| UniProt ID | MYC_HUMAN | |
|---|---|---|
| UniProt AC | P01106 | |
| Protein Name | Myc proto-oncogene protein | |
| Gene Name | MYC | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 439 | |
| Subcellular Localization | Nucleus, nucleoplasm . Nucleus, nucleolus . | |
| Protein Description | 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] | |
| Protein Sequence | MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MPLNVSFTNRNYD --CCCCCEECCCCCC | 25.86 | 23401153 | |
| 8 | Phosphorylation | MPLNVSFTNRNYDLD CCCCCEECCCCCCCC | 26.26 | 30266825 | |
| 12 | Phosphorylation | VSFTNRNYDLDYDSV CEECCCCCCCCCCCC | 18.04 | - | |
| 16 | Phosphorylation | NRNYDLDYDSVQPYF CCCCCCCCCCCCCEE | 19.88 | - | |
| 21 | Phosphorylation | LDYDSVQPYFYCDEE CCCCCCCCEEECCHH | 21.03 | 19664995 | |
| 21 (in isoform 2) | Phosphorylation | - | 21.03 | 19664995 | |
| 22 | Phosphorylation | DYDSVQPYFYCDEEE CCCCCCCEEECCHHH | 7.06 | - | |
| 32 | Phosphorylation | CDEEENFYQQQQQSE CCHHHCHHHHHHHHC | 19.59 | - | |
| 51 | Sumoylation | APSEDIWKKFELLPT CCCHHHHHHHHCCCC | 48.17 | - | |
| 52 | Sumoylation | PSEDIWKKFELLPTP CCHHHHHHHHCCCCC | 29.13 | - | |
| 52 | Sumoylation | PSEDIWKKFELLPTP CCHHHHHHHHCCCCC | 29.13 | 28112733 | |
| 52 | Ubiquitination | PSEDIWKKFELLPTP CCHHHHHHHHCCCCC | 29.13 | 21906983 | |
| 58 | O-linked_Glycosylation | KKFELLPTPPLSPSR HHHHCCCCCCCCCCC | 37.19 | 30130254 | |
| 58 | Phosphorylation | KKFELLPTPPLSPSR HHHHCCCCCCCCCCC | 37.19 | 29255136 | |
| 62 | Phosphorylation | LLPTPPLSPSRRSGL CCCCCCCCCCCCCCC | 26.97 | 29255136 | |
| 64 | Phosphorylation | PTPPLSPSRRSGLCS CCCCCCCCCCCCCCC | 36.63 | 29255136 | |
| 66 | Ubiquitination | PPLSPSRRSGLCSPS CCCCCCCCCCCCCCC | 39.14 | 22817900 | |
| 67 | Phosphorylation | PLSPSRRSGLCSPSY CCCCCCCCCCCCCCE | 34.70 | 22025562 | |
| 67 | Ubiquitination | PLSPSRRSGLCSPSY CCCCCCCCCCCCCCE | 34.70 | 22817900 | |
| 67 (in isoform 2) | Ubiquitination | - | 34.70 | - | |
| 71 | Phosphorylation | SRRSGLCSPSYVAVT CCCCCCCCCCEEEEC | 23.17 | 25159151 | |
| 73 | O-linked_Glycosylation | RSGLCSPSYVAVTPF CCCCCCCCEEEECCC | 18.88 | 20068231 | |
| 73 | Phosphorylation | RSGLCSPSYVAVTPF CCCCCCCCEEEECCC | 18.88 | 21712546 | |
| 73 (in isoform 2) | Phosphorylation | - | 18.88 | 24719451 | |
| 74 | Phosphorylation | SGLCSPSYVAVTPFS CCCCCCCEEEECCCE | 8.87 | 21712546 | |
| 76 | Phosphorylation | LCSPSYVAVTPFSLR CCCCCEEEECCCEEC | 7.39 | 32645325 | |
| 77 | Phosphorylation | CSPSYVAVTPFSLRG CCCCEEEECCCEECC | 5.08 | 10551811 | |
| 77 (in isoform 2) | Phosphorylation | - | 5.08 | 24719451 | |
| 78 | Phosphorylation | SPSYVAVTPFSLRGD CCCEEEECCCEECCC | 14.63 | 24732914 | |
| 79 | Phosphorylation | PSYVAVTPFSLRGDN CCEEEECCCEECCCC | 15.38 | 19651622 | |
| 81 | Phosphorylation | YVAVTPFSLRGDNDG EEEECCCEECCCCCC | 20.54 | 24732914 | |
