dbPTM

FAK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAK2_HUMAN
UniProt AC	Q14289
Protein Name	Protein-tyrosine kinase 2-beta
Gene Name	PTK2B
Organism	Homo sapiens (Human).
Sequence Length	1009
Subcellular Localization	Cytoplasm. Cytoplasm, perinuclear region. Cell membrane Peripheral membrane protein Cytoplasmic side. Cell junction, focal adhesion. Cell projection, lamellipodium. Cytoplasm, cell cortex. Nucleus. Interaction with NPHP1 induces the membrane-associ
Protein Description	Non-receptor protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca(2+) levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2..
Protein Sequence	MSGVSEPLSRVKLGTLRRPEGPAEPMVVVPVDVEKEDVRILKVCFYSNSFNPGKNFKLVKCTVQTEIREIITSILLSGRIGPNIRLAECYGLRLKHMKSDEIHWLHPQMTVGEVQDKYECLHVEAEWRYDLQIRYLPEDFMESLKEDRTTLLYFYQQLRNDYMQRYASKVSEGMALQLGCLELRRFFKDMPHNALDKKSNFELLEKEVGLDLFFPKQMQENLKPKQFRKMIQQTFQQYASLREEECVMKFFNTLAGFANIDQETYRCELIQGWNITVDLVIGPKGIRQLTSQDAKPTCLAEFKQIRSIRCLPLEEGQAVLQLGIEGAPQALSIKTSSLAEAENMADLIDGYCRLQGEHQGSLIIHPRKDGEKRNSLPQIPMLNLEARRSHLSESCSIESDIYAEIPDETLRRPGGPQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEAVIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICKAMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPESINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLYTLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRPKYRPPPQTNLLAPKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMREEDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDPMVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTANLDRTDDLVYLNVMELVRAVLELKNELCQLPPEGYVVVVKNVGLTLRKLIGSVDDLLPSLPSSSRTEIEGTQKLLNKDLAELINKMRLAQQNAVTSLSEECKRQMLTASHTLAVDAKNLLDAVDQAKVLANLAHPPAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGVSEPLS ------CCCCCCCCC	60.24	28857561
5	Phosphorylation	---MSGVSEPLSRVK ---CCCCCCCCCCCC	36.70	20071362
9	Phosphorylation	SGVSEPLSRVKLGTL CCCCCCCCCCCCCCC	45.82	22817900
12	Ubiquitination	SEPLSRVKLGTLRRP CCCCCCCCCCCCCCC	39.84	29967540
15	Phosphorylation	LSRVKLGTLRRPEGP CCCCCCCCCCCCCCC	27.77	22817900
54	Ubiquitination	SNSFNPGKNFKLVKC CCCCCCCCCEEEEEE	61.54	29967540
135	Phosphorylation	RYDLQIRYLPEDFME ECCEEEEECCHHHHH	28.39	19369195
149	Phosphorylation	ESLKEDRTTLLYFYQ HHHHCCHHHHHHHHH	33.83	25262027
150	Phosphorylation	SLKEDRTTLLYFYQQ HHHCCHHHHHHHHHH	18.69	25262027
153	Phosphorylation	EDRTTLLYFYQQLRN CCHHHHHHHHHHHHH	11.89	25262027
155	Phosphorylation	RTTLLYFYQQLRNDY HHHHHHHHHHHHHHH	5.04	25262027
188	Ubiquitination	LELRRFFKDMPHNAL HHHHHHHCCCCCCCC	50.86	21890473
188 (in isoform 1)	Ubiquitination	-	50.86	21890473
188 (in isoform 2)	Ubiquitination	-	50.86	21890473
188	Ubiquitination	LELRRFFKDMPHNAL HHHHHHHCCCCCCCC	50.86	21890473
198	Ubiquitination	PHNALDKKSNFELLE CCCCCCCCCCHHHHH	50.74	30230243
206	Ubiquitination	SNFELLEKEVGLDLF CCHHHHHHHHCCCHH	58.64	30230243
216	Ubiquitination	GLDLFFPKQMQENLK CCCHHCHHHHHHCCC	53.93	29967540
234	Phosphorylation	FRKMIQQTFQQYASL HHHHHHHHHHHHHHH	13.67	27174698
238	Phosphorylation	IQQTFQQYASLREEE HHHHHHHHHHHCHHH	6.33	27174698
