PDLI5_HUMAN - dbPTM
PDLI5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDLI5_HUMAN
UniProt AC Q96HC4
Protein Name PDZ and LIM domain protein 5
Gene Name PDLIM5
Organism Homo sapiens (Human).
Sequence Length 596
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse, synaptosome. Cytoplasm. Detected both at presynaptic and postsynaptic sites..
Protein Description May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity)..
Protein Sequence MSNYSVSLVGPAPWGFRLQGGKDFNMPLTISSLKDGGKAAQANVRIGDVVLSIDGINAQGMTHLEAQNKIKGCTGSLNMTLQRASAAPKPEPVPVQKGEPKEVVKPVPITSPAVSKVTSTNNMAYNKAPRPFGSVSSPKVTSIPSPSSAFTPAHATTSSHASPSPVAAVTPPLFAASGLHANANLSADQSPSALSAGKTAVNVPRQPTVTSVCSETSQELAEGQRRGSQGDSKQQNGPPRKHIVERYTEFYHVPTHSDASKKRLIEDTEDWRPRTGTTQSRSFRILAQITGTEHLKESEADNTKKANNSQEPSPQLASSVASTRSMPESLDSPTSGRPGVTSLTAAAAFKPVGSTGVIKSPSWQRPNQGVPSTGRISNSATYSGSVAPANSALGQTQPSDQDTLVQRAEHIPAGKRTPMCAHCNQVIRGPFLVALGKSWHPEEFNCAHCKNTMAYIGFVEEKGALYCELCYEKFFAPECGRCQRKILGEVISALKQTWHVSCFVCVACGKPIRNNVFHLEDGEPYCETDYYALFGTICHGCEFPIEAGDMFLEALGYTWHDTCFVCSVCCESLEGQTFFSKKDKPLCKKHAHSVNF
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------MSNYSVSLV
------CCCEEEEEE
44.4622223895
2Phosphorylation------MSNYSVSLV
------CCCEEEEEE
44.4622199227
4Phosphorylation----MSNYSVSLVGP
----CCCEEEEEECC
11.8022673903
5Phosphorylation---MSNYSVSLVGPA
---CCCEEEEEECCC
14.9622199227
7Phosphorylation-MSNYSVSLVGPAPW
-CCCEEEEEECCCCC
16.0520873877
31PhosphorylationFNMPLTISSLKDGGK
CCCCEEEEECCCCCC
25.1223403867
32PhosphorylationNMPLTISSLKDGGKA
CCCEEEEECCCCCCE
35.2723403867
34AcetylationPLTISSLKDGGKAAQ
CEEEEECCCCCCEEC
57.1625953088
34MalonylationPLTISSLKDGGKAAQ
CEEEEECCCCCCEEC
57.1626320211
34UbiquitinationPLTISSLKDGGKAAQ
CEEEEECCCCCCEEC
57.16-
71AcetylationLEAQNKIKGCTGSLN
HHHCHHHCCCCCCHH
49.9326051181
71MalonylationLEAQNKIKGCTGSLN
HHHCHHHCCCCCCHH
49.9326320211
74PhosphorylationQNKIKGCTGSLNMTL
CHHHCCCCCCHHHHH
38.1729214152
76PhosphorylationKIKGCTGSLNMTLQR
HHCCCCCCHHHHHHH
9.8325159151
80PhosphorylationCTGSLNMTLQRASAA
CCCCHHHHHHHHHCC
20.7522199227
85PhosphorylationNMTLQRASAAPKPEP
HHHHHHHHCCCCCCC
27.4426437602
89AcetylationQRASAAPKPEPVPVQ
HHHHCCCCCCCCCCC
58.23-
89SuccinylationQRASAAPKPEPVPVQ
HHHHCCCCCCCCCCC
58.23-
89SuccinylationQRASAAPKPEPVPVQ
HHHHCCCCCCCCCCC
58.23-
89SumoylationQRASAAPKPEPVPVQ
HHHHCCCCCCCCCCC
58.2328112733
89UbiquitinationQRASAAPKPEPVPVQ
HHHHCCCCCCCCCCC
58.23-
97AcetylationPEPVPVQKGEPKEVV
CCCCCCCCCCCCCCC
66.5326051181
99 (in isoform 3)Phosphorylation-61.3026437602
105AcetylationGEPKEVVKPVPITSP
CCCCCCCCCCCCCCC
45.5323236377
105MalonylationGEPKEVVKPVPITSP
CCCCCCCCCCCCCCC
45.5326320211
105 (in isoform 2)Phosphorylation-45.5326437602
105 (in isoform 4)Phosphorylation-45.5326437602
