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BRWD1_HUMAN
ID   BRWD1_HUMAN             Reviewed;        2320 AA.
AC   Q9NSI6; C9JK25; O43721; Q5R2V0; Q5R2V1; Q6P2D1; Q8TCV3; Q96QG9; Q96QH0;
AC   Q9NUK1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 4.
DT   03-AUG-2022, entry version 202.
DE   RecName: Full=Bromodomain and WD repeat-containing protein 1;
DE   AltName: Full=WD repeat-containing protein 9;
GN   Name=BRWD1; Synonyms=C21orf107, WDR9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), TISSUE SPECIFICITY, AND VARIANT
RP   PRO-1699.
RX   PubMed=12359327; DOI=10.1016/s0167-4781(02)00421-9;
RA   Ramos V.C., Vidal-Taboada J.M., Bergonon S., Egeo A., Fisher E.M.C.,
RA   Scartezzini P., Oliva R.;
RT   "Characterisation and expression analysis of the WDR9 gene, located in the
RT   Down critical region-2 of the human chromosome 21.";
RL   Biochim. Biophys. Acta 1577:377-383(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANTS PRO-1511 AND
RP   PRO-1699.
RA   Scott H.S., Barras C., Mittaz L., Michaud J., Guidi S., Scamuffa N.,
RA   Antonarakis S.;
RT   "Isolation and characterization of a new chromosome 21 gene, WDR9, with
RT   different alternatively spliced transcripts and different protein forms.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), AND VARIANTS GLU-83 AND
RP   PRO-1699.
RC   TISSUE=Pancreas;
RA   Obayashi I., Shibuya K., Minoshima S., Kudoh J., Shimizu N.;
RT   "Isolation of WDR9 cDNA on human chromosome 21q22.3.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1560-1779, AND VARIANT PRO-1699.
RC   TISSUE=Fetal heart;
RX   PubMed=9480850; DOI=10.1006/bbrc.1998.8141;
RA   Vidal-Taboada J.M., Bergonon S., Sanchez M., Lopez-Acedo C., Groet J.,
RA   Nizetic D., Egeo A., Scartezzini P., Katsanis N., Fisher E.M.C.,
RA   Delabar J.-M., Oliva R.;
RT   "High resolution physical mapping and identification of transcribed
RT   sequences in the Down syndrome region-2.";
RL   Biochem. Biophys. Res. Commun. 243:572-578(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1645-2320 (ISOFORM B), AND
RP   VARIANT PRO-1699.
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1289; SER-1605; SER-1607;
RP   SER-1904; SER-1905; SER-1907; SER-1910; SER-2018 AND SER-2020, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475; SER-1605; SER-1607;
RP   SER-2018 AND SER-2020, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-710; THR-1477;
RP   SER-1479; SER-1605; SER-1607; SER-1686; SER-2018 AND SER-2020,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2214 (ISOFORM B), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   FUNCTION.
RX   PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA   Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA   Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT   "Identification and characterization of a set of conserved and new
RT   regulators of cytoskeletal organisation, cell morphology and migration.";
RL   BMC Biol. 9:54-54(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-701; THR-1477;
RP   SER-1678; SER-1683; SER-1686; SER-2018 AND SER-2020, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-1475 AND SER-1943,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1310-1430.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
CC   -!- FUNCTION: May be a transcriptional activator. May be involved in
CC       chromatin remodeling (By similarity). Plays a role in the regulation of
CC       cell morphology and cytoskeletal organization. Required in the control
CC       of cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}.
