P01106

※ Protein Information

Tag	Content
UniProt Accession	MYC_HUMAN; P01106;
Entrez ID	4609
GenBank Protein ID
GenBank Nucleotide ID
Protein Name	Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64)
Gene Name	MYC; BHLHE39
Organism	Homo sapiens
NCBI Taxa ID	9606
Functional 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). Functional 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).
Sequence (Fasta)	MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP 60 LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD 120 DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPNPARGHSV CSTSSLYLQD 180 LSAAASECID PSVVFPYPLN DSSSPKSCAS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL 240 HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC 300 HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT EENVKRRTHN 360 VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAEE QKLISEEDLL 420 RKRREQLKHK LEQLRNSCA Fasta Sequence >P01106\|MYC; BHLHE39\|Homo sapiens (Human) MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Ubiquitination	Cervical cancer/carcinoma		P		15150404
1	[Reference]: The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation.
2	Threonine Phosphorylation	T cell lymphoma		D	T58	17192266; 10488335
2	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
3	Threonine Phosphorylation	Cervical cancer/carcinoma		N	T58	15150404
3	[Reference]: T58 is the most frequent site of c-myc mutations in lymphoma cells, and our findings suggest that c-Myc activation is one of the key oncogenic consequences of Fbw7 loss in cancer.
4	Threonine Phosphorylation	B-cell lymphoma		P	T58	10706881
4	[Reference]: Our results show that proteasome-mediated turnover of c-Myc is substantially impaired in Burkitt's lymphoma cells with mutated Thr58 or other mutations that abolish Thr58 phosphorylation, whereas endogenous or ectopically expressed wild type c-Myc proteins turn over at normal rates in these cells.
5	Threonine Phosphorylation	Acute myeloid leukaemia/Acute myelogenous leukemia		U	T58	17192266; 10488335
5	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
6	Threonine Phosphorylation	Breast cancer/tumor/carcinoma		U	T58	17192266; 11175856
6	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
7	Threonine Phosphorylation	Papillary adenoma		U	T58	10360173; 17192266
7	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
8	Threonine Phosphorylation	Hepatocellular carcinoma/Hepatocarcinoma/Hepatoma		U	T58	15455033; 17192266
8	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
9	Threonine Phosphorylation	Islet cell carcinoma		U	T58	12015982; 17192266
9	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
10	Threonine Phosphorylation	Osteogenic sarcoma/Osteosarcoma		U	T58	12098700; 17192266
10	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
11	Serine Phosphorylation	T cell lymphoma		D	S62	17192266; 10488335
11	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
12	Serine Phosphorylation	Breast cancer/tumor/carcinoma		P	S62	22307329
12	[Reference]: DYRK2 priming phosphorylation of c-Jun and c-Myc modulates cell cycle progression in human cancer cells
13	Serine Phosphorylation	Hepatocellular carcinoma/Hepatocarcinoma/Hepatoma		U	S62	15455033; 17192266
13	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
14	Serine Phosphorylation	Acute myeloid leukaemia/Acute myelogenous leukemia		U	S62	17192266; 10488335
14	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
15	Serine Phosphorylation	Papillary adenoma		U	S62	10360173; 17192266
15	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
16	Serine Phosphorylation	B-cell lymphoma		U	S62	17192266; 15095297
16	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
17	Serine Phosphorylation	Islet cell carcinoma		U	S62	12015982; 17192266
17	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
18	Serine Phosphorylation	Osteogenic sarcoma/Osteosarcoma		U	S62	12098700; 17192266
18	[Reference]: c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein.
19	Serine Phosphorylation	Chronic myelogenous leukemia/Chronic myeloid leukemia		U	S62	16855632
19	[Reference]: These findings reveal that deregulation of the c-Myc degradation pathway controlled by Serine 62 and Threonine 58 phosphorylation is a novel mechanism for increased expression of a potent oncoprotein known to be involved in hematopoietic malignancies.
20	Tyrosine Phosphorylation	Ovarian cancer/carcinoma		U	Y74	23318434
20	[Reference]: Myc-pY74 constituted a minor fraction of the cellular Myc protein. Thus, our data unravel two potential effects of Abl on Myc: first, Abl signaling can indirectly augment acetylation of Myc by p300, and most likely also its transcriptional activity in the nucleus; second, Abl can directly phosphorylate Myc on tyrosine: the resulting form of Myc appears to be cytoplasmic, and its presence correlates with Abl activation in cancer.
21	Serine Phosphorylation	Prostate cancer/carcinoma/adenocarcinoma	tumor tissue	P	S373	23550155
21	[Reference]: c-Myc phosphorylation by PKCzeta represses prostate tumorigenesis