105 (in isoform 6)Phosphorylation-45.5326437602
105 (in isoform 7)Phosphorylation-45.5326437602
107 (in isoform 3)Phosphorylation-4.4226437602
108 (in isoform 2)Phosphorylation-32.4426437602
108 (in isoform 4)Phosphorylation-32.4426437602
108 (in isoform 6)Phosphorylation-32.4426437602
108 (in isoform 7)Phosphorylation-32.4426437602
110O-linked_GlycosylationVVKPVPITSPAVSKV
CCCCCCCCCCCEEEE
23.6932574038
110O-linked_GlycosylationVVKPVPITSPAVSKV
CCCCCCCCCCCEEEE
23.6920068231
110PhosphorylationVVKPVPITSPAVSKV
CCCCCCCCCCCEEEE
23.6929255136
111O-linked_GlycosylationVKPVPITSPAVSKVT
CCCCCCCCCCEEEEC
16.1620068230
111PhosphorylationVKPVPITSPAVSKVT
CCCCCCCCCCEEEEC
16.1629255136
115O-linked_GlycosylationPITSPAVSKVTSTNN
CCCCCCEEEECCCCC
24.4220068230
115PhosphorylationPITSPAVSKVTSTNN
CCCCCCEEEECCCCC
24.4230278072
116AcetylationITSPAVSKVTSTNNM
CCCCCEEEECCCCCC
42.8226051181
118PhosphorylationSPAVSKVTSTNNMAY
CCCEEEECCCCCCCC
33.3026356563
119O-linked_GlycosylationPAVSKVTSTNNMAYN
CCEEEECCCCCCCCC
31.9320068230
119PhosphorylationPAVSKVTSTNNMAYN
CCEEEECCCCCCCCC
31.9326657352
120PhosphorylationAVSKVTSTNNMAYNK
CEEEECCCCCCCCCC
22.6526356563
124 (in isoform 3)Phosphorylation-13.5825159151
125PhosphorylationTSTNNMAYNKAPRPF
CCCCCCCCCCCCCCC
13.3624927040
128 (in isoform 3)Phosphorylation-11.1627762562
134O-linked_GlycosylationKAPRPFGSVSSPKVT
CCCCCCCCCCCCCCC
21.1420068230
134PhosphorylationKAPRPFGSVSSPKVT
CCCCCCCCCCCCCCC
21.1425159151
136O-linked_GlycosylationPRPFGSVSSPKVTSI
CCCCCCCCCCCCCCC
42.4920068230
136PhosphorylationPRPFGSVSSPKVTSI
CCCCCCCCCCCCCCC
42.4925159151
137O-linked_GlycosylationRPFGSVSSPKVTSIP
CCCCCCCCCCCCCCC
26.9520068230
137PhosphorylationRPFGSVSSPKVTSIP
CCCCCCCCCCCCCCC
26.9519664994
141O-linked_GlycosylationSVSSPKVTSIPSPSS
CCCCCCCCCCCCCCC
27.3720068230
142O-linked_GlycosylationVSSPKVTSIPSPSSA
CCCCCCCCCCCCCCC
35.1720068230
144PhosphorylationSPKVTSIPSPSSAFT
CCCCCCCCCCCCCCC
39.70-
144 (in isoform 2)Phosphorylation-39.7025159151
144 (in isoform 6)Phosphorylation-39.7025159151
144 (in isoform 7)Phosphorylation-39.7025159151
147O-linked_GlycosylationVTSIPSPSSAFTPAH
CCCCCCCCCCCCCCC
38.3420068230
148PhosphorylationTSIPSPSSAFTPAHA
CCCCCCCCCCCCCCC
30.68-
148 (in isoform 2)Phosphorylation-30.6827762562
148 (in isoform 6)Phosphorylation-30.6827762562
148 (in isoform 7)Phosphorylation-30.6827762562
151O-linked_GlycosylationPSPSSAFTPAHATTS
CCCCCCCCCCCCCCC
21.2020068230
156O-linked_GlycosylationAFTPAHATTSSHASP
CCCCCCCCCCCCCCC
19.8320068230
159O-linked_GlycosylationPAHATTSSHASPSPV
CCCCCCCCCCCCCCC
22.4520068230
162O-linked_GlycosylationATTSSHASPSPVAAV
CCCCCCCCCCCCCCC
22.0820068230
164O-linked_GlycosylationTSSHASPSPVAAVTP
CCCCCCCCCCCCCCC
