Skip Header

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

P01106

- MYC_HUMAN

UniProt

P01106 - MYC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Myc proto-oncogene protein

Gene

MYC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. E-box binding Source: UniProtKB
  3. protein complex binding Source: UniProtKB
  4. repressing transcription factor binding Source: UniProtKB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. branching involved in ureteric bud morphogenesis Source: UniProtKB
  2. canonical Wnt signaling pathway Source: UniProtKB
  3. cell cycle arrest Source: UniProtKB
  4. cellular iron ion homeostasis Source: UniProtKB
  5. cellular response to DNA damage stimulus Source: UniProtKB
  6. cellular response to drug Source: UniProtKB
  7. cellular response to UV Source: UniProtKB
  8. chromatin remodeling Source: UniProtKB
  9. chromosome organization Source: UniProtKB
  10. energy reserve metabolic process Source: UniProtKB
  11. fibroblast apoptotic process Source: UniProtKB
  12. gene expression Source: Reactome
  13. MAPK cascade Source: UniProtKB
  14. negative regulation of apoptotic process Source: UniProtKB
  15. negative regulation of cell division Source: UniProtKB
  16. negative regulation of fibroblast proliferation Source: UniProtKB
  17. negative regulation of monocyte differentiation Source: UniProtKB
  18. negative regulation of stress-activated MAPK cascade Source: UniProtKB
  19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  20. Notch signaling pathway Source: Reactome
  21. oxygen transport Source: UniProtKB
  22. positive regulation of cell proliferation Source: MGI
  23. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  24. positive regulation of DNA biosynthetic process Source: UniProtKB
  25. positive regulation of epithelial cell proliferation Source: UniProtKB
  26. positive regulation of fibroblast proliferation Source: UniProtKB
  27. positive regulation of mesenchymal cell proliferation Source: UniProtKB
  28. positive regulation of metanephric cap mesenchymal cell proliferation Source: UniProtKB
  29. positive regulation of response to DNA damage stimulus Source: UniProtKB
  30. positive regulation of transcription, DNA-templated Source: UniProtKB
  31. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  32. regulation of gene expression Source: MGI
  33. regulation of telomere maintenance Source: BHF-UCL
  34. response to drug Source: UniProtKB
  35. response to gamma radiation Source: UniProtKB
  36. response to growth factor Source: UniProtKB
  37. transcription, DNA-templated Source: Reactome
  38. transcription initiation from RNA polymerase II promoter Source: Reactome
  39. transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000136997-MONOMER.
ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP01106.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:7553. MYC.

Subcellular locationi

Nucleusnucleoplasm 1 Publication. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
  2. nucleoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Overexpression of MYC is implicated in the etiology of a variety of hematopoietic tumors.
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.
Burkitt lymphoma (BL) [MIM:113970]: A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass.2 Publications
Note: 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581T → A: Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence. 4 Publications
Mutagenesisi62 – 621S → 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 Publications

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi113970. phenotype.
Orphaneti543. Burkitt lymphoma.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA31353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Myc proto-oncogene proteinPRO_0000127293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei8 – 81Phosphothreonine; by RAF; in vitro1 Publication
Modified residuei58 – 581Phosphothreonine; by GSK3; alternate6 Publications
Glycosylationi58 – 581O-linked (GlcNAc); alternate1 PublicationCAR_000033
Modified residuei62 – 621Phosphoserine; by DYRK2, GSK3 and CDK28 Publications
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei143 – 1431N6-acetyllysine; by PCAF1 Publication
Modified residuei148 – 1481N6-acetyllysine1 Publication
Modified residuei157 – 1571N6-acetyllysine; by PCAF1 Publication
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei275 – 2751N6-acetyllysine; by PCAF1 Publication
Modified residuei317 – 3171N6-acetyllysine; by PCAF1 Publication
Modified residuei323 – 3231N6-acetyllysine; by PCAF1 Publication
Modified residuei329 – 3291Phosphoserine; by PIM2; in vitroBy similarity
Modified residuei371 – 3711N6-acetyllysine; by PCAF1 Publication

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 similarity9 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, due to the lack of interaction between isoform 4 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus. Also polyubiquitinated by the DCX(TRUSS) complex.9 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP01106.
PaxDbiP01106.
PRIDEiP01106.

