FYN_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FYN_RAT
• UniProt AC: Q62844
• Protein Name: Tyrosine-protein kinase Fyn
• Gene Name: Fyn {ECO:0000312|RGD:2641}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 537
• Subcellular Localization: Cell membrane. Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking (By similarity)..
• Protein Description: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1 (By similarity). Interacts with UNC119 (By similarity)..
• Protein Sequence: MGCVQCKDKEAAKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL

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
2	Myristoylation	------MGCVQCKDK ------CCCEECCCH	21.94	-
3	S-palmitoylation	-----MGCVQCKDKE -----CCCEECCCHH	1.52	-
6	S-palmitoylation	--MGCVQCKDKEAAK --CCCEECCCHHHHH	2.84	-
15	Phosphorylation	DKEAAKLTEERDGSL CHHHHHCCHHCCCCC	34.78	25575281
21	Phosphorylation	LTEERDGSLNQSSGY CCHHCCCCCCCCCCC	28.56	27097102
25	Phosphorylation	RDGSLNQSSGYRYGT CCCCCCCCCCCCCCC	25.34	27097102
26	Phosphorylation	DGSLNQSSGYRYGTD CCCCCCCCCCCCCCC	30.04	27097102
28	Phosphorylation	SLNQSSGYRYGTDPT CCCCCCCCCCCCCCC	11.56	27097102
114	Phosphorylation	EKFQILNSSEGDWWE CCEEEEECCCCCEEE	26.73	23800682
115	Phosphorylation	KFQILNSSEGDWWEA CEEEEECCCCCEEEE	44.52	23800682
150	Phosphorylation	SIQAEEWYFGKLGRK CCCCHHHHCCCCCCH	13.01	-
185	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEEEH	20.86	22673903
186	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEEEHH	18.33	22673903
213	Phosphorylation	RKLDNGGYYITTRAQ EECCCCCEEEEEHHH	7.97	27097102
214	Phosphorylation	KLDNGGYYITTRAQF ECCCCCEEEEEHHHH	8.61	27097102
216	Phosphorylation	DNGGYYITTRAQFET CCCCEEEEEHHHHHH	8.29	28689409
217	Phosphorylation	NGGYYITTRAQFETL CCCEEEEEHHHHHHH	17.91	25575281
420	Phosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	23712012
421	Phosphorylation	LIEDNEYTARQGAKF HHCCCCCCCCCCCCC	14.80	27097102
427	Acetylation	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	22902405
440	Phosphorylation	TAPEAALYGRFTIKS CCCCHHHHCCEEECC	11.09	27097102
531	Phosphorylation	FTATEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	19625508

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

Oops, there are no upstream regulatory protein records of FYN_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	C	Palmitoylation	Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.	-
6	C	Palmitoylation	Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	14531861
BCAR1_RAT	Bcar1	physical	11181827

Drug and Disease Associations

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