29.5220068230
170O-linked_GlycosylationPSPVAAVTPPLFAAS
CCCCCCCCCCEEECC
17.9220068230
190PhosphorylationANLSADQSPSALSAG
CCCCCCCCHHHHHCC
22.7526657352
192PhosphorylationLSADQSPSALSAGKT
CCCCCCHHHHHCCCC
47.2726074081
193 (in isoform 3)Phosphorylation-14.6625159151
195PhosphorylationDQSPSALSAGKTAVN
CCCHHHHHCCCCCCC
34.3926074081
199PhosphorylationSALSAGKTAVNVPRQ
HHHHCCCCCCCCCCC
34.6126074081
202UbiquitinationSAGKTAVNVPRQPTV
HCCCCCCCCCCCCCE
35.2921906983
207 (in isoform 3)Phosphorylation-30.0726437602
208PhosphorylationVNVPRQPTVTSVCSE
CCCCCCCCEEEECCH
28.2527273156
210PhosphorylationVPRQPTVTSVCSETS
CCCCCCEEEECCHHH
20.2320873877
211O-linked_GlycosylationPRQPTVTSVCSETSQ
CCCCCEEEECCHHHH
19.4520068230
211PhosphorylationPRQPTVTSVCSETSQ
CCCCCEEEECCHHHH
19.4520873877
213PhosphorylationQPTVTSVCSETSQEL
CCCEEEECCHHHHHH
2.81-
213S-nitrosylationQPTVTSVCSETSQEL
CCCEEEECCHHHHHH
2.8122178444
213 (in isoform 2)Phosphorylation-2.8125159151
214PhosphorylationPTVTSVCSETSQELA
CCEEEECCHHHHHHH
41.5826657352
216PhosphorylationVTSVCSETSQELAEG
EEEECCHHHHHHHHH
21.2920873877
217PhosphorylationTSVCSETSQELAEGQ
EEECCHHHHHHHHHH
20.0127273156
227 (in isoform 2)Phosphorylation-26.8926437602
228PhosphorylationAEGQRRGSQGDSKQQ
HHHHCCCCCCCCCCC
29.2227273156
232PhosphorylationRRGSQGDSKQQNGPP
CCCCCCCCCCCCCCC
38.9126699800
247PhosphorylationRKHIVERYTEFYHVP
CHHHHHHHHEEEECC
9.3421945579
248PhosphorylationKHIVERYTEFYHVPT
HHHHHHHHEEEECCC
26.3221945579
250PhosphorylationIVERYTEFYHVPTHS
HHHHHHEEEECCCCC
3.8417016520
251PhosphorylationVERYTEFYHVPTHSD
HHHHHEEEECCCCCH
8.8221945579
252PhosphorylationERYTEFYHVPTHSDA
HHHHEEEECCCCCHH
25.1318083107
255O-linked_GlycosylationTEFYHVPTHSDASKK
HEEEECCCCCHHHHH
32.68OGP
255PhosphorylationTEFYHVPTHSDASKK
HEEEECCCCCHHHHH
32.6821945579
257PhosphorylationFYHVPTHSDASKKRL
EEECCCCCHHHHHHH
37.0321945579
260PhosphorylationVPTHSDASKKRLIED
CCCCCHHHHHHHCCC
43.6421945579
2612-HydroxyisobutyrylationPTHSDASKKRLIEDT
CCCCHHHHHHHCCCC
43.57-
261AcetylationPTHSDASKKRLIEDT
CCCCHHHHHHHCCCC
43.5730589877
261UbiquitinationPTHSDASKKRLIEDT
CCCCHHHHHHHCCCC
43.57-
262AcetylationTHSDASKKRLIEDTE
CCCHHHHHHHCCCCC
50.3630589871
275PhosphorylationTEDWRPRTGTTQSRS
CCCCCCCCCCCCCCE
41.3828555341
277PhosphorylationDWRPRTGTTQSRSFR
CCCCCCCCCCCCEEE
22.5028102081
278PhosphorylationWRPRTGTTQSRSFRI
CCCCCCCCCCCEEEE
26.3724719451
280PhosphorylationPRTGTTQSRSFRILA
CCCCCCCCCEEEEEE
28.0026434776
282PhosphorylationTGTTQSRSFRILAQI
CCCCCCCEEEEEEEE
24.9126434776
290PhosphorylationFRILAQITGTEHLKE
EEEEEEECCCHHHHH
26.4323403867
292PhosphorylationILAQITGTEHLKESE
EEEEECCCHHHHHHH
16.1623403867
296UbiquitinationITGTEHLKESEADNT
ECCCHHHHHHHCCCC
62.19-
305UbiquitinationSEADNTKKANNSQEP
