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MYC_AVIM2
ID   MYC_AVIM2               Reviewed;         416 AA.
AC   P10395;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   23-FEB-2022, entry version 123.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Avian myelocytomatosis virus CMII.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   unclassified Alpharetrovirus.
OX   NCBI_TaxID=11869;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3019003; DOI=10.1016/0042-6822(86)90444-7;
RA   Walther N., Jansen H.W., Trachmann C., Bister K.;
RT   "Nucleotide sequence of the CMII v-myc allele.";
RL   Virology 154:219-223(1986).
CC   -!- FUNCTION: Transforms avian and murine macrophages and fibroblasts as
CC       well as murine B-lymphoid cells.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-vMyc chimeric
CC       protein. The sequence shown here corresponds to the Myc homolog
CC       fragment of the chimera.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42408.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M15241; AAA42408.1; ALT_INIT; Genomic_RNA.
DR   PIR; A24297; TVFV2C.
DR   SMR; P10395; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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   3: Inferred from homology;
KW   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           1..416
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127307"
FT   DOMAIN          331..383
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          144..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..411
FT                   /note="Leucine-zipper"
FT   COMPBIAS        153..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46098 MW;  6DF5E4BD3A1A5883 CRC64;
     MPLSASLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRG SELQPPAPSE DIWKKFELLP
     TPPLSPSRRS SLAAASCFPS TADQLEMVTE LLGGDMVNQS FICDPDDESF VKSIIIQDCM
     WSGFSAAAKL EKVVSEKLAT YQASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
     LGAAAADCID PSVVFPYPLS ERAPRAAPPG ANPAALLGVD TPPTTSSDSE EEQEEDEEID
     VVTLAEANES ESSTESSTEA SEEHCKPHHS PLVLKRCHVN IHQHNYAAPP STKVEYPAAK
     RLKLDSGRVL KQISNNRKCS SPRTSDSEEN DKRRTHNVLE RQRRNELKLS FFALRDQIPE
     VANNEKAPKV VILKKATEYV LSIQSDEHRL IAEKEQLRRR REQLKHKLEQ LRNSRE
 
 
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