dbPTM

LCK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LCK_HUMAN
UniProt AC	P06239
Protein Name	Tyrosine-protein kinase Lck
Gene Name	LCK
Organism	Homo sapiens (Human).
Sequence Length	509
Subcellular Localization	Cytoplasm . Cell membrane Lipid-anchor Cytoplasmic side . Present in lipid rafts in an inactive form.
Protein Description	Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2. [PubMed: 27335501]
Protein Sequence	MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGCGCSSHP ------CCCCCCCCC	19.27	-
2	Myristoylation	------MGCGCSSHP ------CCCCCCCCC	19.27	-
3	S-palmitoylation	-----MGCGCSSHPE -----CCCCCCCCCC	4.85	-
5	S-palmitoylation	---MGCGCSSHPEDD ---CCCCCCCCCCCC	4.36	8035816
25	Phosphorylation	DVCENCHYPIVPLDG CEECCCCCCEEECCC	9.24	26074081
35	Phosphorylation	VPLDGKGTLLIRNGS EECCCCCEEEEECCC	23.13	26074081
42	Phosphorylation	TLLIRNGSEVRDPLV EEEEECCCEECCCEE	36.15	20164059
42 (in isoform 3)	Phosphorylation	-	36.15	21406692
50	Phosphorylation	EVRDPLVTYEGSNPP EECCCEEEECCCCCC	24.44	26074081
50 (in isoform 3)	Phosphorylation	-	24.44	21406692
51	Phosphorylation	VRDPLVTYEGSNPPA ECCCEEEECCCCCCC	15.71	26074081
51 (in isoform 3)	Phosphorylation	-	15.71	27642862
54	Phosphorylation	PLVTYEGSNPPASPL CEEEECCCCCCCCCC	33.93	28464451
59	Phosphorylation	EGSNPPASPLQDNLV CCCCCCCCCCCCCEE	31.73	28787133
59 (in isoform 3)	Phosphorylation	-	31.73	27642862
71	Phosphorylation	NLVIALHSYEPSHDG CEEEEEEEECCCCCC	31.85	28464451
72	Phosphorylation	LVIALHSYEPSHDGD EEEEEEEECCCCCCC	22.55	28464451
75	Phosphorylation	ALHSYEPSHDGDLGF EEEEECCCCCCCCCC	23.44	26074081
84	Ubiquitination	DGDLGFEKGEQLRIL CCCCCCCCCCEEEEE	66.54	-
94	Phosphorylation	QLRILEQSGEWWKAQ EEEEEEECCCCEEEE	29.33	28464451
99	Ubiquitination	EQSGEWWKAQSLTTG EECCCCEEEEECCCC	37.31	-
99 (in isoform 3)	Ubiquitination	-	37.31	-
102	Phosphorylation	GEWWKAQSLTTGQEG CCCEEEEECCCCCCC	32.32	26074081
104	Phosphorylation	WWKAQSLTTGQEGFI CEEEEECCCCCCCEE	33.84	26074081
105	Phosphorylation	WKAQSLTTGQEGFIP EEEEECCCCCCCEEC	42.01	26074081
118	Ubiquitination	IPFNFVAKANSLEPE ECHHHEEECCCCCCC	42.68	-
121	Phosphorylation	NFVAKANSLEPEPWF HHEEECCCCCCCCCH	38.68	28464451
130	Ubiquitination	EPEPWFFKNLSRKDA CCCCCHHHCCCHHHH	47.72	-
130 (in isoform 3)	Ubiquitination	-	47.72	-
133	Phosphorylation	PWFFKNLSRKDAERQ CCHHHCCCHHHHHHH	46.83	23532336
147	Phosphorylation	QLLAPGNTHGSFLIR HHCCCCCCCCCEEEE	33.26	28464451
150	Phosphorylation	APGNTHGSFLIRESE CCCCCCCCEEEEECC	14.85	28464451
156	Phosphorylation	GSFLIRESESTAGSF CCEEEEECCCCCCEE	27.31	28122231
158	Phosphorylation	FLIRESESTAGSFSL EEEEECCCCCCEEEE	32.60	30576142
159	Phosphorylation	LIRESESTAGSFSLS EEEECCCCCCEEEEE	30.87	28464451
162	Phosphorylation	ESESTAGSFSLSVRD ECCCCCCEEEEEEEE	14.81	21082442
164	Phosphorylation	ESTAGSFSLSVRDFD CCCCCEEEEEEEEEC	22.79	30576142
166	Phosphorylation	TAGSFSLSVRDFDQN CCCEEEEEEEEECCC	17.57	30108239
179	Acetylation	QNQGEVVKHYKIRNL CCCCEEEEEEEEEEC	46.52	23749302
179	Ubiquitination	QNQGEVVKHYKIRNL CCCCEEEEEEEEEEC	46.52	19608861
179 (in isoform 3)	Ubiquitination	-	46.52	-
