dbPTM

ZAP70_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZAP70_HUMAN
UniProt AC	P43403
Protein Name	Tyrosine-protein kinase ZAP-70
Gene Name	ZAP70
Organism	Homo sapiens (Human).
Sequence Length	619
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein . In quiescent T-lymphocytes, it is cytoplasmic. Upon TCR activation, it is recruited at the plasma membrane by interacting with CD247/CD3Z. Colocalizes together with RHOH in the immunological s
Protein Description	Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins: LAT and LCP2. In turn, a large number of signaling molecules are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Furthermore, ZAP70 controls cytoskeleton modifications, adhesion and mobility of T-lymphocytes, thus ensuring correct delivery of effectors to the APC. ZAP70 is also required for TCR-CD247/CD3Z internalization and degradation through interaction with the E3 ubiquitin-protein ligase CBL and adapter proteins SLA and SLA2. Thus, ZAP70 regulates both T-cell activation switch on and switch off by modulating TCR expression at the T-cell surface. During thymocyte development, ZAP70 promotes survival and cell-cycle progression of developing thymocytes before positive selection (when cells are still CD4/CD8 double negative). Additionally, ZAP70-dependent signaling pathway may also contribute to primary B-cells formation and activation through B-cell receptor (BCR)..
Protein Sequence	MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCEFYSRDPDGLPCNLRKPCNRPSGLEPQPGVFDCLRDAMVRDYVRQTWKLEGEALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGAQTDGKFLLRPRKEQGTYALSLIYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYCLKEACPNSSASNASGAAAPTLPAHPSTLTHPQRRIDTLNSDGYTPEPARITSPDKPRPMPMDTSVYESPYSDPEELKDKKLFLKRDNLLIADIELGCGNFGSVRQGVYRMRKKQIDVAIKVLKQGTEKADTEEMMREAQIMHQLDNPYIVRLIGVCQAEALMLVMEMAGGGPLHKFLVGKREEIPVSNVAELLHQVSMGMKYLEEKNFVHRDLAARNVLLVNRHYAKISDFGLSKALGADDSYYTARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEALSYGQKPYKKMKGPEVMAFIEQGKRMECPPECPPELYALMSDCWIYKWEDRPDFLTVEQRMRACYYSLASKVEGPPGSTQKAEAACA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	AAHLPFFYGSISRAE HHCCCCCCCCCCHHH	15.44	28796482
14	Phosphorylation	HLPFFYGSISRAEAE CCCCCCCCCCHHHHH	13.15	28796482
16	Phosphorylation	PFFYGSISRAEAEEH CCCCCCCCHHHHHHH	27.43	28796482
19	Ubiquitination	YGSISRAEAEEHLKL CCCCCHHHHHHHHHH	56.34	29967540
25	Ubiquitination	AEAEEHLKLAGMADG HHHHHHHHHCCHHHH	37.89	22505724
29	Sulfoxidation	EHLKLAGMADGLFLL HHHHHCCHHHHHHHH	2.27	21406390
46	Phosphorylation	CLRSLGGYVLSLVHD HHHHCCHHHHHHHCE	9.09	22817900
54	Ubiquitination	VLSLVHDVRFHHFPI HHHHHCEECHHCCCC	4.20	22505724
