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P21438 (MYC_FLVTT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Viral myc transforming protein

Short name=v-Myc
Gene names
Name:MYC
OrganismFeline leukemia virus FTT
Taxonomic identifier11923 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence CAC[GA]TG. Seems to activate the transcription of growth-related genes By similarity.

Subcellular location

Host nucleus Potential.

Miscellaneous

This protein is synthesized as a Gag-vMyc chimeric protein. The sequence shown here corresponds to the Myc homolog fragment of the chimera.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentHost nucleus
   DiseaseOncogene
   LigandDNA-binding
   Molecular functionActivator
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

cellular iron ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of monocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of telomere maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

response to gamma radiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionE-box binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Viral myc transforming protein
PRO_0000127312

Regions

Domain354 – 40653bHLH
Region413 – 43422Leucine-zipper
Compositional bias33 – 375Poly-Gln
Compositional bias88 – 914Poly-Gly
Compositional bias253 – 2619Poly-Glu

Sequences

Sequence LengthMass (Da)Tools
P21438 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 1C39AD24B1CEB4D7

FASTA43748,309
        10         20         30         40         50         60 
MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP 

        70         80         90        100        110        120 
LSPSRRSGLC SPSYVAFASF SPRGDDDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD 

       130        140        150        160        170        180 
DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPSPARGPGG CPTSSLYLQD 

       190        200        210        220        230        240 
LTAAASECID PSVVFPYPLN DSSSPKPCAS PDSAAFSPSS DSLLSSAESS PRASPKPLGL 

       250        260        270        280        290        300 
HEETPPTTSS DSEEEQEEEE EIDVVSVEKR QPPAKRSESG SPSAGGHSKP PHSPLVLKRC 

       310        320        330        340        350        360 
HVPTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCISPRSSDT EENDKRRTDN 

       370        380        390        400        410        420 
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAGE QKLISEKDLL 

       430 
RKRREQLKHK LEQLRNS 

« Hide

References

[1]"Nucleotide sequence of a transduced myc gene from a defective feline leukemia provirus."
Braun M.J., Deininger P.L., Casey J.W.
J. Virol. 55:177-183(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure, origin, and transforming activity of feline leukemia virus-myc recombinant provirus FTT."
Doggett D.L., Drake A.L., Hirsch V., Rowe M.E., Stallard V., Mullins J.I.
J. Virol. 63:2108-2117(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10973 Genomic DNA. Translation: AAA43059.1. Sequence problems.
M25762 Genomic DNA. Translation: AAA30812.1.
PIRTVMVFT. A26268.

3D structure databases

ProteinModelPortalP21438.
SMRP21438. Positions 353-434.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFPIRSF001705. Myc_protein. 1 hit.
PRINTSPR00044. LEUZIPPRMYC.
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMYC_FLVTT
AccessionPrimary (citable) accession number: P21438
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families