| 86 | Phosphorylation | PFSLRGDNDGGGGSF CCEECCCCCCCCCCC | 53.29 | 10551811 | |
| 86 (in isoform 2) | Phosphorylation | - | 53.29 | 24719451 | |
| 88 | Phosphorylation | SLRGDNDGGGGSFST EECCCCCCCCCCCCH | 42.79 | 20068231 | |
| 143 | Acetylation | SGFSAAAKLVSEKLA CCHHHHHHHHHHHHH | 44.70 | 16126174 | |
| 143 | Sumoylation | SGFSAAAKLVSEKLA CCHHHHHHHHHHHHH | 44.70 | 28112733 | |
| 148 | Sumoylation | AAKLVSEKLASYQAA HHHHHHHHHHHHHHH | 41.67 | - | |
| 148 | Acetylation | AAKLVSEKLASYQAA HHHHHHHHHHHHHHH | 41.67 | 19608861 | |
| 148 | Sumoylation | AAKLVSEKLASYQAA HHHHHHHHHHHHHHH | 41.67 | 28112733 | |
| 148 | Ubiquitination | AAKLVSEKLASYQAA HHHHHHHHHHHHHHH | 41.67 | 20972266 | |
| 148 (in isoform 1) | Ubiquitination | - | 41.67 | 21890473 | |
| 151 | Phosphorylation | LVSEKLASYQAARKD HHHHHHHHHHHHHHC | 28.37 | 21955146 | |
| 157 | Sumoylation | ASYQAARKDSGSPNP HHHHHHHHCCCCCCC | 52.07 | - | |
| 157 | Acetylation | ASYQAARKDSGSPNP HHHHHHHHCCCCCCC | 52.07 | 16126174 | |
| 157 | Ubiquitination | ASYQAARKDSGSPNP HHHHHHHHCCCCCCC | 52.07 | 21906983 | |
| 158 | Ubiquitination | SYQAARKDSGSPNPA HHHHHHHCCCCCCCC | 53.31 | 23000965 | |
| 159 | Phosphorylation | YQAARKDSGSPNPAR HHHHHHCCCCCCCCC | 44.18 | 20068231 | |
| 161 | Phosphorylation | AARKDSGSPNPARGH HHHHCCCCCCCCCCC | 26.00 | 30576142 | |
| 162 | Ubiquitination | ARKDSGSPNPARGHS HHHCCCCCCCCCCCC | 55.11 | 33845483 | |
| 163 | Acetylation | RKDSGSPNPARGHSV HHCCCCCCCCCCCCC | 44.56 | 19608861 | |
| 163 | Ubiquitination | RKDSGSPNPARGHSV HHCCCCCCCCCCCCC | 44.56 | 23000965 | |
| 163 (in isoform 2) | Ubiquitination | - | 44.56 | 21890473 | |
| 169 | Phosphorylation | PNPARGHSVCSTSSL CCCCCCCCCCCCCHH | 27.87 | 26074081 | |
| 172 | Phosphorylation | ARGHSVCSTSSLYLQ CCCCCCCCCCHHHHH | 29.21 | 26074081 | |
| 172 | Ubiquitination | ARGHSVCSTSSLYLQ CCCCCCCCCCHHHHH | 29.21 | 21906983 | |
| 172 (in isoform 2) | Ubiquitination | - | 29.21 | - | |
| 173 | Phosphorylation | RGHSVCSTSSLYLQD CCCCCCCCCHHHHHC | 19.74 | 26074081 | |
| 174 | Phosphorylation | GHSVCSTSSLYLQDL CCCCCCCCHHHHHCH | 11.31 | 26074081 | |
| 175 | Phosphorylation | HSVCSTSSLYLQDLS CCCCCCCHHHHHCHH | 22.56 | 26074081 | |
| 176 | Phosphorylation | SVCSTSSLYLQDLSA CCCCCCHHHHHCHHH | 5.05 | 20068231 | |
| 176 (in isoform 2) | Phosphorylation | - | 5.05 | 24719451 | |
| 202 | Phosphorylation | FPYPLNDSSSPKSCA CCCCCCCCCCCCCCC | 31.48 | 25627689 | |
| 203 | Phosphorylation | PYPLNDSSSPKSCAS CCCCCCCCCCCCCCC | 54.23 | 25627689 | |
| 204 | Phosphorylation | YPLNDSSSPKSCASQ CCCCCCCCCCCCCCC | 40.06 | 26657352 | |
| 249 | Phosphorylation | EETPPTTSSDSEEEQ CCCCCCCCCCCHHHH | 34.33 | 2663470 | |
| 250 | Phosphorylation | ETPPTTSSDSEEEQE CCCCCCCCCCHHHHC | 42.96 | 2663470 | |
| 252 | Phosphorylation | PPTTSSDSEEEQEDE CCCCCCCCHHHHCCH | 49.18 | 22025562 | |
| 275 | Acetylation | EKRQAPGKRSESGSP EECCCCCCCCCCCCC | 52.25 | 16126174 | |