2D gel databases

SWISS-2DPAGEP01106.

PTM databases

PhosphoSiteiP01106.
UniCarbKBiP01106.

Expressioni

Gene expression databases

BgeeiP01106.
CleanExiHS_MYC.
ExpressionAtlasiP01106. baseline and differential.
GenevestigatoriP01106.

Organism-specific databases

HPAiCAB000084.
CAB010307.

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-447544,EBI-617698From a different organism.
AXIN1O1516910EBI-447544,EBI-710484
BIN1O00499-103EBI-447544,EBI-7689134
BIN1O00499-112EBI-447544,EBI-7689211
BRD3Q150593EBI-447544,EBI-1383460
CCAR2Q8N1638EBI-447544,EBI-355410
CDK4P118022EBI-447544,EBI-295644
CEP57Q86XR83EBI-447544,EBI-308614
CHD4Q148392EBI-447544,EBI-372916
CHUKO151113EBI-447544,EBI-81249
E7P031292EBI-447544,EBI-866453From a different organism.
E7P040202EBI-447544,EBI-7005254From a different organism.
E7P067885EBI-447544,EBI-1776887From a different organism.
EFTUD2Q150295EBI-447544,EBI-357897
FBXW7Q969H04EBI-447544,EBI-359574
FBXW8Q8N3Y13EBI-447544,EBI-914770
HDAC2Q927692EBI-447544,EBI-301821
HDAC3O153796EBI-447544,EBI-607682
IKBKGQ9Y6K93EBI-447544,EBI-81279
KIAA1524Q8TCG12EBI-447544,EBI-1379376
MAXP6124421EBI-447544,EBI-751711
MaxP521644EBI-447544,EBI-1184963From a different organism.
MCM7P339936EBI-447544,EBI-355924
PIAS2O759284EBI-447544,EBI-348555
RPL11P629133EBI-447544,EBI-354380
SIRT1Q96EB64EBI-447544,EBI-1802965
SIRT6Q8N6T73EBI-447544,EBI-712415
SKP2Q133092EBI-447544,EBI-456291
SNIP1Q8TAD89EBI-447544,EBI-749336
SP1P080474EBI-447544,EBI-298336
TOP1P113872EBI-447544,EBI-876302
TRRAPQ9Y4A54EBI-447544,EBI-399128
UBCP0CG485EBI-447544,EBI-3390054
UBTFP174802EBI-447544,EBI-396235
ZBTB17Q131054EBI-447544,EBI-372156

Protein-protein interaction databases

BioGridi110694. 568 interactions.
DIPiDIP-28143N.
IntActiP01106. 670 interactions.
MINTiMINT-257327.
STRINGi9606.ENSP00000367207.

Structurei

Secondary structure

1
439
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi353 – 37826
Helixi382 – 3843
Helixi392 – 43443

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A93NMR-A406-434[»]
1EE4X-ray2.10C/D/E/F320-328[»]
1MV0NMR-A55-68[»]
1NKPX-ray1.80A/D353-434[»]
2A93NMR-A406-434[»]
2OR9X-ray2.70P410-419[»]
DisProtiDP00260.
ProteinModelPortaliP01106.
SMRiP01106. Positions 353-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01106.

