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BAHD1_MOUSE
ID   BAHD1_MOUSE             Reviewed;         772 AA.
AC   Q497V6; A2AQV1; A6PWW9; B2RUB2; B7ZNH0; Q6ZQ21; Q80VH7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Bromo adjacent homology domain-containing 1 protein;
DE            Short=BAH domain-containing protein 1;
GN   Name=Bahd1; Synonyms=Gm117, Kiaa0945;
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] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Brain, Mammary tumor, and Thyroid;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, 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: Heterochromatin protein that acts as a transcription
CC       repressor and has the ability to promote the formation of large
CC       heterochromatic domains. May act by recruiting heterochromatin proteins
CC       such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by
CC       binding to its CpG-rich P3 promoter and recruiting heterochromatin
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CBX5 (HP1 alpha), HDAC5, MBD1 and SP1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to
CC       heterochromatin and inactive X chromosome. Colocalizes with histone H3
CC       trimethylated at 'Lys-27' (H3K27me3) (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q497V6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q497V6-2; Sequence=VSP_038527;
CC   -!- DOMAIN: The BAH domain is required for localization at H3K27me3.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98053.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAO77853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK129243; BAC98053.1; ALT_INIT; mRNA.
DR   EMBL; AL845164; CAM19753.1; -; Genomic_DNA.
DR   EMBL; AL845164; CAO77853.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH466519; EDL27930.1; -; Genomic_DNA.
DR   EMBL; BC047433; AAH47433.1; -; mRNA.
DR   EMBL; BC100358; AAI00359.1; -; mRNA.
DR   EMBL; BC141046; AAI41047.1; -; mRNA.
DR   EMBL; BC145233; AAI45234.1; -; mRNA.
DR   CCDS; CCDS38202.1; -. [Q497V6-1]
DR   AlphaFoldDB; Q497V6; -.
DR   SMR; Q497V6; -.
DR   STRING; 10090.ENSMUSP00000043130; -.
DR   iPTMnet; Q497V6; -.
DR   PhosphoSitePlus; Q497V6; -.
DR   jPOST; Q497V6; -.
DR   MaxQB; Q497V6; -.
DR   PaxDb; Q497V6; -.
DR   PRIDE; Q497V6; -.
DR   ProteomicsDB; 273595; -. [Q497V6-1]
DR   ProteomicsDB; 273596; -. [Q497V6-2]
DR   MGI; MGI:2139371; Bahd1.
DR   eggNOG; KOG1886; Eukaryota.
DR   InParanoid; Q497V6; -.
DR   PhylomeDB; Q497V6; -.
DR   TreeFam; TF350135; -.
DR   PRO; PR:Q497V6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q497V6; protein.
DR   GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   Gene3D; 2.30.30.490; -; 1.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   Pfam; PF01426; BAH; 1.
DR   SMART; SM00439; BAH; 1.
DR   PROSITE; PS51038; BAH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..772
FT                   /note="Bromo adjacent homology domain-containing 1 protein"
FT                   /id="PRO_0000287919"
FT   DOMAIN          616..771
FT                   /note="BAH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..581
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBE0"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBE0"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBE0"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBE0"
FT   MOD_RES         580
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBE0"
FT   VAR_SEQ         677..679
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_038527"
FT   CONFLICT        275
FT                   /note="D -> N (in Ref. 2; CAM19753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        550
FT                   /note="T -> A (in Ref. 2; CAM19753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   772 AA;  83871 MW;  537BD20D92AD563D CRC64;
     MTHTRRKSLP MLSSGPTGRG EPLQMEDSNM EQGTEDVEPG MPESPGHLTG RRKNYPLRKR
     SLVPEKPKAC KVLLTRLENV AGPRSADEAD ELPPDLPKPP SPTSSSEDAG LVQPRKRRLA
     SLNAEALNNL LLEREETSSL AGARRSRGGD PHRSRDRATG SWSFSKKRPR LGDLGEGSRD
     LSPELAPDEG ARRDGDPAPK RLASLNAAAF LKLSQERELP LRPSRAQAEA DGRSTEPLAP
     RILRPKVNGK NCPKARQGAG SGEATGPPNW QEQPDERWPS APPHGPPTQP SHQAPGKALE
     NPLRPNLPLL MGGQAALKPE PGRPGEESPA PKQELHQPSF PAPQLSPLPM PGNPADYSGP
     CGGPELTALG SFYLYCGQDG LQCGAYSPCP MLPEGKLSPV AAPNEGLLMA PSSVPSGVPF
     QHPPWSAPRY CSSEDTGANG YSICGVLPLS LTHIGTTCGG CPYKMPFTAE GCRSLGQLEF
     PLPEAGHPAS PAHPLLGCPV PSVPPAAEPI PHLQTPISEP QTVARACPQS AKPPSGSKSG
     LRTGSSCRHT VRSKAARRPS HPKQPRAQRP RPRRRRRRRT NGWVPVGAAC EKAVYVLDEP
     EPAIRKSYQA VERHGETIRV RDTVLLKSGP RKTSTPYVAK ISALWENPES GELMMSLLWY
     YRPEHLQGGR SPSMHEPLQN EVFASRHQDQ NSVACIEEKC YVLTFAEYCR FCAMAKRRGE
     GLPSRKTALV PPSADYSTPP HRTVPEDTDP ELVFLCRHVY DFRHGRILKN PQ
 
 
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