| 277 | Phosphorylation | RQAPGKRSESGSPSA CCCCCCCCCCCCCCC | 39.33 | 23927012 | |
| 279 | Phosphorylation | APGKRSESGSPSAGG CCCCCCCCCCCCCCC | 45.90 | 23927012 | |
| 281 | Phosphorylation | GKRSESGSPSAGGHS CCCCCCCCCCCCCCC | 25.59 | 23401153 | |
| 283 | Phosphorylation | RSESGSPSAGGHSKP CCCCCCCCCCCCCCC | 41.04 | 23927012 | |
| 288 | Phosphorylation | SPSAGGHSKPPHSPL CCCCCCCCCCCCCCC | 50.56 | 23927012 | |
| 292 (in isoform 2) | Phosphorylation | - | 51.04 | 24719451 | |
| 293 | Phosphorylation | GHSKPPHSPLVLKRC CCCCCCCCCCEEEEC | 26.21 | 23401153 | |
| 298 | Sumoylation | PHSPLVLKRCHVSTH CCCCCEEEECCCCCC | 45.56 | 28112733 | |
| 304 | Ubiquitination | LKRCHVSTHQHNYAA EEECCCCCCCCCCCC | 25.19 | 29967540 | |
| 313 | Ubiquitination | QHNYAAPPSTRKDYP CCCCCCCCCCCCCCC | 43.54 | 29967540 | |
| 314 | Phosphorylation | HNYAAPPSTRKDYPA CCCCCCCCCCCCCCC | 39.52 | 28555341 | |
| 315 | Phosphorylation | NYAAPPSTRKDYPAA CCCCCCCCCCCCCCH | 47.73 | 29449344 | |
| 317 | Sumoylation | AAPPSTRKDYPAAKR CCCCCCCCCCCCHHC | 62.80 | - | |
| 317 | Acetylation | AAPPSTRKDYPAAKR CCCCCCCCCCCCHHC | 62.80 | 16126174 | |
| 323 | Sumoylation | RKDYPAAKRVKLDSV CCCCCCHHCCCCCHH | 60.89 | - | |
| 323 | Acetylation | RKDYPAAKRVKLDSV CCCCCCHHCCCCCHH | 60.89 | 16126174 | |
| 323 | Ubiquitination | RKDYPAAKRVKLDSV CCCCCCHHCCCCCHH | 60.89 | 21906983 | |
| 326 | Sumoylation | YPAAKRVKLDSVRVL CCCHHCCCCCHHHHH | 51.08 | - | |
| 326 | Ubiquitination | YPAAKRVKLDSVRVL CCCHHCCCCCHHHHH | 51.08 | - | |
| 329 | Phosphorylation | AKRVKLDSVRVLRQI HHCCCCCHHHHHHHH | 23.43 | 24719451 | |
| 337 | Phosphorylation | VRVLRQISNNRKCTS HHHHHHHHCCCCCCC | 21.51 | 27251275 | |
| 338 | Ubiquitination | RVLRQISNNRKCTSP HHHHHHHCCCCCCCC | 54.69 | 22817900 | |
| 341 | Ubiquitination | RQISNNRKCTSPRSS HHHHCCCCCCCCCCC | 43.94 | 22817900 | |
| 343 | Phosphorylation | ISNNRKCTSPRSSDT HHCCCCCCCCCCCCC | 44.81 | 22115753 | |
| 344 | Phosphorylation | SNNRKCTSPRSSDTE HCCCCCCCCCCCCCH | 27.99 | 25159151 | |
| 344 (in isoform 2) | Phosphorylation | - | 27.99 | 24719451 | |
| 347 | Phosphorylation | RKCTSPRSSDTEENV CCCCCCCCCCCHHHH | 35.63 | 25159151 | |
| 348 | Phosphorylation | KCTSPRSSDTEENVK CCCCCCCCCCHHHHH | 50.24 | 25159151 | |
| 350 | Phosphorylation | TSPRSSDTEENVKRR CCCCCCCCHHHHHHH | 47.34 | 28176443 | |
| 352 (in isoform 2) | Phosphorylation | - | 70.21 | 27251275 | |
| 355 | Sumoylation | SDTEENVKRRTHNVL CCCHHHHHHHHHHHH | 47.98 | - | |
| 355 | Ubiquitination | SDTEENVKRRTHNVL CCCHHHHHHHHHHHH | 47.98 | 21906983 | |
| 358 | Phosphorylation | EENVKRRTHNVLERQ HHHHHHHHHHHHHHH | 23.10 | 33259812 | |
| 358 (in isoform 2) | Phosphorylation | - | 23.10 | 27251275 | |
| 359 | Phosphorylation | ENVKRRTHNVLERQR HHHHHHHHHHHHHHH | 22.16 | 19413330 | |
| 363 | Phosphorylation | RRTHNVLERQRRNEL HHHHHHHHHHHHHHH | 42.35 | 19413330 | |
