ABI1_HUMAN - dbPTM
ABI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABI1_HUMAN
UniProt AC Q8IZP0
Protein Name Abl interactor 1
Gene Name ABI1 {ECO:0000312|HGNC:HGNC:11320}
Organism Homo sapiens (Human).
Sequence Length 508
Subcellular Localization Cytoplasm. Nucleus. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, growth cone. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cytoplasm, cytoskeleton. Localized to protruding lamellipodia and
Protein Description May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons..
Protein Sequence MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANMERPVRYIRKPIDYTVLDDVGHGVKWLKAKHGNNQPARTGTLSRTNPPTQKPPSPPMSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTIGPENISVPPPSGAPPAPPLAPLLPVSTVIAAPGSAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVTAQFSAQPHVNGGPLYSQNSISIAPPPPPMPQLTPQIPLTGFVARVQENIADSPTPPPPPPPDDIPMFDDSPPPPPPPPVDYEDEEAAVVQYNDPYADGDPAWAPKNYIEKVVAIYDYTKDKDDELSFMEGAIIYVIKKNDDGWYEGVCNRVTGLFPGNYVESIMHYTD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAELQMLLE
------CHHHHHHHH		26.6322223895
14PhosphorylationLLEEEIPSGKRALIE
HHHHHCCCCHHHHHH		63.7124719451
22PhosphorylationGKRALIESYQNLTRV
CHHHHHHHHHHHHHH		25.6523403867
23PhosphorylationKRALIESYQNLTRVA
HHHHHHHHHHHHHHH		6.6618083107
37PhosphorylationADYCENNYIQATDKR
HHHHHCCEECCCHHH		13.1446157101
43UbiquitinationNYIQATDKRKALEET
CEECCCHHHHHHHHH		51.98-
53PhosphorylationALEETKAYTTQSLAS
HHHHHHHHCHHHHHH		16.33-
88PhosphorylationSQLRRMESSINHISQ
HHHHHHHHHHHHHHH		27.4628348404
89PhosphorylationQLRRMESSINHISQT
HHHHHHHHHHHHHHH		17.6928348404
1012-HydroxyisobutyrylationSQTVDIHKEKVARRE
HHHHHHHHHHHHHCC		60.61-
123MalonylationKNTSRTHKIIAPANM
CCCCCCEEEECCCCC		34.8826320211
123UbiquitinationKNTSRTHKIIAPANM
CCCCCCEEEECCCCC		34.88-
139UbiquitinationRPVRYIRKPIDYTVL
CCCHHCCCCCCEEEE		36.45-
143PhosphorylationYIRKPIDYTVLDDVG
HCCCCCCEEEECCCC		10.247393235
168PhosphorylationGNNQPARTGTLSRTN
CCCCCCCCCCCCCCC		36.3026074081
170PhosphorylationNQPARTGTLSRTNPP
CCCCCCCCCCCCCCC		22.4326074081
172PhosphorylationPARTGTLSRTNPPTQ
CCCCCCCCCCCCCCC		36.5826074081
174PhosphorylationRTGTLSRTNPPTQKP
CCCCCCCCCCCCCCC		49.0223927012
178PhosphorylationLSRTNPPTQKPPSPP
CCCCCCCCCCCCCCC		50.9421955146
183PhosphorylationPPTQKPPSPPMSGRG
CCCCCCCCCCCCCCC		50.6022167270
187PhosphorylationKPPSPPMSGRGTLGR
CCCCCCCCCCCCCCC		30.9822167270
191PhosphorylationPPMSGRGTLGRNTPY
CCCCCCCCCCCCCCC		25.3621955146
196PhosphorylationRGTLGRNTPYKTLEP
CCCCCCCCCCCCCCC		27.0025159151
198PhosphorylationTLGRNTPYKTLEPVK
CCCCCCCCCCCCCCC		17.9927273156
199AcetylationLGRNTPYKTLEPVKP
CCCCCCCCCCCCCCC		48.0825953088
200PhosphorylationGRNTPYKTLEPVKPP
CCCCCCCCCCCCCCC		30.4321945579
208PhosphorylationLEPVKPPTVPNDYMT
CCCCCCCCCCCCCCC		58.0621945579
212PhosphorylationKPPTVPNDYMTSPAR
CCCCCCCCCCCCCHH		28.6317016520
213PhosphorylationPPTVPNDYMTSPARL
CCCCCCCCCCCCHHC		14.6623927012
215PhosphorylationTVPNDYMTSPARLGS
CCCCCCCCCCHHCCC		25.9023927012
216PhosphorylationVPNDYMTSPARLGSQ
CCCCCCCCCHHCCCC		10.4723927012
222PhosphorylationTSPARLGSQHSPGRT
CCCHHCCCCCCCCCC		29.3428176443
225PhosphorylationARLGSQHSPGRTASL
HHCCCCCCCCCCCCC		22.7822167270
229PhosphorylationSQHSPGRTASLNQRP
CCCCCCCCCCCCCCC		26.8923401153
231PhosphorylationHSPGRTASLNQRPRT