55	Ubiquitination	LSLVHDVRFHHFPIE HHHHCEECHHCCCCC	31.10	22505724
62	Ubiquitination	RFHHFPIERQLNGTY CHHCCCCCHHCCCCE	34.31	29967540
65	Ubiquitination	HFPIERQLNGTYAIA CCCCCHHCCCCEEEC	8.82	29967540
68	Phosphorylation	IERQLNGTYAIAGGK CCHHCCCCEEECCCC	14.54	28796482
69	Phosphorylation	ERQLNGTYAIAGGKA CHHCCCCEEECCCCC	9.45	28796482
70	Ubiquitination	RQLNGTYAIAGGKAH HHCCCCEEECCCCCC	5.74	22505724
75	Ubiquitination	TYAIAGGKAHCGPAE CEEECCCCCCCCHHH	33.76	-
87	Phosphorylation	PAELCEFYSRDPDGL HHHHHHHHCCCCCCC	4.78	28796482
88	Phosphorylation	AELCEFYSRDPDGLP HHHHHHHCCCCCCCC	35.21	28796482
100	Ubiquitination	GLPCNLRKPCNRPSG CCCCCCCCCCCCCCC	58.02	24816145
106	Phosphorylation	RKPCNRPSGLEPQPG CCCCCCCCCCCCCCC	53.42	28464451
126	Phosphorylation	RDAMVRDYVRQTWKL HHHHHHHHHHHHHHC	6.23	7961936
132	Ubiquitination	DYVRQTWKLEGEALE HHHHHHHHCCHHHHH	39.79	22505724
143	Ubiquitination	EALEQAIISQAPQVE HHHHHHHHHCCHHHH	2.53	29967540
148	Ubiquitination	AIISQAPQVEKLIAT HHHHCCHHHHHHHHH	60.04	22505724
151	Ubiquitination	SQAPQVEKLIATTAH HCCHHHHHHHHHCHH	46.46	29967540
164	Phosphorylation	AHERMPWYHSSLTRE HHHHCCCCCCCCCHH	5.97	28796482
166	Phosphorylation	ERMPWYHSSLTREEA HHCCCCCCCCCHHHH	16.02	28857561
167	Phosphorylation	RMPWYHSSLTREEAE HCCCCCCCCCHHHHH	22.05	28857561
169	Ubiquitination	PWYHSSLTREEAERK CCCCCCCCHHHHHHH	37.67	22505724
169	Phosphorylation	PWYHSSLTREEAERK CCCCCCCCHHHHHHH	37.67	26546556
176	Ubiquitination	TREEAERKLYSGAQT CHHHHHHHHHHCCCC	43.19	22505724
177	Ubiquitination	REEAERKLYSGAQTD HHHHHHHHHHCCCCC	5.29	22505724
178	Phosphorylation	EEAERKLYSGAQTDG HHHHHHHHHCCCCCC	14.21	28796482
179	Phosphorylation	EAERKLYSGAQTDGK HHHHHHHHCCCCCCC	37.78	29978859
183	Phosphorylation	KLYSGAQTDGKFLLR HHHHCCCCCCCEEEC	46.30	23532336
186	Ubiquitination	SGAQTDGKFLLRPRK HCCCCCCCEEECCCH	35.33	29967540
186	Acetylation	SGAQTDGKFLLRPRK HCCCCCCCEEECCCH	35.33	25953088
193	Ubiquitination	KFLLRPRKEQGTYAL CEEECCCHHCCCEEE	58.01	22505724
197	Phosphorylation	RPRKEQGTYALSLIY CCCHHCCCEEEEEEE	12.81	28796482
197	Ubiquitination	RPRKEQGTYALSLIY CCCHHCCCEEEEEEE	12.81	29967540
198	Phosphorylation	PRKEQGTYALSLIYG CCHHCCCEEEEEEEC	16.63	28796482
204	Phosphorylation	TYALSLIYGKTVYHY CEEEEEEECCHHHHH	20.19	28796482
206	Ubiquitination	ALSLIYGKTVYHYLI EEEEEECCHHHHHHC	20.18	-
207	Phosphorylation	LSLIYGKTVYHYLIS EEEEECCHHHHHHCC	23.18	28796482
209	Phosphorylation	LIYGKTVYHYLISQD EEECCHHHHHHCCCC	7.03	28796482
211	Phosphorylation	YGKTVYHYLISQDKA ECCHHHHHHCCCCCC	6.50	28796482
217	Ubiquitination	HYLISQDKAGKYCIP HHHCCCCCCCCEECC	51.94	29967540
217	Acetylation	HYLISQDKAGKYCIP HHHCCCCCCCCEECC	51.94	25953088
220	Ubiquitination	ISQDKAGKYCIPEGT CCCCCCCCEECCCCC	41.63	29967540