| 363 (in isoform 2) | Phosphorylation | - | 42.35 | 27251275 | |
| 365 | Phosphorylation | THNVLERQRRNELKR HHHHHHHHHHHHHHH | 39.03 | 19413330 | |
| 369 | Ubiquitination | LERQRRNELKRSFFA HHHHHHHHHHHHHHH | 54.58 | 33845483 | |
| 370 | Ubiquitination | ERQRRNELKRSFFAL HHHHHHHHHHHHHHH | 6.79 | 33845483 | |
| 371 | Acetylation | RQRRNELKRSFFALR HHHHHHHHHHHHHHH | 39.56 | 16126174 | |
| 373 | Phosphorylation | RRNELKRSFFALRDQ HHHHHHHHHHHHHHH | 24.11 | 19574224 | |
| 389 | Sumoylation | PELENNEKAPKVVIL HHHCCCCCCCEEEEE | 72.60 | - | |
| 389 | Ubiquitination | PELENNEKAPKVVIL HHHCCCCCCCEEEEE | 72.60 | 21906983 | |
| 392 | Sumoylation | ENNEKAPKVVILKKA CCCCCCCEEEEEECC | 54.73 | - | |
| 398 | Sumoylation | PKVVILKKATAYILS CEEEEEECCEEEEHH | 47.74 | - | |
| 400 | Phosphorylation | VVILKKATAYILSVQ EEEEECCEEEEHHCC | 28.95 | 22020439 | |
| 404 | Ubiquitination | KKATAYILSVQAEEQ ECCEEEEHHCCHHHH | 2.40 | 21906983 | |
| 404 (in isoform 2) | Ubiquitination | - | 2.40 | - | |
| 405 | Phosphorylation | KATAYILSVQAEEQK CCEEEEHHCCHHHHH | 11.56 | - | |
| 407 | Ubiquitination | TAYILSVQAEEQKLI EEEEHHCCHHHHHCC | 39.41 | 22817900 | |
| 412 | Sumoylation | SVQAEEQKLISEEDL HCCHHHHHCCCHHHH | 51.58 | - | |
| 412 | Ubiquitination | SVQAEEQKLISEEDL HCCHHHHHCCCHHHH | 51.58 | 2190698 | |
| 413 (in isoform 2) | Ubiquitination | - | 5.35 | - | |
| 415 | Phosphorylation | AEEQKLISEEDLLRK HHHHHCCCHHHHHHH | 45.42 | 30001349 | |
| 427 | Ubiquitination | LRKRREQLKHKLEQL HHHHHHHHHHHHHHH | 5.56 | 21906983 | |
| 427 (in isoform 2) | Ubiquitination | - | 5.56 | - | |
| 430 | Sumoylation | RREQLKHKLEQLRNS HHHHHHHHHHHHHHH | 52.73 | - | |
| 437 | Ubiquitination | KLEQLRNSCA----- HHHHHHHHCC----- | 12.65 | 29967540 | |
| 445 | Ubiquitination | CA------------- CC------------- | 27667366 | ||
| 445 (in isoform 2) | Ubiquitination | - | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 8 | T | Phosphorylation | Kinase | RAF | - | Uniprot |
| 8 | T | Phosphorylation | Kinase | RAF1 | P04049 | PSP |
| 32 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
| 58 | T | Phosphorylation | Kinase | GSK-3_GROUP | - | PhosphoELM |
| 58 | T | Phosphorylation | Kinase | GSK3 | - | Uniprot |
| 58 | T | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
| 58 | T | Phosphorylation | Kinase | MAPK10 | P53779 | GPS |
| 58 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
| 58 | T | Phosphorylation | Kinase | GSK3B | P18266 | PSP |
| 58 | T | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
| 58 | T | Phosphorylation | Kinase | GSK3A | P49840 | PSP |
| 62 | S | Phosphorylation | Kinase | DYRK2 | Q92630 | Uniprot |
| 62 | S | Phosphorylation | Kinase | GSK3 | - | Uniprot |
| 62 | S | Phosphorylation | Kinase | CDK2 | P24941 | Uniprot |