※ Disease Cross-ref Annotation

Database	Annotation
Cancer Gene Census	Burkitt lymphoma, amplified in other cancers, B-CLL
CTD (Curated) (count: 39) (view all)	MESH:D000230 ; Adenocarcinoma MESH:C538231 ; Adenocarcinoma of lung MESH:D002051 ; Burkitt Lymphoma MESH:D002277 ; Carcinoma MESH:D006528 ; Carcinoma, Hepatocellular MESH:D015266 ; Carcinoma, Merkel Cell MESH:D002294 ; Carcinoma, Squamous Cell MESH:D002312 ; Cardiomyopathy, Hypertrophic MESH:D002471 ; Cell Transformation, Neoplastic MESH:D019457 ; Chromosome Breakage MESH:D002971 ; Cleft Lip MESH:D002972 ; Cleft Palate MESH:D003110 ; Colonic Neoplasms MESH:D018450 ; Disease Progression MESH:D016889 ; Endometrial Neoplasms MESH:D005234 ; Fatty Liver MESH:D005909 ; Glioblastoma MESH:D006394 ; Hemangiosarcoma MESH:D017379 ; Hypertrophy, Left Ventricular MESH:D015470 ; Leukemia, Myeloid, Acute MESH:D008106 ; Liver Cirrhosis, Experimental MESH:D008113 ; Liver Neoplasms MESH:D008114 ; Liver Neoplasms, Experimental MESH:D008175 ; Lung Neoplasms MESH:D008527 ; Medulloblastoma MESH:D009190 ; Myelodysplastic Syndromes MESH:D009362 ; Neoplasm Metastasis MESH:D009369 ; Neoplasms MESH:D009447 ; Neuroblastoma MESH:D017599 ; Neuroectodermal Tumors MESH:D002289 ; Carcinoma, Non-Small-Cell Lung MESH:D012516 ; Osteosarcoma MESH:D010051 ; Ovarian Neoplasms MESH:D010190 ; Pancreatic Neoplasms MESH:D016891 ; Polycystic Kidney, Autosomal Dominant MESH:D011471 ; Prostatic Neoplasms MESH:D013274 ; Stomach Neoplasms MESH:D001749 ; Urinary Bladder Neoplasms MESH:D002583 ; Uterine Cervical Neoplasms
HGMD (count: 2)	CM057723; Breast cancer, increased risk, association with; Missense/nonsense CM010065; Reduced expression?; Missense/nonsense

