dbPTM

CASL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CASL_HUMAN
UniProt AC	Q14511
Protein Name	Enhancer of filamentation 1
Gene Name	NEDD9
Organism	Homo sapiens (Human).
Sequence Length	834
Subcellular Localization	Cytoplasm, cell cortex. Nucleus. Golgi apparatus. Cell projection, lamellipodium. Cytoplasm. Cell junction, focal adhesion. Localizes to both the cell nucleus and the cell periphery and is differently localized in fibroblasts and epithelial cells. In
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..
Protein Sequence	MKYKNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPMQETASSHEQPASGLMQQTFGQQKLYQVPNPQAAPRDTIYQVPPSYQNQGIYQVPTGHGTQEQEVYQVPPSVQRSIGGTSGPHVGKKVITPVRTGHGYVYEYPSRYQKDVYDIPPSHTTQGVYDIPPSSAKGPVFSVPVGEIKPQGVYDIPPTKGVYAIPPSACRDEAGLREKDYDFPPPMRQAGRPDLRPEGVYDIPPTCTKPAGKDLHVKYNCDIPGAAEPVARRHQSLSPNHPPPQLGQSVGSQNDAYDVPRGVQFLEPPAETSEKANPQERDGVYDVPLHNPPDAKGSRDLVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPAQDKRLFLDPDTAIERLQRLQQALEMGVSSLMALVTTDWRCYGYMERHINEIRTAVDKVELFLKEYLHFVKGAVANAACLPELILHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSLHLKNGPESIMNSTEYPHGGSQGQLLHPGDHKAQAHNKALPPGLSKEQAPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQNKMQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSGVSAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTAQDIRNKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	NLMARALYDNVPECA HHHHHHHHHCCHHHH	12.41	14729942
92	Phosphorylation	TFGQQKLYQVPNPQA HHCCCEEECCCCCCC	17.94	29255136
104	Phosphorylation	PQAAPRDTIYQVPPS CCCCCCCCCEECCHH	23.90	27259358
106	Phosphorylation	AAPRDTIYQVPPSYQ CCCCCCCEECCHHHC	12.92	27259358
111	Phosphorylation	TIYQVPPSYQNQGIY CCEECCHHHCCCCEE	33.03	26356563
112	Phosphorylation	IYQVPPSYQNQGIYQ CEECCHHHCCCCEEE	19.77	26356563
118	Phosphorylation	SYQNQGIYQVPTGHG HHCCCCEEECCCCCC	15.41	26356563
122	Phosphorylation	QGIYQVPTGHGTQEQ CCEEECCCCCCCCCE	42.84	26356563
126	Phosphorylation	QVPTGHGTQEQEVYQ ECCCCCCCCCEEEEE	24.21	26356563
132	Phosphorylation	GTQEQEVYQVPPSVQ CCCCEEEEECCHHHC	11.75	27259358
137	Phosphorylation	EVYQVPPSVQRSIGG EEEECCHHHCCCCCC	25.47	25348954
160	Phosphorylation	KVITPVRTGHGYVYE EEEECCCCCCCEEEE	33.49	21945579
164	Phosphorylation	PVRTGHGYVYEYPSR CCCCCCCEEEECCCC	8.32	21945579
166	Phosphorylation	RTGHGYVYEYPSRYQ CCCCCEEEECCCCCC	10.97	21945579
168	Phosphorylation	GHGYVYEYPSRYQKD CCCEEEECCCCCCCC	6.71	21945579
170	Phosphorylation	GYVYEYPSRYQKDVY CEEEECCCCCCCCCC	42.59	21945579
172	Phosphorylation	VYEYPSRYQKDVYDI EEECCCCCCCCCCCC	25.01	26356563
177	Phosphorylation	SRYQKDVYDIPPSHT CCCCCCCCCCCCCCC	20.49	21082442
182	Phosphorylation	DVYDIPPSHTTQGVY CCCCCCCCCCCCEEE	28.28	27259358
184	Phosphorylation	YDIPPSHTTQGVYDI CCCCCCCCCCEEEEC	25.75	26356563
185	Phosphorylation	DIPPSHTTQGVYDIP CCCCCCCCCEEEECC	20.22	26356563
189	Phosphorylation	SHTTQGVYDIPPSSA CCCCCEEEECCCHHC	18.25	21082442
194	Phosphorylation	GVYDIPPSSAKGPVF EEEECCCHHCCCCEE	37.26	26330541
195	Phosphorylation	VYDIPPSSAKGPVFS EEECCCHHCCCCEEE	39.51	26330541
202	Phosphorylation	SAKGPVFSVPVGEIK HCCCCEEEEECCCCC	26.24	21945579
