MYC_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYC_MOUSE
• UniProt AC: P01108
• Protein Name: Myc proto-oncogene protein
• Gene Name: Myc
• Organism: Mus musculus (Mouse).
• 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..
• Protein Sequence: MPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPLNVNFTNRNYDLD CCCEEECCCCCCCCC	28.23	-
58	Phosphorylation	KKFELLPTPPLSPSR HHHHCCCCCCCCCCC	37.19	17052453
58	O-linked_Glycosylation	KKFELLPTPPLSPSR HHHHCCCCCCCCCCC	37.19	27482104
62	Phosphorylation	LLPTPPLSPSRRSGL CCCCCCCCCCCCCCC	26.97	17283176
64	Phosphorylation	PTPPLSPSRRSGLCS CCCCCCCCCCCCCCC	36.63	28725479
67	Phosphorylation	PLSPSRRSGLCSPSY CCCCCCCCCCCCHHE	34.70	25619855
71	Phosphorylation	SRRSGLCSPSYVAVA CCCCCCCCHHEEEEE	23.17	25619855
73	Phosphorylation	RSGLCSPSYVAVATS CCCCCCHHEEEEEEE	18.88	25619855
74	Phosphorylation	SGLCSPSYVAVATSF CCCCCHHEEEEEEEC	8.87	25619855
79	Phosphorylation	PSYVAVATSFSPRED HHEEEEEEECCCCCC	24.57	25619855
80	Phosphorylation	SYVAVATSFSPREDD HEEEEEEECCCCCCC	17.62	25619855
82	Phosphorylation	VAVATSFSPREDDDG EEEEEECCCCCCCCC	23.86	25619855
137	Phosphorylation	IIQDCMWSGFSAAAK HHHHHCCCCHHHHHH	11.77	22817900
140	Phosphorylation	DCMWSGFSAAAKLVS HHCCCCHHHHHHHHH	22.11	22817900
144	Acetylation	SGFSAAAKLVSEKLA CCHHHHHHHHHHHHH	44.70	-
149	Ubiquitination	AAKLVSEKLASYQAA HHHHHHHHHHHHHHH	41.67	-
149	Acetylation	AAKLVSEKLASYQAA HHHHHHHHHHHHHHH	41.67	23806337
158	Acetylation	ASYQAARKDSTSLSP HHHHHHHCCCCCCCC	51.83	-
160	Phosphorylation	YQAARKDSTSLSPAR HHHHHCCCCCCCCCC	23.96	25266776
161	Phosphorylation	QAARKDSTSLSPARG HHHHCCCCCCCCCCC	43.77	28066266
162	Phosphorylation	AARKDSTSLSPARGH HHHCCCCCCCCCCCC	30.70	28066266
164	Phosphorylation	RKDSTSLSPARGHSV HCCCCCCCCCCCCCC	19.11	24453211
275	Acetylation	EKRQTPAKRSESGSS EECCCCCCCCCCCCC	58.63	-
279	Phosphorylation	TPAKRSESGSSPSRG CCCCCCCCCCCCCCC	45.26	25338131
282	Phosphorylation	KRSESGSSPSRGHSK CCCCCCCCCCCCCCC	30.35	25338131
288	Phosphorylation	SSPSRGHSKPPHSPL CCCCCCCCCCCCCCC	50.08	25266776
293	Phosphorylation	GHSKPPHSPLVLKRC CCCCCCCCCCEEEEC	26.21	28507225
317	Acetylation	AAPPSTRKDYPAAKR CCCCCCCCCCCHHHH	62.80	-
323	Acetylation	RKDYPAAKRAKLDSG CCCCCHHHHCCCCCC	55.80	15572685
329	Phosphorylation	AKRAKLDSGRVLKQI HHHCCCCCCCHHHHH	38.65	18438430
344	Phosphorylation	SNNRKCSSPRSSDTE HCCCCCCCCCCCCCC	33.53	23375375
347	Phosphorylation	RKCSSPRSSDTEEND CCCCCCCCCCCCHHH	35.63	23375375
358	Phosphorylation	EENDKRRTHNVLERQ CHHHHHHHHHHHHHH	23.10	20043278
371	Acetylation	RQRRNELKRSFFALR HHHHHHHHHHHHHHH	39.56	-
373	Phosphorylation	RRNELKRSFFALRDQ HHHHHHHHHHHHHHH	24.11	20043278
400	Phosphorylation	VVILKKATAYILSIQ EEEEECCEEEEHHEE	28.95	20043278
417	Acetylation	EHKLTSEKDLLRKRR HHCCCCHHHHHHHHH	54.14	15572685

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
58	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
58	T	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
58	T	Phosphorylation	Kinase	GSK3	-	Uniprot
62	S	Phosphorylation	Kinase	CDK2	P97377	Uniprot
62	S	Phosphorylation	Kinase	DYRK2	Q5U4C9	Uniprot
62	S	Phosphorylation	Kinase	GSK3	-	Uniprot
329	S	Phosphorylation	Kinase	PIM1	P11309	PSP
329	S	Phosphorylation	Kinase	PIM2	Q9P1W9	PSP
329	S	Phosphorylation	Kinase	PIM2	Q62070	Uniprot
358	T	Phosphorylation	Kinase	PAK2	Q8CIN4	PSP
373	S	Phosphorylation	Kinase	PAK2	Q8CIN4	PSP
400	T	Phosphorylation	Kinase	PAK2	Q8CIN4	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxw7	Q8VBV4	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Skp2	Q9Z0Z3	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Trim32	Q8CH72	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Spop	Q6ZWS8	PMID:28414305

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
58	T	Phosphorylation	Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58.	22328504
58	T	Phosphorylation	Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome.	22328504
58	T	Phosphorylation	Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome.	22328504
58	T	ubiquitylation	Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome.	22328504
58	T	ubiquitylation	Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome.	22328504
62	S	Phosphorylation	Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58.	22328504
62	S	Phosphorylation	Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence (By similarity).	22328504
62	S	Phosphorylation	Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome.	22328504
62	S	Phosphorylation	Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome.	22328504
62	S	ubiquitylation	Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome.	22328504
62	S	ubiquitylation	Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome.	22328504
329	S	Phosphorylation	Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC.	18438430

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MYC_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT2A_HUMAN	KAT2A	physical	10611234
TRRAP_HUMAN	TRRAP	physical	9708738
TRI32_MOUSE	Trim32	physical	19269368
SMCA4_MOUSE	Smarca4	physical	20305087
PRDX1_HUMAN	PRDX1	physical	12196529
CDR2_MOUSE	Cdr2	physical	10465786
CDN2A_MOUSE	Cdkn2a	physical	15361884
ARF_MOUSE	Cdkn2a	physical	15361884

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Pim kinase-dependent inhibition of c-Myc degradation.";
Zhang Y., Wang Z., Li X., Magnuson N.S.;
Oncogene 27:4809-4819(2008).
Cited for: PHOSPHORYLATION AT SER-329, MUTAGENESIS OF SER-329, AND INTERACTIONWITH PIM2.
PubMed: 18438430