DNLI3_HUMAN - dbPTM
DNLI3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNLI3_HUMAN
UniProt AC P49916
Protein Name DNA ligase 3
Gene Name LIG3
Organism Homo sapiens (Human).
Sequence Length 1009
Subcellular Localization Isoform 1: Mitochondrion . Contains an N-terminal mitochondrial transit peptide.
Isoform 2: Mitochondrion . Contains an N-terminal mitochondrial transit peptide.
Isoform 3: Nucleus . Lacks the N-terminal mitochondrial transit peptide.
Is
Protein Description Isoform 3 functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. Isoform 1 is targeted to mitochondria, where it functions as DNA ligase in mitochondrial base-excision DNA repair. [PubMed: 10207110]
Protein Sequence MSLAFKIFFPQTLRALSRKELCLFRKHHWRDVRQFSQWSETDLLHGHPLFLRRKPVLSFQGSHLRSRATYLVFLPGLHVGLCSGPCEMAEQRFCVDYAKRGTAGCKKCKEKIVKGVCRIGKVVPNPFSESGGDMKEWYHIKCMFEKLERARATTKKIEDLTELEGWEELEDNEKEQITQHIADLSSKAAGTPKKKAVVQAKLTTTGQVTSPVKGASFVTSTNPRKFSGFSAKPNNSGEAPSSPTPKRSLSSSKCDPRHKDCLLREFRKLCAMVADNPSYNTKTQIIQDFLRKGSAGDGFHGDVYLTVKLLLPGVIKTVYNLNDKQIVKLFSRIFNCNPDDMARDLEQGDVSETIRVFFEQSKSFPPAAKSLLTIQEVDEFLLRLSKLTKEDEQQQALQDIASRCTANDLKCIIRLIKHDLKMNSGAKHVLDALDPNAYEAFKASRNLQDVVERVLHNAQEVEKEPGQRRALSVQASLMTPVQPMLAEACKSVEYAMKKCPNGMFSEIKYDGERVQVHKNGDHFSYFSRSLKPVLPHKVAHFKDYIPQAFPGGHSMILDSEVLLIDNKTGKPLPFGTLGVHKKAAFQDANVCLFVFDCIYFNDVSLMDRPLCERRKFLHDNMVEIPNRIMFSEMKRVTKALDLADMITRVIQEGLEGLVLKDVKGTYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGQGSKGGMMSIFLMGCYDPGSQKWCTVTKCAGGHDDATLARLQNELDMVKISKDPSKIPSWLKVNKIYYPDFIVPDPKKAAVWEITGAEFSKSEAHTADGISIRFPRCTRIRDDKDWKSATNLPQLKELYQLSKEKADFTVVAGDEGSSTTGGSSEENKGPSGSAVSRKAPSKPSASTKKAEGKLSNSNSKDGNMQTAKPSAMKVGEKLATKSSPVKVGEKRKAADETLCQTKVLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC
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
99AcetylationRFCVDYAKRGTAGCK
HHHHHHHHCCCCCHH
45.1726051181
109UbiquitinationTAGCKKCKEKIVKGV
CCCHHHHHHHHHCCC
71.5624816145
111AcetylationGCKKCKEKIVKGVCR
CHHHHHHHHHCCCCC
37.997683619
114SumoylationKCKEKIVKGVCRIGK
HHHHHHHCCCCCCCC
49.45-
114SumoylationKCKEKIVKGVCRIGK
HHHHHHHCCCCCCCC
49.45-
114UbiquitinationKCKEKIVKGVCRIGK
HHHHHHHCCCCCCCC
49.4529967540
117PhosphorylationEKIVKGVCRIGKVVP
HHHHCCCCCCCCCCC
3.4118669648
118UbiquitinationKIVKGVCRIGKVVPN
HHHCCCCCCCCCCCC
37.9824816145
121UbiquitinationKGVCRIGKVVPNPFS
CCCCCCCCCCCCCCC
37.3729967540
122PhosphorylationGVCRIGKVVPNPFSE
CCCCCCCCCCCCCCC
7.9418669648
123PhosphorylationVCRIGKVVPNPFSES