CC   -!- SUBUNIT: Interacts with SMARCA4. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9NSI6-4; P07550: ADRB2; NbExp=3; IntAct=EBI-10693038, EBI-491169;
CC       Q9NSI6-4; P55212: CASP6; NbExp=3; IntAct=EBI-10693038, EBI-718729;
CC       Q9NSI6-4; P06307: CCK; NbExp=3; IntAct=EBI-10693038, EBI-6624398;
CC       Q9NSI6-4; P28329-3: CHAT; NbExp=3; IntAct=EBI-10693038, EBI-25837549;
CC       Q9NSI6-4; P36544: CHRNA7; NbExp=3; IntAct=EBI-10693038, EBI-79333;
CC       Q9NSI6-4; P99999: CYCS; NbExp=3; IntAct=EBI-10693038, EBI-446479;
CC       Q9NSI6-4; P22607: FGFR3; NbExp=3; IntAct=EBI-10693038, EBI-348399;
CC       Q9NSI6-4; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-10693038, EBI-10242151;
CC       Q9NSI6-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-10693038, EBI-8285963;
CC       Q9NSI6-4; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-10693038, EBI-12094670;
CC       Q9NSI6-4; O00291: HIP1; NbExp=3; IntAct=EBI-10693038, EBI-473886;
CC       Q9NSI6-4; P30519: HMOX2; NbExp=3; IntAct=EBI-10693038, EBI-712096;
CC       Q9NSI6-4; P04792: HSPB1; NbExp=3; IntAct=EBI-10693038, EBI-352682;
CC       Q9NSI6-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10693038, EBI-10975473;
CC       Q9NSI6-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-10693038, EBI-21591415;
CC       Q9NSI6-4; Q16656-4: NRF1; NbExp=3; IntAct=EBI-10693038, EBI-11742836;
CC       Q9NSI6-4; P61970: NUTF2; NbExp=3; IntAct=EBI-10693038, EBI-591778;
CC       Q9NSI6-4; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10693038, EBI-748974;
CC       Q9NSI6-4; P62826: RAN; NbExp=3; IntAct=EBI-10693038, EBI-286642;
CC       Q9NSI6-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10693038, EBI-396669;
CC       Q9NSI6-4; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-10693038, EBI-358489;
CC       Q9NSI6-4; Q5JTV8: TOR1AIP1; NbExp=3; IntAct=EBI-10693038, EBI-2559665;
CC       Q9NSI6-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10693038, EBI-741480;
CC       Q9NSI6-4; O76024: WFS1; NbExp=3; IntAct=EBI-10693038, EBI-720609;
CC       Q9NSI6-4; Q9Y649; NbExp=3; IntAct=EBI-10693038, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=A;
CC         IsoId=Q9NSI6-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9NSI6-2; Sequence=VSP_018526;
CC       Name=C;
CC         IsoId=Q9NSI6-3; Sequence=VSP_018527, VSP_018528;
CC       Name=D;
CC         IsoId=Q9NSI6-4; Sequence=VSP_044245, VSP_044246;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:12359327}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA10896.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ238214; CAC37033.2; -; mRNA.
DR   EMBL; AJ292465; CAC44371.1; -; mRNA.
DR   EMBL; AJ292466; CAC44372.1; -; mRNA.
DR   EMBL; AB080586; BAD74071.1; -; mRNA.
DR   EMBL; AB080587; BAD74072.1; -; mRNA.
DR   EMBL; AF064861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF129408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064602; AAH64602.1; -; mRNA.
DR   EMBL; AL163279; CAB90452.1; -; Genomic_DNA.
DR   EMBL; AJ222636; CAA10896.1; ALT_FRAME; mRNA.
DR   EMBL; AK002177; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS13662.1; -. [Q9NSI6-1]
DR   CCDS; CCDS13663.1; -. [Q9NSI6-2]
DR   CCDS; CCDS33557.1; -. [Q9NSI6-4]
DR   RefSeq; NP_001007247.1; NM_001007246.2. [Q9NSI6-4]
DR   RefSeq; NP_061836.2; NM_018963.4. [Q9NSI6-1]
DR   RefSeq; NP_387505.1; NM_033656.3. [Q9NSI6-2]
DR   PDB; 3Q2E; X-ray; 1.74 A; A=1310-1430.
DR   PDBsum; 3Q2E; -.
DR   AlphaFoldDB; Q9NSI6; -.
DR   SMR; Q9NSI6; -.
DR   BioGRID; 119828; 36.
DR   IntAct; Q9NSI6; 46.
DR   STRING; 9606.ENSP00000330753; -.
DR   BindingDB; Q9NSI6; -.
DR   ChEMBL; CHEMBL3351192; -.
DR   GlyGen; Q9NSI6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NSI6; -.
DR   PhosphoSitePlus; Q9NSI6; -.
DR   BioMuta; BRWD1; -.
DR   DMDM; 313104296; -.
DR   EPD; Q9NSI6; -.
DR   jPOST; Q9NSI6; -.
DR   MassIVE; Q9NSI6; -.
DR   MaxQB; Q9NSI6; -.
DR   PaxDb; Q9NSI6; -.