221	Phosphorylation	SQDKAGKYCIPEGTK CCCCCCCEECCCCCC	8.49	28796482
223	Ubiquitination	DKAGKYCIPEGTKFD CCCCCEECCCCCCHH	2.94	24816145
227	Phosphorylation	KYCIPEGTKFDTLWQ CEECCCCCCHHHHHH	27.20	22985185
237	Ubiquitination	DTLWQLVEYLKLKAD HHHHHHHHHHHHCCC	54.46	29967540
242	Ubiquitination	LVEYLKLKADGLIYC HHHHHHHCCCCEEEE	42.73	29967540
248	Phosphorylation	LKADGLIYCLKEACP HCCCCEEEEHHHHCC	9.21	22322096
249	Ubiquitination	KADGLIYCLKEACPN CCCCEEEEHHHHCCC	3.29	22505724
251	Ubiquitination	DGLIYCLKEACPNSS CCEEEEHHHHCCCCC	39.44	29967540
255	Ubiquitination	YCLKEACPNSSASNA EEHHHHCCCCCCCCC	51.27	22505724
257	Phosphorylation	LKEACPNSSASNASG HHHHCCCCCCCCCCC	16.66	-
258	Phosphorylation	KEACPNSSASNASGA HHHCCCCCCCCCCCC	42.21	-
263	Phosphorylation	NSSASNASGAAAPTL CCCCCCCCCCCCCCC	32.96	-
278	Phosphorylation	PAHPSTLTHPQRRID CCCHHHCCCCCHHHH	31.44	-
286	Phosphorylation	HPQRRIDTLNSDGYT CCCHHHHCCCCCCCC	26.01	26552605
289	Phosphorylation	RRIDTLNSDGYTPEP HHHHCCCCCCCCCCC	35.21	15570572
292	Phosphorylation	DTLNSDGYTPEPARI HCCCCCCCCCCCCCC	24.90	15100278
293	Phosphorylation	TLNSDGYTPEPARIT CCCCCCCCCCCCCCC	27.06	28796482
296	Ubiquitination	SDGYTPEPARITSPD CCCCCCCCCCCCCCC	28.21	22505724
299	Ubiquitination	YTPEPARITSPDKPR CCCCCCCCCCCCCCC	4.93	22505724
300	Phosphorylation	TPEPARITSPDKPRP CCCCCCCCCCCCCCC	28.75	22322096
301	Phosphorylation	PEPARITSPDKPRPM CCCCCCCCCCCCCCC	28.82	28464451
304	Ubiquitination	ARITSPDKPRPMPMD CCCCCCCCCCCCCCC	46.43	PubMed
306	Ubiquitination	ITSPDKPRPMPMDTS CCCCCCCCCCCCCCC	45.98	22505724
312	Phosphorylation	PRPMPMDTSVYESPY CCCCCCCCCCCCCCC	17.53	22322096
313	Phosphorylation	RPMPMDTSVYESPYS CCCCCCCCCCCCCCC	20.59	22322096
315	Phosphorylation	MPMDTSVYESPYSDP CCCCCCCCCCCCCCH	15.51	15100278
317	Phosphorylation	MDTSVYESPYSDPEE CCCCCCCCCCCCHHH	16.08	22322096
319	Phosphorylation	TSVYESPYSDPEELK CCCCCCCCCCHHHHC	34.68	15268851
320	Phosphorylation	SVYESPYSDPEELKD CCCCCCCCCHHHHCC	50.50	22322096
326	Ubiquitination	YSDPEELKDKKLFLK CCCHHHHCCCCCCHH	71.44	24816145
326	Acetylation	YSDPEELKDKKLFLK CCCHHHHCCCCCCHH	71.44	25953088
329	Ubiquitination	PEELKDKKLFLKRDN HHHHCCCCCCHHCCC	55.39	-
351	Phosphorylation	LGCGNFGSVRQGVYR ECCCCCHHHHHHHHH	15.25	26074081
357	Phosphorylation	GSVRQGVYRMRKKQI HHHHHHHHHHHHHHH	12.91	26074081
361	Ubiquitination	QGVYRMRKKQIDVAI HHHHHHHHHHHHHHH	39.42	22505724
362	Ubiquitination	GVYRMRKKQIDVAIK HHHHHHHHHHHHHHH	41.96	22505724
369	Ubiquitination	KQIDVAIKVLKQGTE HHHHHHHHHHHCCCC	31.60	29967540
369	Acetylation	KQIDVAIKVLKQGTE HHHHHHHHHHHCCCC	31.60	25953088
372	Ubiquitination	DVAIKVLKQGTEKAD HHHHHHHHCCCCCCC	50.06	29967540
372	Acetylation	DVAIKVLKQGTEKAD HHHHHHHHCCCCCCC	50.06	25953088
