GenomeNet

Database: UniProt
Entry: A0A3Q4HPZ1_NEOBR
LinkDB: A0A3Q4HPZ1_NEOBR
Original site: A0A3Q4HPZ1_NEOBR 
ID   A0A3Q4HPZ1_NEOBR        Unreviewed;      1614 AA.
AC   A0A3Q4HPZ1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Protein polybromo-1-like {ECO:0000313|Ensembl:ENSNBRP00000022953.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000022953.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000022953.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   STRING; 32507.ENSNBRP00000022953; -.
DR   Ensembl; ENSNBRT00000023553.1; ENSNBRP00000022953.1; ENSNBRG00000017496.1.
DR   GeneTree; ENSGT00390000003017; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000017496; Expressed in blood and 8 other cell types or tissues.
DR   GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   CDD; cd04717; BAH_polybromo; 2.
DR   CDD; cd05524; Bromo_polybromo_I; 1.
DR   CDD; cd05517; Bromo_polybromo_II; 1.
DR   CDD; cd05520; Bromo_polybromo_III; 1.
DR   CDD; cd05518; Bromo_polybromo_IV; 1.
DR   CDD; cd05515; Bromo_polybromo_V; 1.
DR   CDD; cd05526; Bromo_polybromo_VI; 1.
DR   CDD; cd21984; HMG-box_PB1; 1.
DR   Gene3D; 2.30.30.490; -; 2.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR037968; PBRM1_BD5.
DR   InterPro; IPR037382; Rsc/polybromo.
DR   PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR   PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF00439; Bromodomain; 6.
DR   Pfam; PF00505; HMG_box; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00439; BAH; 2.
DR   SMART; SM00297; BROMO; 6.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47370; Bromodomain; 6.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 5.
DR   PROSITE; PS50014; BROMODOMAIN_2; 5.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT   DOMAIN          66..128
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          218..288
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          387..457
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          522..592
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          659..729
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          940..1058
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          1131..1247
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          1352..1402
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        1352..1402
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1298..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1454..1518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..188
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..909
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1298..1312
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1614 AA;  185786 MW;  E4A04707B471C8DF CRC64;
     MSASSKRRRA TSPSSSVSGG GDLDDVSSST PGSGRKRKRV SNVPPVDTIA VCHELFNTIR
     DYKDDQGRQL SEVFQRVPKR RNQPDYYEVV SQPIDMTKIQ CKLKSEDYND VEQLTADFQL
     LFNNARSFYK VAFTYVCISQ CKPYRDSEEY QAACKLWEVY FQTRNEFVQP GDRDEDDEDG
     DDMDNPGMAT EEEVSPHYIL KEVLEQLLEA IVSHADPSGR LVSELFQKLP SKVHYPDYYA
     IIKEPIDLRT IAQRIQIGYY KNVNAMAKDV ELMTKNAKTY NEPGSQVFKD ANTIKKVFIQ
     RKTELEHAEP TKSSLRIRNR RSGQGDRISG VSVALQYGSE SEDDPVLSGS VCYDEGESEA
     ESQSSSMEMS NPIFQLYEAV RGARNNQGQM FSEPFQQLPS RREYPDYYQQ IKQPISLQQI
     RAKMKNGEYE SVEQIEADLN LMFENAKRYN MPNSSIYKRA FRLQQIMQAK KRELLRRDDE
     DGDSILSSDA GSVKRKSHKK NVKKNRMKAF YAAVTEAREA GTNRRLCDLF MVKPSKKDYP
     DYYNVILEPM DLKTIEHNVR NERYATEEAL MEDMKLMFRN ARHYNEEGSQ VYNDADILEK
     ILKDKRKEMG PPPEEEDVGS PKLKLRKSGV SPKKSKYLTP LQQRLNELYD AVRNFTDRRG
     RRLSAIFLRL PSRAELPDYY ATIKRPIDME RVRSHMAAGR YQDVDALVED FALMFNNACI
     YNEPESLIYR DALVLHRVLL ETRKQQEGGE EFGPPGVGLL VRELIRNLFV SVMGHQDEEG
     RCYSDSLAEI PAVDPAAPEK PPLNFDVIKM NVERGRYRRL DVFQEHMFEV LEKARRLHRT
     DSEIFEDAVE LQQFFIKIRD ELCKNGEILL SVALNYTLKH LHSDVDQEKR EKIPKEIEED
     KQKKDEDENQ EDEKPEDLAG EVWQSKPEHV YSQDCRFENS TYHVGDFVYV EPSEPNLKPH
     IVCIERLWED EAGEKWLYGC WFYRPSETFH LATRKFLEKE VFKSDYYNKV SISKVLGKCV
     VIFVKDYFKM QPEGFRPEDV YVCESRYTAR NKFFKKIKIW AMPESSFKLV PREAPLPVVR
     VASMFVKPDQ EKPLAYTVNG FVEKEREDVP TEMSGAEPGC QYYEQLCYKN MWFKVGDCVY
     IQSHGLSKPR VARIEKLWQQ NGTTFFFGPI FIHPEETEHE PTKMFYKREV FLSHLEETLP
     MTCVIGKCVV SSFKDYLSCR PTELSEDDVL LCESRYIESE KMMKKFKGLK RFSYSSKVVE
     DEIYYFRKLI VPQKEASPIL DKKIDELEVK LADMEDADDD MEDMDEDEEA PETPSLPQMQ
     TPLTNDMDVM PYTPSQTTPK VKGLSKKEGA KRKINMSGYI LFSSEMRAVI KARHPDFSFG
     ELSRLVGTEW RNLEASKKAE YEGMMGAYGP PYMPMQGPHE GLLSVAPMPP HPTGGPHLPP
     HHLQQGMPGY PGMPHQGKGH CPSRTCSVTS SRVSPAGGGL PGPQQVSLSP GMFSPGQHAP
     PPYPGQGQLG QPSHLQPTTP MFVAPPPKTQ RVLHSEAYLK YIEGLNSDSS TVSKWDQALK
     AQRRDSHLTK EQESRLPAHW LKSKGAHTTM VDALWRLRDL MLRDSLNICQ AHNL
//
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