dbPTM

PTN6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN6_HUMAN
UniProt AC	P29350
Protein Name	Tyrosine-protein phosphatase non-receptor type 6
Gene Name	PTPN6
Organism	Homo sapiens (Human).
Sequence Length	595
Subcellular Localization	Cytoplasm. Nucleus. In neurons, translocates into the nucleus after treatment with angiotensin II (By similarity). Shuttles between the cytoplasm and nucleus via its association with PDPK1..
Protein Description	Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis..
Protein Sequence	MVRWFHRDLSGLDAETLLKGRGVHGSFLARPSRKNQGDFSLSVRVGDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGVLQDRDGTIIHLKYPLNCSDPTSERWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGLETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKGKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYIKNQLLGPDENAKTYIASQGCLEATVNDFWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGDLIREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEVLQSQKGQESEYGNITYPPAMKNAHAKASRTSSKHKEDVYENLHTKNKREEKVKKQRSADKEKSKGSLKRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RWFHRDLSGLDAETL CCCCCCCCCCCHHHH	41.41	23401153
10 (in isoform 4)	Phosphorylation	-	41.41	27251275
12 (in isoform 3)	Phosphorylation	-	5.18	24719451
16	Phosphorylation	LSGLDAETLLKGRGV CCCCCHHHHHCCCCC	38.83	30108239
19	Acetylation	LDAETLLKGRGVHGS CCHHHHHCCCCCCCE	50.07	25953088
19	Ubiquitination	LDAETLLKGRGVHGS CCHHHHHCCCCCCCE	50.07	21906983
19 (in isoform 1)	Ubiquitination	-	50.07	21890473
21 (in isoform 3)	Ubiquitination	-	42.23	21890473
26	Phosphorylation	KGRGVHGSFLARPSR CCCCCCCEEEECCCC	11.38	23401153
26 (in isoform 4)	Phosphorylation	-	11.38	27251275
32	Phosphorylation	GSFLARPSRKNQGDF CEEEECCCCCCCCCE	50.78	30108239
34	Ubiquitination	FLARPSRKNQGDFSL EEECCCCCCCCCEEE	58.94	-
40	Phosphorylation	RKNQGDFSLSVRVGD CCCCCCEEEEEEECC	25.19	30108239
42	Phosphorylation	NQGDFSLSVRVGDQV CCCCEEEEEEECCEE	13.48	30108239
57	Phosphorylation	THIRIQNSGDFYDLY EEEEECCCCCCCCCC	24.30	30108239
57 (in isoform 4)	Phosphorylation	-	24.30	27251275
61	Phosphorylation	IQNSGDFYDLYGGEK ECCCCCCCCCCCCEE	15.13	28796482
63 (in isoform 3)	Phosphorylation	-	2.66	27642862
64	Phosphorylation	SGDFYDLYGGEKFAT CCCCCCCCCCEEEEE	21.86	28796482
66 (in isoform 3)	Phosphorylation	-	22.74	25147952
97	Acetylation	DGTIIHLKYPLNCSD CCCEEEEEEECCCCC	30.57	25953088
97	Ubiquitination	DGTIIHLKYPLNCSD CCCEEEEEEECCCCC	30.57	-
98	Phosphorylation	GTIIHLKYPLNCSDP CCEEEEEEECCCCCC	21.22	-
111	Phosphorylation	DPTSERWYHGHMSGG CCCCCCEEECCCCCC	12.25	-
116	Phosphorylation	RWYHGHMSGGQAETL CEEECCCCCCCHHHH	33.81	24247654
138	Phosphorylation	WTFLVRESLSQPGDF CEEEEEECCCCCCCE	23.82	26657352
140	Phosphorylation	FLVRESLSQPGDFVL EEEEECCCCCCCEEE	43.54	26657352