377	Ubiquitination	VLKQGTEKADTEEMM HHHCCCCCCCHHHHH	51.94	22505724
397	Phosphorylation	MHQLDNPYIVRLIGV HHHCCCHHHHHHHHH	20.50	28796482
427	Ubiquitination	GPLHKFLVGKREEIP CCHHHHHCCCCCCCC	10.79	24816145
429	Ubiquitination	LHKFLVGKREEIPVS HHHHHCCCCCCCCCC	49.51	-
443	Ubiquitination	SNVAELLHQVSMGMK CCHHHHHHHHHHHHH	38.32	24816145
449	Ubiquitination	LHQVSMGMKYLEEKN HHHHHHHHHHHHHCC	1.61	24816145
450	Ubiquitination	HQVSMGMKYLEEKNF HHHHHHHHHHHHCCC	40.74	29967540
451	Phosphorylation	QVSMGMKYLEEKNFV HHHHHHHHHHHCCCC	15.51	-
455	Ubiquitination	GMKYLEEKNFVHRDL HHHHHHHCCCCCHHH	46.43	29967540
474	Phosphorylation	VLLVNRHYAKISDFG EEEECCCEECHHHHC	13.32	22817900
476	Ubiquitination	LVNRHYAKISDFGLS EECCCEECHHHHCHH	35.26	22505724
478	Ubiquitination	NRHYAKISDFGLSKA CCCEECHHHHCHHHH	26.61	22505724
479	Ubiquitination	RHYAKISDFGLSKAL CCEECHHHHCHHHHH	45.14	22505724
484	Ubiquitination	ISDFGLSKALGADDS HHHHCHHHHHCCCCC	53.31	22505724
484	Acetylation	ISDFGLSKALGADDS HHHHCHHHHHCCCCC	53.31	25953088
485	Ubiquitination	SDFGLSKALGADDSY HHHCHHHHHCCCCCC	14.09	22505724
491	Phosphorylation	KALGADDSYYTARSA HHHCCCCCCCCCHHC	22.16	28796482
492	Phosphorylation	ALGADDSYYTARSAG HHCCCCCCCCCHHCC	16.30	7781602
493	Phosphorylation	LGADDSYYTARSAGK HCCCCCCCCCHHCCC	9.62	7781602
494	Phosphorylation	GADDSYYTARSAGKW CCCCCCCCCHHCCCC	13.83	22322096
494	Ubiquitination	GADDSYYTARSAGKW CCCCCCCCCHHCCCC	13.83	22505724
497	Phosphorylation	DSYYTARSAGKWPLK CCCCCCHHCCCCCCE	38.62	-
497	O-linked_Glycosylation	DSYYTARSAGKWPLK CCCCCCHHCCCCCCE	38.62	27655845
500	Ubiquitination	YTARSAGKWPLKWYA CCCHHCCCCCCEEEC	45.41	22505724
504	Ubiquitination	SAGKWPLKWYAPECI HCCCCCCEEECCCCC	33.79	29967540
506	Phosphorylation	GKWPLKWYAPECINF CCCCCEEECCCCCCC	15.64	-
520	Phosphorylation	FRKFSSRSDVWSYGV CEECCCCHHHHHHCC	38.16	14560012
534	Phosphorylation	VTMWEALSYGQKPYK CHHHHHHHCCCCCCC	33.98	-
535	Phosphorylation	TMWEALSYGQKPYKK HHHHHHHCCCCCCCC	25.15	-
538	Ubiquitination	EALSYGQKPYKKMKG HHHHCCCCCCCCCCC	46.05	PubMed
544	Ubiquitination	QKPYKKMKGPEVMAF CCCCCCCCCHHHHHH	78.99	PubMed
556	Ubiquitination	MAFIEQGKRMECPPE HHHHHCCCCCCCCCC	48.55	22505724
556	Acetylation	MAFIEQGKRMECPPE HHHHHCCCCCCCCCC	48.55	25953088
569	Phosphorylation	PECPPELYALMSDCW CCCCHHHHHHHCCCE	8.95	-
593	Ubiquitination	FLTVEQRMRACYYSL CCCHHHHHHHHHHHH	2.96	22505724
597	Phosphorylation	EQRMRACYYSLASKV HHHHHHHHHHHHHHC	8.63	28796482
598	Phosphorylation	QRMRACYYSLASKVE HHHHHHHHHHHHHCC	9.33	28796482
599	Phosphorylation	RMRACYYSLASKVEG HHHHHHHHHHHHCCC	7.32	28796482
599	Ubiquitination	RMRACYYSLASKVEG HHHHHHHHHHHHCCC	7.32	22505724
601	Ubiquitination	RACYYSLASKVEGPP HHHHHHHHHHCCCCC	11.02	22505724