240	Phosphorylation	QTFQQYASLREEECV HHHHHHHHHCHHHHH	24.03	27174698
295	Ubiquitination	QLTSQDAKPTCLAEF HCCCCCCCCCHHHHH	49.50	30230243
303	Ubiquitination	PTCLAEFKQIRSIRC CCHHHHHHHHCEEEE	36.00	29967540
307	Phosphorylation	AEFKQIRSIRCLPLE HHHHHHCEEEEEECC	18.93	24702127
332	Phosphorylation	EGAPQALSIKTSSLA CCCCCCEEEEHHCHH	25.67	22817900
361	Phosphorylation	LQGEHQGSLIIHPRK CCCCCCCCEEEEECC	15.15	28450419
375	Phosphorylation	KDGEKRNSLPQIPML CCCCCCCCCCCCCCC	45.52	22167270
389	Phosphorylation	LNLEARRSHLSESCS CCHHHHHHHCCCCCC	24.19	18691976
392	Phosphorylation	EARRSHLSESCSIES HHHHHHCCCCCCCCC	23.26	19060867
394	Phosphorylation	RRSHLSESCSIESDI HHHHCCCCCCCCCCE	15.13	18691976
396	Phosphorylation	SHLSESCSIESDIYA HHCCCCCCCCCCEEE	38.37	26657352
399	Phosphorylation	SESCSIESDIYAEIP CCCCCCCCCEEEECC	27.86	21082442
402	Dephosphorylation	CSIESDIYAEIPDET CCCCCCEEEECCCHH	11.81	12231407
402	Phosphorylation	CSIESDIYAEIPDET CCCCCCEEEECCCHH	11.81	14712221
409	Phosphorylation	YAEIPDETLRRPGGP EEECCCHHCCCCCCC	32.70	22817900
418	Phosphorylation	RRPGGPQYGIAREDV CCCCCCCCCCCHHHH	17.40	-
440	Phosphorylation	EGFFGEVYEGVYTNH CCCCCEEEEEEEECC	11.58	19060867
451	Ubiquitination	YTNHKGEKINVAVKT EECCCCCEEEEEEEC	48.53	29967540
457	Ubiquitination	EKINVAVKTCKKDCT CEEEEEEECCCCCCC	38.17	29967540
463	S-palmitoylation	VKTCKKDCTLDNKEK EECCCCCCCCCCHHH	5.82	29575903
473	Phosphorylation	DNKEKFMSEAVIMKN CCHHHHHCHHHHHHC	26.07	-
479	Ubiquitination	MSEAVIMKNLDHPHI HCHHHHHHCCCCHHH	43.14	29967540
525	Phosphorylation	KNSLKVLTLVLYSLQ CCHHHHHHHHHHHHH	20.15	28270605
529	Phosphorylation	KVLTLVLYSLQICKA HHHHHHHHHHHHHHH	10.39	28270605
530	Phosphorylation	VLTLVLYSLQICKAM HHHHHHHHHHHHHHH	15.05	22817900
559	Phosphorylation	VRNILVASPECVKLG HHHEEEECHHHEECC	17.47	22817900
564	Acetylation	VASPECVKLGDFGLS EECHHHEECCCCCCC	59.41	23749302
564	Ubiquitination	VASPECVKLGDFGLS EECHHHEECCCCCCC	59.41	30230243
571	Phosphorylation	KLGDFGLSRYIEDED ECCCCCCCCCCCCCC	24.34	29255136
573	Phosphorylation	GDFGLSRYIEDEDYY CCCCCCCCCCCCCCH	12.80	26356563
579	Dephosphorylation	RYIEDEDYYKASVTR CCCCCCCCHHEECEE	12.57	11337490
579	Phosphorylation	RYIEDEDYYKASVTR CCCCCCCCHHEECEE	12.57	21945579
580	Dephosphorylation	YIEDEDYYKASVTRL CCCCCCCHHEECEEC	16.64	11337490
580	Phosphorylation	YIEDEDYYKASVTRL CCCCCCCHHEECEEC	16.64	21945579
581	Ubiquitination	IEDEDYYKASVTRLP CCCCCCHHEECEECC	28.14	30230243
583	Phosphorylation	DEDYYKASVTRLPIK CCCCHHEECEECCCC	21.62	19369195
585	Phosphorylation	DYYKASVTRLPIKWM CCHHEECEECCCCCC	24.80	28796482
640	Ubiquitination	DVIGVLEKGDRLPKP CEEEEECCCCCCCCC	63.05	29967540
683	Phosphorylation	VCSLSDVYQMEKDIA HHHHHHHHHHHHHHH	13.72	22817900
699	Phosphorylation	EQERNARYRTPKILE HHHHHHHHCCCCCCC	19.21	22817900
701	Phosphorylation	ERNARYRTPKILEPT HHHHHHCCCCCCCCC	21.72	-
703	Ubiquitination	NARYRTPKILEPTAF HHHHCCCCCCCCCCC	60.35	29967540
718	Phosphorylation	QEPPPKPSRPKYRPP CCCCCCCCCCCCCCC	68.30	22817900
722	Phosphorylation	PKPSRPKYRPPPQTN CCCCCCCCCCCCCCC	30.91	25394399
734	Ubiquitination	QTNLLAPKLQFQVPE CCCCCCCEECCCCCC	49.68	29967540
746	Phosphorylation	VPEGLCASSPTLTSP CCCCCCCCCCCCCCC	35.53	22617229