140 (in isoform 4)	Phosphorylation	-	43.54	27251275
151	O-linked_Glycosylation	DFVLSVLSDQPKAGP CEEEEEECCCCCCCC	31.85	30379171
155	Ubiquitination	SVLSDQPKAGPGSPL EEECCCCCCCCCCCC	61.41	-
160	Phosphorylation	QPKAGPGSPLRVTHI CCCCCCCCCCEEEEE	24.72	25003641
168	Ubiquitination	PLRVTHIKVMCEGGR CCEEEEEEEEECCCC	19.13	-
176	Phosphorylation	VMCEGGRYTVGGLET EEECCCCEEECCEEC	14.73	-
177	Phosphorylation	MCEGGRYTVGGLETF EECCCCEEECCEECC	16.00	22115753
183	Phosphorylation	YTVGGLETFDSLTDL EEECCEECCCHHHHH	37.47	28450419
186	Phosphorylation	GGLETFDSLTDLVEH CCEECCCHHHHHHHH	29.04	28450419
188	Phosphorylation	LETFDSLTDLVEHFK EECCCHHHHHHHHHH	31.10	26657352
195	Ubiquitination	TDLVEHFKKTGIEEA HHHHHHHHHHCCHHC	51.86	-
196	Ubiquitination	DLVEHFKKTGIEEAS HHHHHHHHHCCHHCC	51.55	-
213	Phosphorylation	FVYLRQPYYATRVNA EEEECCCCCEECCCH	9.44	-
214	Phosphorylation	VYLRQPYYATRVNAA EEECCCCCEECCCHH	14.26	25839225
232	Ubiquitination	NRVLELNKKQESEDT HHHHHHHCCCCCHHH	69.34	-
233	Ubiquitination	RVLELNKKQESEDTA HHHHHHCCCCCHHHH	59.22	-
236	Phosphorylation	ELNKKQESEDTAKAG HHHCCCCCHHHHHHC	37.97	30624053
238 (in isoform 2)	Ubiquitination	-	62.33	21890473
241	Ubiquitination	QESEDTAKAGFWEEF CCCHHHHHHCHHHHH	51.65	-
250	O-linked_Glycosylation	GFWEEFESLQKQEVK CHHHHHHHHHHHHHH	41.23	30379171
250	Phosphorylation	GFWEEFESLQKQEVK CHHHHHHHHHHHHHH	41.23	28450419
250 (in isoform 4)	Phosphorylation	-	41.23	27251275
253	Ubiquitination	EEFESLQKQEVKNLH HHHHHHHHHHHHHHH	54.44	-
257	Ubiquitination	SLQKQEVKNLHQRLE HHHHHHHHHHHHHHC	53.70	-
271	Ubiquitination	EGQRPENKGKNRYKN CCCCCCCCCCCCCCC	70.38	-
276	Phosphorylation	ENKGKNRYKNILPFD CCCCCCCCCCCCCCC	20.13	28796482
277	Acetylation	NKGKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	19608861
277	Ubiquitination	NKGKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	21890473
277 (in isoform 1)	Ubiquitination	-	33.98	21890473
277	Ubiquitination	NKGKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	21890473
278 (in isoform 3)	Phosphorylation	-	31.90	27642862
279 (in isoform 3)	Ubiquitination	-	4.52	21890473
285	Phosphorylation	NILPFDHSRVILQGR CCCCCCCCEEEEECC	30.04	23312004
286	Methylation	ILPFDHSRVILQGRD CCCCCCCEEEEECCC	18.97	115916953
294	Phosphorylation	VILQGRDSNIPGSDY EEEECCCCCCCCCCC	34.99	30108239
299	Phosphorylation	RDSNIPGSDYINANY CCCCCCCCCCCCHHH	23.14	28796482
301	Phosphorylation	SNIPGSDYINANYIK CCCCCCCCCCHHHHC	9.58	28796482
303 (in isoform 3)	Phosphorylation	-	18.86	27642862
306	Phosphorylation	SDYINANYIKNQLLG CCCCCHHHHCCCCCC	15.74	28796482
308	Ubiquitination	YINANYIKNQLLGPD CCCHHHHCCCCCCCC	28.42	-
308 (in isoform 3)	Phosphorylation	-	28.42	27642862
350	O-linked_Glycosylation	NSRVIVMTTREVEKG CCEEEEEECCCHHCC	16.29	30379171