CCCCCCCCCCCCCCC		27.5225159151
233 (in isoform 5)Phosphorylation-33.0623909892
235 (in isoform 5)Phosphorylation-22.9223909892
237 (in isoform 5)Phosphorylation-47.4623909892
238PhosphorylationSLNQRPRTHSGSSGG
CCCCCCCCCCCCCCC		24.0726699800
238 (in isoform 3)Phosphorylation-24.0723909892
238 (in isoform 5)Phosphorylation-24.0723909892
238 (in isoform 9)Phosphorylation-24.0723909892
240PhosphorylationNQRPRTHSGSSGGSG
CCCCCCCCCCCCCCC		39.4926699800
240 (in isoform 3)Phosphorylation-39.4923909892
240 (in isoform 9)Phosphorylation-39.4923909892
241 (in isoform 5)Phosphorylation-20.4423909892
242PhosphorylationRPRTHSGSSGGSGSR
CCCCCCCCCCCCCCC		28.9129743597
242 (in isoform 3)Phosphorylation-28.9123909892
242 (in isoform 9)Phosphorylation-28.9123909892
243PhosphorylationPRTHSGSSGGSGSRE
CCCCCCCCCCCCCCC		51.1826699800
243 (in isoform 3)Phosphorylation-51.1823909892
243 (in isoform 5)Phosphorylation-51.1823909892
243 (in isoform 9)Phosphorylation-51.1823909892
246PhosphorylationHSGSSGGSGSRENSG
CCCCCCCCCCCCCCC		36.8021981627
246 (in isoform 3)Phosphorylation-36.8023909892
246 (in isoform 9)Phosphorylation-36.8023909892
247 (in isoform 5)Phosphorylation-33.7223909892
248PhosphorylationGSSGGSGSRENSGSS
CCCCCCCCCCCCCCC		37.8130849831
248 (in isoform 3)Phosphorylation-37.8123909892
248 (in isoform 9)Phosphorylation-37.8123909892
249 (in isoform 5)Phosphorylation-51.1227251275
250 (in isoform 5)Phosphorylation-58.4023909892
251 (in isoform 5)Phosphorylation-51.0327251275
252PhosphorylationGSGSRENSGSSSIGI
CCCCCCCCCCCCCCC		34.9935198805
252 (in isoform 3)Phosphorylation-34.9923909892
252 (in isoform 9)Phosphorylation-34.9923909892
254PhosphorylationGSRENSGSSSIGIPI
CCCCCCCCCCCCCEE		22.26-
254 (in isoform 3)Phosphorylation-22.2627251275
254 (in isoform 9)Phosphorylation-22.2627251275
255PhosphorylationSRENSGSSSIGIPIA
CCCCCCCCCCCCEEE		29.51-
255 (in isoform 3)Phosphorylation-29.5123909892
255 (in isoform 9)Phosphorylation-29.5123909892
256 (in isoform 3)Phosphorylation-26.9127251275
256 (in isoform 9)Phosphorylation-26.9127251275
260 (in isoform 2)Phosphorylation-11.8528348404
260 (in isoform 5)Phosphorylation-11.8528348404
262 (in isoform 2)Phosphorylation-8.9027251275
262 (in isoform 5)Phosphorylation-8.9028348404
265PhosphorylationGIPIAVPTPSPPTIG
CCEEEECCCCCCCCC		29.7837430807
265 (in isoform 2)Phosphorylation-29.78-
265 (in isoform 3)Phosphorylation-29.7828348404
265 (in isoform 4)Phosphorylation-29.7828348404
265 (in isoform 5)Phosphorylation-29.78-
265 (in isoform 6)Phosphorylation-29.7828348404
265 (in isoform 9)Phosphorylation-29.7828348404
267PhosphorylationPIAVPTPSPPTIGPE
EEEECCCCCCCCCCC		46.0937430805
267 (in isoform 3)Phosphorylation-46.0928348404
267 (in isoform 4)Phosphorylation-46.0927251275
267 (in isoform 6)Phosphorylation-46.0927251275
267 (in isoform 9)Phosphorylation-46.0928348404
270PhosphorylationVPTPSPPTIGPENIS
ECCCCCCCCCCCCCC		41.78-
270 (in isoform 3)Phosphorylation-41.78-
270 (in isoform 4)Phosphorylation-41.78-
270 (in isoform 6)Phosphorylation-41.78-
270 (in isoform 9)Phosphorylation-41.78-
273 (in isoform 5)Phosphorylation-27.8428348404
276 (in isoform 2)Phosphorylation-4.1325884760
277 (in isoform 5)Phosphorylation-39.9025884760
278 (in isoform 3)Phosphorylation-7.9528348404