746 (in isoform 2)	Phosphorylation	-	35.53	19369195
747	Phosphorylation	PEGLCASSPTLTSPM CCCCCCCCCCCCCCC	11.90	28450419
749	Phosphorylation	GLCASSPTLTSPMEY CCCCCCCCCCCCCCC	44.61	28450419
751	Phosphorylation	CASSPTLTSPMEYPS CCCCCCCCCCCCCCC	33.01	28450419
752	Phosphorylation	ASSPTLTSPMEYPSP CCCCCCCCCCCCCCC	25.92	25106551
756	Phosphorylation	TLTSPMEYPSPVNSL CCCCCCCCCCCCCCC	11.62	27794612
758	Phosphorylation	TSPMEYPSPVNSLHT CCCCCCCCCCCCCCC	40.35	27794612
759	Ubiquitination	SPMEYPSPVNSLHTP CCCCCCCCCCCCCCC	25.46	29967540
762	Phosphorylation	EYPSPVNSLHTPPLH CCCCCCCCCCCCCCC	23.05	27794612
765	Phosphorylation	SPVNSLHTPPLHRHN CCCCCCCCCCCCCCC	31.71	22617229
768	Ubiquitination	NSLHTPPLHRHNVFK CCCCCCCCCCCCCHH	6.12	29967540
778	Phosphorylation	HNVFKRHSMREEDFI CCCHHHHCCCCCCCC	24.46	23401153
801	Ubiquitination	QQLWEAEKVKMRQIL HHHHHHHHHHHHHHH	54.96	29967540
810	Ubiquitination	KMRQILDKQQKQMVE HHHHHHHHHHHHHHH	51.70	29967540
819	Phosphorylation	QKQMVEDYQWLRQEE HHHHHHHHHHHHHHH	6.51	22322096
828	Phosphorylation	WLRQEEKSLDPMVYM HHHHHHHCCCCCEEC	41.08	23090842
834	Phosphorylation	KSLDPMVYMNDKSPL HCCCCCEECCCCCCC	5.50	22115753
839	Phosphorylation	MVYMNDKSPLTPEKE CEECCCCCCCCCCCC	28.18	22115753
842	Phosphorylation	MNDKSPLTPEKEVGY CCCCCCCCCCCCCCE	32.55	22115753
849	Phosphorylation	TPEKEVGYLEFTGPP CCCCCCCEEEECCCC	14.29	21082442
853	Phosphorylation	EVGYLEFTGPPQKPP CCCEEEECCCCCCCC	39.13	30108239
858	Ubiquitination	EFTGPPQKPPRLGAQ EECCCCCCCCCCCCC	63.86	-
866	Phosphorylation	PPRLGAQSIQPTANL CCCCCCCCCCCCCCC	23.74	25159151
881	Phosphorylation	DRTDDLVYLNVMELV CCCCCCHHHHHHHHH	10.39	10880513
902	Ubiquitination	KNELCQLPPEGYVVV HHHHHCCCCCCEEEE	10.06	21890473
902 (in isoform 2)	Ubiquitination	-	10.06	21890473
906	Dephosphorylation	CQLPPEGYVVVVKNV HCCCCCCEEEEEECC	6.60	10880513
906	Phosphorylation	CQLPPEGYVVVVKNV HCCCCCCEEEEEECC	6.60	10880513
906	Ubiquitination	CQLPPEGYVVVVKNV HCCCCCCEEEEEECC	6.60	22817900
911	Ubiquitination	EGYVVVVKNVGLTLR CCEEEEEECCCHHHH	34.01	-
914	Ubiquitination	VVVVKNVGLTLRKLI EEEEECCCHHHHHHH	23.49	29967540
919	Ubiquitination	NVGLTLRKLIGSVDD CCCHHHHHHHCCHHH	47.79	21890473
923	Phosphorylation	TLRKLIGSVDDLLPS HHHHHHCCHHHHHHC	18.51	-
923	Ubiquitination	TLRKLIGSVDDLLPS HHHHHHCCHHHHHHC	18.51	22817900
931	Ubiquitination	VDDLLPSLPSSSRTE HHHHHHCCCCCCCCC	4.50	21890473
932	Ubiquitination	DDLLPSLPSSSRTEI HHHHHCCCCCCCCCC	36.18	21890473
935	Ubiquitination	LPSLPSSSRTEIEGT HHCCCCCCCCCCHHH	47.78	22817900
936	Ubiquitination	PSLPSSSRTEIEGTQ HCCCCCCCCCCHHHH	38.02	22817900
944	Ubiquitination	TEIEGTQKLLNKDLA CCCHHHHHHCCHHHH	55.57	22817900
944 (in isoform 1)	Ubiquitination	-	55.57	21890473
944	Ubiquitination	TEIEGTQKLLNKDLA CCCHHHHHHCCHHHH	55.57	21890473
948	Ubiquitination	GTQKLLNKDLAELIN HHHHHCCHHHHHHHH	54.83	22817900
956	Ubiquitination	DLAELINKMRLAQQN HHHHHHHHHHHHHHH	20.57	29967540
966	Phosphorylation	LAQQNAVTSLSEECK HHHHHHHHCCCHHHH	22.88	19060867
973	Acetylation	TSLSEECKRQMLTAS HCCCHHHHHHHHCCC	49.28	25953088
973	Ubiquitination	TSLSEECKRQMLTAS HCCCHHHHHHHHCCC	49.28	30230243
