ID A0A1S3FXH0_DIPOR Unreviewed; 1056 AA.
AC A0A1S3FXH0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Bromodomain-containing protein 1 isoform X2 {ECO:0000313|RefSeq:XP_012881256.1};
GN Name=Brd1 {ECO:0000313|RefSeq:XP_012881256.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881256.1};
RN [1] {ECO:0000313|RefSeq:XP_012881256.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881256.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_012881256.1; XM_013025802.1.
DR AlphaFoldDB; A0A1S3FXH0; -.
DR GeneID; 105992755; -.
DR CTD; 23774; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 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}; 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:UP000081671};
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 213..263
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 267..388
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 927..1010
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..557
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 790..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 119371 MW; 255E12ECBA9446D8 CRC64;
MRRKGRCHRG SAARHPSSPC VKHSPTRETL TYAQAQRMVE IEIEGRLHRI SIFDPLEIIL
EDDLTAQEMS ECNSNKENSE RPPVCLRTKR HKNNRVKKKN EVLPSSHGTP ASASALPEPK
VRIVEYSPPS APRRPPVYYK FIEKSAEELD KEVEYDMDEE DYAWLEIINE KRKSDCVSAV
SQNMFEFLMD RFEKESYCEN QKQGEQQSLI DEDAVCCICM DGECQNSNVI LFCDMCNLAV
HQECYGVPYI PEGQWLCRHC LQSRSRPADC VLCPNKGGAF KKTDDDRWGH VVCALWIPEV
GFANTVFIEP IDGVRNIPPA RWKLTCYLCK QKGVGACIQC HKANCYTAFH VTCAQKAGLY
MKMEPVKELT GGSTTFSVRK TAYCDVHTPP GCTRRPLNIY GDVEMKNGVC RKESSVKTVR
STSKVRKKAK KGKKTVAEPC AVLPTVCAPY IPPQRLNRIA NQVAIQRKKQ FVERVHSYWL
LKRLSRNGAP LLRRLQSSLQ SQRSSQQREN DEEMKAAKEK LKYWQRLRHD LERARLLIEL
LRKREKLKRE QVKVEQMAVE LRLTPLTVLL RSVLERLQEK DPAKIFAQPV SLKEVPDYLD
HIKHPMDFAT MRKRLEAQGY KNLHAFEEDF NLIVDNCMKY NAKDTVFYRA AVRLRDQGGV
VLRQAQREVD SIGLEEASGM HLPERPVAAP RRPFSWEDVD RLLDPANRAH LSLEEQLREL
LDKLDLTCSM KSSGSRSKRA KLLKKEIALL RNKLSQQHSS PPVGPGTGGF EEDAAPLGPD
TGEDVLPRLE TLLQPRKRSR STCGDSEAEE ESPGKRLDTG LTNGFGGARS EQEPGSGPGR
RATPRRRCAS ESSVSSSSSP LCDSSFSAPK CGRGKPALVR RHTLEDRSEL ISCIENGNYA
KAARIAAEVG QNSMWISTDA AASALEPLKV VWAKCSGYPS YPALIIDPKM PRVPGHHNGV
TIPAPPLDVL KIGEHMQTKS EEKLFLVLFF DNKRSWQWLP KSKMVPLGID ETIDKLKMME
GRNSSIRKAV RVAFDRAMNH LSRVHGEPAS DLSDID
//
