dbPTM

FYN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FYN_HUMAN
UniProt AC	P06241
Protein Name	Tyrosine-protein kinase Fyn
Gene Name	FYN
Organism	Homo sapiens (Human).
Sequence Length	537
Subcellular Localization	Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking.
Protein Description	Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1..
Protein Sequence	MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGCVQCKDK ------CCCEECCCH	21.94	-
2	Myristoylation	------MGCVQCKDK ------CCCEECCCH	21.94	1699196
3	S-palmitoylation	-----MGCVQCKDKE -----CCCEECCCHH	1.52	7673226
6	S-palmitoylation	--MGCVQCKDKEATK --CCCEECCCHHHCC	2.84	7673226
12	Phosphorylation	QCKDKEATKLTEERD ECCCHHHCCCCCCCC	27.90	24732914
13	Ubiquitination	CKDKEATKLTEERDG CCCHHHCCCCCCCCC	61.53	21963094
15	Phosphorylation	DKEATKLTEERDGSL CHHHCCCCCCCCCCC	37.04	19369195
21	Phosphorylation	LTEERDGSLNQSSGY CCCCCCCCCCCCCCC	28.56	29255136
25	Phosphorylation	RDGSLNQSSGYRYGT CCCCCCCCCCCCCCC	25.34	22167270
26	Phosphorylation	DGSLNQSSGYRYGTD CCCCCCCCCCCCCCC	30.04	23401153
28	Phosphorylation	SLNQSSGYRYGTDPT CCCCCCCCCCCCCCC	11.56	21082442
30	Phosphorylation	NQSSGYRYGTDPTPQ CCCCCCCCCCCCCCC	18.85	9425276
39	Phosphorylation	TDPTPQHYPSFGVTS CCCCCCCCCCCCCCC	8.70	25884760
91	Phosphorylation	VTLFVALYDYEARTE EEEEEEEEECCCCCC	13.52	25884760
132	Phosphorylation	LTTGETGYIPSNYVA CCCCCCCCCCCCCEE	19.65	27196784
178	Phosphorylation	GTFLIRESETTKGAY CEEEEEECCCCCCEE	30.32	28152594
180	Phosphorylation	FLIRESETTKGAYSL EEEEECCCCCCEEEE	42.99	28152594
181	Phosphorylation	LIRESETTKGAYSLS EEEECCCCCCEEEEE	24.35	28152594
182 (in isoform 1)	Ubiquitination	-	49.30	21890473
182	Ubiquitination	IRESETTKGAYSLSI EEECCCCCCEEEEEE	49.30	21890473
182	Ubiquitination	IRESETTKGAYSLSI EEECCCCCCEEEEEE	49.30	23000965
182 (in isoform 2)	Ubiquitination	-	49.30	21890473
182 (in isoform 3)	Ubiquitination	-	49.30	21890473
185	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEEEH	20.86	30266825
186	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEEEHH	18.33	30266825
188	Phosphorylation	TKGAYSLSIRDWDDM CCCEEEEEEEEHHHC	15.05	28152594
196	Ubiquitination	IRDWDDMKGDHVKHY EEEHHHCCCCCEEEE	69.08	29967540
213	Phosphorylation	RKLDNGGYYITTRAQ EECCCCCEEEEEHHH	7.97	21945579
214	Phosphorylation	KLDNGGYYITTRAQF ECCCCCEEEEEHHHH	8.61	21945579
216	Phosphorylation	DNGGYYITTRAQFET CCCCEEEEEHHHHHH	8.29	21945579
217	Phosphorylation	NGGYYITTRAQFETL CCCEEEEEHHHHHHH	17.91	21945579
254	Phosphorylation	HKGMPRLTDLSVKTK CCCCCCCCCCCEECC	35.85	23312004
257	Phosphorylation	MPRLTDLSVKTKDVW CCCCCCCCEECCCHH	25.11	17192257
259	Ubiquitination	RLTDLSVKTKDVWEI CCCCCCEECCCHHHC	46.62	32015554
261	Ubiquitination	TDLSVKTKDVWEIPR CCCCEECCCHHHCCH	44.56	29967540
264	Ubiquitination	SVKTKDVWEIPRESL CEECCCHHHCCHHHH	14.13	29967540
267 (in isoform 2)	Phosphorylation	-	23.59	28634120