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

eggNOGiNOG42590.
GeneTreeiENSGT00510000046414.
HOGENOMiHOG000043075.
HOVERGENiHBG000472.
InParanoidiP01106.
KOiK04377.
OrthoDBiEOG7GJ6CX.
PhylomeDBiP01106.
TreeFamiTF106001.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72SF → TI no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti10 – 101R → K no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti56 – 561L → LL no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti62 – 621S → P in CAA25288. (PubMed:6547209)Curated
Sequence conflicti88 – 881G → D no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti92 – 921S → N no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti114 – 1141S → N no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti120 – 1201D → G no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti171 – 1711C → S no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti203 – 2031S → R no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti230 – 2301S → A no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti240 – 2401L → F no nucleotide entry (PubMed:6419122)Curated
Sequence conflicti245 – 2451P → S no nucleotide entry (PubMed:6419122)Curated
Isoform 2 (identifier: P01106-2)
Sequence conflicti2 – 21D → N in BAA01374. (PubMed:6547209)Curated
Sequence conflicti6 – 61V → E in BAA01374. (PubMed:6547209)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111N → S.1 Publication
Corresponds to variant rs4645959 [ dbSNP | Ensembl ].
VAR_016327
Natural varianti39 – 391E → D in a Burkitt lymphoma symple. 2 Publications
VAR_063384
Natural varianti57 – 571P → S in a Burkitt lymphoma sample. 1 Publication
VAR_063385
Natural varianti59 – 591P → A in a Burkitt lymphoma sample. 1 Publication
VAR_063386
Natural varianti86 – 861N → T in a Burkitt lymphoma sample. 1 Publication
VAR_063387
Natural varianti160 – 1601G → C.1 Publication
Corresponds to variant rs4645960 [ dbSNP | Ensembl ].
VAR_016328
Natural varianti170 – 1701V → I.1 Publication
Corresponds to variant rs4645961 [ dbSNP | Ensembl ].
VAR_016329
Natural varianti322 – 3221A → V.1 Publication
Corresponds to variant rs4645968 [ dbSNP | Ensembl ].
VAR_016330

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDFFRVVENQQPPATM in isoform 2. 1 PublicationVSP_037813

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
GeneIDi4609.
KEGGihsa:4609.
UCSCiuc003ysi.3. human. [P01106-2]
uc022bbe.1. human. [P01106-1]

Polymorphism databases

DMDMi127619.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

Myc entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6359.2. [P01106-2 ]
PIRi A01349. TVHUM.
A01350. TVHUT.
RefSeqi NP_002458.2. NM_002467.4. [P01106-2 ]
UniGenei Hs.202453.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A93 NMR - A 406-434 [» ]
1EE4 X-ray 2.10 C/D/E/F 320-328 [» ]
1MV0 NMR - A 55-68 [» ]
1NKP X-ray 1.80 A/D 353-434 [» ]
2A93 NMR - A 406-434 [» ]
2OR9 X-ray 2.70 P 410-419 [» ]
DisProti DP00260.
ProteinModelPortali P01106.
SMRi P01106. Positions 353-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110694. 568 interactions.
DIPi DIP-28143N.
IntActi P01106. 670 interactions.
MINTi MINT-257327.
STRINGi 9606.ENSP00000367207.

Chemistry

BindingDBi P01106.
ChEMBLi CHEMBL1250348.
DrugBanki DB08813. Nadroparin.

PTM databases

PhosphoSitei P01106.
UniCarbKBi P01106.

Polymorphism databases

DMDMi 127619.

2D gel databases

SWISS-2DPAGE P01106.

Proteomic databases

MaxQBi P01106.
PaxDbi P01106.
PRIDEi P01106.

Protocols and materials databases

DNASUi 4609.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377970 ; ENSP00000367207 ; ENSG00000136997 . [P01106-1 ]
GeneIDi 4609.
KEGGi hsa:4609.
UCSCi uc003ysi.3. human. [P01106-2 ]
uc022bbe.1. human. [P01106-1 ]

Organism-specific databases

CTDi 4609.
GeneCardsi GC08P128748.
H-InvDB HIX0007784.
HGNCi HGNC:7553. MYC.
HPAi CAB000084.
CAB010307.
MIMi 113970. phenotype.
190080. gene.
neXtProti NX_P01106.
Orphaneti 543. Burkitt lymphoma.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBi PA31353.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42590.
GeneTreei ENSGT00510000046414.
HOGENOMi HOG000043075.
HOVERGENi HBG000472.
InParanoidi P01106.
KOi K04377.
OrthoDBi EOG7GJ6CX.
PhylomeDBi P01106.
TreeFami TF106001.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000136997-MONOMER.
Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200799. binding of TCF/LEF:CTNNB1 to target gene promoters.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinki P01106.