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 38) (view all)	12 VSFTNRNYDLDYDSV dbPAF 16 NRNYDLDYDSVQPYF dbPAF 161 AARKDSGSPNPARGH dbPAF 202 FPYPLNDSSSPKSCA dbPAF 203 PYPLNDSSSPKSCAS dbPAF 204 YPLNDSSSPKSCASQ dbPAF 22 DYDSVQPYFYCDEEE dbPAF 249 EETPPTTSSDSEEEQ dbPAF 250 ETPPTTSSDSEEEQE dbPAF 252 PPTTSSDSEEEQEDE dbPAF 277 RQAPGKRSESGSPSA dbPAF 279 APGKRSESGSPSAGG dbPAF 281 GKRSESGSPSAGGHS dbPAF 283 RSESGSPSAGGHSKP dbPAF 288 SPSAGGHSKPPHSPL dbPAF 293 GHSKPPHSPLVLKRC dbPAF 32 CDEEENFYQQQQQSE dbPAF 337 VRVLRQISNNRKCTS dbPAF 343 ISNNRKCTSPRSSDT dbPAF 344 SNNRKCTSPRSSDTE dbPAF 347 RKCTSPRSSDTEENV dbPAF 348 KCTSPRSSDTEENVK dbPAF 350 TSPRSSDTEENVKRR dbPAF 358 EENVKRRTHNVLERQ dbPAF 373 RRNELKRSFFALRDQ dbPAF 400 VVILKKATAYILSVQ dbPAF 405 KATAYILSVQAEEQK dbPAF 58 KKFELLPTPPLSPSR dbPAF 6 **MPLNVSFTNRNYD dbPAF 62 LLPTPPLSPSRRSGL dbPAF 64 PTPPLSPSRRSGLCS dbPAF 67 PLSPSRRSGLCSPSY dbPAF 71 SRRSGLCSPSYVAVT dbPAF 73 RSGLCSPSYVAVTPF dbPAF 74 SGLCSPSYVAVTPFS dbPAF 78 SPSYVAVTPFSLRGD dbPAF 8 MPLNVSFTNRNYDLD dbPAF 81 YVAVTPFSLRGDNDG dbPAF
Acetylation (count: 7) (view all)	143 SGFSAAAKLVSEKLA PLMD 148 AAKLVSEKLASYQAA PLMD 157 ASYQAARKDSGSPNP PLMD 275 EKRQAPGKRSESGSP PLMD 317 AAPPSTRKDYPAAKR PLMD 323 RKDYPAAKRVKLDSV PLMD 371 RQRRNELKRSFFALR PLMD
Ubiquitination (count: 12) (view all)	143 SGFSAAAKLVSEKLA PLMD 148 AAKLVSEKLASYQAA PLMD 157 ASYQAARKDSGSPNP PLMD 323 RKDYPAAKRVKLDSV PLMD 326 YPAAKRVKLDSVRVL PLMD 355 SDTEENVKRRTHNVL PLMD 389 PELENNEKAPKVVIL PLMD 398 PKVVILKKATAYILS PLMD 412 SVQAEEQKLISEEDL PLMD 430 RREQLKHKLEQLRNS PLMD 51 APSEDIWKKFELLPT PLMD 52 PSEDIWKKFELLPTP PLMD
Sumoylation (count: 13) (view all)	148 AAKLVSEKLASYQAA PLMD 157 ASYQAARKDSGSPNP PLMD 298 PHSPLVLKRCHVSTH PLMD 317 AAPPSTRKDYPAAKR PLMD 323 RKDYPAAKRVKLDSV PLMD 326 YPAAKRVKLDSVRVL PLMD 355 SDTEENVKRRTHNVL PLMD 389 PELENNEKAPKVVIL PLMD 392 ENNEKAPKVVILKKA PLMD 398 PKVVILKKATAYILS PLMD 412 SVQAEEQKLISEEDL PLMD 430 RREQLKHKLEQLRNS PLMD 52 PSEDIWKKFELLPTP PLMD

※ Protein-Protein Interaction

Network

Interaction

Source

O15169	P01106	MINT
P01106	P04049	HPRD
P01106	P06400	HPRD
P01106	P06493	HPRD
P01106	P08047	HPRD
P01106	P10415	HPRD
P01106	P27361	HPRD
P01106	P28749	HPRD
P01106	P29590	HPRD
P01106	P38398	DIP
P01106	P40692	HPRD
P01106	P45983	HPRD
P01106	P49715	HPRD
P01106	P49841	DIP
P01106	P62988	DIP
P01106	P67775	MINT
P01106	Q02750	HPRD
P01106	Q04206	HPRD
P01106	Q06830	HPRD
P01106	Q13526	MINT
P01106	Q15796	HPRD
P01106	Q8N726	HPRD
P01106	Q9UQ07	HPRD
P01106	Q9Y230	DIP

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites

※ Protein-Protein Interaction