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Database: UniProt
Entry: Q0P4R0_XENTR
LinkDB: Q0P4R0_XENTR
Original site: Q0P4R0_XENTR 
ID   Q0P4R0_XENTR            Unreviewed;      1185 AA.
AC   Q0P4R0; F6WNN1;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Bromodomain-containing 1 {ECO:0000313|EMBL:AAI21943.1, ECO:0000313|Ensembl:ENSXETP00000031780};
DE   SubName: Full=Bromodomain-containing protein 1 {ECO:0000313|RefSeq:NP_001073031.1};
GN   Name=brd1 {ECO:0000313|Ensembl:ENSXETP00000031780,
GN   ECO:0000313|RefSeq:NP_001073031.1,
GN   ECO:0000313|Xenbase:XB-GENE-949377};
GN   Synonyms=LOC733743 {ECO:0000313|EMBL:AAI21943.1};
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|EMBL:AAI21943.1};
RN   [1] {ECO:0000313|RefSeq:NP_001073031.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI21943.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testes {ECO:0000313|EMBL:AAI21943.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSXETP00000031780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000031780};
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   [4] {ECO:0000313|Ensembl:ENSXETP00000031780}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2020) to UniProtKB.
RN   [5] {ECO:0000313|RefSeq:NP_001073031.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; BC121942; AAI21943.1; -; mRNA.
DR   RefSeq; NP_001073031.1; NM_001079563.1.
DR   RefSeq; XP_012814620.1; XM_012959166.2.
DR   STRING; 8364.ENSXETP00000031174; -.
DR   PaxDb; 8364-ENSXETP00000031780; -.
DR   Ensembl; ENSXETT00000031780; ENSXETP00000031780; ENSXETG00000014519.
DR   GeneID; 733743; -.
DR   KEGG; xtr:733743; -.
DR   AGR; Xenbase:XB-GENE-949377; -.
DR   CTD; 23774; -.
DR   Xenbase; XB-GENE-949377; brd1.
DR   eggNOG; KOG0955; Eukaryota.
DR   HOGENOM; CLU_003589_1_0_1; -.
DR   OMA; GMWISTD; -.
DR   OrthoDB; 163389at2759; -.
DR   TreeFam; TF316118; -.
DR   Reactome; R-XTR-3214847; HATs acetylate histones.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Bgee; ENSXETG00000014519; Expressed in testis and 13 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; cd15702; ePHD_BRPF2; 1.
DR   CDD; cd15677; PHD_BRPF2; 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; IPR042009; BRPF2_PHD.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR000313; PWWP_dom.
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; PS50016; ZF_PHD_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
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          214..264
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          268..389
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          578..648
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1056..1139
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          514..557
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  135033 MW;  1BEC413A8EEF45DE CRC64;
     MRRKGRWHRV SAPRSSTSPC SIKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEIV
     SEDDLTAQEI NECNSNKENS EQPPQVCLRS KRHKASKEKK KSEVLPTAHG HTTTSVLPEP
     KVRVIECSPP SAPNRSPSYY KFQDKSPEEL DKEVEYDMDE EDYAWLEIIN EKRKSEGFSA
     VSQDIFEFLM DRFEKESYCE NQKQGDQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA
     VHQECYGVPY IPEGQWLCRH CLQSRNIPID CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
     VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
     YMKMEPVKEV AGSITTFSVK KTAYCDAHTP PGCVRRPLNI YEEPESKNGI CRKSSDKNIR
     STSKARRKTT KAKKELNETC NVLPTITVPD IPPQRVNKII NQVSIPRKKQ FIERVHSYWM
     LKRLSRNGIP LLRRLQSSLQ SQRNIQESED DEEVQALKKK LKYLQRLRHD LERARLLIEL
     IRKREKLKRE QVKVEQVAME LKLTPLTVLL RSLLEQLQEK DPARIFAHPV NLTEVPDYLD
     HIKHPMDFST MKKRLEDQRY RNLNEFEEDF NLIIENCMKY NAKDTIFYRA AVRLRDHGGV
     LLRQARREAN VIGFDEETGM HLPEQPKIEA PPQFSWEDVD KLLNPNNRAH MALEEQLKEL
     LEKLDLTFAM KSSGSRSKRL KLLKREIANV RQMLSQQHVQ PPQIESGIGS FEEDGSMLND
     GEEEGDKSPP KLEPSDALPL PSNSETNSEP PTLKPIELNP EQSKLYKRVT FDNELHSTTI
     QNEMINGHTP ENLLKDSNLN ESSDSEVAES STDVNRRTSI LFRKSKSVSP QKPSKNTETQ
     PTSPQLGTKT FLSVVLPRLE TLLQPRKRSR STCGDSEVDG ESPVKRLDTG LSNGYGEGEK
     EKEFNITPGR KLEPRRRCAS ESSISSNNSI LCNPSFGLPK CGKGKPALIR RHTIEDRSEL
     ISCIENGNYA RAARIAAEVG QTNMWVAAST SAFLEPLKVV WAKCSGYPSY PALIIDPKMP
     RVGCHHNGVA IPVPPMDVLK TGDQMQTRAE EKLFLVLFFD NKRSWQWLPK SKMVPLGVDE
     TIDKLKMMEG RNSSIRKAVR VAYDRALNHL SRVQGESVSD FSDID
//
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