HHCCCCCCCCCCCCC
55.0721890473
309O-linked_GlycosylationNTKKANNSQEPSPQL
CCCCCCCCCCCCHHH
35.4120068230
309PhosphorylationNTKKANNSQEPSPQL
CCCCCCCCCCCCHHH
35.4129255136
313O-linked_GlycosylationANNSQEPSPQLASSV
CCCCCCCCHHHHHHH
25.2420068230
313PhosphorylationANNSQEPSPQLASSV
CCCCCCCCHHHHHHH
25.2419664994
318PhosphorylationEPSPQLASSVASTRS
CCCHHHHHHHHHCCC
33.6630266825
319O-linked_GlycosylationPSPQLASSVASTRSM
CCHHHHHHHHHCCCC
18.9820068230
319PhosphorylationPSPQLASSVASTRSM
CCHHHHHHHHHCCCC
18.9830266825
322PhosphorylationQLASSVASTRSMPES
HHHHHHHHCCCCCHH
23.3830266825
323PhosphorylationLASSVASTRSMPESL
HHHHHHHCCCCCHHC
19.6130266825
325PhosphorylationSSVASTRSMPESLDS
HHHHHCCCCCHHCCC
38.4820873877
329PhosphorylationSTRSMPESLDSPTSG
HCCCCCHHCCCCCCC
31.4426657352
332PhosphorylationSMPESLDSPTSGRPG
CCCHHCCCCCCCCCC
35.0628192239
334PhosphorylationPESLDSPTSGRPGVT
CHHCCCCCCCCCCCC
48.0029255136
335O-linked_GlycosylationESLDSPTSGRPGVTS
HHCCCCCCCCCCCCC
35.8720068230
335PhosphorylationESLDSPTSGRPGVTS
HHCCCCCCCCCCCCC
35.8729255136
350AcetylationLTAAAAFKPVGSTGV
HHEHCCCCCCCCCCC
33.78-
354PhosphorylationAAFKPVGSTGVIKSP
CCCCCCCCCCCEECC
23.4025850435
355PhosphorylationAFKPVGSTGVIKSPS
CCCCCCCCCCEECCC
29.5525850435
360PhosphorylationGSTGVIKSPSWQRPN
CCCCCEECCCCCCCC
17.0325159151
362PhosphorylationTGVIKSPSWQRPNQG
CCCEECCCCCCCCCC
42.8222167270
372PhosphorylationRPNQGVPSTGRISNS
CCCCCCCCCCEECCC
40.8823927012
373PhosphorylationPNQGVPSTGRISNSA
CCCCCCCCCEECCCC
25.1423927012
375MethylationQGVPSTGRISNSATY
CCCCCCCEECCCCEE
29.29115482099
377PhosphorylationVPSTGRISNSATYSG
CCCCCEECCCCEECC
24.3021945579
379PhosphorylationSTGRISNSATYSGSV
CCCEECCCCEECCCE
18.3921945579
381PhosphorylationGRISNSATYSGSVAP
CEECCCCEECCCEEC
20.3121945579
382PhosphorylationRISNSATYSGSVAPA
EECCCCEECCCEECC
15.6821945579
383PhosphorylationISNSATYSGSVAPAN
ECCCCEECCCEECCC
21.9021945579
385PhosphorylationNSATYSGSVAPANSA
CCCEECCCEECCCCC
14.7921945579
391PhosphorylationGSVAPANSALGQTQP
CCEECCCCCCCCCCC
27.2921945579
396PhosphorylationANSALGQTQPSDQDT
CCCCCCCCCCCCHHH
40.4221945579
399PhosphorylationALGQTQPSDQDTLVQ
CCCCCCCCCHHHHHH
37.7821945579
403PhosphorylationTQPSDQDTLVQRAEH
CCCCCHHHHHHHHHH
24.1621945579
4152-HydroxyisobutyrylationAEHIPAGKRTPMCAH
HHHCCCCCCCCCCCC
56.03-
415AcetylationAEHIPAGKRTPMCAH
HHHCCCCCCCCCCCC
56.0325953088
415UbiquitinationAEHIPAGKRTPMCAH
HHHCCCCCCCCCCCC
56.03-
417PhosphorylationHIPAGKRTPMCAHCN
HCCCCCCCCCCCCCC
20.8929214152
419SulfoxidationPAGKRTPMCAHCNQV
CCCCCCCCCCCCCCE
2.8930846556
438PhosphorylationFLVALGKSWHPEEFN
HHHCCCCCCCHHHCC
28.9020873877
452PhosphorylationNCAHCKNTMAYIGFV
CCHHCCCCHHEEEEE
6.6721406692
453SulfoxidationCAHCKNTMAYIGFVE
CHHCCCCHHEEEEEE
3.5930846556