CCCCCCCCCCCCCCC
4.2818669648
128PhosphorylationKVVPNPFSESGGDMK
CCCCCCCCCCCCCHH
31.9128348404
130PhosphorylationVPNPFSESGGDMKEW
CCCCCCCCCCCHHHH
47.0525159151
140PhosphorylationDMKEWYHIKCMFEKL
CHHHHHHHHHHHHHH
1.8418669648
146AcetylationHIKCMFEKLERARAT
HHHHHHHHHHHHHHH
44.3725953088
146UbiquitinationHIKCMFEKLERARAT
HHHHHHHHHHHHHHH
44.3729967540
154PhosphorylationLERARATTKKIEDLT
HHHHHHHCCCHHHHH
29.3818669648
155PhosphorylationERARATTKKIEDLTE
HHHHHHCCCHHHHHH
47.6118669648
156UbiquitinationRARATTKKIEDLTEL
HHHHHCCCHHHHHHC
49.5929967540
161PhosphorylationTKKIEDLTELEGWEE
CCCHHHHHHCCCHHH
51.34-
191PhosphorylationLSSKAAGTPKKKAVV
HHHHCCCCCCCCEEE
27.4922817900
203PhosphorylationAVVQAKLTTTGQVTS
EEEEEEEECCCCCCC
22.9323927012
204PhosphorylationVVQAKLTTTGQVTSP
EEEEEEECCCCCCCC
39.0923927012
204 (in isoform 2)Phosphorylation-39.09-
205PhosphorylationVQAKLTTTGQVTSPV
EEEEEECCCCCCCCC
22.0023927012
209PhosphorylationLTTTGQVTSPVKGAS
EECCCCCCCCCCCCE
21.3029255136
209 (in isoform 2)Phosphorylation-21.30-
210PhosphorylationTTTGQVTSPVKGASF
ECCCCCCCCCCCCEE
28.9219664994
210 (in isoform 2)Phosphorylation-28.92-
213MethylationGQVTSPVKGASFVTS
CCCCCCCCCCEEECC
52.74115972503
213UbiquitinationGQVTSPVKGASFVTS
CCCCCCCCCCEEECC
52.7432015554
216PhosphorylationTSPVKGASFVTSTNP
CCCCCCCEEECCCCC
28.9923927012
219PhosphorylationVKGASFVTSTNPRKF
CCCCEEECCCCCCCC
28.0228152594
220PhosphorylationKGASFVTSTNPRKFS
CCCEEECCCCCCCCC
22.3825159151
221PhosphorylationGASFVTSTNPRKFSG
CCEEECCCCCCCCCC
39.6225159151
227PhosphorylationSTNPRKFSGFSAKPN
CCCCCCCCCCCCCCC
41.8023927012
227 (in isoform 2)Phosphorylation-41.80-
230PhosphorylationPRKFSGFSAKPNNSG
CCCCCCCCCCCCCCC
38.6223927012
232AcetylationKFSGFSAKPNNSGEA
CCCCCCCCCCCCCCC
47.2626051181
232UbiquitinationKFSGFSAKPNNSGEA
CCCCCCCCCCCCCCC
47.2632015554
236PhosphorylationFSAKPNNSGEAPSSP
CCCCCCCCCCCCCCC
44.6522167270
236 (in isoform 2)Phosphorylation-44.65-
241PhosphorylationNNSGEAPSSPTPKRS
CCCCCCCCCCCCCCC
56.8722167270
241UbiquitinationNNSGEAPSSPTPKRS
CCCCCCCCCCCCCCC
56.8724816145
241 (in isoform 2)Phosphorylation-56.87-
242PhosphorylationNSGEAPSSPTPKRSL
CCCCCCCCCCCCCCC
31.5629255136
242 (in isoform 2)Phosphorylation-31.56-
244PhosphorylationGEAPSSPTPKRSLSS
CCCCCCCCCCCCCCC
43.3122167270
244 (in isoform 2)Phosphorylation-43.31-
248PhosphorylationSSPTPKRSLSSSKCD
CCCCCCCCCCCCCCC
38.4427282143
250PhosphorylationPTPKRSLSSSKCDPR
CCCCCCCCCCCCCHH
33.5427282143
251PhosphorylationTPKRSLSSSKCDPRH