998	Ubiquitination	LDAVDQAKVLANLAH HHHHHHHHHHHHHCC	31.95	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
402	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
402	Y	Phosphorylation	Kinase	SYK	P43405	GPS
402	Y	Phosphorylation	Kinase	SRC	P12931	PSP
402	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
579	Y	Phosphorylation	Kinase	LCK	P06239	GPS
579	Y	Phosphorylation	Kinase	LYN	P07948	GPS
579	Y	Phosphorylation	Kinase	SRC	P12931	GPS
580	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot
580	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot
580	Y	Phosphorylation	Kinase	LYN	P07948	GPS
580	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
778	S	Phosphorylation	Kinase	PKACA	P17612	PSP
881	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAK2_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 FAK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGFI1_HUMAN	TGFB1I1	physical	11856738
CBL_HUMAN	CBL	physical	15128873
GELS_HUMAN	GSN	physical	12578912
DLG3_HUMAN	DLG3	physical	12576483
PTN6_HUMAN	PTPN6	physical	10747947
FYN_HUMAN	FYN	physical	9091579
FAK2_HUMAN	PTK2B	physical	9512511
JAK3_HUMAN	JAK3	physical	9512511
JAK1_HUMAN	JAK1	physical	10702271
IL7RA_HUMAN	IL7R	physical	10702271
PAXI_HUMAN	PXN	physical	9099734
KCNA2_HUMAN	KCNA2	physical	11739373
TGFI1_HUMAN	TGFB1I1	physical	9422762
PAXI_HUMAN	PXN	physical	9422762
LYN_HUMAN	LYN	physical	11311138
BCAR1_HUMAN	BCAR1	physical	9020138
CASL_HUMAN	NEDD9	physical	9020138
BCAR1_HUMAN	BCAR1	physical	11036077
PAXI_HUMAN	PXN	physical	11036077
PITM3_HUMAN	PITPNM3	physical	10022914
PITM1_HUMAN	PITPNM1	physical	10022914
PITM2_HUMAN	PITPNM2	physical	10022914
BCAR1_HUMAN	BCAR1	physical	8995252
ASAP2_HUMAN	ASAP2	physical	10022920
ITB2_HUMAN	ITGB2	physical	10961871
TLN1_HUMAN	TLN1	physical	9442086
ITB3_HUMAN	ITGB3	physical	11683411
PTN11_HUMAN	PTPN11	physical	10880513
PTN6_HUMAN	PTPN6	physical	10521452
GRB2_HUMAN	GRB2	physical	10329689
RBCC1_HUMAN	RB1CC1	physical	10769033
RBCC1_HUMAN	RB1CC1	genetic	10769033
VAV_HUMAN	VAV1	physical	10867021
FYN_HUMAN	FYN	physical	10867021
RASA1_HUMAN	RASA1	physical	10708762
ERBB2_HUMAN	ERBB2	physical	10713673
RASA1_HUMAN	RASA1	physical	10713673
MBD2_HUMAN	MBD2	physical	19661918
SOCS2_HUMAN	SOCS2	physical	20543098
SH3K1_HUMAN	SH3KBP1	physical	12771190
PDC6I_HUMAN	PDCD6IP	physical	12771190
CBL_HUMAN	CBL	physical	12771190
ALG2_HUMAN	ALG2	physical	12771190
SRC_HUMAN	SRC	physical	19380485
DYN1_HUMAN	DNM1	physical	19380485
GRB2_HUMAN	GRB2	physical	19380485
BCAR1_HUMAN	BCAR1	physical	12893833
SKAP2_HUMAN	SKAP2	physical	12893833
TAU_HUMAN	MAPT	physical	17512525
PAXI_HUMAN	PXN	physical	10980697
EGFR_HUMAN	EGFR	physical	10980697
ERBB2_HUMAN	ERBB2	physical	25241761

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
DB01097	Leflunomide

