIEHIPPA RWKLTCYICK QRGSGACIQC HKANCYTAFH VTCAQQAGLY
MKMEPVRETG ANGTSFSVRK TAYCDIHTPP GSVCKLPALS HSEGEEEDDE EEEDGKGWSS
EKVKKAKAKS RIKMKKARKI LAEKRAAAPV VSVPCIPPHR LSKITNRLTI QRKSQFMQRL
HSYWTLKRQS RNGVPLLRRL QTHLQSQRNC DQNDPTDKNW VLKEQLKSWQ RLRHDLERAR
LLVELIRKRE KLKRETIKVQ QMALEMQLTP FLILLRKTLE LLQEKDTSNI FTEPVPLSEV
PDYLEHVKKP MDFQTMKRNL EAFRYQNFDQ FEEDFNLIVN NCIKYNAKDT IFYRAASRLR
EQGAALLRQA RKQAEKIGID FETGMHIHPV ITGNEIGRHD FERAHLSDSR KQLPLEEQLK
VQLARLDEVN ASKQSIGRAR RAKMIRKEIT SIRRKMVYQQ ESRRDGGSER HSSAGRGALP
LHGPSEKDGQ TDSAAEESSS QETGKGLGPN TSSTNAHEVG RRTSVLFSKK NPKTAGPPKR
PGRPPKNRDN QLSSGQISSP IGPPQLSVTG GSQRRKRVRS PRPTSSSDSD SDSEKSAEEP
SLDLPTNGFS SSTQQVKKSF LVYRTDCNLP RSSSDSESST TSSSSAASDR TSTTPSKQGR
GKPSFSRDNF ADYSSEDTSG TENESYSVGG RVGHGLVRKG LESRGAGWLS EDEDSPLEAL
DLVWAKCRGY PSYPALIIDP KMPREGVFHH GVPIPVPPVD VLKLGEQMAQ EAQEHLYLVL
FFDNKRTWQW LPRTKLVPLG MNRELDKEKM LEGRKSNIRK SVQIAYDRAM QHRNKVQGDP
SSESSESD
//