dbPTM

CD2AP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD2AP_HUMAN
UniProt AC	Q9Y5K6
Protein Name	CD2-associated protein
Gene Name	CD2AP
Organism	Homo sapiens (Human).
Sequence Length	639
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, ruffle . Cell junction . Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (PubMed:10339567). Located at podocyte slit diaphragm between podocyte foot processes (By similarity). During late anap
Protein Description	Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. [PubMed: 10339567 In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis]
Protein Sequence	MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEFKDDSLPIKRERHGNVASLVQRISTYGLPAGGIQPHPQTKNIKKKTKKRQCKVLFEYIPQNEDELELKVGDIIDINEEVEEGWWSGTLNNKLGLFPSNFVKELEVTDDGETHEAQDDSETVLAGPTSPIPSLGNVSETASGSVTQPKKIRGIGFGDIFKEGSVKLRTRTSSSETEEKKPEKPLILQSLGPKTQSVEITKTDTEGKIKAKEYCRTLFAYEGTNEDELTFKEGEIIHLISKETGEAGWWRGELNGKEGVFPDNFAVQINELDKDFPKPKKPPPPAKAPAPKPELIAAEKKYFSLKPEEKDEKSTLEQKPSKPAAPQVPPKKPTPPTKASNLLRSSGTVYPKRPEKPVPPPPPIAKINGEVSSISSKFETEPVSKLKLDSEQLPLRPKSVDFDSLTVRTSKETDVVNFDDIASSENLLHLTANRPKMPGRRLPGRFNGGHSPTHSPEKILKLPKEEDSANLKPSELKKDTCYSPKPSVYLSTPSSASKANTTAFLTPLEIKAKVETDDVKKNSLDELRAQIIELLCIVEALKKDHGKELEKLRKDLEEEKTMRSNLEMEIEKLKKAVLSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Ubiquitination	YDYDAVHDDELTIRV ECCCCCCCCCEEEEH	44.47	24816145
53	Ubiquitination	RGMFPDNFVKEIKRE CCCCCHHHHHHHHHH	12.38	21963094
55	Acetylation	MFPDNFVKEIKRETE CCCHHHHHHHHHHHC	49.97	19813661
58	Sumoylation	DNFVKEIKRETEFKD HHHHHHHHHHHCCCC	45.32	-
58	Sumoylation	DNFVKEIKRETEFKD HHHHHHHHHHHCCCC	45.32	25218447
64	Ubiquitination	IKRETEFKDDSLPIK HHHHHCCCCCCCCCC	55.16	24816145
67	Phosphorylation	ETEFKDDSLPIKRER HHCCCCCCCCCCHHH	46.29	29514088
71	Ubiquitination	KDDSLPIKRERHGNV CCCCCCCCHHHCCCH	46.39	29967540
80	Phosphorylation	ERHGNVASLVQRIST HHCCCHHHHHHHHHH	25.45	22617229
86	Phosphorylation	ASLVQRISTYGLPAG HHHHHHHHHHCCCCC	20.12	23401153
87	Phosphorylation	SLVQRISTYGLPAGG HHHHHHHHHCCCCCC	21.16	30266825
88	Phosphorylation	LVQRISTYGLPAGGI HHHHHHHHCCCCCCC	15.18	30266825
101	Phosphorylation	GIQPHPQTKNIKKKT CCCCCCCCCCCCHHC	30.43	29978859
102	Ubiquitination	IQPHPQTKNIKKKTK CCCCCCCCCCCHHCC	51.97	21963094
119	Phosphorylation	QCKVLFEYIPQNEDE HEEEEEEECCCCCCC	15.57	20068231
147	Phosphorylation	EVEEGWWSGTLNNKL HHHCCCCCCCCCCCC	18.52	26074081
149	Phosphorylation	EEGWWSGTLNNKLGL HCCCCCCCCCCCCCC	22.31	26074081
159	Phosphorylation	NKLGLFPSNFVKELE CCCCCCCCCCEEEEE	35.25	26074081