352 (in isoform 2)	Ubiquitination	-	36.48	21890473
360	Ubiquitination	EVEKGRNKCVPYWPE CHHCCCCCCCCCCCC	34.94	-
364	Phosphorylation	GRNKCVPYWPEVGMQ CCCCCCCCCCCCCCC	17.13	-
374	Phosphorylation	EVGMQRAYGPYSVTN CCCCCEECCCCCCCC	22.33	28796482
377	Phosphorylation	MQRAYGPYSVTNCGE CCEECCCCCCCCCCC	16.06	28796482
378	Phosphorylation	QRAYGPYSVTNCGEH CEECCCCCCCCCCCC	26.12	28796482
379 (in isoform 3)	Phosphorylation	-	3.53	27642862
380	Phosphorylation	AYGPYSVTNCGEHDT ECCCCCCCCCCCCCC	20.89	28796482
387	Phosphorylation	TNCGEHDTTEYKLRT CCCCCCCCCEEEECE	24.35	28796482
388	Phosphorylation	NCGEHDTTEYKLRTL CCCCCCCCEEEECEE	43.29	28796482
390	Phosphorylation	GEHDTTEYKLRTLQV CCCCCCEEEECEEEE	17.15	28796482
391	Ubiquitination	EHDTTEYKLRTLQVS CCCCCEEEECEEEEC	25.84	2190698
391 (in isoform 1)	Ubiquitination	-	25.84	21890473
393 (in isoform 3)	Ubiquitination	-	29.28	21890473
394	Phosphorylation	TTEYKLRTLQVSPLD CCEEEECEEEECCCC	31.79	28450419
398	Phosphorylation	KLRTLQVSPLDNGDL EECEEEECCCCCCHH	13.54	30108239
453	S-nitrosocysteine	AGPIIVHCSAGIGRT CCCEEEECCCCCCCC	1.75	-
453	S-nitrosylation	AGPIIVHCSAGIGRT CCCEEEECCCCCCCC	1.75	22178444
462	Phosphorylation	AGIGRTGTIIVIDML CCCCCCCEEEEECCC	13.61	28674151
474	Phosphorylation	DMLMENISTKGLDCD CCCCCCCCCCCCCCC	35.33	28674151
486	Ubiquitination	DCDIDIQKTIQMVRA CCCCCHHHHHHHHHH	48.18	-
496	Phosphorylation	QMVRAQRSGMVQTEA HHHHHHHCCCCCCHH	21.11	-
509	Phosphorylation	EAQYKFIYVAIAQFI HHHHHHHHHHHHHHH	6.22	19060867
521	Ubiquitination	QFIETTKKKLEVLQS HHHHHHHHHHHHHHH	61.57	-
522	Ubiquitination	FIETTKKKLEVLQSQ HHHHHHHHHHHHHHC	51.97	-
528	Phosphorylation	KKLEVLQSQKGQESE HHHHHHHHCCCCCCC	29.69	24247654
528 (in isoform 4)	Phosphorylation	-	29.69	27251275
530	Ubiquitination	LEVLQSQKGQESEYG HHHHHHCCCCCCCCC	68.74	-
530 (in isoform 3)	Phosphorylation	-	68.74	27642862
534	Phosphorylation	QSQKGQESEYGNITY HHCCCCCCCCCCCCC	28.38	21945579
534 (in isoform 4)	Phosphorylation	-	28.38	27251275
536	Phosphorylation	QKGQESEYGNITYPP CCCCCCCCCCCCCCH	25.42	21945579
536 (in isoform 3)	Phosphorylation	-	25.42	27642862
536 (in isoform 4)	Phosphorylation	-	25.42	27251275
538 (in isoform 3)	Phosphorylation	-	23.64	27642862
540	Phosphorylation	ESEYGNITYPPAMKN CCCCCCCCCCHHHHH	33.69	21945579
541	Phosphorylation	SEYGNITYPPAMKNA CCCCCCCCCHHHHHH	11.92	21945579
543 (in isoform 3)	Phosphorylation	-	34.27	27642862
546	Ubiquitination	ITYPPAMKNAHAKAS CCCCHHHHHHHHHHH	53.76	-
553	Phosphorylation	KNAHAKASRTSSKHK HHHHHHHHCCCHHHH	35.07	26074081
555	Phosphorylation	AHAKASRTSSKHKED HHHHHHCCCHHHHHH	34.55	23927012
556	Phosphorylation	HAKASRTSSKHKEDV HHHHHCCCHHHHHHH	35.96	23927012
557	Phosphorylation	AKASRTSSKHKEDVY HHHHCCCHHHHHHHH	37.86	23401153