DR   PeptideAtlas; Q9NSI6; -.
DR   PRIDE; Q9NSI6; -.
DR   ProteomicsDB; 66890; -.
DR   ProteomicsDB; 82555; -. [Q9NSI6-1]
DR   ProteomicsDB; 82556; -. [Q9NSI6-2]
DR   ProteomicsDB; 82557; -. [Q9NSI6-3]
DR   Antibodypedia; 23299; 105 antibodies from 22 providers.
DR   DNASU; 54014; -.
DR   Ensembl; ENST00000333229.6; ENSP00000330753.2; ENSG00000185658.14. [Q9NSI6-1]
DR   Ensembl; ENST00000341322.4; ENSP00000342106.4; ENSG00000185658.14. [Q9NSI6-4]
DR   Ensembl; ENST00000342449.8; ENSP00000344333.3; ENSG00000185658.14. [Q9NSI6-2]
DR   Ensembl; ENST00000380800.7; ENSP00000370178.3; ENSG00000185658.14. [Q9NSI6-3]
DR   GeneID; 54014; -.
DR   KEGG; hsa:54014; -.
DR   MANE-Select; ENST00000342449.8; ENSP00000344333.3; NM_033656.4; NP_387505.1. [Q9NSI6-2]
DR   UCSC; uc002yxk.3; human. [Q9NSI6-1]
DR   CTD; 54014; -.
DR   DisGeNET; 54014; -.
DR   GeneCards; BRWD1; -.
DR   HGNC; HGNC:12760; BRWD1.
DR   HPA; ENSG00000185658; Low tissue specificity.
DR   MIM; 617824; gene.
DR   neXtProt; NX_Q9NSI6; -.
DR   OpenTargets; ENSG00000185658; -.
DR   PharmGKB; PA134906879; -.
DR   VEuPathDB; HostDB:ENSG00000185658; -.
DR   eggNOG; KOG0644; Eukaryota.
DR   GeneTree; ENSGT00950000183107; -.
DR   HOGENOM; CLU_001108_0_1_1; -.
DR   InParanoid; Q9NSI6; -.
DR   OMA; EGEWGMK; -.
DR   OrthoDB; 240778at2759; -.
DR   PhylomeDB; Q9NSI6; -.
DR   TreeFam; TF324197; -.
DR   PathwayCommons; Q9NSI6; -.
DR   Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR   Reactome; R-HSA-3247509; Chromatin modifying enzymes.
DR   SignaLink; Q9NSI6; -.
DR   BioGRID-ORCS; 54014; 33 hits in 1131 CRISPR screens.
DR   ChiTaRS; BRWD1; human.
DR   EvolutionaryTrace; Q9NSI6; -.
DR   GeneWiki; BRWD1; -.
DR   GenomeRNAi; 54014; -.
DR   Pharos; Q9NSI6; Tbio.
DR   PRO; PR:Q9NSI6; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; Q9NSI6; protein.
DR   Bgee; ENSG00000185658; Expressed in cortical plate and 177 other tissues.
DR   ExpressionAtlas; Q9NSI6; baseline and differential.
DR   Genevisible; Q9NSI6; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.20.920.10; -; 2.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00439; Bromodomain; 2.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF47370; SSF47370; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Bromodomain; Cytoplasm;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; WD repeat.