272	Ubiquitination	EIPRESLQLIKRLGN HCCHHHHHHHHHHCC	50.88	29967540
275	Ubiquitination	RESLQLIKRLGNGQF HHHHHHHHHHCCCCC	50.60	-
289	Phosphorylation	FGEVWMGTWNGNTKV CCEEEEEECCCCEEE	10.31	-
294	Phosphorylation	MGTWNGNTKVAIKTL EEECCCCEEEEEEEE	28.44	-
299	Ubiquitination	GNTKVAIKTLKPGTM CCEEEEEEEECCCCC	37.76	-
300	Ubiquitination	NTKVAIKTLKPGTMS CEEEEEEEECCCCCC	33.62	29967540
300	Phosphorylation	NTKVAIKTLKPGTMS CEEEEEEEECCCCCC	33.62	-
302	Ubiquitination	KVAIKTLKPGTMSPE EEEEEEECCCCCCHH	46.78	-
305	Phosphorylation	IKTLKPGTMSPESFL EEEECCCCCCHHHHH	24.01	29759185
307	Phosphorylation	TLKPGTMSPESFLEE EECCCCCCHHHHHHH	25.92	29759185
316	Ubiquitination	ESFLEEAQIMKKLKH HHHHHHHHHHHHCCC	39.32	29967540
319	Ubiquitination	LEEAQIMKKLKHDKL HHHHHHHHHCCCCCE	57.49	29967540
339	Phosphorylation	VVSEEPIYIVTEYMN EECCCCEEEEEEECC	10.47	22817900
349	Phosphorylation	TEYMNKGSLLDFLKD EEECCCCCHHHHHHC	27.63	21712546
352	Ubiquitination	MNKGSLLDFLKDGEG CCCCCHHHHHHCCCC	52.72	29967540
355	Ubiquitination	GSLLDFLKDGEGRAL CCHHHHHHCCCCCCC	64.78	29967540
365	Phosphorylation	EGRALKLPNLVDMAA CCCCCCCCCHHHHHH	30.44	32142685
372	Ubiquitination	PNLVDMAAQVAAGMA CCHHHHHHHHHHHHH	9.57	22817900
376	Ubiquitination	DMAAQVAAGMAYIER HHHHHHHHHHHHHHH	14.94	21890473
376 (in isoform 3)	Ubiquitination	-	14.94	21890473
405	Ubiquitination	VGNGLICKIADFGLA ECCCEEEEEHHHHHH	33.66	-
417	Phosphorylation	GLARLIEDNEYTARQ HHHHHHCCCCCCCCC	46.39	32142685
420	Dephosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	11983687
420	Phosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	19664994
421	Phosphorylation	LIEDNEYTARQGAKF HHCCCCCCCCCCCCC	14.80	29255136
424	Ubiquitination	DNEYTARQGAKFPIK CCCCCCCCCCCCCCE	54.45	22817900
427	Acetylation	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	25953088
427	Malonylation	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	26320211
427	Ubiquitination	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	22817900
428 (in isoform 2)	Ubiquitination	-	8.19	21890473
428	Ubiquitination	TARQGAKFPIKWTAP CCCCCCCCCCEECCC	8.19	21890473
431	Ubiquitination	QGAKFPIKWTAPEAA CCCCCCCEECCCCHH	38.44	21890473
431 (in isoform 1)	Ubiquitination	-	38.44	21890473
431	Ubiquitination	QGAKFPIKWTAPEAA CCCCCCCEECCCCHH	38.44	21890473
440	Phosphorylation	TAPEAALYGRFTIKS CCCCHHHHCCEEECC	11.09	27273156
449	Ubiquitination	RFTIKSDVWSFGILL CEEECCCHHHHHHHH	6.27	32015554
457	Phosphorylation	WSFGILLTELVTKGR HHHHHHHHHHHHCCC	24.67	20068231
467	Phosphorylation	VTKGRVPYPGMNNRE HHCCCCCCCCCCHHH	15.01	27174698
483	Phosphorylation	LEQVERGYRMPCPQD HHHHHHHCCCCCCCC	15.23	-
501	Ubiquitination	SLHELMIHCWKKDPE CHHHHHHHHHCCCHH	9.45	32015554
504	Ubiquitination	ELMIHCWKKDPEERP HHHHHHHCCCHHHCC	53.33	32015554
512	Phosphorylation	KDPEERPTFEYLQSF CCHHHCCHHHHHHHH	35.01	26356563