181	Phosphorylation	QGEVVKHYKIRNLDN CCEEEEEEEEEECCC	11.46	-
182	Ubiquitination	GEVVKHYKIRNLDNG CEEEEEEEEEECCCC	34.60	-
182 (in isoform 3)	Ubiquitination	-	34.60	-
192	Phosphorylation	NLDNGGFYISPRITF ECCCCCEEECCCEEC	12.08	19664994
192 (in isoform 3)	Phosphorylation	-	12.08	27642862
194	Phosphorylation	DNGGFYISPRITFPG CCCCEEECCCEECCC	9.21	21082442
198	Phosphorylation	FYISPRITFPGLHEL EEECCCEECCCHHHH	25.67	26546556
209	Phosphorylation	LHELVRHYTNASDGL HHHHHHHHCCCCCCC	7.36	28796482
210	Phosphorylation	HELVRHYTNASDGLC HHHHHHHCCCCCCCC	20.41	30108239
213	Phosphorylation	VRHYTNASDGLCTRL HHHHCCCCCCCCHHC	33.99	17192257
218	Phosphorylation	NASDGLCTRLSRPCQ CCCCCCCHHCCCCCC	39.42	28111955
228	Ubiquitination	SRPCQTQKPQKPWWE CCCCCCCCCCCCCCC	53.45	-
231	Ubiquitination	CQTQKPQKPWWEDEW CCCCCCCCCCCCCCC	51.65	-
246	Ubiquitination	EVPRETLKLVERLGA CCCHHHHHHHHHHCC	58.88	-
246 (in isoform 3)	Ubiquitination	-	58.88	-
246	Acetylation	EVPRETLKLVERLGA CCCHHHHHHHHHHCC	58.88	25953088
263	Phosphorylation	FGEVWMGYYNGHTKV CCCEEEEEECCCCEE	4.25	25147952
264	Phosphorylation	GEVWMGYYNGHTKVA CCEEEEEECCCCEEE	14.67	25147952
268	Phosphorylation	MGYYNGHTKVAVKSL EEEECCCCEEEEEHH	28.72	28122231
269	Ubiquitination	GYYNGHTKVAVKSLK EEECCCCEEEEEHHH	23.63	-
269 (in isoform 3)	Ubiquitination	-	23.63	-
273	Ubiquitination	GHTKVAVKSLKQGSM CCCEEEEEHHHCCCC	40.09	-
273 (in isoform 3)	Ubiquitination	-	40.09	-
273	Acetylation	GHTKVAVKSLKQGSM CCCEEEEEHHHCCCC	40.09	25953088
274	Phosphorylation	HTKVAVKSLKQGSMS CCEEEEEHHHCCCCC	33.91	24719451
276	Ubiquitination	KVAVKSLKQGSMSPD EEEEEHHHCCCCCHH	60.75	-
276 (in isoform 3)	Ubiquitination	-	60.75	-
281	Phosphorylation	SLKQGSMSPDAFLAE HHHCCCCCHHHHHHH	22.71	-
293	Ubiquitination	LAEANLMKQLQHQRL HHHHHHHHHHHHHHH	51.53	-
293 (in isoform 3)	Ubiquitination	-	51.53	-
313	Phosphorylation	VVTQEPIYIITEYME EECCCCEEEEEEECC	9.29	29438985
318	Phosphorylation	PIYIITEYMENGSLV CEEEEEEECCCCCEE	10.90	29438985
318 (in isoform 3)	Phosphorylation	-	10.90	26657352
323	Phosphorylation	TEYMENGSLVDFLKT EEECCCCCEEEEHHC	36.48	29438985
330	Phosphorylation	SLVDFLKTPSGIKLT CEEEEHHCCCCCEEH	25.49	29438985
335	Ubiquitination	LKTPSGIKLTINKLL HHCCCCCEEHHHHHH	43.00	-
335	Acetylation	LKTPSGIKLTINKLL HHCCCCCEEHHHHHH	43.00	25953088
365 (in isoform 3)	Ubiquitination	-	3.96	-
373	Phosphorylation	RAANILVSDTLSCKI HHHCEEEECCCCCEE	22.79	28122231
375	Phosphorylation	ANILVSDTLSCKIAD HCEEEECCCCCEEHH	17.05	28122231
377	Phosphorylation	ILVSDTLSCKIADFG EEEECCCCCEEHHHH	18.56	26546556
379	Ubiquitination	VSDTLSCKIADFGLA EECCCCCEEHHHHHH	37.24	-
393	Phosphorylation	ARLIEDNEYTAREGA HHHHCCCCCCCCCCC	57.49	17016520
394	Phosphorylation	RLIEDNEYTAREGAK HHHCCCCCCCCCCCC	16.38	19664994
394	Dephosphorylation	RLIEDNEYTAREGAK HHHCCCCCCCCCCCC	16.38	12589038
395	Phosphorylation	LIEDNEYTAREGAKF HHCCCCCCCCCCCCC	17.04	29255136
401	Ubiquitination	YTAREGAKFPIKWTA CCCCCCCCCCCEECC	63.63	-
401	Acetylation	YTAREGAKFPIKWTA CCCCCCCCCCCEECC	63.63	25953088
405	Ubiquitination	EGAKFPIKWTAPEAI CCCCCCCEECCCCCC	38.44	-
409 (in isoform 3)	Ubiquitination	-	24.95	-