602	Phosphorylation	ACYYSLASKVEGPPG HHHHHHHHHCCCCCC	42.39	26552605
603	Acetylation	CYYSLASKVEGPPGS HHHHHHHHCCCCCCC	38.40	19608861
603	Ubiquitination	CYYSLASKVEGPPGS HHHHHHHHCCCCCCC	38.40	22505724
607	Ubiquitination	LASKVEGPPGSTQKA HHHHCCCCCCCCHHH	19.30	22505724
610	Phosphorylation	KVEGPPGSTQKAEAA HCCCCCCCCHHHHHH	33.18	26552605
611	Phosphorylation	VEGPPGSTQKAEAAC CCCCCCCCHHHHHHC	39.75	26552605
613	Ubiquitination	GPPGSTQKAEAACA- CCCCCCHHHHHHCC-	48.56	22505724
617	Ubiquitination	STQKAEAACA----- CCHHHHHHCC-----	4.93	22505724
623	Ubiquitination	AACA----------- HHCC-----------		22505724
673	Ubiquitination	------------------------------------------------------------- -------------------------------------------------------------		22505724
679	Ubiquitination	------------------------------------------------------------------- -------------------------------------------------------------------		22505724
720	Ubiquitination	------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------		22505724
726	Ubiquitination	------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------		22505724
730	Ubiquitination	---------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------		22505724
736	Ubiquitination	---------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------		22505724

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
69	Y	Phosphorylation	Kinase	LCK	P06239	PSP
126	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
126	Y	Phosphorylation	Kinase	LCK	P06239	PSP
126	Y	Phosphorylation	Kinase	PKCT	Q04759	PSP
178	Y	Phosphorylation	Kinase	LCK	P06239	PSP
292	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
292	Y	Phosphorylation	Kinase	LCK	P06239	PSP
293	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
315	Y	Phosphorylation	Kinase	PKCT	Q04759	PSP
315	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot
315	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
319	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
319	Y	Phosphorylation	Kinase	LCK	P06239	PSP
319	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
319	Y	Phosphorylation	Kinase	PKCT	Q04759	PSP
474	Y	Phosphorylation	Kinase	LCK	P06239	PSP
492	Y	Phosphorylation	Kinase	LCK	P06240	PSP
492	Y	Phosphorylation	Kinase	LCK	P06239	PSP
492	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
493	Y	Phosphorylation	Kinase	LCK	P06240	PSP
493	Y	Phosphorylation	Kinase	PKCT	Q04759	PSP
493	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
493	Y	Phosphorylation	Kinase	LCK	P06239	PSP
597	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