515	Phosphorylation	EERPTFEYLQSFLED HHCCHHHHHHHHHHH	13.07	20068231
518	Phosphorylation	PTFEYLQSFLEDYFT CHHHHHHHHHHHHHC	29.24	20068231
523	Phosphorylation	LQSFLEDYFTATEPQ HHHHHHHHHCCCCCC	8.08	20068231
525	Phosphorylation	SFLEDYFTATEPQYQ HHHHHHHCCCCCCCC	26.83	18691976
527	Phosphorylation	LEDYFTATEPQYQPG HHHHHCCCCCCCCCC	45.18	20068231
531	Phosphorylation	FTATEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	27273156
531	Dephosphorylation	FTATEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	9535845

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
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
21	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
28	Y	Phosphorylation	Kinase	FYN	P06241	PSP
28	Y	Phosphorylation	Kinase	PGFRB	P09619	PhosphoELM
30	Y	Phosphorylation	Kinase	FYN	P06241	PSP
39	Y	Phosphorylation	Kinase	FYN	P06241	PSP
185	Y	Phosphorylation	Kinase	FYN	P06241	PSP
213	Y	Phosphorylation	Kinase	FYN	P06241	PSP
214	Y	Phosphorylation	Kinase	FYN	P06241	PSP
420	Y	Phosphorylation	Kinase	FYN	P06241	PSP
420	Y	Phosphorylation	Kinase	AXL	P30530	PSP
531	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
531	Y	Phosphorylation	Kinase	CSK	P41241	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:15190072
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
3	C	Palmitoylation	-
Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.
6	C	Palmitoylation	-
Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.
12	T	Phosphorylation	15537652
Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus.

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 FYN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P85A_HUMAN	PIK3R1	physical	8294442
TRPC6_HUMAN	TRPC6	physical	14761972
U119A_HUMAN	UNC119	physical	14757743
NMDE1_HUMAN	GRIN2A	physical	12932824
CTND1_HUMAN	CTNND1	physical	12835311
RHG32_HUMAN	ARHGAP32	physical	12788081
NPHN_HUMAN	NPHS1	physical	12668668
CTNB1_HUMAN	CTNNB1	physical	12640114
CTND1_HUMAN	CTNND1	physical	12640114
CADH1_HUMAN	CDH1	physical	12640114
MTA1_MOUSE	Mta1	physical	11483358
MTA3_MOUSE	Mta3	physical	11483358
WASP_HUMAN	WAS	physical	8805332
ACHA7_HUMAN	CHRNA7	physical	11278378
JAK2_HUMAN	JAK2	physical	10551884
NMDE1_HUMAN	GRIN2A	physical	9892651
DLG4_HUMAN	DLG4	physical	9892651
KHDR1_HUMAN	KHDRBS1	physical	11960376
GRB10_HUMAN	GRB10	physical	10871840
3BP2_HUMAN	SH3BP2	physical	9846481
SOCS1_HUMAN	SOCS1	physical	10022833
KPCT_HUMAN	PRKCQ	physical	10383400
CBLC_HUMAN	CBLC	physical	10571044
P85B_HUMAN	PIK3R2	physical	1334406
PLCG2_HUMAN	PLCG2	physical	8395016
DLG4_HUMAN	DLG4	physical	12419528
NMDE1_HUMAN	GRIN2A	physical	12419528
GAB3_HUMAN	GAB3	physical	11739737
SKAP2_HUMAN	SKAP2	physical	9837776
CDK1_HUMAN	CDK1	physical	8910336
ADDB_HUMAN	ADD2	physical	11526103
FYB1_HUMAN	FYB	physical	7504057
RAF1_HUMAN	RAF1	physical	7517401