| 62 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| 62 | S | Phosphorylation | Kinase | GSK-FAMILY | - | GPS |
| 62 | S | Phosphorylation | Kinase | PLK1 | P53350 | PSP |
| 62 | S | Phosphorylation | Kinase | MTOR | P42345 | PSP |
| 62 | S | Phosphorylation | Kinase | MAPK10 | P53779 | GPS |
| 62 | S | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
| 62 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| 62 | S | Phosphorylation | Kinase | ERK5 | Q13164 | PSP |
| 62 | S | Phosphorylation | Kinase | MAPK3 | P21708 | GPS |
| 62 | S | Phosphorylation | Kinase | MAPK1 | P63086 | GPS |
| 62 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
| 62 | S | Phosphorylation | Kinase | MK01 | P28482 | PhosphoELM |
| 67 | S | Phosphorylation | Kinase | CK1A | P48729 | PSP |
| 71 | S | Phosphorylation | Kinase | MAPK9 | P45984 | GPS |
| 71 | S | Phosphorylation | Kinase | MAPK10 | P53779 | GPS |
| 71 | S | Phosphorylation | Kinase | MAPK8 | P45983 | GPS |
| 74 | Y | Phosphorylation | Kinase | ABL1 | P00519 | GPS |
| 249 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 250 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 252 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 252 | S | Phosphorylation | Kinase | CK1A | P48729 | PSP |
| 293 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
| 293 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
| 293 | S | Phosphorylation | Kinase | PIM3 | Q86V86 | PSP |
| 329 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | Uniprot |
| 347 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 348 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 358 | T | Phosphorylation | Kinase | PAK2 | Q13177 | PSP |
| 373 | S | Phosphorylation | Kinase | PAK2 | Q13177 | PSP |
| 400 | T | Phosphorylation | Kinase | PAK2 | Q13177 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | HUWE1 | Q7Z6Z7 | PMID:16269333 |
| - | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:20852628 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXW7 | Q969H0 | PMID:15103331 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRPC4AP | Q8TEL6 | PMID:20551172 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:12769843 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM32 | Q13049 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:23175188 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXO32 | Q969P5 | PMID:25944903 |
| - | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:22543587 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 58 | T | Phosphorylation |
| 8386367 |
| 58 | T | Phosphorylation |
| 8386367 |
| 58 | T | Phosphorylation |
| 8386367 |
| 58 | T | ubiquitylation |
| 8386367 |
| 58 | T | ubiquitylation |
| 8386367 |
| 62 | S | Phosphorylation |
| 8386367 |
| 62 | S | Phosphorylation |
| 8386367 |
| 62 | S | Phosphorylation |
| 8386367 |
