dbPTM

PUR9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PUR9_HUMAN
UniProt AC	P31939
Protein Name	Bifunctional purine biosynthesis protein PURH
Gene Name	ATIC
Organism	Homo sapiens (Human).
Sequence Length	592
Subcellular Localization
Protein Description	Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.; Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization. [PubMed: 25687571]
Protein Sequence	MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MAPGQLAL -------CCCCCEEE	10.29	19413330
9 (in isoform 2)	Phosphorylation	-	5.88	25106551
10	Phosphorylation	PGQLALFSVSDKTGL CCCEEEEEECCCCCH	22.89	25850435
11 (in isoform 2)	Phosphorylation	-	7.22	25106551
12	Phosphorylation	QLALFSVSDKTGLVE CEEEEEECCCCCHHH	31.99	25850435
14	Ubiquitination	ALFSVSDKTGLVEFA EEEEECCCCCHHHHH	36.67	21890473
25	Phosphorylation	VEFARNLTALGLNLV HHHHHHHHHHCCEEE	24.32	20068231
34	Phosphorylation	LGLNLVASGGTAKAL HCCEEEECCHHHHHH	30.21	20068231
37	Phosphorylation	NLVASGGTAKALRDA EEEECCHHHHHHHHC	28.63	20068231
38	Ubiquitination	LVASGGTAKALRDAG EEECCHHHHHHHHCC	9.82	21890473
38	Ubiquitination	LVASGGTAKALRDAG EEECCHHHHHHHHCC	9.82	21906983
39	Acetylation	VASGGTAKALRDAGL EECCHHHHHHHHCCC	48.03	25953088
39	Ubiquitination	VASGGTAKALRDAGL EECCHHHHHHHHCCC	48.03	21890473
42	Methylation	GGTAKALRDAGLAVR CHHHHHHHHCCCCCC	36.27	-
52	Phosphorylation	GLAVRDVSELTGFPE CCCCCCHHHHHCCHH	31.04	21712546
60	Sulfoxidation	ELTGFPEMLGGRVKT HHHCCHHHHCCCCCC	4.25	21406390
65	Ubiquitination	PEMLGGRVKTLHPAV HHHHCCCCCCCCHHH	6.67	21890473
65	Ubiquitination	PEMLGGRVKTLHPAV HHHHCCCCCCCCHHH	6.67	21906983
66	Malonylation	EMLGGRVKTLHPAVH HHHCCCCCCCCHHHH	43.97	26320211
66	Ubiquitination	EMLGGRVKTLHPAVH HHHCCCCCCCCHHHH	43.97	21890473
67	Phosphorylation	MLGGRVKTLHPAVHA HHCCCCCCCCHHHHH	27.69	28857561
79	Methylation	VHAGILARNIPEDNA HHHHHHHCCCCCCCC	37.86	-
101	Glutathionylation	NLIRVVACNLYPFVK HHHHHHHCCCHHHHC	2.14	22555962
104	Phosphorylation	RVVACNLYPFVKTVA HHHHCCCHHHHCCCC	4.80	21082442
108	Ubiquitination	CNLYPFVKTVASPGV CCCHHHHCCCCCCCC	37.35	-
109	Phosphorylation	NLYPFVKTVASPGVT CCHHHHCCCCCCCCC	18.92	28450419
112	Phosphorylation	PFVKTVASPGVTVEE HHHCCCCCCCCCHHH	20.18	29496963
116	Phosphorylation	TVASPGVTVEEAVEQ CCCCCCCCHHHHHHH	28.28	30087585
137	Ubiquitination	TLLRAAAKNHARVTV HHHHHHHHCCCEEEE	44.53	-
146	Glutathionylation	HARVTVVCEPEDYVV CCEEEEEECCCCEEE	6.67	22555962
158	Sulfoxidation	YVVVSTEMQSSESKD EEEEEEECCCCCCCC	4.79	30846556
160	Phosphorylation	VVSTEMQSSESKDTS EEEEECCCCCCCCCC	34.46	20068231
161	Phosphorylation	VSTEMQSSESKDTSL EEEECCCCCCCCCCH	29.06	20068231