Miscellaneous databases

ChiTaRSi MYC. human.
EvolutionaryTracei P01106.
GeneWikii Myc.
GenomeRNAii 4609.
NextBioi 17740.
PROi P01106.
SOURCEi Search...

Gene expression databases

Bgeei P01106.
CleanExi HS_MYC.
ExpressionAtlasi P01106. baseline and differential.
Genevestigatori P01106.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
IPR003327. Myc-LZ.
IPR002418. Tscrpt_reg_Myc.
IPR012682. Tscrpt_reg_Myc_N.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
PF02344. Myc-LZ. 1 hit.
PF01056. Myc_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001705. Myc_protein. 1 hit.
PRINTSi PR00044. LEUZIPPRMYC.
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human c-myc oncogene: structural consequences of translocation into the IgH locus in Burkitt lymphoma."
    Battey J., Moulding C., Taub R., Murphy W., Stewart T., Potter H., Lenoir G., Leder P.
    Cell 34:779-787(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  2. "Sequence of the murine and human cellular myc oncogenes and two modes of myc transcription resulting from chromosome translocation in B lymphoid tumours."
    Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M.
    EMBO J. 2:2375-2383(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  3. "Identification and nucleotide sequence of a human locus homologous to the v-myc oncogene of avian myelocytomatosis virus MC29."
    Colby W.W., Chen E.Y., Smith D.H., Levinson A.D.
    Nature 301:722-725(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  4. "Nucleotide sequence of cloned cDNA of human c-myc oncogene."
    Watt R., Stanton L.W., Marcu K.B., Gallo R.C., Croce C.M., Rovera G.
    Nature 303:725-728(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Altered nucleotide sequences of a translocated c-myc gene in Burkitt lymphoma."
    Rabbitts T.H., Hamlyn P.H., Baer R.
    Nature 306:760-765(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-39.
  6. "Nucleotide sequence analysis of human c-myc locus, chicken homologue, and myelocytomatosis virus MC29 transforming gene reveals a highly conserved gene product."
    Watson D.K., Psallidopoulos M.C., Samuel K.P., Dalla-Favera R., Papas T.S.
    Proc. Natl. Acad. Sci. U.S.A. 80:3642-3645(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  7. "Effect of somatic mutation within translocated c-myc genes in Burkitt's lymphoma."
    Rabbitts T.H., Forster A., Hamlyn P., Baer R.
    Nature 309:592-597(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
  8. "Nucleotide sequence of the human c-myc locus: provocative open reading frame within the first exon."
    Gazin C., Dupont S., de Dinechin D., Hampe A., Masson J.-M., Martin P., Stehelin D., Galibert F.
    EMBO J. 3:383-387(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  9. "Allele-specific activation of the c-myc gene in an atypical Burkitt's lymphoma carrying the t(2;8) chromosomal translocation 250 kb downstream from c-myc."
    Tachibana K., Takayama N., Matsuo K., Kato S., Yamamoto K., Ohyama K., Umezawa A., Takano T.
    Gene 124:231-237(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  11. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-11; CYS-160; ILE-170 AND VAL-322.
  12. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  13. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cervix, Placenta and Testis.
  16. "Novel promoter upstream of the human c-myc gene and regulation of c-myc expression in B-cell lymphomas."
    Bentley D.L., Groudine M.
    Mol. Cell. Biol. 6:3481-3489(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORM 1).
    Tissue: Promyelocytic leukemia.
  17. "The pathogenesis of Burkitt's lymphoma."
    Magrath I.
    Adv. Cancer Res. 55:133-270(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN BURKITT LYMPHOMA.
  18. "DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein."
    Iijima S., Teraoka H., Date T., Tsukada K.
    Eur. J. Biochem. 206:595-603(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  19. "Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas."
    Bhatia K., Huppi K., Spangler G., Siwarski D., Iyer R., Magrath I.