214	Phosphorylation	EIKPQGVYDIPPTKG CCCCCCEEECCCCCC	18.25	21945579
219	Phosphorylation	GVYDIPPTKGVYAIP CEEECCCCCCEEECC	34.77	21945579
223	Phosphorylation	IPPTKGVYAIPPSAC CCCCCCEEECCHHHC	13.90	19534553
228	Phosphorylation	GVYAIPPSACRDEAG CEEECCHHHCCCCCC	34.35	-
241	Phosphorylation	AGLREKDYDFPPPMR CCCCCCCCCCCCCCH	30.47	21082442
261	Phosphorylation	DLRPEGVYDIPPTCT CCCCCCCCCCCCCCC	21.00	22461510
266	Phosphorylation	GVYDIPPTCTKPAGK CCCCCCCCCCCCCCC	27.70	26330541
268	Phosphorylation	YDIPPTCTKPAGKDL CCCCCCCCCCCCCCC	42.41	26330541
296	Phosphorylation	PVARRHQSLSPNHPP HHHHHCCCCCCCCCC	25.37	19539609
298	Phosphorylation	ARRHQSLSPNHPPPQ HHHCCCCCCCCCCCC	28.98	26356563
309	Phosphorylation	PPPQLGQSVGSQNDA CCCCCCCCCCCCCCC	27.01	26356563
312	Phosphorylation	QLGQSVGSQNDAYDV CCCCCCCCCCCCCCC	24.53	29255136
317	Phosphorylation	VGSQNDAYDVPRGVQ CCCCCCCCCCCCCCE	21.97	29255136
332	Phosphorylation	FLEPPAETSEKANPQ ECCCCCCCCCCCCCC	44.27	26330541
333	Phosphorylation	LEPPAETSEKANPQE CCCCCCCCCCCCCCC	28.71	26330541
345	Phosphorylation	PQERDGVYDVPLHNP CCCCCCCCCCCCCCC	19.42	30266825
369	Phosphorylation	VDGINRLSFSSTGST CCCCCCEEECCCCCC	21.61	28348404
371	Phosphorylation	GINRLSFSSTGSTRS CCCCEEECCCCCCCC	24.50	28450419
372	Phosphorylation	INRLSFSSTGSTRSN CCCEEECCCCCCCCC	34.47	25849741
373	Phosphorylation	NRLSFSSTGSTRSNM CCEEECCCCCCCCCC	33.67	28857561
375	Phosphorylation	LSFSSTGSTRSNMST EEECCCCCCCCCCCC	22.27	25849741
376	Phosphorylation	SFSSTGSTRSNMSTS EECCCCCCCCCCCCC	39.19	22210691
385	Phosphorylation	SNMSTSSTSSKESSL CCCCCCCCCCCCCCC	36.47	30576142
388	Ubiquitination	STSSTSSKESSLSAS CCCCCCCCCCCCCCC	62.47	21906983
393	Phosphorylation	SSKESSLSASPAQDK CCCCCCCCCCHHHCC	28.75	25849741
395	Phosphorylation	KESSLSASPAQDKRL CCCCCCCCHHHCCCC	19.86	25849741
400	Ubiquitination	SASPAQDKRLFLDPD CCCHHHCCCCCCCHH	38.63	2190698
546	Phosphorylation	PDDAKQLTTTINTNA CCCHHHHHEEECCCC	21.28	24043423
547	Phosphorylation	DDAKQLTTTINTNAE CCHHHHHEEECCCCH	33.98	24043423
548	Phosphorylation	DAKQLTTTINTNAEA CHHHHHEEECCCCHH	13.64	24043423
551	Phosphorylation	QLTTTINTNAEALFR HHHEEECCCCHHHCC	31.77	24043423
563	Phosphorylation	LFRPGPGSLHLKNGP HCCCCCCCEECCCCC	18.75	23312004
576	Phosphorylation	GPESIMNSTEYPHGG CCHHHHCCCCCCCCC	12.77	-
616	Phosphorylation	KEQAPDCSSSDGSER HHHCCCCCCCCCCCC	40.01	-
617	Phosphorylation	EQAPDCSSSDGSERS HHCCCCCCCCCCCCC	38.49	-
618	Phosphorylation	QAPDCSSSDGSERSW HCCCCCCCCCCCCCC	29.69	-
621	Phosphorylation	DCSSSDGSERSWMDD CCCCCCCCCCCCCCC	34.52	-
629	Phosphorylation	ERSWMDDYDYVHLQG CCCCCCCCCEEECCC	12.62	24927040
631	Phosphorylation	SWMDDYDYVHLQGKE CCCCCCCEEECCCHH	5.41	27259358
650	Ubiquitination	QQKELLEKENIMKQN HHHHHHHHHHHHHHH	56.90	-
690	Phosphorylation	DISKWKPSQSLPTTN CHHHCCCCCCCCCCC	28.77	28857561
692	Phosphorylation	SKWKPSQSLPTTNSG HHCCCCCCCCCCCCC	40.42	28857561
695	Phosphorylation	KPSQSLPTTNSGVSA CCCCCCCCCCCCCCH	43.85	28857561
775	Ubiquitination	TAQDIRNKVMNSSNQ HHHHHHHHHHCCHHH	32.77	-
780	Phosphorylation	RNKVMNSSNQLCEQL HHHHHCCHHHHHHHH	24.48	-
804	Phosphorylation	AALHYPSTTALQEMV HHHCCCCHHHHHHHH	16.16	-