414	Phosphorylation	TAPEAINYGTFTIKS CCCCCCCCCCEEEEC	16.07	25147952
416	Phosphorylation	PEAINYGTFTIKSDV CCCCCCCCEEEECHH	13.77	28122231
418	Phosphorylation	AINYGTFTIKSDVWS CCCCCCEEEECHHHH	27.60	28122231
431 (in isoform 3)	Ubiquitination	-	21.88	-
435 (in isoform 3)	Ubiquitination	-	25.03	-
441	Phosphorylation	VTHGRIPYPGMTNPE HHCCCCCCCCCCCHH	15.28	27174698
445	Phosphorylation	RIPYPGMTNPEVIQN CCCCCCCCCHHHHHH	54.24	27174698
457	Phosphorylation	IQNLERGYRMVRPDN HHHHHHHCCCCCCCC	11.19	27174698
470	Phosphorylation	DNCPEELYQLMRLCW CCCCHHHHHHHHHHH	11.68	28796482
478	Ubiquitination	QLMRLCWKERPEDRP HHHHHHHHCCCCCCC	42.73	-
489	Phosphorylation	EDRPTFDYLRSVLED CCCCCHHHHHHHHHH	10.38	-
492	Phosphorylation	PTFDYLRSVLEDFFT CCHHHHHHHHHHHHH	28.58	28796482
499	Phosphorylation	SVLEDFFTATEGQYQ HHHHHHHHHCCCCCC	32.44	28796482
500 (in isoform 3)	Phosphorylation	-	9.86	27642862
501	Phosphorylation	LEDFFTATEGQYQPQ HHHHHHHCCCCCCCC	37.28	21082442
505	Phosphorylation	FTATEGQYQPQP--- HHHCCCCCCCCC---	32.77	22322096
505	Dephosphorylation	FTATEGQYQPQP--- HHHCCCCCCCCC---	32.77	8663450
535 (in isoform 3)	Phosphorylation	-		27642862

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
42	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
42	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
42	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
42	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
59	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
59	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
59	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
192	Y	Phosphorylation	Kinase	SYK	P43405	GPS
394	Y	Phosphorylation	Kinase	LCK	P06239	PSP
394	Y	Phosphorylation	Kinase	AXL	P30530	PSP
394	Y	Phosphorylation	Kinase	YOPH	P08538	PSP
505	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
505	Y	Phosphorylation	Kinase	LCK	P06239	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:11904433
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P85A_HUMAN	PIK3R1	physical	8294442
U119A_HUMAN	UNC119	physical	14757743
PK3CA_HUMAN	PIK3CA	physical	14583609
NOTC1_HUMAN	NOTCH1	physical	14583609
CTND1_HUMAN	CTNND1	physical	12835311
FAK2_HUMAN	PTK2B	physical	9091579
CD44_HUMAN	CD44	physical	8576267
CBL_HUMAN	CBL	physical	11904433
KIT_HUMAN	KIT	physical	9788619
SKAP1_HUMAN	SKAP1	physical	9195899
PK3CA_HUMAN	PIK3CA	physical	8246987
PHAG1_HUMAN	PAG1	physical	10790433
TRAT1_HUMAN	TRAT1	physical	10790433
ZAP70_HUMAN	ZAP70	physical	10318843
PECA1_HUMAN	PECAM1	physical	9624175
TNR6_HUMAN	FAS	physical	8864141
SQSTM_HUMAN	SQSTM1	physical	8650207
RASA1_HUMAN	RASA1	physical	11389730
KSYK_HUMAN	SYK	physical	7539035
ZAP70_HUMAN	ZAP70	physical	7539035
PTN6_HUMAN	PTPN6	physical	8114715
PTPRC_HUMAN	PTPRC	physical	15085197
NEF_HV1H2	nef	physical	9778343
HS90A_HUMAN	HSP90AA1	physical	16888650
GCR_HUMAN	NR3C1	physical	16888650
KHDR1_HUMAN	KHDRBS1	physical	16888650
SH3K1_HUMAN	SH3KBP1	physical	15707590
SKAP1_HUMAN	SKAP1	physical	10229084
LAT_HUMAN	LAT	physical	14523017
