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UniProtKB - P01106 (MYC_HUMAN)

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Protein

Myc proto-oncogene protein

Gene

MYC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000).2 Publications

GO - Molecular functioni

  • activating transcription factor binding Source: CAFA
  • DNA binding Source: UniProtKB
  • DNA binding transcription factor activity Source: UniProtKB
  • E-box binding Source: UniProtKB
  • protein-containing complex binding Source: UniProtKB
  • protein dimerization activity Source: InterPro
  • repressing transcription factor binding Source: UniProtKB
  • RNA polymerase II proximal promoter sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding Source: NTNU_SB
  • transcription factor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • branching involved in ureteric bud morphogenesis Source: UniProtKB
  • canonical Wnt signaling pathway Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cellular iron ion homeostasis Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • cellular response to hypoxia Source: CAFA
  • cellular response to UV Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • chromosome organization Source: UniProtKB
  • cytokine-mediated signaling pathway Source: Reactome
  • energy reserve metabolic process Source: UniProtKB
  • ERK1 and ERK2 cascade Source: CAFA
  • fibroblast apoptotic process Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: Reactome
  • MAPK cascade Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell division Source: UniProtKB
  • negative regulation of fibroblast proliferation Source: UniProtKB
  • negative regulation of monocyte differentiation Source: UniProtKB
  • negative regulation of stress-activated MAPK cascade Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: UniProtKB
  • Notch signaling pathway Source: Reactome
  • oxygen transport Source: UniProtKB
  • positive regulation of cell proliferation Source: CAFA
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of gene expression Source: CAFA
  • positive regulation of mesenchymal cell proliferation Source: UniProtKB
  • positive regulation of metanephric cap mesenchymal cell proliferation Source: UniProtKB
  • positive regulation of response to DNA damage stimulus Source: UniProtKB
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription by RNA polymerase II Source: NTNU_SB
  • protein deubiquitination Source: Reactome
  • protein-DNA complex disassembly Source: CAFA
  • regulation of gene expression Source: MGI
  • regulation of telomere maintenance Source: BHF-UCL
  • regulation of transcription by RNA polymerase II Source: Reactome
  • response to drug Source: UniProtKB
  • response to gamma radiation Source: UniProtKB
  • response to growth factor Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000136997-MONOMER
ReactomeiR-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-4411364 Binding of TCF/LEF:CTNNB1 to target gene promoters
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6785807 Interleukin-4 and 13 signaling
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8866911 TFAP2 (AP-2) family regulates transcription of cell cycle factors
R-HSA-8951430 RUNX3 regulates WNT signaling
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP01106
SIGNORiP01106

Names & Taxonomyi

Protein namesi
Recommended name:
Myc proto-oncogene protein
Alternative name(s):
Class E basic helix-loop-helix protein 39
Short name:
bHLHe39
Proto-oncogene c-Myc
Transcription factor p64
Gene namesi
Name:MYC
Synonyms:BHLHE39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000136997.15
HGNCiHGNC:7553 MYC
MIMi190080 gene
neXtProtiNX_P01106

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MYC may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with BTG1.1 Publication
Burkitt lymphoma (BL)2 Publications
The gene represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci.
Disease descriptionA form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass.
See also OMIM:113970

Biotechnological usei

POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58T → A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence. 4 Publications1
Mutagenesisi62S → A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Impaired inhibition of Ras-induced senescence. Abolishes phosphorylation by DYRK2, and subsequent phosphorylation by GSK3B at Thr-58. 5 Publications1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi4609
MalaCardsiMYC
MIMi113970 phenotype
OpenTargetsiENSG00000136997
Orphaneti543 Burkitt lymphoma
99861 Precursor T-cell acute lymphoblastic leukemia
PharmGKBiPA31353