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
296	S	Phosphorylation	Kinase	AURKA	O14965	GPS
780	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
804	T	Phosphorylation	Kinase	CSNK1D	P48730	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:15051726
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:15144564

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
369	S	Phosphorylation		19539609
Phosphorylation at Ser-369 induces proteasomal degradation.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD3_HUMAN	SMAD3	physical	15051726
ITCH_HUMAN	ITCH	physical	15051726
LYN_HUMAN	LYN	physical	9020138
CRKL_HUMAN	CRKL	physical	9020138
RPGF1_HUMAN	RAPGEF1	physical	9498705
PTN12_HUMAN	PTPN12	physical	9748319
BCAR1_HUMAN	BCAR1	physical	10502414
CASL_HUMAN	NEDD9	physical	10502414
ID2_HUMAN	ID2	physical	10502414
FYN_HUMAN	FYN	physical	9360983
CRK_HUMAN	CRK	physical	8879209
LCK_HUMAN	LCK	physical	8879209
NCK1_HUMAN	NCK1	physical	8879209
ABL1_HUMAN	ABL1	physical	8879209
CASL_HUMAN	NEDD9	physical	8668148
FAK1_HUMAN	PTK2	physical	8668148
CRK_HUMAN	CRK	physical	9497377
MICA1_HUMAN	MICAL1	physical	11827972
A4_HUMAN	APP	physical	21832049
IKBA_HUMAN	NFKBIA	physical	25416956
REL_HUMAN	REL	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
BCAR3_HUMAN	BCAR3	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
BANP_HUMAN	BANP	physical	25416956
PR20E_HUMAN	PRR20A	physical	25416956
PR20C_HUMAN	PRR20A	physical	25416956
PR20D_HUMAN	PRR20A	physical	25416956
PR20B_HUMAN	PRR20A	physical	25416956
PR20A_HUMAN	PRR20A	physical	25416956
RFX6_HUMAN	RFX6	physical	25416956
FZR1_HUMAN	FZR1	physical	15144564
AURKA_HUMAN	AURKA	physical	23539442
FZR1_HUMAN	FZR1	physical	23539442
TFE2_HUMAN	TCF3	physical	10502414
BANP_HUMAN	BANP	physical	21516116
TRI27_HUMAN	TRIM27	physical	21516116
DMRTB_HUMAN	DMRTB1	physical	21516116
TFCP2_HUMAN	TFCP2	physical	21516116
SMUF2_HUMAN	SMURF2	physical	20825672
RHEB_HUMAN	RHEB	physical	28514442
KLH18_HUMAN	KLHL18	physical	28514442

Drug and Disease Associations

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

Regulatory Network of CASL_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of human enhancer of filamentation (HEF1) on serine369 induces its proteasomal degradation."; Hivert V., Pierre J., Raingeaud J.; Biochem. Pharmacol. 78:1017-1025(2009). Cited for: PHOSPHORYLATION AT SER-296 AND SER-369.	19539609 [Abstract]
"T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDaCrk-associated substrate-related protein, and its association of Crkand C3G."; Ohashi Y., Tachibana K., Kamiguchi K., Fujita H., Morimoto C.; J. Biol. Chem. 273:6446-6451(1998). Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES UPON CD3 CROSS-LINKING.	9497377 [Abstract]
"Tyrosine phosphorylation of Crk-associated substrates by focaladhesion kinase. A putative mechanism for the integrin-mediatedtyrosine phosphorylation of Crk-associated substrates."; Tachibana K., Urano T., Fujita H., Ohashi Y., Kamiguchi K., Iwata S.,Hirai H., Morimoto C.; J. Biol. Chem. 272:29083-29090(1997). Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES BY PTK2/FAK1.	9360983 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92; TYR-166; TYR-189;TYR-214; TYR-223; TYR-241; TYR-261; TYR-317 AND TYR-345, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-317 AND TYR-345, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND MASSSPECTROMETRY.	15144186 [Abstract]
"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-166, AND MASSSPECTROMETRY.	12522270 [Abstract]

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