MYC_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MYC_RAT
• UniProt AC: P09416
• Protein Name: Myc proto-oncogene protein
• Gene Name: Myc
• Organism: Rattus norvegicus (Rat).
• 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. [PubMed: 17304222 Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (By similarity]
• Protein Sequence: MPLNVSFANRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSSSSDSLLSSESSPRATPEPLVLHEETPPTTSSDSEEEQDDEEEIDVVSVEKRQPPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQADEHKLISEKDLLRKRREQLKHKLEQLRNSGA

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
6	Phosphorylation	--MPLNVSFANRNYD --CCCCCEECCCCCC	19.98	-
58	Phosphorylation	KKFELLPTPPLSPSR HHHHCCCCCCCCCCC	37.19	27097102
58	O-linked_Glycosylation	KKFELLPTPPLSPSR HHHHCCCCCCCCCCC	37.19	-
62	Phosphorylation	LLPTPPLSPSRRSGL CCCCCCCCCCCCCCC	26.97	27097102
64	Phosphorylation	PTPPLSPSRRSGLCS CCCCCCCCCCCCCCC	36.63	27097102
71	Phosphorylation	SRRSGLCSPSYVAVA CCCCCCCCCCEEEEE	23.17	-
144	Acetylation	SGFSAAAKLVSEKLA CCHHHHHHHHHHHHH	44.70	-
149	Acetylation	AAKLVSEKLASYQAA HHHHHHHHHHHHHHH	41.67	25786129
158	Acetylation	ASYQAARKDSTSLSP HHHHHHHCCCCCCCC	51.83	-
160	Phosphorylation	YQAARKDSTSLSPAR HHHHHCCCCCCCCCC	23.96	26022182
161	Phosphorylation	QAARKDSTSLSPARG HHHHCCCCCCCCCCC	43.77	30181290
162	Phosphorylation	AARKDSTSLSPARGH HHHCCCCCCCCCCCC	30.70	30181290
164	Phosphorylation	RKDSTSLSPARGHSV HCCCCCCCCCCCCCC	19.11	30181290
210	Phosphorylation	SSSPKSCTSSDSTAF CCCCCCCCCCCCCCC	38.05	28689409
214	Phosphorylation	KSCTSSDSTAFSSSS CCCCCCCCCCCCCCC	24.47	28689409
221	Phosphorylation	STAFSSSSDSLLSSE CCCCCCCCCCCCCCC	32.92	28689409
230	Phosphorylation	SLLSSESSPRATPEP CCCCCCCCCCCCCCC	17.85	28689409
247	Phosphorylation	LHEETPPTTSSDSEE ECCCCCCCCCCCCHH	40.28	28689409
248	Phosphorylation	HEETPPTTSSDSEEE CCCCCCCCCCCCHHH	31.82	28689409
249	Phosphorylation	EETPPTTSSDSEEEQ CCCCCCCCCCCHHHC	34.33	28689409
250	Phosphorylation	ETPPTTSSDSEEEQD CCCCCCCCCCHHHCC	42.96	28689409
252	Phosphorylation	PPTTSSDSEEEQDDE CCCCCCCCHHHCCCH	49.18	28689409
275	Acetylation	EKRQPPAKRSESGSS EECCCCCCCCCCCCC	63.33	-
293	Phosphorylation	GHSKPPHSPLVLKRC CCCCCCCCCCEEEEC	26.21	27097102
317	Acetylation	AAPPSTRKDYPAAKR CCCCCCCCCCCHHHH	62.80	-
323	Acetylation	RKDYPAAKRAKLDSG CCCCCHHHHCCCCCC	55.80	-
329	Phosphorylation	AKRAKLDSGRVLKQI HHHCCCCCCCHHHHH	38.65	-
371	Acetylation	RQRRNELKRSFFALR HHHHHHHHHHHHHHH	39.56	-

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	GSK3	-	Uniprot
62	S	Phosphorylation	Kinase	CDK2	Q63699	Uniprot
62	S	Phosphorylation	Kinase	DYRK2	-	Uniprot
62	S	Phosphorylation	Kinase	GSK3	-	Uniprot
329	S	Phosphorylation	Kinase	PIM2	-	Uniprot

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

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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