168	Phosphorylation	FVKELEVTDDGETHE CEEEEEECCCCCEEE	20.99	30278072
173	Phosphorylation	EVTDDGETHEAQDDS EECCCCCEEEEECCC	30.46	30576142
180	Phosphorylation	THEAQDDSETVLAGP EEEEECCCCEEECCC	43.38	28176443
182	Phosphorylation	EAQDDSETVLAGPTS EEECCCCEEECCCCC	25.44	29496963
188	Phosphorylation	ETVLAGPTSPIPSLG CEEECCCCCCCCCCC	46.33	30278072
189	Phosphorylation	TVLAGPTSPIPSLGN EEECCCCCCCCCCCC	24.78	30278072
193	Phosphorylation	GPTSPIPSLGNVSET CCCCCCCCCCCCCCC	50.02	30576142
198	Phosphorylation	IPSLGNVSETASGSV CCCCCCCCCCCCCCC	32.98	30278072
200	Phosphorylation	SLGNVSETASGSVTQ CCCCCCCCCCCCCCC	20.72	28176443
202	Phosphorylation	GNVSETASGSVTQPK CCCCCCCCCCCCCCC	38.73	28176443
204	Phosphorylation	VSETASGSVTQPKKI CCCCCCCCCCCCCEE	21.35	28176443
206	Phosphorylation	ETASGSVTQPKKIRG CCCCCCCCCCCEECC	40.63	28176443
221	2-Hydroxyisobutyrylation	IGFGDIFKEGSVKLR CCCCHHHCCCEEEEE	62.59	-
221	Ubiquitination	IGFGDIFKEGSVKLR CCCCHHHCCCEEEEE	62.59	32015554
224	Phosphorylation	GDIFKEGSVKLRTRT CHHHCCCEEEEEECC	19.71	23401153
226	Ubiquitination	IFKEGSVKLRTRTSS HHCCCEEEEEECCCC	33.67	-
229	Phosphorylation	EGSVKLRTRTSSSET CCEEEEEECCCCCCC	49.05	23927012
231	Phosphorylation	SVKLRTRTSSSETEE EEEEEECCCCCCCCC	32.14	27273156
232	Phosphorylation	VKLRTRTSSSETEEK EEEEECCCCCCCCCC	28.69	23927012
233	Phosphorylation	KLRTRTSSSETEEKK EEEECCCCCCCCCCC	31.42	27273156
234	Phosphorylation	LRTRTSSSETEEKKP EEECCCCCCCCCCCC	48.59	30278072
236	Phosphorylation	TRTSSSETEEKKPEK ECCCCCCCCCCCCCC	51.93	30278072
243	Ubiquitination	TEEKKPEKPLILQSL CCCCCCCCCEEEHHC	54.36	29967540
249	Phosphorylation	EKPLILQSLGPKTQS CCCEEEHHCCCCCCE	31.67	23927012
254	Phosphorylation	LQSLGPKTQSVEITK EHHCCCCCCEEEEEE	29.25	28450419
256	Phosphorylation	SLGPKTQSVEITKTD HCCCCCCEEEEEECC	27.27	20164059
260	Phosphorylation	KTQSVEITKTDTEGK CCCEEEEEECCCCCC	17.87	28450419
262	Phosphorylation	QSVEITKTDTEGKIK CEEEEEECCCCCCCC	39.23	29978859
264	Phosphorylation	VEITKTDTEGKIKAK EEEEECCCCCCCCHH	52.44	23312004
316	Ubiquitination	WRGELNGKEGVFPDN EEEEECCCCCCCCCC	50.66	27667366
333	Ubiquitination	VQINELDKDFPKPKK EEHHHCCCCCCCCCC	74.10	29967540
359	2-Hydroxyisobutyrylation	PELIAAEKKYFSLKP HHHHEEEHHHHCCCH	48.31	-
359	Acetylation	PELIAAEKKYFSLKP HHHHEEEHHHHCCCH	48.31	25953088
359	Ubiquitination	PELIAAEKKYFSLKP HHHHEEEHHHHCCCH	48.31	29967540
360	Acetylation	ELIAAEKKYFSLKPE HHHEEEHHHHCCCHH	42.93	24471353
361	Phosphorylation	LIAAEKKYFSLKPEE HHEEEHHHHCCCHHH	14.96	25159151
361	Ubiquitination	LIAAEKKYFSLKPEE HHEEEHHHHCCCHHH	14.96	27667366
