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BRWD3_MOUSE
ID   BRWD3_MOUSE             Reviewed;        1799 AA.
AC   A2AHJ4; Q3TQR7; Q3UTB6; Q640P3; Q8C7D5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Bromodomain and WD repeat-containing protein 3;
GN   Name=Brwd3; Synonyms=Gm596;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1595-1799 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1390-1799 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884; SER-885; SER-1576 AND
RP   SER-1760, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the control of cell shape (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AHJ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AHJ4-2; Sequence=VSP_024310, VSP_024311;
CC       Name=3;
CC         IsoId=A2AHJ4-3; Sequence=VSP_024308, VSP_024309;
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DR   EMBL; AK050539; BAC34314.1; -; mRNA.
DR   EMBL; AK139563; BAE24064.1; -; mRNA.
DR   EMBL; AK163354; BAE37315.1; -; mRNA.
DR   EMBL; AL731764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX000698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC082562; AAH82562.1; -; mRNA.
DR   CCDS; CCDS41100.1; -. [A2AHJ4-1]
DR   RefSeq; NP_001074946.1; NM_001081477.1. [A2AHJ4-1]
DR   AlphaFoldDB; A2AHJ4; -.
DR   SMR; A2AHJ4; -.
DR   BioGRID; 238286; 64.
DR   IntAct; A2AHJ4; 54.
DR   STRING; 10090.ENSMUSP00000123588; -.
DR   iPTMnet; A2AHJ4; -.
DR   PhosphoSitePlus; A2AHJ4; -.
DR   EPD; A2AHJ4; -.
DR   MaxQB; A2AHJ4; -.
DR   PaxDb; A2AHJ4; -.
DR   PeptideAtlas; A2AHJ4; -.
DR   PRIDE; A2AHJ4; -.
DR   ProteomicsDB; 265242; -. [A2AHJ4-1]
DR   ProteomicsDB; 265243; -. [A2AHJ4-2]
DR   ProteomicsDB; 265244; -. [A2AHJ4-3]
DR   Antibodypedia; 537; 52 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000101283; ENSMUSP00000098841; ENSMUSG00000063663. [A2AHJ4-3]
DR   Ensembl; ENSMUST00000150434; ENSMUSP00000123588; ENSMUSG00000063663. [A2AHJ4-1]
DR   GeneID; 382236; -.
DR   KEGG; mmu:382236; -.
DR   UCSC; uc009ucm.1; mouse. [A2AHJ4-1]
DR   UCSC; uc009ucn.1; mouse. [A2AHJ4-2]
DR   CTD; 254065; -.
DR   MGI; MGI:3029414; Brwd3.
DR   VEuPathDB; HostDB:ENSMUSG00000063663; -.
DR   eggNOG; KOG0644; Eukaryota.
DR   GeneTree; ENSGT00950000183107; -.
DR   HOGENOM; CLU_001108_0_0_1; -.
DR   InParanoid; A2AHJ4; -.
DR   OMA; TVVTSWK; -.
DR   OrthoDB; 240778at2759; -.
DR   PhylomeDB; A2AHJ4; -.
DR   TreeFam; TF324197; -.
DR   BioGRID-ORCS; 382236; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Brwd3; mouse.
DR   PRO; PR:A2AHJ4; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2AHJ4; protein.
DR   Bgee; ENSMUSG00000063663; Expressed in embryonic post-anal tail and 212 other tissues.
DR   ExpressionAtlas; A2AHJ4; baseline and differential.
DR   Genevisible; A2AHJ4; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS: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; 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; PS50014; BROMODOMAIN_2; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Bromodomain; Phosphoprotein; Reference proteome;
KW   Repeat; WD repeat.
