dbPTM

CASL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASL_MOUSE
UniProt AC	O35177
Protein Name	Enhancer of filamentation 1
Gene Name	Nedd9
Organism	Mus musculus (Mouse).
Sequence Length	833
Subcellular Localization	Cytoplasm, cell cortex. Nucleus. Cytoplasm, cytoskeleton. Localizes to both the cell nucleus and the cell periphery..
Protein Description	Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May function in transmitting growth control signals between focal adhesions at the cell periphery and the mitotic spindle in response to adhesion or growth factor signals initiating cell proliferation. May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRK, NCK and SHPTP2 to the tyrosine phosphorylated form (By similarity)..
Protein Sequence	MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPVQETPGHEQPTPGPMHQTFGQQKLYQVPNSQAASRDTIYQVPPSYQNQGIYQVPTGHGTPEQDVYQVPPSVQRNIGGTNGPLLSKKVITPVRTGHGYVYEYPSRYQKDVYDVPPSHSTQGVYDIPPSSVKGPVFSVPVGEIKPQGVYDIPPTQGVYAIPPSACRDEAGLREKEYDFPPPMKQDGKPDTRPEGVYDIPPTSTKTAGKDLHIKFPCDAPGGVEPMARRHQSFSLHHAPSQLGQSGDTQSDAYDVPRGVQFLEVPTETSEKANPEERDGVYDVPLHNPADAKGSRDVVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPSQDKRLRLDPDTAIEKLYRLQQTLEMGVCSLMSLVTTDWRCYGYMERHINEIRTAVDKVELFLREYLHFAKGALANASCLPELVLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTISTYAETLFRADPANSHLKNGPNSIMNSSEYTHPGSQMQPLHPGDYKAQVHSKPLPPSLSKDQPPDCGSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQSKAQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNNSVGAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDIRNKVRNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	NLMARALYDNVPECA HHHHHHHHHCCHHHH	12.41	-
91	Phosphorylation	TFGQQKLYQVPNSQA CCCCEEEEECCCCCC	17.94	12522270
96	Phosphorylation	KLYQVPNSQAASRDT EEEECCCCCCCCCCC	18.35	-
105	Phosphorylation	AASRDTIYQVPPSYQ CCCCCCCEECCHHHC	12.92	22817900
117	Phosphorylation	SYQNQGIYQVPTGHG HHCCCCEEECCCCCC	15.41	-
131	Phosphorylation	GTPEQDVYQVPPSVQ CCCHHHCCCCCHHHC	16.45	-
163	Phosphorylation	PVRTGHGYVYEYPSR CCCCCCCEEEECCCC	8.32	22499769
165	Phosphorylation	RTGHGYVYEYPSRYQ CCCCCEEEECCCCCC	10.97	22499769
167	Phosphorylation	GHGYVYEYPSRYQKD CCCEEEECCCCCCCC	6.71	22499769
169	Phosphorylation	GYVYEYPSRYQKDVY CEEEECCCCCCCCCC	42.59	22499769
176	Phosphorylation	SRYQKDVYDVPPSHS CCCCCCCCCCCCCCC	22.74	12522270
181	Phosphorylation	DVYDVPPSHSTQGVY CCCCCCCCCCCCCEE	24.81	-
183	Phosphorylation	YDVPPSHSTQGVYDI CCCCCCCCCCCEEEC	27.11	-
188	Phosphorylation	SHSTQGVYDIPPSSV CCCCCCEEECCHHHC	18.25	12522270
194	Phosphorylation	VYDIPPSSVKGPVFS EEECCHHHCCCCEEE	33.35	22817900
240	Phosphorylation	AGLREKEYDFPPPMK CCCCCCCCCCCCCCC	33.67	22817900
254	Phosphorylation	KQDGKPDTRPEGVYD CCCCCCCCCCCCCCC	57.56	26026062
260	Phosphorylation	DTRPEGVYDIPPTST CCCCCCCCCCCCCCC	21.00	22817900
295	Phosphorylation	PMARRHQSFSLHHAP CCHHHCCCEECCCCC	15.63	22499769
297	Phosphorylation	ARRHQSFSLHHAPSQ HHHCCCEECCCCCHH	31.85	22499769
303	Phosphorylation	FSLHHAPSQLGQSGD EECCCCCHHCCCCCC	38.53	22499769
308	Phosphorylation	APSQLGQSGDTQSDA CCHHCCCCCCCCCCC	36.52	22499769
311	Phosphorylation	QLGQSGDTQSDAYDV HCCCCCCCCCCCCCC	33.23	22499769
313	Phosphorylation	GQSGDTQSDAYDVPR CCCCCCCCCCCCCCC	26.71	22499769
316	Phosphorylation	GDTQSDAYDVPRGVQ CCCCCCCCCCCCCCE	23.59	20116462
329	Phosphorylation	VQFLEVPTETSEKAN CEEEECCCCCCCCCC	58.01	29895711
344	Phosphorylation	PEERDGVYDVPLHNP HHHCCCCCCCCCCCC	19.42	25521595
368	Phosphorylation	VDGINRLSFSSTGST CCCCCEEEECCCCCC	21.61	27566939
371	Phosphorylation	INRLSFSSTGSTRSN CCEEEECCCCCCCCC	34.47	25338131
380	Phosphorylation	GSTRSNMSTSSTSSK CCCCCCCCCCCCCCC	29.41	29895711
382	Phosphorylation	TRSNMSTSSTSSKES CCCCCCCCCCCCCCC	25.06	29895711
383	Phosphorylation	RSNMSTSSTSSKESS CCCCCCCCCCCCCCC	32.18	29895711
384	Phosphorylation	SNMSTSSTSSKESSL CCCCCCCCCCCCCCC	36.47	29895711
385	Phosphorylation	NMSTSSTSSKESSLS CCCCCCCCCCCCCCC	41.16	29895711
386	Phosphorylation	MSTSSTSSKESSLSA CCCCCCCCCCCCCCC	40.30	29895711
390	Phosphorylation	STSSKESSLSASPSQ CCCCCCCCCCCCCCC	27.69	28285833
394	Phosphorylation	KESSLSASPSQDKRL CCCCCCCCCCCCCCC	23.00	28285833
418	Phosphorylation	KLYRLQQTLEMGVCS HHHHHHHHHHHHHHH	16.24	24719451
628	Phosphorylation	ERSWMDDYDYVHLQG CCCCCCCCCEEECCC	12.62	22817900
630	Phosphorylation	SWMDDYDYVHLQGKE CCCCCCCEEECCCHH	5.41	22817900
691	Phosphorylation	SKWKPSQSLPTTNNS HHCCCCCCCCCCCCC	40.42	25266776

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
368	S	Phosphorylation		-
Phosphorylation at Ser-368 induces proteasomal degradation (By similarity).

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 CASL_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CRK_MOUSE	Crk	physical	20697350
MY18A_MOUSE	Myo18a	physical	20697350
RACK1_MOUSE	Gnb2l1	physical	20697350
SRC8_MOUSE	Cttn	physical	24574519
AURKA_MOUSE	Aurka	physical	24574519

Drug and Disease Associations

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

Regulatory Network of CASL_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91; TYR-176 AND TYR-188,AND MASS SPECTROMETRY.	12522270 [Abstract]

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