Search Keyword:


Search option:


IID00012
 UniprotP01106
ProteinMyc proto-oncogene protein
GeneMYC
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
454
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 16-103
 Evidence NMR The resolution in the HSQC spectrum of Myc 1-88 is characteristic of an intrinsically disordered protein, while Myc 1-88 contains multiple regions of transient secondary structure. Note: Myc 1-88 corresponds to Myc 16-103 of the current canonical sequence P01106-2. Reference
       Region 16-103 disorder
Seq 62-81 Hetero tetramer : Q969H0
 Evidence X-RAY 7t1z C Reference
       Region 7t1z C 62-65 disorder
       Region 7t1z C 66-77 order
       Region 7t1z C 78-81 disorder
Seq 69-77 Hetero dodecamer : IID50168Complex
 Evidence X-RAY 6c4u L Reference
       Region 6c4u L 69-70 disorder
       Region 6c4u L 71-76 order
       Region 6c4u L 77-77 disorder
 Evidence X-RAY 6c4u K Reference
       Region 6c4u K 69-76 order
       Region 6c4u K 77-77 disorder
 Evidence X-RAY 6c4u J Reference
       Region 6c4u J 69-69 disorder
       Region 6c4u J 70-77 order
 Evidence X-RAY 6c4u I Reference
       Region 6c4u I 69-69 disorder
       Region 6c4u I 70-77 order
 Evidence X-RAY 6c4u H Reference
       Region 6c4u H 69-69 disorder
       Region 6c4u H 70-77 order
 Evidence X-RAY 6c4u G Reference
       Region 6c4u G 69-69 disorder
       Region 6c4u G 70-77 order
Seq 70-83 Hetero dimer : IID00748Complex
 Evidence NMR 1mv0 A Reference
       Region 1mv0 A 70-83 order
Seq 111-140 Hetero trimer : P13393,P46677
 Evidence X-RAY 6e24 A Reference
       Region 6e24 A 111-111 disorder
       Region 6e24 A 112-122 order
       Region 6e24 A 123-140 disorder
Seq 111-140 Hetero trimer : P13393,P46677
 Evidence X-RAY 6e16 A Reference
       Region 6e16 A 111-111 disorder
       Region 6e16 A 112-126 order
       Region 6e16 A 127-140 disorder
Seq 250-273,275-280 Hetero trimer : Q969H0
 Evidence X-RAY 7t1y C Reference
       Region 7t1y C 250-255 disorder
       Region 7t1y C 256-263 order
       Region 7t1y C 264-273 disorder
       Region 7t1y C 275-280 disorder
Seq 275-282 Hetero dimer : IID00377Complex
 Evidence X-RAY 4y7r B Reference
       Region 4y7r B 275-282 order
Seq 335-343 Hetero trimer : IID50012Complex
 Evidence X-RAY 1ee4 C Reference
       Region 1ee4 C 335-343 order
 Evidence X-RAY 1ee4 D Reference
       Region 1ee4 D 335-337 disorder
       Region 1ee4 D 338-342 order
       Region 1ee4 D 343-343 disorder
 Evidence X-RAY 1ee4 E Reference
       Region 1ee4 E 335-343 order
 Evidence X-RAY 1ee4 F Reference
       Region 1ee4 F 335-337 disorder
       Region 1ee4 F 338-341 order
       Region 1ee4 F 342-343 disorder
Seq 365-454 Homo dimer :
 Evidence X-RAY 5i4z A Reference
       Region 5i4z A 365-380 disorder
       Region 5i4z A 381-454 order
 Evidence X-RAY 5i4z B Reference
       Region 5i4z B 365-380 disorder
       Region 5i4z B 381-454 order
 Evidence X-RAY 5i50 A Reference
       Region 5i50 A 365-454 order
 Evidence X-RAY 5i50 B Reference
       Region 5i50 B 365-454 order
Seq 366-452 Hetero octamer : IID00814Complex
 Evidence X-RAY 6g6l G Reference
       Region 6g6l G 366-375 disorder
       Region 6g6l G 376-452 order
 Evidence X-RAY 6g6l E Reference
       Region 6g6l E 366-374 disorder
       Region 6g6l E 375-452 order
 Evidence X-RAY 6g6l C Reference