SKAP1_HUMAN	SKAP1	physical	9195899
TBA3C_HUMAN	TUBA3C	physical	11826099
TAU_HUMAN	MAPT	physical	11826099
VAV_HUMAN	VAV1	physical	9822663
NTRK2_HUMAN	NTRK2	physical	9648856
SLAF1_HUMAN	SLAMF1	physical	12545174
SH21A_HUMAN	SH2D1A	physical	12545174
PECA1_HUMAN	PECAM1	physical	10858437
PHAG1_HUMAN	PAG1	physical	10790433
TRAT1_HUMAN	TRAT1	physical	10790433
CBL_HUMAN	CBL	physical	12244174
NMT1_HUMAN	NMT1	physical	11594778
CSF1R_HUMAN	CSF1R	physical	7681396
SYUA_HUMAN	SNCA	physical	11162638
EPHB3_HUMAN	EPHB3	physical	9674711
ADA15_HUMAN	ADAM15	physical	11741929
PTN11_HUMAN	PTPN11	physical	10212213
RL10_HUMAN	RPL10	physical	12138090
EFS_MOUSE	Efs	physical	9750131
SKAP1_HUMAN	SKAP1	physical	12171928
TM1L1_HUMAN	TOM1L1	physical	11711534
BCL3_HUMAN	BCL3	physical	9576921
TNR6_HUMAN	FAS	physical	8626376
TNFL6_HUMAN	FASLG	physical	7589480
FYN_HUMAN	FYN	physical	7687536
PTPRA_HUMAN	PTPRA	physical	9535845
PTN5_HUMAN	PTPN5	physical	11983687
EPHA4_HUMAN	EPHA4	physical	12084815
CD36_HUMAN	CD36	physical	7521304
TYK2_HUMAN	TYK2	physical	9196040
CBL_HUMAN	CBL	physical	9535867
KSYK_HUMAN	SYK	physical	9535867
ACK1_HUMAN	TNK2	physical	11087735
RACK1_HUMAN	GNB2L1	physical	11943848
FAK2_HUMAN	PTK2B	physical	9104812
EPHA3_HUMAN	EPHA3	physical	9632142
SKAP1_HUMAN	SKAP1	physical	9748251
FYB1_HUMAN	FYB	physical	9748251
TNFL6_HUMAN	FASLG	physical	17164290
ITCH_HUMAN	ITCH	physical	16387660
NEF_HV1H2	nef	physical	8681387
NEF_HV1H2	nef	physical	9351809
NEF_HV1H2	nef	physical	9778343
CBL_HUMAN	CBL	physical	15208330
HS90A_HUMAN	HSP90AA1	physical	16888650
GCR_HUMAN	NR3C1	physical	16888650
KHDR1_HUMAN	KHDRBS1	physical	16888650
WASP_HUMAN	WAS	physical	12431372
KHDR1_HUMAN	KHDRBS1	physical	22745667
SH3K1_HUMAN	SH3KBP1	physical	15707590
CBL_HUMAN	CBL	physical	12941616
FRK_HUMAN	FRK	physical	10229084
SKAP1_HUMAN	SKAP1	physical	10229084
FAK2_HUMAN	PTK2B	physical	10229084
FYB1_HUMAN	FYB	physical	10229084
CBL_HUMAN	CBL	physical	9311917
CBL_HUMAN	CBL	physical	10829062
CBL_HUMAN	CBL	physical	16503409
KHDR1_HUMAN	KHDRBS1	physical	15190072
CBL_HUMAN	CBL	physical	15190072
FGFR2_HUMAN	FGFR2	physical	15190072
EFS_HUMAN	EFS	physical	12471123
CBL_HUMAN	CBL	physical	8900205
CBL_HUMAN	CBL	physical	7782294
TM1L1_HUMAN	TOM1L1	physical	20182632
CAV1_HUMAN	CAV1	physical	9252391
CBL_HUMAN	CBL	physical	8626543
VAV2_HUMAN	VAV2	physical	11262396
VAV_HUMAN	VAV1	physical	11262396
KCNA2_HUMAN	KCNA2	physical	11149959
KCNA4_HUMAN	KCNA4	physical	11149959
PTN11_HUMAN	PTPN11	physical	11157475
CBL_HUMAN	CBL	physical	15556646
FYN_HUMAN	FYN	physical	11157475
CBL_HUMAN	CBL	physical	7642581
LAT_HUMAN	LAT	physical	16938345
SKAP2_HUMAN	SKAP2	physical	12893833
ENOA_HUMAN	ENO1	physical	14530346
FYB1_HUMAN	FYB	physical	9207119
CBL_HUMAN	CBL	physical	8995358
CLH1_HUMAN	CLTC	physical	17785434
SYUA_HUMAN	SNCA	physical	15033366