163	Phosphorylation	TEMQSSESKDTSLET EECCCCCCCCCCHHH	37.47	20068231
166	Phosphorylation	QSSESKDTSLETRRQ CCCCCCCCCHHHHHH	38.66	-
176	Ubiquitination	ETRRQLALKAFTHTA HHHHHHHHHHHHHHH	5.82	21890473
176	Ubiquitination	ETRRQLALKAFTHTA HHHHHHHHHHHHHHH	5.82	21906983
177	Ubiquitination	TRRQLALKAFTHTAQ HHHHHHHHHHHHHHH	35.53	21906983
180	Phosphorylation	QLALKAFTHTAQYDE HHHHHHHHHHHHHHH	24.15	-
182	Phosphorylation	ALKAFTHTAQYDEAI HHHHHHHHHHHHHHH	16.64	-
190	Phosphorylation	AQYDEAISDYFRKQY HHHHHHHHHHHHHHH	33.05	28152594
192	Phosphorylation	YDEAISDYFRKQYSK HHHHHHHHHHHHHCC	9.86	28152594
197	Phosphorylation	SDYFRKQYSKGVSQM HHHHHHHHCCCCCCC	18.51	22817900
198	Ubiquitination	DYFRKQYSKGVSQMP HHHHHHHCCCCCCCC	22.05	21890473
198	Ubiquitination	DYFRKQYSKGVSQMP HHHHHHHCCCCCCCC	22.05	21906983
199	Acetylation	YFRKQYSKGVSQMPL HHHHHHCCCCCCCCC	59.40	19608861
199	Ubiquitination	YFRKQYSKGVSQMPL HHHHHHCCCCCCCCC	59.40	21890473
202	Phosphorylation	KQYSKGVSQMPLRYG HHHCCCCCCCCCCCC	29.45	28857561
204	Sulfoxidation	YSKGVSQMPLRYGMN HCCCCCCCCCCCCCC	2.35	21406390
208	Phosphorylation	VSQMPLRYGMNPHQT CCCCCCCCCCCCCCC	28.54	21945579
215	Phosphorylation	YGMNPHQTPAQLYTL CCCCCCCCHHHEEEC	19.98	21945579
220	Phosphorylation	HQTPAQLYTLQPKLP CCCHHHEEECCCCCC	8.04	21945579
221	Phosphorylation	QTPAQLYTLQPKLPI CCHHHEEECCCCCCE	27.75	21945579
241	S-palmitoylation	APGFINLCDALNAWQ CCCHHHHHHHHCHHH	2.19	29575903
253	Ubiquitination	AWQLVKELKEALGIP HHHHHHHHHHHHCCC	5.14	-
254	Ubiquitination	WQLVKELKEALGIPA HHHHHHHHHHHCCCC	41.87	-
264	Phosphorylation	LGIPAAASFKHVSPA HCCCCHHCCCCCCCC	30.05	30108239
265	Acetylation	GIPAAASFKHVSPAG CCCCHHCCCCCCCCC	5.63	-
265	Ubiquitination	GIPAAASFKHVSPAG CCCCHHCCCCCCCCC	5.63	-
266	Acetylation	IPAAASFKHVSPAGA CCCHHCCCCCCCCCC	40.37	23954790
266	Malonylation	IPAAASFKHVSPAGA CCCHHCCCCCCCCCC	40.37	26320211
266	Ubiquitination	IPAAASFKHVSPAGA CCCHHCCCCCCCCCC	40.37	-
269	Phosphorylation	AASFKHVSPAGAAVG HHCCCCCCCCCCEEC	14.57	27067055
280	Phosphorylation	AAVGIPLSEDEAKVC CEECCCCCHHHHHHH	37.33	28450419
284	Ubiquitination	IPLSEDEAKVCMVYD CCCCHHHHHHHHHHH	23.15	-
285	Ubiquitination	PLSEDEAKVCMVYDL CCCHHHHHHHHHHHH	33.64	-
287	Glutathionylation	SEDEAKVCMVYDLYK CHHHHHHHHHHHHHH	1.18	22555962
287	S-palmitoylation	SEDEAKVCMVYDLYK CHHHHHHHHHHHHHH	1.18	26865113
290	Phosphorylation	EAKVCMVYDLYKTLT HHHHHHHHHHHHHCC	3.55	20090780
293	Ubiquitination	VCMVYDLYKTLTPIS HHHHHHHHHHCCHHH	10.07	-
293	Phosphorylation	VCMVYDLYKTLTPIS HHHHHHHHHHCCHHH	10.07	27259358
294	Ubiquitination	CMVYDLYKTLTPISA HHHHHHHHHCCHHHH	44.34	-