FT   CHAIN           1..2320
FT                   /note="Bromodomain and WD repeat-containing protein 1"
FT                   /id="PRO_0000050888"
FT   REPEAT          184..223
FT                   /note="WD 1"
FT   REPEAT          226..265
FT                   /note="WD 2"
FT   REPEAT          268..311
FT                   /note="WD 3"
FT   REPEAT          322..365
FT                   /note="WD 4"
FT   REPEAT          366..405
FT                   /note="WD 5"
FT   REPEAT          424..463
FT                   /note="WD 6"
FT   REPEAT          466..506
FT                   /note="WD 7"
FT   REPEAT          514..553
FT                   /note="WD 8"
FT   DOMAIN          1177..1247
FT                   /note="Bromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          1330..1400
FT                   /note="Bromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          668..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1434..1593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1670..1805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1817..1839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..1899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2014..2077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2112..2184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..855
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1470..1507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1521..1550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1560..1584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1673..1697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1712..1732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1751..1768
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1769..1784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1865..1881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2021..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2044..2077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2116..2137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2138..2169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         687
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         696
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1477
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT   MOD_RES         1607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT   MOD_RES         1678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1756
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1786
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1793
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1867
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         1904
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1907
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1910
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1943
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1955
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         2018
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         2020
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         2052
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         2164
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   MOD_RES         2166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921C3"
FT   VAR_SEQ         117..120
FT                   /note="DCRH -> GTLI (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044245"
FT   VAR_SEQ         121..2320
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044246"
FT   VAR_SEQ         2191..2320
FT                   /note="EFVPRDREPNTKVRTCMHNQKDAVQMPSETLKAKMVPEKVPRRCATVAANKI
FT                   KIMSNLKETISGPENVWIRKSSRKLPHRNASAAAKKKLLNVYKEDDTTINSESEKELED
FT                   INRKMLFLRGFRSWKENAQ -> GKTFTANISKTVRRQRQSKRPRLSVDDNDWEDLDYA
FT                   KSKRVLRRSKIKTRNQGRRTVRYHDGDDDRSLENVLDFNGCTL (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12359327,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_018526"
FT   VAR_SEQ         2191..2285
FT                   /note="EFVPRDREPNTKVRTCMHNQKDAVQMPSETLKAKMVPEKVPRRCATVAANKI
FT                   KIMSNLKETISGPENVWIRKSSRKLPHRNASAAAKKKLLNVYK -> DKTFSPVYL
FT                   (in isoform C)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_018527"
FT   VAR_SEQ         2286..2320
FT                   /note="Missing (in isoform C)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_018528"
FT   VARIANT         83
