dbPTM

EFS_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EFS_MOUSE
UniProt AC	Q64355
Protein Name	Embryonal Fyn-associated substrate
Gene Name	Efs
Organism	Mus musculus (Mouse).
Sequence Length	560
Subcellular Localization
Protein Description	Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES..
Protein Sequence	MAIATSAQLARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPANRVKLLPAGPAPKPSLCPASPTQPGSSCPTPERGCEEQEVYVIPPPARPCSASGLPARSCSPSSDSIYKVPRGNGMQLTASRDVAEVYDVPPNILRAPSSCPYDSPASFSCPVAPVVPQPPREDEAPYDVPLALKPPAELERDPEWEGGREPGPPLYAAPSNLKRASALLNLYEAPEELLANGESRDADEGIYDVPLLGPEPPSPEPPVASSSTDLDTVAQLPTRSSPPQHRPRLPSTESLSRRPLPALPVSEAPAPSPAPSPAPGRKGSIQDRPLPPPPPCLPGYGGLKPEGDPECREVANDPAGPHNEYEGIPMAEEYDYVHLKGVDTAQGSRPLDKAFPVDPELLERGLAERKEALSPEEPLVLSTGDLQLLHFYAGQCQSHYSALQAAVAALVASTQANQPPCLFVPHGKRVVVAAHRLVFVGDTLGRLAASAALRAQVGAAGTMLAQTLRATVLAVKGAALGYPSDTAVQEMARCVAELAGQALRFTTLLDGLLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	LYDNTAESPQELSFR HHHCCCCCCHHHCCC	29.44	-
119	Phosphorylation	ASGLPARSCSPSSDS CCCCCCCCCCCCCCC	22.51	26643407
121	Phosphorylation	GLPARSCSPSSDSIY CCCCCCCCCCCCCCE	29.12	25521595
123	Phosphorylation	PARSCSPSSDSIYKV CCCCCCCCCCCCEEC	30.40	26643407
124	Phosphorylation	ARSCSPSSDSIYKVP CCCCCCCCCCCEECC	38.47	22871156
128	Phosphorylation	SPSSDSIYKVPRGNG CCCCCCCEECCCCCC	15.19	-
227	Phosphorylation	PSNLKRASALLNLYE CCCHHHHHHHHHHHH	24.39	27180971
233	Phosphorylation	ASALLNLYEAPEELL HHHHHHHHHCCHHHH	14.68	21183079
253	Phosphorylation	RDADEGIYDVPLLGP CCCCCCCCCCCCCCC	23.03	8647432
297	Phosphorylation	QHRPRLPSTESLSRR CCCCCCCCCCCCCCC	49.77	27180971
298	Phosphorylation	HRPRLPSTESLSRRP CCCCCCCCCCCCCCC	27.88	26643407
300	Phosphorylation	PRLPSTESLSRRPLP CCCCCCCCCCCCCCC	31.56	22817900
318	Phosphorylation	VSEAPAPSPAPSPAP CCCCCCCCCCCCCCC	35.48	-
322	Phosphorylation	PAPSPAPSPAPGRKG CCCCCCCCCCCCCCC	35.48	-
508	Phosphorylation	AQVGAAGTMLAQTLR HHHHHHHHHHHHHHH	12.32	24719451

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
253	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
253	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EFS_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EFS_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAK1_MOUSE	Ptk2	physical	9750131
FAK2_RAT	Ptk2b	physical	9750131
FYN_HUMAN	FYN	physical	9750131

Drug and Disease Associations

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

Regulatory Network of EFS_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Coordinate activation of c-Src by SH3- and SH2-binding sites on anovel p130Cas-related protein, Sin."; Alexandropoulos K., Baltimore D.; Genes Dev. 10:1341-1355(1996). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT TYR-253, ANDMUTAGENESIS OF TYR-253.	8647432 [Abstract]