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PB1_CHICK
ID   PB1_CHICK               Reviewed;        1633 AA.
AC   Q90941;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Protein polybromo-1;
GN   Name=PBRM1; Synonyms=PB1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=8917104; DOI=10.1016/0378-1119(96)82845-9;
RA   Nicolas R.H., Goodwin G.H.;
RT   "Molecular cloning of polybromo, a nuclear protein containing multiple
RT   domains including five bromodomains, a turncated HMG-box, and two repeats
RT   of a novel domain.";
RL   Gene 175:233-240(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 932-1103, AND STRUCTURE BY NMR.
RX   PubMed=15839835; DOI=10.1042/bj20050310;
RA   Oliver A.W., Jones S.A., Roe S.M., Matthews S., Goodwin G.H., Pearl L.H.;
RT   "Crystal structure of the proximal BAH domain of the polybromo protein.";
RL   Biochem. J. 389:657-664(2005).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin-remodeling
CC       complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:8917104}.
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DR   EMBL; X90849; CAA62353.1; -; mRNA.
DR   PIR; JC5056; JC5056.
DR   RefSeq; NP_990496.1; NM_205165.1.
DR   PDB; 1W4S; X-ray; 1.55 A; A=932-1103.
DR   PDBsum; 1W4S; -.
DR   AlphaFoldDB; Q90941; -.
DR   SMR; Q90941; -.
DR   STRING; 9031.ENSGALP00000040734; -.
DR   PaxDb; Q90941; -.
DR   PRIDE; Q90941; -.
DR   GeneID; 396074; -.
DR   KEGG; gga:396074; -.
DR   CTD; 55193; -.
DR   VEuPathDB; HostDB:geneid_396074; -.
DR   eggNOG; KOG1827; Eukaryota.
DR   InParanoid; Q90941; -.
DR   PhylomeDB; Q90941; -.
DR   EvolutionaryTrace; Q90941; -.
DR   PRO; PR:Q90941; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   CDD; cd05515; Bromo_polybromo_V; 1.
DR   Gene3D; 1.20.920.10; -; 6.
DR   Gene3D; 2.30.30.490; -; 2.
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; PTHR16062; 2.
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; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF47370; SSF47370; 6.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 5.
DR   PROSITE; PS50014; BROMODOMAIN_2; 6.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bromodomain; Chromatin regulator; DNA-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1633
FT                   /note="Protein polybromo-1"
FT                   /id="PRO_0000223186"
FT   DOMAIN          65..135
FT                   /note="Bromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          197..267
FT                   /note="Bromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          398..468
FT                   /note="Bromo 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          536..606
FT                   /note="Bromo 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          674..744
FT                   /note="Bromo 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          790..860
FT                   /note="Bromo 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          954..1072
FT                   /note="BAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          1155..1271
FT                   /note="BAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DNA_BIND        1378..1446
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1509..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          961..964
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          974..983
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          989..997
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   HELIX           999..1001
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1009..1011
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1014..1025
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   HELIX           1026..1028
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1029..1037
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   HELIX           1038..1041
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1044..1046
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   HELIX           1051..1053
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1054..1062
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   TURN            1063..1066
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1067..1070
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1083..1085
FT                   /evidence="ECO:0007829|PDB:1W4S"
FT   STRAND          1094..1096
FT                   /evidence="ECO:0007829|PDB:1W4S"
SQ   SEQUENCE   1633 AA;  187055 MW;  E4CA350E1087F888 CRC64;
     MGSKRRRATS PSSSVSGGDF DDGHHSTNIP GPSRKRRRLS NLPTVDPIAV CHELYNTIRD
     YKDEQGRLLC ELFIRAPKRR NQPDYYEVVS QPIDLMKIQQ KLKMEEYDDV NVLTADFQLL
     FNNAKAYYKP DSPEYKAACK LWELYLRTKN EFVQKGDAEE EDEDEEGHDS QELSSPGYLK
     EILEQLLEAV AVATNPSGRL ISELFQKLPS KVQYPDYYAI IKEPIDLKTI AQRIQNGTYK
     SIHAMAKDID LLAKNAKTYN EPGSQVFKDA NAIKKIFNMK KAEIEHSELA KSSLRLRTPS
     NLTASKLTGP SSQGKGSVGD ERNSSNKYFR NKRSAQGDRL SAITMALQYG SESDEDAALA
     AAARYEGESE AESITSFMDT SNPLYQLYDT VRSCRNNQGQ LISEPFFQLP SKKKYPDYYQ
     QIKTPISLQQ IRAKLKNHEY ETLDQLEADL NLMFENAKRY NVPNSAIYKR VLKMQQVMQA
     KKKELARRDD IEDGDSMISS ATSDTGSSKR KSKKNMRKQR MKILYNAVLE ARESGTGRRL
     CDLFMVKPSK KDYPDYYKII LEPMDLKMIE HNIRNDKYVG EEAMIDDMKL MFRNARHYNE
     EGSQVYNDAH MLEKILKEKR KELGPLPEDD DVASPKLKLS RKSGISPKKS KYMTPMQQKL
     NEVYEAVKNY TDKRGRRLSA IFLRLPSRSE LPDYYITIKK PVDMEKIRSH MMANKYQDID
     SMVEDFVMMF NNACTYNEPE SLIYKDALVL HKVLLETRRE IEGDEDSHVP NVTLLIQELI
     HNLFVSVMSH QDDEGRCYSD SLAEIPAVDP NFPNKPPLTF DIIRKNVENN RYRRLDLFQE
     NMFEVLERAR RMNRTDSEIY EDAVELQQFF IKIRDELCKN GEILLSPALS YTTKHLHNDV
     EKEKKEKLPK EIEEDKLKRE EEKREAEKSE DSSGSAGLSS LHRTYSQDCS FKNSMYHVGD
     YVYVEPAEAN LQPHIVCIER LWEDSAGEKW LYGCWFYRPN ETFHLATRKF LEKEVFKSDY
     YNKVPVSKIL GKCVVMFVKE YFKLCPENFR DEDVYVCESR YSAKTKSFKK IKLWTMPVSS
     VRFVPRDVPL PVVRVASVFA NTDKAEEEKH SDTLDDSKVG ESILHLEKDK EDVPVEMSNG
     EPGCHYFEQL CYNDMWLKVG DCVFIKSHGL VRPRVGRIEK MWVRDGAAYF FGPIFIHPEE
     TEHEPTKMFY KKEVFLSNLE ETCPMSCILG KCAVLSFKDF LCCRPTEISE NDVFLCESRY
     NESDKQMKKF KGLKRFSLSA KVVDDEIYYF RKPIVPQKEP SPLLEKKIQQ LEAKFAELGG
     GDEDMEEMGE EEGDITETPS MPQLQTPLTS ELDIMPYTPP QSTPKSVKGS TKKEGSKRKI
     NMSGYILFSS EMRPVIKAQH PDYSFGELSR LVGTEWRNLE ATKKAEYEGM ISGYPPVLPP
     LQGPVDGIVS MGSMQPLHPG VPPPHQLPPG MPGIPGIPPP GVIGQNVSPM VGTPAPGAGP
     FGQQIGILGP PGQQAPPPYP GQSPATQPVM QQPSTPMFVS PPPKTQRLLH SEAYLKYIEG
     LSAESNSISK WDQTLAARRR DVHLSKEQES RLPSHWLKSK GAHTTMADAL WRLRDLMLRD
     TLNIRQAYNI ENV
 
 
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