    Nat. Genet. 5:56-61(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN BURKITT LYMPHOMA, VARIANTS ASP-39; SER-57; ALA-59 AND THR-86.
  20. "Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62."
    Gupta S., Seth A., Davis R.J.
    Proc. Natl. Acad. Sci. U.S.A. 90:3216-3220(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-58 AND SER-62.
  21. "c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas."
    Chou T.-Y., Hart G.W., Dang C.V.
    J. Biol. Chem. 270:18961-18965(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-58.
  22. Cited for: PHOSPHORYLATION AT THR-8.
  23. "Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7."
    Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R., Imaki H., Ishida N., Okumura F., Nakayama K., Nakayama K.I.
    EMBO J. 23:2116-2125(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH FBXW7, PHOSPHORYLATION AT THR-58 AND SER-62, MUTAGENESIS OF THR-58 AND SER-62.
  24. "Six lysine residues on c-Myc are direct substrates for acetylation by p300."
    Zhang K., Faiola F., Martinez E.
    Biochem. Biophys. Res. Commun. 336:274-280(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 AND LYS-371, IDENTIFICATION BY MASS SPECTROMETRY.
  25. "c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I."
    Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C., Galloway D.A., Eisenman R.N., White R.J.
    Nat. Cell Biol. 7:311-318(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF1C.
  26. Cited for: INTERACTION WITH PARP10.
  27. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Induction of pluripotent stem cells from adult human fibroblasts by defined factors."
    Takahashi K., Tanabe K., Ohnuki M., Narita M., Ichisaka T., Tomoda K., Yamanaka S.
    Cell 131:861-872(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY.
  29. "Fbw7 and Usp28 regulate myc protein stability in response to DNA damage."
    Popov N., Herold S., Llamazares M., Schulein C., Eilers M.
    Cell Cycle 6:2327-2331(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7.
  30. "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth."
    Secombe J., Li L., Carlos L., Eisenman R.N.
    Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDM5A AND KDM5B.
  31. "Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer."
    Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T., Tsuchiya E., Nakamura Y., Daigo Y.
    Mol. Cancer Ther. 6:542-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NO66.
  32. Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-58 AND SER-62, MUTAGENESIS OF THR-58 AND SER-62.
  33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Tipping the balance: Cdk2 enables Myc to suppress senescence."
    Hydbring P., Larsson L.-G.
    Cancer Res. 70:6687-6691(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON SENESCENCE, PHOSPHORYLATION AT SER-62 BY CDK2, MUTAGENESIS OF THR-58 AND SER-62.
  37. Cited for: PHOSPHORYLATION AT SER-62 BY CDK2, MUTAGENESIS OF THR-58 AND SER-62.
  38. "Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."
    Choi S.H., Wright J.B., Gerber S.A., Cole M.D.
    Genes Dev. 24:1236-1241(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  39. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells."
    Taira N., Mimoto R., Kurata M., Yamaguchi T., Kitagawa M., Miki Y., Yoshida K.
    J. Clin. Invest. 122:859-872(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-62, MUTAGENESIS OF SER-62.
  42. "Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper."
    Lavigne P., Crump M.P., Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D.
    J. Mol. Biol. 281:165-181(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 402-434 IN COMPLEX WITH MAX.

Entry informationi

Entry nameiMYC_HUMAN
AccessioniPrimary (citable) accession number: P01106
Secondary accession number(s): A8WFE7, P01107, Q14026
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 195 of the entry and version 1 of the sequence. [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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3