557 (in isoform 3)	Phosphorylation	-	37.86	27642862
558 (in isoform 3)	Phosphorylation	-	59.47	24719451
559 (in isoform 3)	Phosphorylation	-	40.46	27642862
560	Ubiquitination	SRTSSKHKEDVYENL HCCCHHHHHHHHHHH	60.38	-
563 (in isoform 4)	Phosphorylation	-	7.28	-
564	Phosphorylation	SKHKEDVYENLHTKN HHHHHHHHHHHHHCC	16.06	21945579
566 (in isoform 3)	Phosphorylation	-	21.31	25147952
569	Phosphorylation	DVYENLHTKNKREEK HHHHHHHHCCHHHHH	39.21	21945579
570	Ubiquitination	VYENLHTKNKREEKV HHHHHHHCCHHHHHH	50.12	-
582	Phosphorylation	EKVKKQRSADKEKSK HHHHHHHHHHHHHHC	38.02	-
588	Phosphorylation	RSADKEKSKGSLKRK HHHHHHHHCCCCCCC	43.25	-
591	Phosphorylation	DKEKSKGSLKRK--- HHHHHCCCCCCC---	34.16	15269224

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
536	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
536	Y	Phosphorylation	Kinase	INSR	P06213	PSP
536	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
536	Y	Phosphorylation	Kinase	LCK	P06239	PSP
536	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
536	Y	Phosphorylation	Kinase	LYN	P07948	PSP
536	Y	Phosphorylation	Kinase	SRC	P12931	PSP
538	Y	Phosphorylation	Kinase	INSR	P06213	GPS
538	Y	Phosphorylation	Kinase	PDGFRB	P09619	GPS
553	S	Phosphorylation	Kinase	PKG2	Q13237	PSP
556	S	Phosphorylation	Kinase	PKG2	Q13237	PSP
557	S	Phosphorylation	Kinase	PKG2	Q13237	PSP
564	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
564	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
564	Y	Phosphorylation	Kinase	SRC	P12931	PSP
564	Y	Phosphorylation	Kinase	LYN	P07948	Uniprot
564	Y	Phosphorylation	Kinase	LCK	P06239	PSP
564	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
591	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTN6_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 PTN6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCR_HUMAN	BCR	physical	9788431
CD72_HUMAN	CD72	physical	12882840
CD22_HUMAN	CD22	physical	9890995
FAK2_HUMAN	PTK2B	physical	10747947
KSYK_HUMAN	SYK	physical	10747947
ROS1_HUMAN	ROS1	physical	11266449
LCP2_HUMAN	LCP2	physical	9765283
LCK_HUMAN	LCK	physical	10617656
IL3RB_HUMAN	CSF2RB	physical	8246974
INSR_HUMAN	INSR	physical	7512963
LAIR1_HUMAN	LAIR1	physical	11160222
P85A_HUMAN	PIK3R1	physical	11160222
EPOR_HUMAN	EPOR	physical	7889566
NOS1_HUMAN	NOS1	physical	11511520
PHAG1_HUMAN	PAG1	physical	10790433
CAV1_HUMAN	CAV1	physical	12176037
HXA10_HUMAN	HOXA10	physical	12145285
TYK2_HUMAN	TYK2	physical	7629131
JAK1_HUMAN	JAK1	physical	7629131
SSR2_HUMAN	SSTR2	physical	9305905
EGFR_HUMAN	EGFR	physical	9733788
KIT_HUMAN	KIT	physical	9528781
KIT_HUMAN	KIT	physical	7684496
LAIR1_HUMAN	LAIR1	physical	10660620
SHPS1_HUMAN	SIRPA	physical	10660620
PILRA_HUMAN	PILRA	physical	10660620