295	Phosphorylation	MVYDLYKTLTPISAA HHHHHHHHCCHHHHH	23.47	19835603
297	Phosphorylation	YDLYKTLTPISAAYA HHHHHHCCHHHHHHH	24.65	20873877
300	Phosphorylation	YKTLTPISAAYARAR HHHCCHHHHHHHHHC	14.19	28152594
303	Phosphorylation	LTPISAAYARARGAD CCHHHHHHHHHCCCC	9.06	28152594
305	Methylation	PISAAYARARGADRM HHHHHHHHHCCCCCC	16.49	-
312	Sulfoxidation	RARGADRMSSFGDFV HHCCCCCCCCCCCCC	3.96	21406390
313	Phosphorylation	ARGADRMSSFGDFVA HCCCCCCCCCCCCCH	24.33	28348404
314	Phosphorylation	RGADRMSSFGDFVAL CCCCCCCCCCCCCHH	24.73	28348404
325	Glutathionylation	FVALSDVCDVPTAKI CCHHHHCCCCCCCEE	5.39	22555962
330	Ubiquitination	DVCDVPTAKIISREV HCCCCCCCEEEEEEC	8.59	-
331	Acetylation	VCDVPTAKIISREVS CCCCCCCEEEEEECC	42.95	25953088
331	Ubiquitination	VCDVPTAKIISREVS CCCCCCCEEEEEECC	42.95	21890473
338	Phosphorylation	KIISREVSDGIIAPG EEEEEECCCCCCCCC	25.93	20873877
346	Phosphorylation	DGIIAPGYEEEALTI CCCCCCCCHHHHHHH	21.07	20873877
355	Ubiquitination	EEALTILSKKKNGNY HHHHHHHEECCCCCE	38.28	21890473
355	Acetylation	EEALTILSKKKNGNY HHHHHHHEECCCCCE	38.28	-
355	Ubiquitination	EEALTILSKKKNGNY HHHHHHHEECCCCCE	38.28	21906983
355	Phosphorylation	EEALTILSKKKNGNY HHHHHHHEECCCCCE	38.28	21712546
356	Ubiquitination	EALTILSKKKNGNYC HHHHHHEECCCCCEE	65.41	-
356	Acetylation	EALTILSKKKNGNYC HHHHHHEECCCCCEE	65.41	23954790
356	Ubiquitination	EALTILSKKKNGNYC HHHHHHEECCCCCEE	65.41	21890473
357	Ubiquitination	ALTILSKKKNGNYCV HHHHHEECCCCCEEE	48.36	-
357	Acetylation	ALTILSKKKNGNYCV HHHHHEECCCCCEEE	48.36	25953088
357	Ubiquitination	ALTILSKKKNGNYCV HHHHHEECCCCCEEE	48.36	-
358	Malonylation	LTILSKKKNGNYCVL HHHHEECCCCCEEEE	74.05	32601280
358	Ubiquitination	LTILSKKKNGNYCVL HHHHEECCCCCEEEE	74.05	-
370	Phosphorylation	CVLQMDQSYKPDENE EEEEECCCCCCCHHH	30.75	20873877
371	Ubiquitination	VLQMDQSYKPDENEV EEEECCCCCCCHHHH	22.40	-
371	Phosphorylation	VLQMDQSYKPDENEV EEEECCCCCCCHHHH	22.40	20873877
372	Ubiquitination	LQMDQSYKPDENEVR EEECCCCCCCHHHHH	51.76	-
380	Phosphorylation	PDENEVRTLFGLHLS CCHHHHHHHHHHHHC	31.45	20873877
387	Phosphorylation	TLFGLHLSQKRNNGV HHHHHHHCCCCCCCC	23.94	28450419
388	Ubiquitination	LFGLHLSQKRNNGVV HHHHHHCCCCCCCCC	55.90	21890473
388	Ubiquitination	LFGLHLSQKRNNGVV HHHHHHCCCCCCCCC	55.90	21906983
389	2-Hydroxyisobutyrylation	FGLHLSQKRNNGVVD HHHHHCCCCCCCCCC	54.43	-
389	Acetylation	FGLHLSQKRNNGVVD HHHHHCCCCCCCCCC	54.43	25953088
389	Ubiquitination	FGLHLSQKRNNGVVD HHHHHCCCCCCCCCC	54.43	21890473
396	Ubiquitination	KRNNGVVDKSLFSNV CCCCCCCCHHHHHCC	32.21	21890473
396	Ubiquitination	KRNNGVVDKSLFSNV CCCCCCCCHHHHHCC	32.21	21906983