363	Phosphorylation	AAEKKYFSLKPEEKD EEEHHHHCCCHHHCC	32.18	28152594
365	Ubiquitination	EKKYFSLKPEEKDEK EHHHHCCCHHHCCCC	49.54	27667366
369	Ubiquitination	FSLKPEEKDEKSTLE HCCCHHHCCCCCCCC	70.31	29967540
380	Phosphorylation	STLEQKPSKPAAPQV CCCCCCCCCCCCCCC	59.30	25159151
387	Ubiquitination	SKPAAPQVPPKKPTP CCCCCCCCCCCCCCC	9.49	21963094
393	Phosphorylation	QVPPKKPTPPTKASN CCCCCCCCCCCCHHH	51.27	28985074
396	Phosphorylation	PKKPTPPTKASNLLR CCCCCCCCCHHHHHH	40.21	29396449
397	Methylation	KKPTPPTKASNLLRS CCCCCCCCHHHHHHC	56.44	-
397	Ubiquitination	KKPTPPTKASNLLRS CCCCCCCCHHHHHHC	56.44	29967540
399	Phosphorylation	PTPPTKASNLLRSSG CCCCCCHHHHHHCCC	29.57	28555341
404	Phosphorylation	KASNLLRSSGTVYPK CHHHHHHCCCCCCCC	32.84	25159151
405	Phosphorylation	ASNLLRSSGTVYPKR HHHHHHCCCCCCCCC	31.86	25159151
407	Phosphorylation	NLLRSSGTVYPKRPE HHHHCCCCCCCCCCC	20.86	25159151
409	Phosphorylation	LRSSGTVYPKRPEKP HHCCCCCCCCCCCCC	11.68	28152594
415	Ubiquitination	VYPKRPEKPVPPPPP CCCCCCCCCCCCCCC	54.73	29967540
425	Acetylation	PPPPPIAKINGEVSS CCCCCCEEECCEEEC	37.11	19828529
431	Phosphorylation	AKINGEVSSISSKFE EEECCEEECCCCCCC	20.04	26437602
432	Phosphorylation	KINGEVSSISSKFET EECCEEECCCCCCCC	31.50	26437602
432	Ubiquitination	KINGEVSSISSKFET EECCEEECCCCCCCC	31.50	21963094
434	Phosphorylation	NGEVSSISSKFETEP CCEEECCCCCCCCCC	29.44	21406692
435	Phosphorylation	GEVSSISSKFETEPV CEEECCCCCCCCCCC	39.43	21406692
436	Acetylation	EVSSISSKFETEPVS EEECCCCCCCCCCCC	40.19	26051181
436	Ubiquitination	EVSSISSKFETEPVS EEECCCCCCCCCCCC	40.19	21963094
439	Phosphorylation	SISSKFETEPVSKLK CCCCCCCCCCCCCCC	49.04	21406692
443	Phosphorylation	KFETEPVSKLKLDSE CCCCCCCCCCCCCHH	42.88	21406692
444	Ubiquitination	FETEPVSKLKLDSEQ CCCCCCCCCCCCHHH	50.29	29967540
446	Ubiquitination	TEPVSKLKLDSEQLP CCCCCCCCCCHHHCC	54.72	29967540
449	Phosphorylation	VSKLKLDSEQLPLRP CCCCCCCHHHCCCCC	37.36	23312004
457	Ubiquitination	EQLPLRPKSVDFDSL HHCCCCCCCCCCCCC	57.59	29967540
458	Phosphorylation	QLPLRPKSVDFDSLT HCCCCCCCCCCCCCE	29.60	19664994
463	O-linked_Glycosylation	PKSVDFDSLTVRTSK CCCCCCCCCEEECCC	26.40	23301498
463	Phosphorylation	PKSVDFDSLTVRTSK CCCCCCCCCEEECCC	26.40	22167270
465	Phosphorylation	SVDFDSLTVRTSKET CCCCCCCEEECCCCC	16.34	23927012
468	Phosphorylation	FDSLTVRTSKETDVV CCCCEEECCCCCCCC	39.55	22199227
469	Phosphorylation	DSLTVRTSKETDVVN CCCEEECCCCCCCCC	20.24	22199227
470	Ubiquitination	SLTVRTSKETDVVNF CCEEECCCCCCCCCH	65.11	29967540
471	Ubiquitination	LTVRTSKETDVVNFD CEEECCCCCCCCCHH	50.43	21890473