598	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZAP70_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 ZAP70_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DBNL_HUMAN	DBNL	physical	14557276
FYN_HUMAN	FYN	genetic	7760813
FYN_HUMAN	FYN	physical	7760813
ABL1_HUMAN	ABL1	physical	7760813
RASA1_HUMAN	RASA1	physical	7760813
PPAC_HUMAN	ACP1	physical	11976341
LAT_HUMAN	LAT	physical	11368773
SHC1_HUMAN	SHC1	physical	9685404
PHAG1_HUMAN	PAG1	physical	10790433
PLCG1_HUMAN	PLCG1	physical	7629168
GRB2_HUMAN	GRB2	physical	7629168
LCP2_HUMAN	LCP2	physical	9047237
CD3E_HUMAN	CD3E	physical	7761456
PTN6_HUMAN	PTPN6	physical	8638162
LAT_HUMAN	LAT	physical	12186560
CD5_HUMAN	CD5	physical	9378960
TYOBP_HUMAN	TYROBP	physical	9490415
TBA1A_HUMAN	TUBA1A	physical	8530437
TBB5_HUMAN	TUBB	physical	8530437
VAV_HUMAN	VAV1	physical	8530437
HSP74_HUMAN	HSPA4	physical	16888650
CBL_HUMAN	CBL	physical	9407100
LCP2_HUMAN	LCP2	physical	12190313
CD3Z_HUMAN	CD247	physical	9036949
A4_HUMAN	APP	physical	21832049
GRB2_HUMAN	GRB2	physical	23267066
SHC1_HUMAN	SHC1	physical	23267066
CD3Z_HUMAN	CD247	physical	20637659
ZAP70_HUMAN	ZAP70	physical	8906806
PLCG1_HUMAN	PLCG1	physical	8906806

Drug and Disease Associations

Kegg Disease
H00005	Chronic lymphocytic leukemia (CLL)
H00093	Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
OMIM Disease
269840	Selective T-cell defect (STCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ZAP70_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-289, AND MASSSPECTROMETRY.	15144186 [Abstract]
"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 TYR-292 AND TYR-492, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248; TYR-292 ANDTYR-492, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-315; TYR-319;TYR-492 AND TYR-493, AND MASS SPECTROMETRY.	16094384 [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-248; TYR-292; TYR-315;TYR-319; TYR-492 AND TYR-493, AND MASS SPECTROMETRY.	15592455 [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-292; TYR-315; TYR-319;TYR-492 AND TYR-493, AND MASS SPECTROMETRY.	12522270 [Abstract]
"Tyrosine 319, a newly identified phosphorylation site of ZAP-70,plays a critical role in T cell antigen receptor signaling."; Di Bartolo V., Mege D., Germain V., Pelosi M., Dufour E., Michel F.,Magistrelli G., Isacchi A., Acuto O.; J. Biol. Chem. 274:6285-6294(1999). Cited for: PHOSPHORYLATION AT TYR-315 AND TYR-319, AND MUTAGENESIS OF TYR-315 ANDTYR-319.	10037717 [Abstract]
"Enhancement of lymphocyte responsiveness by a gain-of-functionmutation of ZAP-70."; Zhao Q., Weiss A.; Mol. Cell. Biol. 16:6765-6774(1996). Cited for: PHOSPHORYLATION AT TYR-292, AND MUTAGENESIS OF TYR-292.	8943331 [Abstract]