Chemistry databases

ChEMBLiCHEMBL1250348
DrugBankiDB08813 Nadroparin

Polymorphism and mutation databases

BioMutaiMYC
DMDMi127619

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001272931 – 439Myc proto-oncogene proteinAdd BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6PhosphoserineCombined sources1
Modified residuei8Phosphothreonine; by RAF; in vitro1 Publication1
Cross-linki52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei58Phosphothreonine; by GSK3; alternateCombined sources3 Publications1
GlycosylationiCAR_00003358O-linked (GlcNAc) threonine; alternate1 Publication1
Modified residuei62Phosphoserine; by DYRK2, GSK3 and CDK2Combined sources6 Publications1
Modified residuei71PhosphoserineCombined sources1
Modified residuei143N6-acetyllysine; by PCAF; alternate1 Publication1
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei148N6-acetyllysine; alternateCombined sources1
Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei157N6-acetyllysine; by PCAF1 Publication1
Modified residuei161PhosphoserineCombined sources1
Modified residuei275N6-acetyllysine; by PCAF1 Publication1
Modified residuei293PhosphoserineCombined sources1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei317N6-acetyllysine; by PCAF1 Publication1
Modified residuei323N6-acetyllysine; by PCAF1 Publication1
Modified residuei329Phosphoserine; by PIM2; in vitroBy similarity1
Modified residuei371N6-acetyllysine; by PCAF1 Publication1

Post-translational modificationi

Phosphorylated by PRKDC. Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. 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 similarity6 Publications
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 isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation. In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus (PubMed:25775507,PubMed:17558397). Also polyubiquitinated by the DCX(TRUSS) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity).By similarity7 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP01106
MaxQBiP01106
PaxDbiP01106
PeptideAtlasiP01106
PRIDEiP01106
ProteomicsDBi51318
51319 [P01106-2]

2D gel databases

SWISS-2DPAGEiP01106

PTM databases

GlyConnecti426
iPTMnetiP01106
PhosphoSitePlusiP01106
UniCarbKBiP01106

Expressioni

Gene expression databases

BgeeiENSG00000136997
CleanExiHS_MYC
ExpressionAtlasiP01106 baseline and differential
GenevisibleiP01106 HS

Organism-specific databases

HPAiCAB000084
CAB010307
HPA055893
HPA066556

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (PubMed:9680483). Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7(PubMed:25775507, PubMed:17558397). Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (PubMed:25956029). Interacts with CIP2A; leading to the stabilization of MYC (PubMed:17632056).By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-447544,EBI-617698From Simian virus 40.
ARHGEF2Q929742EBI-447544,EBI-302405
ATP2A2P166152EBI-447544,EBI-358933
AXIN1O1516910EBI-447544,EBI-710484
BIN1O00499-103EBI-447544,EBI-7689134
BIN1O00499-112EBI-447544,EBI-7689211
BRD3Q150593EBI-447544,EBI-1383460
CCAR2Q8N1639EBI-447544,EBI-355410
CDK4P118022EBI-447544,EBI-295644
CEP57Q86XR83EBI-447544,EBI-308614
CHD4Q148392EBI-447544,EBI-372916
CHUKO151113EBI-447544,EBI-81249
CIP2AQ8TCG12EBI-447544,EBI-1379376
COPG1Q9Y6782EBI-447544,EBI-1049127
CTPS1P178122EBI-447544,EBI-1042983
DDX20Q9UHI62EBI-447544,EBI-347658
DDX24Q9GZR72EBI-447544,EBI-713081
E6P031262EBI-447544,EBI-1177242From Human papillomavirus type 16.
E7P031292EBI-447544,EBI-866453From Human papillomavirus type 16.
E7P040202EBI-447544,EBI-7005254From Human papillomavirus type 11.
E7P067885EBI-447544,EBI-1776887From Human papillomavirus type 18.
EBNA6P0320411EBI-447544,EBI-9255985From Epstein-Barr virus (strain B95-8).
EFTUD2Q150296EBI-447544,EBI-357897
EP400Q96L914EBI-447544,EBI-399163
EP400Q96L91-22EBI-447544,EBI-15698003
FBXW7Q969H04EBI-447544,EBI-359574
FBXW8Q8N3Y13EBI-447544,EBI-914770
FOXO3O435243EBI-447544,EBI-1644164
GSK3BP49841-23EBI-447544,EBI-15870655
GTF3C3Q9Y5Q92EBI-447544,EBI-1054873
HDAC2Q927692EBI-447544,EBI-301821
HDAC3O153796EBI-447544,EBI-607682
HELLSQ9NRZ92EBI-447544,EBI-1056215
HNRNPCP079102EBI-447544,EBI-357966
IKBKGQ9Y6K93EBI-447544,EBI-81279
IPO4Q8TEX92EBI-447544,EBI-395967
IPO9Q96P702EBI-447544,EBI-356319
IQGAP2Q135762EBI-447544,EBI-357571
LRPPRCP427043EBI-447544,EBI-1050853
MAP7D1Q3KQU32EBI-447544,EBI-713229
MARSP561922EBI-447544,EBI-355848
MAXP6124437EBI-447544,EBI-751711
MaxP521644EBI-447544,EBI-1184963From Rattus norvegicus.
MBD3O959833EBI-447544,EBI-1783068
MCM7P339937EBI-447544,EBI-355924
METTL13Q8N6R02EBI-447544,EBI-1053295
MMS19Q96T762EBI-447544,EBI-1044169
MSH6P527012EBI-447544,EBI-395529
MYBBP1AQ9BQG02EBI-447544,EBI-676973
NOP56O005672EBI-447544,EBI-396034
NUP133Q8WUM02EBI-447544,EBI-295695
NUP93Q8N1F72EBI-447544,EBI-1042703
OPA1O603132EBI-447544,EBI-1054131
PDS5BQ9NTI52EBI-447544,EBI-1175604
PIAS2O759284EBI-447544,EBI-348555
PIN1Q135265EBI-447544,EBI-714158
POLEQ078642EBI-447544,EBI-348526
POLR2BP308762EBI-447544,EBI-394712
PRPF6O949063EBI-447544,EBI-536755
RFC4P352492EBI-447544,EBI-476655
RPL11P629133EBI-447544,EBI-354380
SIN3BO751827EBI-447544,EBI-540462
Sin3bQ621418EBI-447544,EBI-591450From Mus musculus.
SIRT1Q96EB64EBI-447544,EBI-1802965
SIRT6Q8N6T73EBI-447544,EBI-712415
SKP2Q133092EBI-447544,EBI-456291
SMARCC1Q929222EBI-447544,EBI-355653
SMC2O953472EBI-447544,EBI-355822
SMC4Q9NTJ33EBI-447544,EBI-356173
SNIP1Q8TAD89EBI-447544,EBI-749336
SNRNP200O756432EBI-447544,EBI-1045395
SP1P080474EBI-447544,EBI-298336
TOP1P113872EBI-447544,EBI-876302
TRIM28Q132632EBI-447544,EBI-78139
TRIP12Q146697EBI-447544,EBI-308443
TRRAPQ9Y4A55EBI-447544,EBI-399128
UBCP0CG485EBI-447544,EBI-3390054
UBTFP174802EBI-447544,EBI-396235
XPO5Q9HAV42EBI-447544,EBI-517949
ZBTB17Q131059EBI-447544,EBI-372156