LAIR1_HUMAN	LAIR1	physical	10764762
CTND1_HUMAN	CTNND1	physical	10835420
KPCD_HUMAN	PRKCD	physical	11723252
KSYK_HUMAN	SYK	physical	10072516
BLNK_HUMAN	BLNK	physical	11356834
CD22_HUMAN	CD22	physical	11356834
FAK2_HUMAN	PTK2B	physical	10521452
SHPS1_HUMAN	SIRPA	physical	10660565
LCP2_HUMAN	LCP2	physical	8760799
LCK_HUMAN	LCK	physical	11294838
STA5B_HUMAN	STAT5B	physical	9211920
THIO_HUMAN	TXN	physical	19561639
SMAG2_HUMAN	SAMD4B	physical	22939629
SIG12_MOUSE	Siglece	physical	11171044
AIMP1_HUMAN	AIMP1	physical	26344197
SYDC_HUMAN	DARS	physical	26344197
PTN2_HUMAN	PTPN2	physical	26344197
TRIP6_HUMAN	TRIP6	physical	26344197
SYVC_HUMAN	VARS	physical	26344197
OLIG1_HUMAN	OLIG1	physical	25814554
FAK1_HUMAN	PTK2	physical	25814554
LAT_HUMAN	LAT	physical	27221712
PLCG1_HUMAN	PLCG1	physical	27221712
PLCG2_HUMAN	PLCG2	physical	27221712
ERBB4_HUMAN	ERBB4	physical	28065597
PTN12_HUMAN	PTPN12	physical	28514442
PTN6_HUMAN	PTPN6	physical	27432908
NUD16_HUMAN	NUDT16	physical	27432908
NMNA1_HUMAN	NMNAT1	physical	27432908
PTN12_HUMAN	PTPN12	physical	27432908
BCR_HUMAN	BCR	physical	27432908
MACD1_HUMAN	MACROD1	physical	27432908
RL7L_HUMAN	RPL7L1	physical	27432908
AROS_HUMAN	RPS19BP1	physical	27432908
RL37A_HUMAN	RPL37A	physical	27432908
BRX1_HUMAN	BRIX1	physical	27432908
SRP14_HUMAN	SRP14	physical	27432908
RL36L_HUMAN	RPL36AL	physical	27432908
G45IP_HUMAN	GADD45GIP1	physical	27432908
RL30_HUMAN	RPL30	physical	27432908
EBP2_HUMAN	EBNA1BP2	physical	27432908
DIM1_HUMAN	DIMT1	physical	27432908
RPF2_HUMAN	RPF2	physical	27432908
RRS1_HUMAN	RRS1	physical	27432908
CH033_HUMAN	C8orf33	physical	27432908
RL35A_HUMAN	RPL35A	physical	27432908
SRSF5_HUMAN	SRSF5	physical	27432908
CLH2_HUMAN	CLTCL1	physical	27432908
PA2G4_HUMAN	PA2G4	physical	27432908
RL18A_HUMAN	RPL18A	physical	27432908
RL22L_HUMAN	RPL22L1	physical	27432908
RPP30_HUMAN	RPP30	physical	27432908
CDK1_HUMAN	CDK1	physical	14699166

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 PTN6_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-277, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-10; TYR-64 AND TYR-564,AND MASS SPECTROMETRY.	19690332 [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-536, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-509, AND MASSSPECTROMETRY.	18187866 [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-536 AND TYR-564, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Functional interaction between SHPTP1 and the Lyn tyrosine kinase inthe apoptotic response to DNA damage."; Yoshida K., Kharbanda S., Kufe D.; J. Biol. Chem. 274:34663-34668(1999). Cited for: INTERACTION WITH LYN, AND PHOSPHORYLATION AT TYR-564.	10574931 [Abstract]