       Region 6g6l C 366-373 disorder
       Region 6g6l C 374-452 order
 Evidence X-RAY 6g6l A Reference
       Region 6g6l A 366-374 disorder
       Region 6g6l A 375-452 order
Seq 366-452 Hetero tetramer : IID00814Complex
 Evidence X-RAY 6g6j C Reference
       Region 6g6j C 366-374 disorder
       Region 6g6j C 375-452 order
 Evidence X-RAY 6g6j A Reference
       Region 6g6j A 366-372 disorder
       Region 6g6j A 373-452 order
Seq 366-452 Hetero tetramer : IID00814Complex
 Evidence X-RAY 6g6k C Reference
       Region 6g6k C 366-452 order
 Evidence X-RAY 6g6k A Reference
       Region 6g6k A 366-452 order
Seq 368-449 Hetero dimer : IID00814Complex
 Evidence X-RAY 1nkp A Reference
       Region 1nkp A 368-449 order
 Evidence X-RAY 1nkp D Reference
       Region 1nkp D 368-449 order
Seq 421-449 Hetero dimer : IID50243Complex
 Evidence 1a93 A Reference
       Region 1a93 A 421-449 order
 Evidence NMR 2a93 A Reference
       Region 2a93 A 421-449 order
       Region 2a93 A 448-449 high_rmsd
Seq 425-434 Hetero trimer : P01654
 Evidence X-RAY 2or9 P Reference
       Region 2or9 P 425-434 order
SeqProS verified 66-77 Hetero tetramer : Q969H0
       Region 7t1z C 66-77 order
       Region 16-103 disorder
SeqProS verified 70-83 Hetero dimer : IID00748Complex
       Region 1mv0 A 70-83 order
       Region 16-103 disorder
SeqProS predicted 256-263 This region is predicted to be disordered by AlphaFold (pLDDT <68.5) and NeProc. Hetero trimer : Q969H0
       Region 7t1y C 256-263 order
SeqProS predicted 275-282 This region is predicted to be disordered by AlphaFold and NeProc. Hetero dimer : IID00377Complex
       Region 4y7r B 275-282 order
SeqProS possible 335-343 Nuclear Localization Signal (NLS) Hetero trimer : IID50012Complex
       Region 1ee4 C 335-343 order
       Region 1ee4 D 338-342 order
       Region 1ee4 E 335-343 order
       Region 1ee4 F 338-341 order
Seqphosphorylation
    86-86 Phosphoserine
    344-344 Phosphoserine; by PIM2; in vitro
    176-176 Phosphoserine
    308-308 Phosphoserine
    77-77 Phosphoserine; by DYRK2
    73-73 Phosphothreonine; by GSK3; alternate
    23-23 Phosphothreonine; by RAF; in vitro
    21-21 Phosphoserine
Seqacetylation
    386-386 N6-acetyllysine; by PCAF
    290-290 N6-acetyllysine; by PCAF
    332-332 N6-acetyllysine; by PCAF
    338-338 N6-acetyllysine; by PCAF
    172-172 N6-acetyllysine; by PCAF
    163-163 N6-acetyllysine; alternate
    158-158 N6-acetyllysine; by PCAF; alternate
 
Prediction
NeProc
Disorder 1-28,40-44,49-375
Order 29-39,45-48,376-454
ProS 1-8,23-28,40-44,62-93,99-177,188-221,233-258,274-284,309-315,328-331,351-362
AlphaFold
Disorder 1-45,47-48,50-94,101-149,152-152,154-186,195-195,197-260,262-262,264-307,309-309,311-349,439-439
Order 46-46,49-49,95-100,150-151,153-153,187-194,196-196,261-261,263-263,308-308,310-310,350-438
Pfam Hmmer
PF01056 16-360 5.1e-206
PF00010 370-422 7.3e-19
PF02344 423-454 7.1e-17
SEG 48-52 ,70-88 ,222-252 ,257-283
Function
Function in SwissProt
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808).
Biological Process
Diagram with PDB data
MYC/BIN1NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC
MYC/WDR5Crystal structure of WDR5 in complex with MYC MbIIIb peptide
MYC/FBXW7/SKP1Structure of the Fbw7-Skp1-MycCdegron complex
See also
Diagram with PDB data
MAX/MYC/DNACrystal structure of Myc-Max recognizing DNA