FT   CHAIN           1..1799
FT                   /note="Bromodomain and WD repeat-containing protein 3"
FT                   /id="PRO_0000283090"
FT   REPEAT          170..209
FT                   /note="WD 1"
FT   REPEAT          213..251
FT                   /note="WD 2"
FT   REPEAT          255..297
FT                   /note="WD 3"
FT   REPEAT          307..347
FT                   /note="WD 4"
FT   REPEAT          353..393
FT                   /note="WD 5"
FT   REPEAT          400..452
FT                   /note="WD 6"
FT   REPEAT          456..495
FT                   /note="WD 7"
FT   REPEAT          502..542
FT                   /note="WD 8"
FT   DOMAIN          1156..1226
FT                   /note="Bromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          1315..1409
FT                   /note="Bromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          766..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1258..1291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1321..1367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1517..1723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1450..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1518..1532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1533..1547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1563..1598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1599..1623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1624..1645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1646..1660
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1691
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         693
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RI45"
FT   MOD_RES         884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         885
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1574
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RI45"
FT   MOD_RES         1576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1760
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         144..181
FT                   /note="VNITSARQLTGCSRFSHVFPSSAYQHIKMHKRILGHLS -> GFFFVALTVL
FT                   ELYVDQAGLCLSSAGIKVVCHMTSYITF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024308"
FT   VAR_SEQ         182..1799
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024309"
FT   VAR_SEQ         272..283
FT                   /note="FCPSTKGTTRYL -> VRIMISSLPG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024310"
FT   VAR_SEQ         284..1799
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024311"
SQ   SEQUENCE   1799 AA;  202942 MW;  57E01C1ECBDD2D31 CRC64;
     MAAAPTQIEA ELYYLIARFL QSGPCNKSAQ VLVQELEEHQ LIPRRLDWEG KEHRRSFEDL
     VAANAHIPPD YLLKICERIG PLLDKEIPQS VPGVQTLLGV GRQSLLRDAK DCKSTLWNGS
     AFAALHRGRP PELPVNYVKP PNVVNITSAR QLTGCSRFSH VFPSSAYQHI KMHKRILGHL
     SSVYCVAFDR SGRRIFTGSD DCLVKIWATD DGRLLATLRG HSAEISDMAV NYENTLIAAG
     SCDKVVRVWC LRTCAPVAVL QGHSASITSI QFCPSTKGTT RYLTSTGADG TICFWQWHVK
     TMKFRDRPVK FTERSRPGVQ ISCSSFSSGG MFITTGSTDH VIRIYYLGSE IPEKIAELES
     HTDKVVAVQF CNNGDSLRFV SGSRDGTARI WQYQQQEWKS IVLDMATKMS GNNLTSAEDK
     VTKLKVTMVA WDRYDTTVIT AVNNFLLKVW NSVTGQLLHT LSGHDDEVFV LEAHPFDQRI
     ILSAGHDGNI FIWDLDRGTK IRNYFNMIEG QGHGAVFDCK FSPDGNHFAC TDSHGHLLLF
     GFGCSKYYEK IPDQMFFHTD YRPLIRDANN YVLDEQTQQA PHLMPPPFLV DVDGNPHPTK
     FQRLVPGREN CKDEQLIPQL GYVANGDGEV VEQVIGQQTN DQEESILDGI IRELQREQDL
     RLINEGDVPH FPINRSYSVN GALSSPNMDI PSSPNIGLRR SGQIEGVRQM HNNAPRSQMA
     TERDLMAWSR RVVVNELNSG VSRVQEECRN AKGDLEVSLY TVEKKKKPSY PIQRNDYQPS
     CGRSLRRTQR KRQHTYLTRS NIEHNSQASS QTSGVQEDSD SSSEEDETVG TSDASVEDPV
     VEWQSESSSS DSSSEYSDWI ADAGINLQPP KRQTRQATQK IYSSSEDENL KLEDRQKKPK
     QTKKKKGGLV SMAGEPNEEW LAPQWILDTI PRRSPFVPQM GDELIYFRQG HEAYVRAVRK
     SKIYSVNLQK QPWNKMDLRE QEFVKIVGIK YEIGPPTLCC LKLAFLDPIS GKMTGESFSI
     KYHDMPDVID FLVLHQFYNE AKERNWQIGD RFRSIIDDAW WFGTVESQQP FQPEYPDSSF
     QCYSVHWDNN EREKMSPWDM EPIPDGTAFP DEVGAGIPVS QEELTALLYK PQEGEWGAHS
     RDEECERVIQ GINNLLSLDF ASPFAVPVDL SAYPLYCTVV AYPTDLNTIK QRLENRFYRR
     ISALMWEVRY IEHNARTFNE PDSPIVKAAK IVTDVLLRFI GDQSCSDILD TYNKIKAEDP
     DSSDLEEDSE MVDLDSDGPG TSSGRRAKCR GRRQSLKCNP DAWKKQCEEL LSLIYEREDS
     EPFRQPADPQ SYPVQQQQEG ESSQSVPPDR QDPSLSEDYQ DGIDTPMDFS TVKETLESGN
     YDSPLEFYKD VRQIFSNSKA YTSNKKSRIY SMTLRLSALF ENHIKNIISD YKSAIQSQKR
     RRPRYRKRLR SSSSSLSSSR APSPKGKQKQ MKLQPKNDQN TSVAYARTSS PFSSPVSDAA
     EGVSLYLLDD EGDGPFSPSS FSGYSRSGNS HDPGKAKSFR NRVLPAKQDH SLDGPLTNVD
     GREPRTGAKR KLLSASEEDE SMGGEEKEMK ETKEQVHLSS SESGELGSSL SSESTSGSDS
     DSESTSRTDQ DYVDGDHDYS KFIQTRPKRK LRKQHTNGKR NWKTRGTGGR GRWGRWGRWS
     RGGRGRGGRG RGGRGRGGGG GRGRGRGRGG RGASRGSSRA KRARVADDEF DTMFSGRFSR
     LPRIKTRNQG RRTVLYNDDS DNDNFVSTED PLNLGTSRSG RVRKMTEKAR VSHLMGWNY
 
 
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