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MYCB_DANRE
ID   MYCB_DANRE              Reviewed;         396 AA.
AC   Q7ZVS9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Transcriptional regulator Myc-B;
DE            Short=c-Myc-B;
GN   Name=mycb {ECO:0000312|EMBL:AAH45424.1}; ORFNames=zgc:55680;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH45424.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB {ECO:0000312|EMBL:AAH45424.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC       yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'.
CC       Activates the transcription of growth-related genes.
CC       {ECO:0000250|UniProtKB:P01106}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with max (By similarity).
CC       {ECO:0000250|UniProtKB:P01106}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P01106}.
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DR   EMBL; BC045424; AAH45424.1; -; mRNA.
DR   RefSeq; NP_956466.1; NM_200172.1.
DR   AlphaFoldDB; Q7ZVS9; -.
DR   SMR; Q7ZVS9; -.
DR   STRING; 7955.ENSDARP00000010970; -.
DR   PaxDb; Q7ZVS9; -.
DR   Ensembl; ENSDART00000005143; ENSDARP00000010970; ENSDARG00000007241.
DR   GeneID; 393141; -.
DR   KEGG; dre:393141; -.
DR   CTD; 393141; -.
DR   ZFIN; ZDB-GENE-040426-780; mycb.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00940000155285; -.
DR   HOGENOM; CLU_052560_0_0_1; -.
DR   InParanoid; Q7ZVS9; -.
DR   OMA; RCHVNIQ; -.
DR   OrthoDB; 877891at2759; -.
DR   PhylomeDB; Q7ZVS9; -.
DR   TreeFam; TF106001; -.
DR   PRO; PR:Q7ZVS9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000007241; Expressed in tail bud paraxial mesoderm and 40 other tissues.
DR   ExpressionAtlas; Q7ZVS9; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0060216; P:definitive hemopoiesis; IMP:ZFIN.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR003327; Myc-LZ.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF02344; Myc-LZ; 1.
DR   Pfam; PF01056; Myc_N; 1.
DR   PIRSF; PIRSF001705; Myc_protein; 1.
DR   PRINTS; PR00044; LEUZIPPRMYC.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Glycoprotein; Nucleus; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..396
FT                   /note="Transcriptional regulator Myc-B"
FT                   /id="PRO_0000271254"
FT   DOMAIN          313..365
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          183..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..393
FT                   /note="Leucine-zipper"
FT   MOTIF           79..87
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
FT   COMPBIAS        197..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        56
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
SQ   SEQUENCE   396 AA;  44919 MW;  849A0AE3BBC18BAA CRC64;
     MPLNSSMECK NYDYDYDSYQ PYFYFDNEDE DFYNHQHGQP PAPSEDIWKK FELLPTPPLS
     PSRRPSLSDP FPSTADKLEM VSEFLGDDVV NHSIICDADY SQSFLKSIII QDCMWSGFSA
     AAKLEKVVSE RLASLQAARK ESSRTESADI CRSVGFLQDM STPASQCIDP SVVFPFPLTD
     STKPCKPAPT PASTTLPLDT PPNSGSSSSS SDSESDDEDD EDEEEEEEID VVTVEKRKSV
     KKSDANATHQ SPVVLKRCHV NIHQHNYAAH PSTRNEQPAV KRIKFESHIR VFKQISHNRK
     CASPRTSDSE DNDKRRTHNV LERQRRNELK LSFFALRDVI PDVANNEKAA KVVILKKATE
     CIASMQEDEQ RLISLKEQLR RKCEHLKQRL EQLSCS
 
 
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