397	Acetylation	RNNGVVDKSLFSNVV CCCCCCCHHHHHCCC	37.13	25953088
397	Ubiquitination	RNNGVVDKSLFSNVV CCCCCCCHHHHHCCC	37.13	21890473
398	Phosphorylation	NNGVVDKSLFSNVVT CCCCCCHHHHHCCCC	30.13	20873877
401	Phosphorylation	VVDKSLFSNVVTKNK CCCHHHHHCCCCCCC	33.73	20068231
405	Ubiquitination	SLFSNVVTKNKDLPE HHHHCCCCCCCCCCH	25.31	21890473
405	Ubiquitination	SLFSNVVTKNKDLPE HHHHCCCCCCCCCCH	25.31	21906983
405	Phosphorylation	SLFSNVVTKNKDLPE HHHHCCCCCCCCCCH	25.31	20068231
406	Acetylation	LFSNVVTKNKDLPES HHHCCCCCCCCCCHH	50.84	25953088
406	Ubiquitination	LFSNVVTKNKDLPES HHHCCCCCCCCCCHH	50.84	21890473
407	Ubiquitination	FSNVVTKNKDLPESA HHCCCCCCCCCCHHH	33.44	-
408	Ubiquitination	SNVVTKNKDLPESAL HCCCCCCCCCCHHHH	63.30	-
413	Phosphorylation	KNKDLPESALRDLIV CCCCCCHHHHHHHHH	30.57	-
422	Phosphorylation	LRDLIVATIAVKYTQ HHHHHHHHHEEEECC	9.89	24667141
427	Phosphorylation	VATIAVKYTQSNSVC HHHHEEEECCCCCEE	11.92	28152594
428	Phosphorylation	ATIAVKYTQSNSVCY HHHEEEECCCCCEEE	21.58	28152594
430	Phosphorylation	IAVKYTQSNSVCYAK HEEEECCCCCEEEEE	24.23	28152594
432	Phosphorylation	VKYTQSNSVCYAKNG EEECCCCCEEEEECC	20.86	28857561
434	S-nitrosocysteine	YTQSNSVCYAKNGQV ECCCCCEEEEECCEE	2.47	-
434	S-nitrosylation	YTQSNSVCYAKNGQV ECCCCCEEEEECCEE	2.47	19483679
435	Phosphorylation	TQSNSVCYAKNGQVI CCCCCEEEEECCEEE	20.60	28152594
436	Ubiquitination	QSNSVCYAKNGQVIG CCCCEEEEECCEEEE	8.16	-
437	Acetylation	SNSVCYAKNGQVIGI CCCEEEEECCEEEEE	34.83	26051181
437	Ubiquitination	SNSVCYAKNGQVIGI CCCEEEEECCEEEEE	34.83	-
450	Phosphorylation	GIGAGQQSRIHCTRL EECCCCCCEEEEEEE	25.89	28857561
460	Ubiquitination	HCTRLAGDKANYWWL EEEEECCCCCCCHHH	41.09	-
461	Acetylation	CTRLAGDKANYWWLR EEEECCCCCCCHHHH	37.30	25953088
461	Ubiquitination	CTRLAGDKANYWWLR EEEECCCCCCCHHHH	37.30	-
464	Phosphorylation	LAGDKANYWWLRHHP ECCCCCCCHHHHCCH	11.65	28152594
475	Phosphorylation	RHHPQVLSMKFKTGV HCCHHHEEEEECCCC	22.52	28857561
476	Ubiquitination	HHPQVLSMKFKTGVK CCHHHEEEEECCCCC	5.31	-
477	Acetylation	HPQVLSMKFKTGVKR CHHHEEEEECCCCCH	40.09	25953088
477	Ubiquitination	HPQVLSMKFKTGVKR CHHHEEEEECCCCCH	40.09	-
506	Ubiquitination	IGEDEDLIKWKALFE CCCCHHHHHHHHHHH	8.49	-
507	Acetylation	GEDEDLIKWKALFEE CCCHHHHHHHHHHHH	50.36	25953088
507	Sumoylation	GEDEDLIKWKALFEE CCCHHHHHHHHHHHH	50.36	-
507	Ubiquitination	GEDEDLIKWKALFEE CCCHHHHHHHHHHHH	50.36	21906983
508	Ubiquitination	EDEDLIKWKALFEEV CCHHHHHHHHHHHHH	5.55	-
509	Sumoylation	DEDLIKWKALFEEVP CHHHHHHHHHHHHHH	30.15	-
509	Ubiquitination	DEDLIKWKALFEEVP CHHHHHHHHHHHHHH	30.15	20639865
520	Phosphorylation	EEVPELLTEAEKKEW HHHHHHHHHHHHHHH	45.86	-