SYUA_HUMAN	SNCA	physical	11078745
ENOA_HUMAN	ENO1	physical	11078745
PDE4D_HUMAN	PDE4D	physical	10571082
HS90A_HUMAN	HSP90AA1	physical	22939624
CBL_HUMAN	CBL	physical	8662998
NMDZ1_HUMAN	GRIN1	physical	9670010
NMDE2_HUMAN	GRIN2B	physical	9670010
TNFA_HUMAN	TNF	physical	9230816
IL1B_HUMAN	IL1B	physical	9230816
TELT_HUMAN	TCAP	physical	21988832
KDM1A_HUMAN	KDM1A	physical	23455924
ANM6_HUMAN	PRMT6	physical	23455924
SUV91_HUMAN	SUV39H1	physical	23455924
NEMO_HUMAN	IKBKG	physical	23131831
TAU_HUMAN	MAPT	physical	16115884
EFS_HUMAN	EFS	physical	25416956
WBP11_HUMAN	WBP11	physical	25416956
CBLB_HUMAN	CBLB	physical	25814554
CTLA4_HUMAN	CTLA4	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761
KS6A1_HUMAN	RPS6KA1	physical	28514442
SRC_HUMAN	SRC	physical	28514442
KS6A3_HUMAN	RPS6KA3	physical	28514442
KS6A2_HUMAN	RPS6KA2	physical	28514442
YES_HUMAN	YES1	physical	28514442
KPCI_HUMAN	PRKCI	physical	28514442
PTPRD_HUMAN	PTPRD	physical	28514442
HS90B_HUMAN	HSP90AB1	physical	28514442
HS90A_HUMAN	HSP90AA1	physical	28514442
TR10B_HUMAN	TNFRSF10B	physical	28514442
CDC37_HUMAN	CDC37	physical	28514442
GRM1_HUMAN	GRM1	physical	15173175
GRASP_HUMAN	GRASP	physical	15173175

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 FYN_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts."; Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.; Oncogene 5:1313-1319(1990). Cited for: MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT TYR-531.	1699196 [Abstract]
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 THR-15; SER-21; THR-512 ANDTYR-531, AND MASS SPECTROMETRY.	19369195 [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-21, AND MASSSPECTROMETRY.	18669648 [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-21; SER-25; SER-257 ANDTYR-531, 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-21 AND TYR-420, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	19007248 [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-21 AND TYR-420, AND MASSSPECTROMETRY.	17192257 [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-420, AND MASSSPECTROMETRY.	19690332 [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-213; TYR-214; TYR-420AND TYR-440, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Regulation of the p59fyn protein tyrosine kinase by the CD45phosphotyrosine phosphatase."; Mustelin T., Pessa-Morikawa T., Autero M., Gassmann M.,Andersson L.C., Gahmberg C.G., Burn P.; Eur. J. Immunol. 22:1173-1178(1992). Cited for: DEPHOSPHORYLATION AT TYR-531 BY PTPRC.	1533589 [Abstract]
"In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts."; Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.; Oncogene 5:1313-1319(1990). Cited for: MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT TYR-531.	1699196 [Abstract]

show

show

show