FER_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FER_MOUSE
• UniProt AC: P70451
• Protein Name: Tyrosine-protein kinase Fer
• Gene Name: Fer
• Organism: Mus musculus (Mouse).
• Sequence Length: 823
• Subcellular Localization: Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Detected on microtubules in po
• Protein Description: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity..
• Protein Sequence: MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKESTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDDYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQQMLLHKEAAVLELEKRIEESFETCEKKSDIVLLLGQKQALEELKQSVQQLRCTEAKCAAQKALLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIKSPKSVLGSSTQVCDVISVGERPLAEHDWYHGAIPRIEAQELLKQQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQFVDNLYRFEGTGFSNIPQLIDHHFNTKQVITKKSGVVLLNPIPKDKKWVLNHEDVSLGELLGKGNFGEVYKGTLKDKTPVAIKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVPGGDFLTFLRKRKDELKLKQLVRFSLDVAAGMLYLESKNCIHRDLAARNCLVGENNTLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQNCPEEVFTIMMKCWDYKPENRPKFNDLHKELTVIKKMIT

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
63	Phosphorylation	ESTVQVNYVSNVSKS CCCEEEEEEECCCHH	13.34	29514104
65 (in isoform 4)	Phosphorylation	-	22.58	29514104
70	Phosphorylation	YVSNVSKSWLLMIQQ EEECCCHHHHHHHHH	18.56	22802335
78	Phosphorylation	WLLMIQQTEQLSRIM HHHHHHHHHHHHHHH	14.88	22802335
82	Phosphorylation	IQQTEQLSRIMKTHA HHHHHHHHHHHHHCH	21.32	22802335
135	Malonylation	VTKTELEKLKSSYRQ CCHHHHHHHHHHHHH	74.06	26073543
166	Acetylation	AKGKETEKAKERYDK HHCCHHHHHHHHHHH	72.65	6570121
200	Phosphorylation	QLHQSQYYDTTLPLL CCCHHHCCCCHHHHH	10.12	29514104
340	Phosphorylation	LEKRIEESFETCEKK HHHHHHHHHHHHCCH	18.65	29550500
343	Phosphorylation	RIEESFETCEKKSDI HHHHHHHHHCCHHHH	24.77	29550500
402	Phosphorylation	EPPPVVNYEEDARSV CCCCCCCHHHCCCCC	14.75	26824392
408	Phosphorylation	NYEEDARSVTSMERK CHHHCCCCCCCHHHH	31.31	29899451
410	Phosphorylation	EEDARSVTSMERKER HHCCCCCCCHHHHHH	24.49	19060867
411	Phosphorylation	EDARSVTSMERKERL HCCCCCCCHHHHHHH	19.25	23684622
419	Phosphorylation	MERKERLSKFESIRH HHHHHHHHHHHHHHH	41.33	21454597
423	Phosphorylation	ERLSKFESIRHSIAG HHHHHHHHHHHHHHH	28.23	26824392
427	Phosphorylation	KFESIRHSIAGIIKS HHHHHHHHHHHHHCC	12.32	26824392
434	Phosphorylation	SIAGIIKSPKSVLGS HHHHHHCCCCHHCCC	27.44	28507225
434 (in isoform 5)	Phosphorylation	-	27.44	29514104
493	Phosphorylation	SHGKPGEYVLSVYSD CCCCCCEEEEEEEEC	16.77	29514104
498	Phosphorylation	GEYVLSVYSDGQRRH CEEEEEEEECCCEEE	9.54	29514104
579	Phosphorylation	KGNFGEVYKGTLKDK CCCCCCEECCCCCCC	10.21	29514104
587	Phosphorylation	KGTLKDKTPVAIKTC CCCCCCCCCEEEEEC	32.88	24719451
616	Phosphorylation	EAKILKQYDHPNIVK HHHHHHHCCCCCHHH	18.03	19159681
715	Phosphorylation	RQEDGGVYSSSGLKQ CCCCCCEECCCCCCC	13.20	19159681
716	Phosphorylation	QEDGGVYSSSGLKQI CCCCCEECCCCCCCC	18.67	25619855
717	Phosphorylation	EDGGVYSSSGLKQIP CCCCEECCCCCCCCC	15.67	25619855
718	Phosphorylation	DGGVYSSSGLKQIPI CCCEECCCCCCCCCC	42.05	25619855
735	Phosphorylation	TAPEALNYGRYSSES ECCCHHCCCCCCCHH	12.11	29514104

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
715	Y	Phosphorylation	Kinase	FER	P70451	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FER_MOUSE !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT3_MOUSE	Stat3	physical	12738762

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND MASSSPECTROMETRY.
PubMed: 19131326

"Hsp90 and a tyrosine embedded in the Hsp90 recognition loop arerequired for the Fer tyrosine kinase activity.";
Hikri E., Shpungin S., Nir U.;
Cell. Signal. 21:588-596(2009).
Cited for: FUNCTION IN STAT3 PHOSPHORYLATION, INTERACTION WITH HSP90,AUTOPHOSPHORYLATION AT TYR-616, MUTAGENESIS OF TYR-616,UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
PubMed: 19159681

"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND MASSSPECTROMETRY.
PubMed: 17947660