523	Ubiquitination	PELLTEAEKKEWVEK HHHHHHHHHHHHHHH	59.43	-
524	Ubiquitination	ELLTEAEKKEWVEKL HHHHHHHHHHHHHHH	64.14	-
524	2-Hydroxyisobutyrylation	ELLTEAEKKEWVEKL HHHHHHHHHHHHHHH	64.14	-
524	Ubiquitination	ELLTEAEKKEWVEKL HHHHHHHHHHHHHHH	64.14	2190698
525	Ubiquitination	LLTEAEKKEWVEKLT HHHHHHHHHHHHHHH	48.60	-
529	Ubiquitination	AEKKEWVEKLTEVSI HHHHHHHHHHHCCEE	43.34	-
530	Ubiquitination	EKKEWVEKLTEVSIS HHHHHHHHHHCCEEC	51.60	-
532	Phosphorylation	KEWVEKLTEVSISSD HHHHHHHHCCEECCC	45.46	20873877
535	Phosphorylation	VEKLTEVSISSDAFF HHHHHCCEECCCCCC	15.55	28857561
537	Phosphorylation	KLTEVSISSDAFFPF HHHCCEECCCCCCCC	18.05	20873877
538	Phosphorylation	LTEVSISSDAFFPFR HHCCEECCCCCCCCC	31.15	20873877
554	Phosphorylation	NVDRAKRSGVAYIAA CHHHHHHCCCEEEEC	36.59	21406692
558	Phosphorylation	AKRSGVAYIAAPSGS HHHCCCEEEECCCCC	6.67	21406692
563	Phosphorylation	VAYIAAPSGSAADKV CEEEECCCCCCHHHH	40.42	25159151
565	Phosphorylation	YIAAPSGSAADKVVI EEECCCCCCHHHHHH	25.31	25159151

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
104	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PUR9_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 PUR9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JAK1_HUMAN	JAK1	physical	17353931
RADIL_HUMAN	RADIL	physical	17353931
STOM_HUMAN	STOM	physical	17353931
HNRDL_HUMAN	HNRNPDL	physical	17353931
SNRPA_HUMAN	SNRPA	physical	17353931
CIA30_HUMAN	NDUFAF1	physical	17353931
CMBL_HUMAN	CMBL	physical	17353931
TYSY_HUMAN	TYMS	physical	22939629
SCOT1_HUMAN	OXCT1	physical	22939629
RBBP6_HUMAN	RBBP6	physical	22939629
TADBP_HUMAN	TARDBP	physical	22939629
SUMO2_HUMAN	SUMO2	physical	22939629
THIO_HUMAN	TXN	physical	22939629
ASB6_HUMAN	ASB6	physical	22863883
IPO5_HUMAN	IPO5	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MOES_HUMAN	MSN	physical	22863883
ULA1_HUMAN	NAE1	physical	22863883
NSF1C_HUMAN	NSFL1C	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
A16A1_HUMAN	ALDH16A1	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
RNZ2_HUMAN	ELAC2	physical	26344197
PUR2_HUMAN	GART	physical	26344197
RTN4_HUMAN	RTN4	physical	26344197
TRNT1_HUMAN	TRNT1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608688	AICAR transformylase/IMP cyclohydrolase deficiency (AICAR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00563	Methotrexate
DB00642	Pemetrexed
DB00116	Tetrahydrofolic acid

Regulatory Network of PUR9_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-199, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-104, AND MASSSPECTROMETRY.	18083107 [Abstract]