Regulatory Network of FAK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-15; SER-361;SER-375; SER-389; SER-392; SER-394; SER-396; SER-399; SER-559;TYR-579; TYR-580; SER-583; TYR-722; SER-746; SER-762; SER-778;TYR-819; TYR-834; SER-839; TYR-849; SER-866 AND THR-966, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-399; SER-758;SER-762; THR-765; SER-839 AND THR-842, AND MASS SPECTROMETRY.	18691976 [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-375, AND MASSSPECTROMETRY.	18088087 [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 SER-375 AND TYR-579, ANDMASS SPECTROMETRY.	17192257 [Abstract]
"T cell receptor activation leads to two distinct phases of Pyk2activation and actin cytoskeletal rearrangement in human T cells."; Collins M., Bartelt R.R., Houtman J.C.; Mol. Immunol. 47:1665-1674(2010). Cited for: FUNCTION IN T CELL RECEPTOR-MEDIATED SIGNALING, AND PHOSPHORYLATION ATTYR-402 AND TYR-580.	20381867 [Abstract]
"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402and 580 occurs via a distinct mechanism than other receptor systems."; Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B.,Houtman J.C.; J. Leukoc. Biol. 87:691-701(2010). Cited for: PHOSPHORYLATION AT TYR-402 AND TYR-580 BY FYN AND LCK.	20028775 [Abstract]
"Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-I-dependent mitogenic signaling in vascular smooth muscle cells."; Shen X., Xi G., Radhakrishnan Y., Clemmons D.R.; Cell. Mol. Life Sci. 67:3893-3903(2010). Cited for: FUNCTION IN IGF1 SIGNALING AND ACTIVATION OF MAPK1/ERK2 ANDMAPK3/ERK1, INTERACTION WITH SRC AND GRB2, PHOSPHORYLATION AT TYR-402AND TYR-881, AND MUTAGENESIS OF TYR-881.	20521079 [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-579 AND TYR-580, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiateRho activation."; Gao C., Blystone S.D.; Biochem. J. 420:49-56(2009). Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON REORGANIZATION ANDACTIVATION OF RHO FAMILY GTPASES, PHOSPHORYLATION AT TYR-402,SUBCELLULAR LOCATION, AND INTERACTION WITH VAV1.	19207108 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-580, AND MASSSPECTROMETRY.	17389395 [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-579 AND TYR-580, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancercells."; Sahu S.N., Nunez S., Bai G., Gupta A.; Am. J. Physiol. 292:C2288-C2296(2007). Cited for: INTERACTION WITH LPXN AND PTPN12, PHOSPHORYLATION AT TYR-402, ANDDEPHOSPHORYLATION BY PTPN12.	17329398 [Abstract]
"RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylationin a Src-independent manner."; Park S.Y., Avraham H.K., Avraham S.; J. Biol. Chem. 279:33315-33322(2004). Cited for: PHOSPHORYLATION AT TYR-402, CATALYTIC ACTIVITY, FUNCTION INSRC-MEDIATED PHOSPHORYLATION OF PXN, AND MUTAGENESIS OF LYS-457.	15166227 [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-579 AND TYR-580, ANDMASS SPECTROMETRY.	12522270 [Abstract]
"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggersphosphorylation of Pyk2."; Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.; Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001). Cited for: PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF PRO-859, AND INTERACTIONWITH NPHP1.	11493697 [Abstract]