278 (in isoform 9)Phosphorylation-7.9528348404
279 (in isoform 5)Phosphorylation-28.4425884760
281 (in isoform 4)Phosphorylation-39.0525884760
281 (in isoform 6)Phosphorylation-39.0525884760
282 (in isoform 3)Phosphorylation-54.0525884760
282 (in isoform 9)Phosphorylation-54.0525884760
283 (in isoform 5)Phosphorylation-48.1228348404
284 (in isoform 3)Phosphorylation-15.9625884760
284 (in isoform 9)Phosphorylation-15.9625884760
288 (in isoform 3)Phosphorylation-30.1628348404
288 (in isoform 9)Phosphorylation-30.1628348404
305PhosphorylationTVIAAPGSAPGSQYG
EEEECCCCCCCCHHH		30.17-
309PhosphorylationAPGSAPGSQYGTMTR
CCCCCCCCHHHHCEE		21.12-
311PhosphorylationGSAPGSQYGTMTRQI
CCCCCCHHHHCEEEE		19.09-
319PhosphorylationGTMTRQISRHNSTTS
HHCEEEEECCCCCCC		21.1022617229
323PhosphorylationRQISRHNSTTSSTSS
EEEECCCCCCCCCCC		27.2622617229
324PhosphorylationQISRHNSTTSSTSSG
EEECCCCCCCCCCCC		35.6921955146
325PhosphorylationISRHNSTTSSTSSGG
EECCCCCCCCCCCCC		22.0921955146
326PhosphorylationSRHNSTTSSTSSGGY
ECCCCCCCCCCCCCC		31.5421955146
327PhosphorylationRHNSTTSSTSSGGYR
CCCCCCCCCCCCCCC		30.1621955146
328PhosphorylationHNSTTSSTSSGGYRR
CCCCCCCCCCCCCCC		27.0321955146
329PhosphorylationNSTTSSTSSGGYRRT
CCCCCCCCCCCCCCC		29.0021955146
330PhosphorylationSTTSSTSSGGYRRTP
CCCCCCCCCCCCCCC		36.0026055452
333PhosphorylationSSTSSGGYRRTPSVT
CCCCCCCCCCCCCEE		10.6327273156
336PhosphorylationSSGGYRRTPSVTAQF
CCCCCCCCCCEEEEE		15.777311121
338PhosphorylationGGYRRTPSVTAQFSA
CCCCCCCCEEEEEEC		31.3320736484
340PhosphorylationYRRTPSVTAQFSAQP
CCCCCCEEEEEECCC		21.0528348404
344PhosphorylationPSVTAQFSAQPHVNG
CCEEEEEECCCCCCC		17.5728348404
355PhosphorylationHVNGGPLYSQNSISI
CCCCCCCCCCCCEEE		16.0246157095
361PhosphorylationLYSQNSISIAPPPPP
CCCCCCEEECCCCCC		16.7217855441
392PhosphorylationVQENIADSPTPPPPP
HHHHCCCCCCCCCCC		22.9621419341
394PhosphorylationENIADSPTPPPPPPP
HHCCCCCCCCCCCCC		52.9921419341
410PhosphorylationDIPMFDDSPPPPPPP
CCCCCCCCCCCCCCC		40.9421419341
421PhosphorylationPPPPPVDYEDEEAAV
CCCCCCCCCCCCEEE		26.0520598684
431PhosphorylationEEAAVVQYNDPYADG
CCEEEEEECCCCCCC		15.2125884760
435PhosphorylationVVQYNDPYADGDPAW
EEEECCCCCCCCCCC		21.8625884760
455PhosphorylationIEKVVAIYDYTKDKD
HCEEEEEEECCCCCC		7.9926657352
457PhosphorylationKVVAIYDYTKDKDDE
EEEEEEECCCCCCCC		9.9428060719
458PhosphorylationVVAIYDYTKDKDDEL
EEEEEECCCCCCCCC		29.84-
466PhosphorylationKDKDDELSFMEGAII
CCCCCCCCCCCEEEE		22.0926657352
474PhosphorylationFMEGAIIYVIKKNDD
CCCEEEEEEEEECCC		7.0426657352
484PhosphorylationKKNDDGWYEGVCNRV
EECCCCCEECHHHHC		14.3425147952
499PhosphorylationTGLFPGNYVESIMHY
CCCCCCCHHHHHHCC		16.1226356563
502PhosphorylationFPGNYVESIMHYTD-
CCCCHHHHHHCCCC-		18.3726356563
506PhosphorylationYVESIMHYTD-----
HHHHHHCCCC-----		8.6728796482
507PhosphorylationVESIMHYTD------
HHHHHCCCC------		22.1322115753
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
183SPhosphorylationKinaseMAPK1P28482
GPS
183SPhosphorylationKinaseMAPK3P27361
GPS
213YPhosphorylationKinaseABLP00519
PSP
213YPhosphorylationKinaseABL-FAMILY-GPS
216SPhosphorylationKinaseCDK1P06493
PSP
216SPhosphorylationKinaseMAPK3P27361
GPS
216SPhosphorylationKinaseMAPK1P28482
GPS
225SPhosphorylationKinaseMAPK1P28482
GPS
225SPhosphorylationKinaseMAPK3P27361
GPS