GO - Molecular functioni

  • activating transcription factor binding Source: CAFA
  • protein dimerization activity Source: InterPro
  • repressing transcription factor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110694, 619 interactors
ComplexPortaliCPX-1123 FOXO3-MYC complex
CPX-514 c-MYC-BIN1 complex
CPX-91 Transcriptional activator Myc-Max complex
CORUMiP01106
DIPiDIP-28143N
IntActiP01106, 787 interactors
MINTiP01106
STRINGi9606.ENSP00000367207

Chemistry databases

BindingDBiP01106

Structurei

Secondary structure

1439
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi353 – 378Combined sources26
Helixi382 – 384Combined sources3
Helixi392 – 434Combined sources43

3D structure databases

DisProtiDP00260
ProteinModelPortaliP01106
SMRiP01106
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01106

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini354 – 406bHLHPROSITE-ProRule annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni413 – 434Leucine-zipperAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi33 – 37Poly-Gln5
Compositional biasi88 – 91Poly-Gly4

Phylogenomic databases

eggNOGiENOG410IFSM Eukaryota
ENOG41124Q3 LUCA
GeneTreeiENSGT00510000046414
HOGENOMiHOG000043075
HOVERGENiHBG000472
InParanoidiP01106
KOiK04377
PhylomeDBiP01106
TreeFamiTF106001

Family and domain databases

CDDicd00083 HLH, 1 hit
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR003327 Myc-LZ
IPR002418 Tscrpt_reg_Myc
IPR012682 Tscrpt_reg_Myc_N
PfamiView protein in Pfam
PF00010 HLH, 1 hit
PF02344 Myc-LZ, 1 hit
PF01056 Myc_N, 1 hit
PIRSFiPIRSF001705 Myc_protein, 1 hit
PRINTSiPR00044 LEUZIPPRMYC
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SUPFAMiSSF47459 SSF47459, 1 hit
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P01106-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW 
        60         70         80         90        100
KKFELLPTPP LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE 
       110        120        130        140        150
MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA 
       160        170        180        190        200
SYQAARKDSG SPNPARGHSV CSTSSLYLQD LSAAASECID PSVVFPYPLN 
       210        220        230        240        250
DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL HEETPPTTSS 
       260        270        280        290        300
DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC 
       310        320        330        340        350
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT 
       360        370        380        390        400
EENVKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT 
       410        420        430 
AYILSVQAEE QKLISEEDLL RKRREQLKHK LEQLRNSCA
Length:439
Mass (Da):48,804
Last modified:August 13, 1987 - v1
Checksum:iED5C028029A4C5D1
GO
Isoform 2 (identifier: P01106-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDFFRVVENQQPPATM

Note: Initiates from CTG codon.Curated
Show »
Length:454
Mass (Da):50,565
Checksum:i8B4107BB740689E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6 – 7SF → TI no nucleotide entry (PubMed:6419122).Curated2
Sequence conflicti10R → K no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti56L → LL no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti62S → P in CAA25288 (PubMed:6547209).Curated1
Sequence conflicti88G → D no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti92S → N no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti114S → N no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti120D → G no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti171C → S no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti203S → R no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti230S → A no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti240L → F no nucleotide entry (PubMed:6419122).Curated1
Sequence conflicti245P → S no nucleotide entry (PubMed:6419122).Curated1
Isoform 2 (identifier: P01106-2)
Sequence conflicti2D → N in BAA01374 (PubMed:6547209).Curated1
Sequence conflicti6V → E in BAA01374 (PubMed:6547209).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01632711N → S1 PublicationCorresponds to variant dbSNP:rs4645959Ensembl.1
Natural variantiVAR_06338439E → D in a Burkitt lymphoma symple. 2 PublicationsCorresponds to variant dbSNP:rs121918684Ensembl.1
Natural variantiVAR_06338557P → S in a Burkitt lymphoma sample. 1 PublicationCorresponds to variant dbSNP:rs28933407Ensembl.1
Natural variantiVAR_06338659P → A in a Burkitt lymphoma sample. 1 PublicationCorresponds to variant dbSNP:rs121918685Ensembl.1
Natural variantiVAR_06338786N → T in a Burkitt lymphoma sample. 1 PublicationCorresponds to variant dbSNP:rs121918683Ensembl.1
Natural variantiVAR_016328160G → C1 PublicationCorresponds to variant dbSNP:rs4645960Ensembl.1
Natural variantiVAR_016329170V → I1 PublicationCorresponds to variant dbSNP:rs4645961Ensembl.1
Natural variantiVAR_016330322A → V1 PublicationCorresponds to variant dbSNP:rs4645968Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0378131M → MDFFRVVENQQPPATM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00058, L00057 Genomic DNA Translation: AAA59882.1
K00535, K00534 Genomic DNA Translation: AAA59880.1
K00535, K00534 Genomic DNA Translation: ABW69847.1
X00196, X00198 Genomic DNA Translation: CAA25015.2
X00364 Genomic DNA Translation: CAA25106.1
V00568 mRNA Translation: CAA23831.1
K01906, K01905 Genomic DNA Translation: AAA59881.1
K02276 mRNA Translation: AAA36340.1
X00676 Genomic DNA Translation: CAA25288.1
D10493 Genomic DNA Translation: BAA01374.2
D10493 Genomic DNA Translation: BAA01375.1
BT019768 mRNA Translation: AAV38573.1
AY214166 Genomic DNA Translation: AAO21131.1
AK312883 mRNA Translation: BAG35731.1
AC103819 Genomic DNA No translation available.
CH471060 Genomic DNA Translation: EAW92098.1
BC000141 mRNA Translation: AAH00141.2
BC000917 mRNA Translation: AAH00917.2
BC058901 mRNA Translation: AAH58901.2
M13929 mRNA Translation: AAA88092.1
CCDSiCCDS6359.2 [P01106-2]
PIRiA01349 TVHUM
A01350 TVHUT
RefSeqiNP_002458.2, NM_002467.4 [P01106-2]
UniGeneiHs.202453

Genome annotation databases

EnsembliENST00000377970; ENSP00000367207; ENSG00000136997 [P01106-1]
ENST00000613283; ENSP00000479618; ENSG00000136997 [P01106-2]
GeneIDi4609
KEGGihsa:4609
UCSCiuc064qdj.1 human [P01106-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMYC_HUMAN
AccessioniPrimary (citable) accession number: P01106
Secondary accession number(s): A8WFE7, P01107, Q14026
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: July 18, 2018
This is version 235 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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