455PhosphorylationHCKNTMAYIGFVEEK
HCCCCHHEEEEEECC
7.2521406692
466PhosphorylationVEEKGALYCELCYEK
EECCCCEEEEHHHHH
5.3728152594
471PhosphorylationALYCELCYEKFFAPE
CEEEEHHHHHHHCCC
34.4828152594
473AcetylationYCELCYEKFFAPECG
EEEHHHHHHHCCCCC
21.2126051181
485UbiquitinationECGRCQRKILGEVIS
CCCHHHHHHHHHHHH
19.1921890473
5822-HydroxyisobutyrylationGQTFFSKKDKPLCKK
CCCCCCCCCCCCHHH
70.55-
5882-HydroxyisobutyrylationKKDKPLCKKHAHSVN
CCCCCCHHHCCCCCC
56.10-
589UbiquitinationKDKPLCKKHAHSVNF
CCCCCHHHCCCCCCC
45.06-
593PhosphorylationLCKKHAHSVNF----
CHHHCCCCCCC----
21.3824670416

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

Oops, there are no upstream regulatory protein records of PDLI5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDLI5_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
89Sumoylation92 (3)PLrs200495769
  • Asparaginase-induced acute pancreatitis in acute lymphoblastic leukemia (onset time)
27114598
97Acetylation92 (5)PLrs200495769
  • Asparaginase-induced acute pancreatitis in acute lymphoblastic leukemia (onset time)
27114598
134Phosphorylation136 (2)SFrs2452600
  • Coronary artery disease
29212778
136Phosphorylation136 (0)SFrs2452600
  • Coronary artery disease
29212778
137Phosphorylation136 (1)SFrs2452600
  • Coronary artery disease
29212778
138Phosphorylation136 (2)SFrs2452600
  • Coronary artery disease
29212778
141Phosphorylation136 (5)SFrs2452600
  • Coronary artery disease
29212778
142Phosphorylation136 (6)SFrs2452600
  • Coronary artery disease
29212778

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI39_HUMANTRIM39physical
16189514
CAC1B_HUMANCACNA1Bphysical
12665800
KPCB_HUMANPRKCBphysical
8940095
KPCE_HUMANPRKCEphysical
8940095
SIN3A_HUMANSIN3Aphysical
22939629
CALU_HUMANCALUphysical
22863883
IF4A3_HUMANEIF4A3physical
22863883
TRMB_HUMANMETTL1physical
22863883
NPL4_HUMANNPLOC4physical
22863883
PDE12_HUMANPDE12physical
22863883
RD23B_HUMANRAD23Bphysical
22863883
TPD52_HUMANTPD52physical
22863883
CC136_HUMANCCDC136physical
25416956
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
DNJC8_HUMANDNAJC8physical
26344197
MP2K1_HUMANMAP2K1physical
26344197
MP2K2_HUMANMAP2K2physical
26344197
TPM2_HUMANTPM2physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDLI5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-111; SER-137; SER-309AND SER-313, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-136; SER-137AND TYR-251, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-111 ANDSER-137, AND MASS SPECTROMETRY.
"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-309 AND SER-313, ANDMASS SPECTROMETRY.
"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-251, AND MASSSPECTROMETRY.

TOP