CD3E_HUMAN	CD3E	physical	14523017
CD3Z_HUMAN	CD247	physical	14523017
F174A_HUMAN	FAM174A	physical	16274251
SOS1_HUMAN	SOS1	physical	16274251
KHDR1_HUMAN	KHDRBS1	physical	16274251
IL2RB_HUMAN	IL2RB	physical	21834013
CBL_HUMAN	CBL	physical	8626543
SOCS1_HUMAN	SOCS1	physical	21234523
SOCS2_HUMAN	SOCS2	physical	21234523
SOCS3_HUMAN	SOCS3	physical	21234523
CISH_HUMAN	CISH	physical	21234523
LCK_HUMAN	LCK	physical	20372794
ZAP70_HUMAN	ZAP70	physical	8798643
LAT_HUMAN	LAT	physical	16938345
KHDR1_HUMAN	KHDRBS1	physical	16107303
CBL_HUMAN	CBL	physical	16107303
WASP_HUMAN	WAS	physical	16107303
G3BP1_HUMAN	G3BP1	physical	15743820
MK01_HUMAN	MAPK1	physical	15967991
SMAD2_HUMAN	SMAD2	physical	16806069
SMAD3_HUMAN	SMAD3	physical	16806069
WASP_HUMAN	WAS	physical	16293614
WASL_HUMAN	WASL	physical	16293614
BAG6_HUMAN	BAG6	physical	22863785
CDKAL_HUMAN	CDKAL1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
DAF_HUMAN	CD55	physical	25241761
DLG1_HUMAN	DLG1	physical	25241761

Drug and Disease Associations

Kegg Disease
H00093	Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
OMIM Disease
	Note=A chromosomal aberration involving LCK is found in leukemias. Translocation t(1
	7)(p34
	q34) with TCRB.
615758
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LCK_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-179, 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-102; THR-159; SER-162;TYR-192; SER-194 AND TYR-505, AND MASS 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 SER-162; TYR-192; SER-213;TYR-394; THR-501 AND TYR-505, AND MASS SPECTROMETRY.	17192257 [Abstract]
"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 TYR-505, 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 TYR-505, AND MASSSPECTROMETRY.	18691976 [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-192 AND TYR-505, ANDMASS SPECTROMETRY.	18083107 [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-394 AND TYR-505, ANDMASS SPECTROMETRY.	15592455 [Abstract]
"Detection of a physical and functional interaction between Csk andLck which involves the SH2 domain of Csk and is mediated byautophosphorylation of Lck on tyrosine 394."; Bougeret C., Delaunay T., Romero F., Jullien P., Sabe H., Hanafusa H.,Benarous R., Fischer S.; J. Biol. Chem. 271:7465-7472(1996). Cited for: PHOSPHORYLATION AT TYR-505 BY CSK, AND AUTOPHOSPHORYLATION.	8631775 [Abstract]
"The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 anddown regulates its catalytic activity."; Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A.,Amrein K.E., Autero M., Burn P., Alitalo K.; EMBO J. 11:2919-2924(1992). Cited for: PHOSPHORYLATION AT TYR-505.	1639064 [Abstract]
"Oncogenic activation of the Lck protein accompanies translocation ofthe LCK gene in the human HSB2 T-cell leukemia."; Wright D.D., Sefton B.M., Kamps M.P.; Mol. Cell. Biol. 14:2429-2437(1994). Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-28; GLN-LYS-PRO-232 INS;VAL-353 AND LEU-447, AND PHOSPHORYLATION AT TYR-394 AND TYR-505.	8139546 [Abstract]