Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myc proto-oncogene protein

Gene

MYC

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • E-box binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myc proto-oncogene protein
Alternative name(s):
Proto-oncogene c-Myc
Transcription factor p64
Gene namesi
Name:MYC
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Myc proto-oncogene proteinPRO_0000127290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei58 – 581Phosphothreonine; by GSK3; alternateBy similarity
Glycosylationi58 – 581O-linked (GlcNAc); alternateBy similarity
Modified residuei62 – 621Phosphoserine; by DYRK2, GSK3 and CDK2By similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei143 – 1431N6-acetyllysine; by PCAFBy similarity
Modified residuei148 – 1481N6-acetyllysineBy similarity
Modified residuei157 – 1571N6-acetyllysine; by PCAFBy similarity
Modified residuei161 – 1611PhosphoserineBy similarity
Modified residuei275 – 2751N6-acetyllysine; by PCAFBy similarity
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei317 – 3171N6-acetyllysine; by PCAFBy similarity
Modified residuei323 – 3231N6-acetyllysine; by PCAFBy similarity
Modified residuei329 – 3291Phosphoserine; by PIM2; in vitroBy similarity
Modified residuei371 – 3711N6-acetyllysine; by PCAFBy similarity

Post-translational modificationi

Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC. Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence (By similarity).By similarity
Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRUSS) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ28350.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX. Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7. Interacts with PIM2. Interacts with NO66. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000001523.

Structurei

3D structure databases

ProteinModelPortaliQ28350.
SMRiQ28350. Positions 353-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 40653bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 43422Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 375Poly-Gln
Compositional biasi88 – 914Poly-Gly

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IFSM. Eukaryota.
ENOG41124Q3. LUCA.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiQ28350.
KOiK04377.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001705. Myc_protein. 1 hit.
PRINTSiPR00044. LEUZIPPRMYC.
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q28350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW
60 70 80 90 100
KKFELLPTPP LSPSRRSGLC SPSYVAVASF SPRGDDDGGG GSFSTADQLE
110 120 130 140 150
MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA
160 170 180 190 200
SYQAARKDSG SPSPARGPGG CSTSSLYLQD LSAAASECID PSVVFPYPLN
210 220 230 240 250
DSSSPKPCAS PDSAAFSPSS DSLLSSAESS PRASPEPLAL HEETPPTTSS
260 270 280 290 300
DSEEEQEDEE EIDVVSVEKR QAPAKRSESG SPSAGGHSKP PHSPLVLKRC
310 320 330 340 350
HVSTHQHNYA APPSTRKDYP AAKRARLDSG RVLKQISNNR KCASPRSSDT
360 370 380 390 400
EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT
410 420 430
AYILSVQAEE QKLLSEKDLL RKRREQLKHK LEQLRNSGA
Length:439
Mass (Da):48,410
Last modified:November 1, 1996 - v1
Checksum:i9A1D9F31C66C7C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95367 mRNA. Translation: CAA64654.1.
RefSeqiNP_001003246.2. NM_001003246.2.
UniGeneiCfa.3786.

Genome annotation databases

GeneIDi403924.
KEGGicfa:403924.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95367 mRNA. Translation: CAA64654.1.
RefSeqiNP_001003246.2. NM_001003246.2.
UniGeneiCfa.3786.

3D structure databases

ProteinModelPortaliQ28350.
SMRiQ28350. Positions 353-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000001523.

Proteomic databases

PaxDbiQ28350.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403924.
KEGGicfa:403924.

Organism-specific databases

CTDi4609.

Phylogenomic databases

eggNOGiENOG410IFSM. Eukaryota.
ENOG41124Q3. LUCA.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiQ28350.
KOiK04377.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001705. Myc_protein. 1 hit.
PRINTSiPR00044. LEUZIPPRMYC.
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMYC_CANLF
AccessioniPrimary (citable) accession number: Q28350
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.