265TPhosphorylationKinaseMAPK1P28482
GPS
265TPhosphorylationKinaseMAPK3P27361
GPS
267SPhosphorylationKinaseMAPK1P28482
GPS
267SPhosphorylationKinaseMAPK3P27361
GPS
392SPhosphorylationKinaseMAPK3P27361
GPS
392SPhosphorylationKinaseMAPK1P28482
GPS
394TPhosphorylationKinaseMAPK3P27361
GPS
394TPhosphorylationKinaseMAPK1P28482
GPS
398YPhosphorylationKinaseABL-FAMILY-GPS
410SPhosphorylationKinaseMAPK1P28482
GPS
410SPhosphorylationKinaseMAPK3P27361
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABI1_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 ABI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ENAH_HUMANENAHphysical
12672821
ABL1_HUMANABL1physical
12672821
EPS8_HUMANEPS8physical
9010225
NCK1_HUMANNCK1physical
11418237
ABL1_HUMANABL1physical
11418237
CBL_HUMANCBLphysical
17395426
NCK2_HUMANNCK2physical
11557983
NCK1_HUMANNCK1physical
11557983
CD123_HUMANCDC123physical
22939629
SRC8_HUMANCTTNphysical
22939629
P85A_HUMANPIK3R1physical
20598684
SRRM1_HUMANSRRM1physical
21988832
ABL1_HUMANABL1physical
18328268
ENAH_HUMANENAHphysical
17101133
WASF2_HUMANWASF2physical
17101133
CYFP1_HUMANCYFIP1physical
26344197
CYFP2_HUMANCYFIP2physical
26344197
NCKP1_HUMANNCKAP1physical
26344197
NCKPL_HUMANNCKAP1Lphysical
26344197
SF3A3_HUMANSF3A3physical
26344197
LA_HUMANSSBphysical
26344197
WASF1_HUMANWASF1physical
26344197
WASF2_HUMANWASF2physical
26344197
WASL_HUMANWASLphysical
26344197
KI67_HUMANMKI67physical
26496610
NHS_HUMANNHSphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
WASF1_HUMANWASF1physical
26496610
HOME3_HUMANHOMER3physical
26496610
ABI2_HUMANABI2physical
26496610
WASF2_HUMANWASF2physical
26496610
RBM14_HUMANRBM14physical
26496610
BAIP2_HUMANBAIAP2physical
26496610
NCKP1_HUMANNCKAP1physical
26496610
CYFP1_HUMANCYFIP1physical
26496610
ENAH_HUMANENAHphysical
26496610
BRK1_HUMANBRK1physical
26496610
NHSL1_HUMANNHSL1physical
26496610
K1522_HUMANKIAA1522physical
26496610
RAPH1_HUMANRAPH1physical
26496610
THOC6_HUMANTHOC6physical
26496610
NXN_HUMANNXNphysical
27173435
CYFP1_HUMANCYFIP1physical
27173435
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 ABI1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-225, AND MASSSPECTROMETRY.
"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-183 AND SER-216, ANDMASS SPECTROMETRY.
"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-225, AND MASSSPECTROMETRY.
"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-225, AND MASSSPECTROMETRY.
"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 SER-183, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"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-213, AND MASSSPECTROMETRY.
"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinaseby phosphopeptides derived from Abi1/Hssh3bp1.";
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X.,Debnath A.K., Cowburn D., Kotula L.;
Biochim. Biophys. Acta 1783:737-747(2008).
Cited for: FUNCTION, AND PHOSPHORYLATION AT TYR-213.
"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-213, AND MASSSPECTROMETRY.
"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, AND MASSSPECTROMETRY.
"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-333, AND MASSSPECTROMETRY.

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