FT                   /note="Q -> E (in dbSNP:rs2056844)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_026435"
FT   VARIANT         1511
FT                   /note="S -> P (in dbSNP:rs2183573)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_026436"
FT   VARIANT         1699
FT                   /note="L -> P (in dbSNP:rs1041439)"
FT                   /evidence="ECO:0000269|PubMed:12359327,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9480850,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT                   /id="VAR_026437"
FT   VARIANT         2156
FT                   /note="K -> R (in dbSNP:rs2234548)"
FT                   /id="VAR_057584"
FT   CONFLICT        1560..1562
FT                   /note="SSS -> GTR (in Ref. 6; CAA10896)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1840
FT                   /note="M -> V (in Ref. 7; AK002177)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2134
FT                   /note="E -> G (in Ref. 7; AK002177)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1318..1330
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   HELIX           1333..1338
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   TURN            1344..1346
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   HELIX           1350..1353
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   HELIX           1360..1368
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   HELIX           1375..1392
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   HELIX           1399..1422
FT                   /evidence="ECO:0007829|PDB:3Q2E"
FT   MOD_RES         Q9NSI6-2:2214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
SQ   SEQUENCE   2320 AA;  262936 MW;  109714D79B9057E9 CRC64;
     MAEPSSARRP VPLIESELYF LIARYLSAGP CRRAAQVLVQ ELEQYQLLPK RLDWEGNEHN
     RSYEELVLSN KHVAPDHLLQ ICQRIGPMLD KEIPPSISRV TSLLGAGRQS LLRTAKDCRH
     TVWKGSAFAA LHRGRPPEMP VNYGSPPNLV EIHRGKQLTG CSTFSTAFPG TMYQHIKMHR
     RILGHLSAVY CVAFDRTGHR IFTGSDDCLV KIWSTHNGRL LSTLRGHSAE ISDMAVNYEN
     TMIAAGSCDK IIRVWCLRTC APVAVLQGHT GSITSLQFSP MAKGSQRYMV STGADGTVCF
     WQWDLESLKF SPRPLKFTEK PRPGVQMLCS SFSVGGMFLA TGSTDHVIRM YFLGFEAPEK
     IAELESHTDK VDSIQFCNNG DRFLSGSRDG TARIWRFEQL EWRSILLDMA TRISGDLSSE
     EERFMKPKVT MIAWNQNDSI VVTAVNDHVL KVWNSYTGQL LHNLMGHADE VFVLETHPFD
     SRIMLSAGHD GSIFIWDITK GTKMKHYFNM IEGQGHGAVF DCKFSQDGQH FACTDSHGHL
     LIFGFGCSKP YEKIPDQMFF HTDYRPLIRD SNNYVLDEQT QQAPHLMPPP FLVDVDGNPH
     PTKYQRLVPG RENSADEHLI PQLGYVATSD GEVIEQIISL QTNDNDERSP ESSILDGMIR
     QLQQQQDQRM GADQDTIPRG LSNGEETPRR GFRRLSLDIQ SPPNIGLRRS GQVEGVRQMH
     QNAPRSQIAT ERDLQAWKRR VVVPEVPLGI FRKLEDFRLE KGEEERNLYI IGRKRKTLQL
     SHKSDSVVLV SQSRQRTCRR KYPNYGRRNR SWRELSSGNE SSSSVRHETS CDQSEGSGSS
     EEDEWRSDRK SESYSESSSD SSSRYSDWTA DAGINLQPPL RTSCRRRITR FCSSSEDEIS
     TENLSPPKRR RKRKKENKPK KENLRRMTPA ELANMEHLYE FHPPVWITDT TLRKSPFVPQ
     MGDEVIYFRQ GHEAYIEAVR RNNIYELNPN KEPWRKMDLR DQELVKIVGI RYEVGPPTLC
     CLKLAFIDPA TGKLMDKSFS IRYHDMPDVI DFLVLRQFYD EARQRNWQSC DRFRSIIDDA
     WWFGTVLSQE PYQPQYPDSH FQCYIVRWDN TEIEKLSPWD MEPIPDNVDP PEELGASISV
     TTDELEKLLY KPQAGEWGQK SRDEECDRII SGIDQLLNLD IAAAFAGPVD LCTYPKYCTV
     VAYPTDLYTI RMRLVNRFYR RLSALVWEVR YIEHNARTFN EPESVIARSA KKITDQLLKF
     IKNQHCTNIS ELSNTSENDE QNAEDLDDSD LPKTSSGRRR VHDGKKSIRA TNYVESNWKK
     QCKELVNLIF QCEDSEPFRQ PVDLVEYPDY RDIIDTPMDF GTVRETLDAG NYDSPLEFCK
     DIRLIFSNAK AYTPNKRSKI YSMTLRLSAL FEEKMKKISS DFKIGQKFNE KLRRSQRFKQ
     RQNCKGDSQP NKSIRNLKPK RLKSQTKIIP ELVGSPTQST SSRTAYLGTH KTSAGISSGV
     TSGDSSDSAE SSERRKRNRP ITNGSTLSES EVEDSLATSL SSSASSSSEE SKESSRARES
     SSRSGLSRSS NLRVTRTRAA QRKTGPVSLA NGCGRKATRK RVYLSDSDNN SLETGEILKA
     RAGNNRKVLR KCAAVAANKI KLMSDVEENS SSESVCSGRK LPHRNASAVA RKKLLHNSED
     EQSLKSEIEE EELKDENQLL PVSSSHTAQS NVDESENRDS ESESDLRVAR KNWHANGYKS
     HTPAPSKTKF LKIESSEEDS KSHDSDHACN RTAGPSTSVQ KLKAESISEE ADSEPGRSGG
     RKYNTFHKNA SFFKKTKILS DSEDSESEEQ DREDGKCHKM EMNPISGNLN CDPIAMSQCS
     SDHGCETDLD SDDDKIEKPN NFMKDSASQD NGLSRKISRK RVCSSDSDSS LQVVKKSSKA
     RTGLLRITRR CAATAANKIK LMSDVEDVSL ENVHTRSKNG RKKPLHLACT TAKKKLSDCE
     GSVHCEVPSE QYACEGKPPD PDSEGSTKVL SQALNGDSDS EDMLNSEHKH RHTNIHKIDA
     PSKRKSSSVT SSGEDSKSHI PGSETDRTFS SESTLAQKAT AENNFEVELN YGLRRWNGRR
     LRTYGKAPFS KTKVIHDSQE TAEKEVKRKR SHPELENVKI SETTGNSKFR PDTSSKSSDL
     GSVTESDIDC TDNTKTKRRK TKGKAKVVRK EFVPRDREPN TKVRTCMHNQ KDAVQMPSET
     LKAKMVPEKV PRRCATVAAN KIKIMSNLKE TISGPENVWI RKSSRKLPHR NASAAAKKKL
     LNVYKEDDTT INSESEKELE DINRKMLFLR GFRSWKENAQ
 
 
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