482	Phosphorylation	VNFDDIASSENLLHL CCHHHCCCCCCCHHH	38.22	28348404
483	Phosphorylation	NFDDIASSENLLHLT CHHHCCCCCCCHHHH	22.83	28348404
490	Phosphorylation	SENLLHLTANRPKMP CCCCHHHHCCCCCCC	15.90	27251275
495	Methylation	HLTANRPKMPGRRLP HHHCCCCCCCCCCCC	55.26	-
495	Ubiquitination	HLTANRPKMPGRRLP HHHCCCCCCCCCCCC	55.26	29967540
510	Phosphorylation	GRFNGGHSPTHSPEK CCCCCCCCCCCCHHH	34.47	29255136
512	Phosphorylation	FNGGHSPTHSPEKIL CCCCCCCCCCHHHHH	37.69	29255136
514	Phosphorylation	GGHSPTHSPEKILKL CCCCCCCCHHHHHCC	36.91	29255136
516	Ubiquitination	HSPTHSPEKILKLPK CCCCCCHHHHHCCCH	56.60	21890473
520	Ubiquitination	HSPEKILKLPKEEDS CCHHHHHCCCHHHCC	67.24	21890473
523	Sumoylation	EKILKLPKEEDSANL HHHHCCCHHHCCCCC	81.70	28112733
523	Ubiquitination	EKILKLPKEEDSANL HHHHCCCHHHCCCCC	81.70	29967540
539	Phosphorylation	PSELKKDTCYSPKPS HHHHCCCCCCCCCCC	23.40	30278072
541	Phosphorylation	ELKKDTCYSPKPSVY HHCCCCCCCCCCCEE	30.05	30278072
542	Phosphorylation	LKKDTCYSPKPSVYL HCCCCCCCCCCCEEE	28.70	30278072
544	Acetylation	KDTCYSPKPSVYLST CCCCCCCCCCEEEEC	43.94	26051181
544	Ubiquitination	KDTCYSPKPSVYLST CCCCCCCCCCEEEEC	43.94	29967540
546	Phosphorylation	TCYSPKPSVYLSTPS CCCCCCCCEEEECCC	29.53	30278072
548	Phosphorylation	YSPKPSVYLSTPSSA CCCCCCEEEECCCCC	10.16	25159151
550	Phosphorylation	PKPSVYLSTPSSASK CCCCEEEECCCCCCC	22.15	25159151
551	Phosphorylation	KPSVYLSTPSSASKA CCCEEEECCCCCCCC	25.29	25159151
553	Phosphorylation	SVYLSTPSSASKANT CEEEECCCCCCCCCC	38.33	25159151
554	Phosphorylation	VYLSTPSSASKANTT EEEECCCCCCCCCCC	37.45	25159151
556	Phosphorylation	LSTPSSASKANTTAF EECCCCCCCCCCCCE	33.96	24260401
557	Ubiquitination	STPSSASKANTTAFL ECCCCCCCCCCCCEE	45.43	29967540
560	Phosphorylation	SSASKANTTAFLTPL CCCCCCCCCCEECCE	25.10	28450419
561	Phosphorylation	SASKANTTAFLTPLE CCCCCCCCCEECCEE	18.41	28450419
565	Phosphorylation	ANTTAFLTPLEIKAK CCCCCEECCEEEEEE	21.26	25159151
570	Ubiquitination	FLTPLEIKAKVETDD EECCEEEEEEECCCC	32.55	32015554
575	Phosphorylation	EIKAKVETDDVKKNS EEEEEECCCCHHCCC	40.25	28857561
582	Phosphorylation	TDDVKKNSLDELRAQ CCCHHCCCHHHHHHH	46.18	23401153
613	Ubiquitination	KELEKLRKDLEEEKT HHHHHHHHHHHHHHH	76.68	29967540
623	Phosphorylation	EEEKTMRSNLEMEIE HHHHHHHHHHHHHHH	34.64	22210691
627	Sulfoxidation	TMRSNLEMEIEKLKK HHHHHHHHHHHHHHH	7.67	21406390
631	Ubiquitination	NLEMEIEKLKKAVLS HHHHHHHHHHHHHHC	71.86	29967540

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 CD2AP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CD2AP_HUMAN !!