| 62 | S | Phosphorylation |
| 8386367 |
| 62 | S | ubiquitylation |
| 8386367 |
| 62 | S | ubiquitylation |
| 8386367 |
| 329 | S | Phosphorylation |
| 22307329 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MYC_HUMAN !! | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND MASS SPECTROMETRY. | |
| "Six lysine residues on c-Myc are direct substrates for acetylation byp300."; Zhang K., Faiola F., Martinez E.; Biochem. Biophys. Res. Commun. 336:274-280(2005). Cited for: ACETYLATION AT LYS-143; LYS-157; LYS-275; LYS-317; LYS-323 ANDLYS-371, AND MASS SPECTROMETRY. | |
| O-linked Glycosylation | |
| Reference | PubMed |
| "c-Myc is glycosylated at threonine 58, a known phosphorylation siteand a mutational hot spot in lymphomas."; Chou T.-Y., Hart G.W., Dang C.V.; J. Biol. Chem. 270:18961-18965(1995). Cited for: GLYCOSYLATION AT THR-58. | |
| Phosphorylation | |
| Reference | PubMed |
| "Phosphorylation by Cdk2 is required for Myc to repress Ras-inducedsenescence in cotransformation."; Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K.,von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S.,Vervoorts J., Henriksson M., Grandien A., Luescher B., Larsson L.-G.; Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010). Cited for: PHOSPHORYLATION AT SER-62 BY CDK2, AND MUTAGENESIS OF THR-58 ANDSER-62. | |
| "Tipping the balance: Cdk2 enables Myc to suppress senescence."; Hydbring P., Larsson L.-G.; Cancer Res. 70:6687-6691(2010). Cited for: REVIEW ON SENESCENCE, PHOSPHORYLATION AT SER-62 BY CDK2, ANDMUTAGENESIS OF THR-58 AND SER-62. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-344 AND SER-348,AND MASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58; SER-62 AND SER-71,AND MASS SPECTROMETRY. | |
| "The ubiquitin-specific protease USP28 is required for MYCstability."; Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R.,Bernards R., Moll R., Elledge S.J., Eilers M.; Nat. Cell Biol. 9:765-774(2007). Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP28, INTERACTION WITH FBXW7,SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-58 AND SER-62, ANDMUTAGENESIS OF THR-58 AND SER-62. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-62, AND MASSSPECTROMETRY. | |
| "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). Cited for: UBIQUITINATION, INTERACTION WITH FBXW7, PHOSPHORYLATION AT THR-58 ANDSER-62, AND MUTAGENESIS OF THR-58 AND SER-62. | |
| "Transactivation of gene expression by Myc is inhibited by mutation atthe 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). Cited for: PHOSPHORYLATION AT THR-58 AND SER-62. | |
| "c-Raf kinase binds to N-terminal domain of c-Myc."; Alexandrov I., Shlyakhova L., Vartanian A., Zajac-Kaye M.,Alexandrova N.; FEBS Lett. 414:465-470(1997). Cited for: PHOSPHORYLATION AT THR-8. | |