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 CD2AP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB4A_HUMAN	RAB4A	physical	12559036
CBL_HUMAN	CBL	physical	15128873
CAZA1_HUMAN	CAPZA1	physical	12690097
CBL_HUMAN	CBL	physical	11067845
CD2AP_HUMAN	CD2AP	physical	12559036
CBL_HUMAN	CBL	physical	12559036
CD2AP_HUMAN	CD2AP	physical	10339567
NR4A1_HUMAN	NR4A1	physical	18654987
NR2C2_HUMAN	NR2C2	physical	18654987
HBP1_HUMAN	HBP1	physical	18654987
HXC11_HUMAN	HOXC11	physical	18654987
ACTC_HUMAN	ACTC1	physical	17606992
CBLB_HUMAN	CBLB	physical	17020880
CD2_HUMAN	CD2	physical	17020880
CD2AP_HUMAN	CD2AP	physical	17020880
MB12A_HUMAN	MVB12A	physical	16895919
SRC8_HUMAN	CTTN	physical	12672817
EGFR_HUMAN	EGFR	physical	12672817
CBL_HUMAN	CBL	physical	12672817
SH3G2_HUMAN	SH3GL2	physical	12672817
DYN2_HUMAN	DNM2	physical	12672817
CD2_HUMAN	CD2	physical	12618476
CBL_HUMAN	CBL	physical	12618476
BCAR1_HUMAN	BCAR1	physical	12618476
SHIP1_HUMAN	INPP5D	physical	22706086
CAZA1_HUMAN	CAPZA1	physical	22706086
CAPZB_HUMAN	CAPZB	physical	22706086
CBL_HUMAN	CBL	physical	22706086
CBLC_HUMAN	CBLC	physical	18753381
CBL_HUMAN	CBL	physical	17188587
CAZA2_HUMAN	CAPZA2	physical	20697350
CAZA1_HUMAN	CAPZA1	physical	20697350
CAPZB_HUMAN	CAPZB	physical	20697350
3BP1_HUMAN	SH3BP1	physical	20697350
RASN_HUMAN	NRAS	physical	22939629
GRB2_HUMAN	GRB2	physical	21988832
TEBP_HUMAN	PTGES3	physical	21988832
ARHGA_HUMAN	ARHGEF10	physical	22863883
BRCC3_HUMAN	BRCC3	physical	22863883
ELP1_HUMAN	IKBKAP	physical	22863883
WASC5_HUMAN	KIAA0196	physical	22863883
WASC4_HUMAN	KIAA1033	physical	22863883
LARP7_HUMAN	LARP7	physical	22863883
NOLC1_HUMAN	NOLC1	physical	22863883
NRBP_HUMAN	NRBP1	physical	22863883
RABE2_HUMAN	RABEP2	physical	22863883
T22D1_HUMAN	TSC22D1	physical	22863883
UBP34_HUMAN	USP34	physical	22863883
WDHD1_HUMAN	WDHD1	physical	22863883
CD2_HUMAN	CD2	physical	23663663
CBLB_HUMAN	CBLB	physical	23663663
NIT1_HUMAN	NIT1	physical	26344197
CBL_HUMAN	CBL	physical	25872741

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607832	Focal segmental glomerulosclerosis 3 (FSGS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CD2AP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-458, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88, AND MASSSPECTROMETRY.	15592455 [Abstract]