CCCCCCCCCCCCHHH
38.8327282143
316AcetylationLLLPGVIKTVYNLND
HHHHHHHHHHCCCCH
29.5423236377
316 (in isoform 2)Acetylation-29.54-
317PhosphorylationLLPGVIKTVYNLNDK
HHHHHHHHHCCCCHH
19.6628348404
324AcetylationTVYNLNDKQIVKLFS
HHCCCCHHHHHHHHH
40.6325953088
324UbiquitinationTVYNLNDKQIVKLFS
HHCCCCHHHHHHHHH
40.6329967540
328AcetylationLNDKQIVKLFSRIFN
CCHHHHHHHHHHHHC
45.5025953088
369UbiquitinationKSFPPAAKSLLTIQE
CCCCHHHHHCCCHHH
43.68-
389UbiquitinationLRLSKLTKEDEQQQA
HHHHHCCCHHHHHHH
73.8629967540
402PhosphorylationQALQDIASRCTANDL
HHHHHHHHHCCHHHH
28.3729978859
427UbiquitinationLKMNSGAKHVLDALD
HCCCCCCCHHHHHCC
37.4629967540
438PhosphorylationDALDPNAYEAFKASR
HHCCCCHHHHHHHHC
17.9028152594
442AcetylationPNAYEAFKASRNLQD
CCHHHHHHHHCCHHH
53.1225953088
442MalonylationPNAYEAFKASRNLQD
CCHHHHHHHHCCHHH
53.1226320211
442UbiquitinationPNAYEAFKASRNLQD
CCHHHHHHHHCCHHH
53.1232015554
451UbiquitinationSRNLQDVVERVLHNA
HCCHHHHHHHHHHHH
5.3822505724
463AcetylationHNAQEVEKEPGQRRA
HHHHHHHCCCCCCCC
74.5126051181
463UbiquitinationHNAQEVEKEPGQRRA
HHHHHHHCCCCCCCC
74.5124816145
472PhosphorylationPGQRRALSVQASLMT
CCCCCCHHHHHHHCC
15.9330108239
472UbiquitinationPGQRRALSVQASLMT
CCCCCCHHHHHHHCC
15.9324816145
476PhosphorylationRALSVQASLMTPVQP
CCHHHHHHHCCCCHH
11.1130108239
479PhosphorylationSVQASLMTPVQPMLA
HHHHHHCCCCHHHHH
26.1230108239
497UbiquitinationKSVEYAMKKCPNGMF
HHHHHHHHHCCCCCC
42.9532015554
498UbiquitinationSVEYAMKKCPNGMFS
HHHHHHHHCCCCCCC
41.6729967540
508AcetylationNGMFSEIKYDGERVQ
CCCCCEEEECCEEEE
32.9826051181
524PhosphorylationHKNGDHFSYFSRSLK
ECCCCCCCCCCCCCC
23.1129978859
525PhosphorylationKNGDHFSYFSRSLKP
CCCCCCCCCCCCCCC
12.4829978859
527PhosphorylationGDHFSYFSRSLKPVL
CCCCCCCCCCCCCCC
16.8429978859
529PhosphorylationHFSYFSRSLKPVLPH
CCCCCCCCCCCCCCC
39.2820873877
531UbiquitinationSYFSRSLKPVLPHKV
CCCCCCCCCCCCCCC
34.03-
568PhosphorylationVLLIDNKTGKPLPFG
EEEEECCCCCCCCCC
57.6120860994
570UbiquitinationLIDNKTGKPLPFGTL
EEECCCCCCCCCCCC
48.9229967540
581UbiquitinationFGTLGVHKKAAFQDA
CCCCCCCCHHHHCCC
41.5229967540
615AcetylationRPLCERRKFLHDNMV
CCHHHHHHCCHHCCC
59.5025953088
615MalonylationRPLCERRKFLHDNMV
CCHHHHHHCCHHCCC
59.5026320211
615UbiquitinationRPLCERRKFLHDNMV
CCHHHHHHCCHHCCC
59.50-
637PhosphorylationFSEMKRVTKALDLAD
HHHHHHHHHHHHHHH
18.03-
638AcetylationSEMKRVTKALDLADM
HHHHHHHHHHHHHHH
44.0626051181
638UbiquitinationSEMKRVTKALDLADM
HHHHHHHHHHHHHHH
44.06-
647PhosphorylationLDLADMITRVIQEGL
HHHHHHHHHHHHHHH
16.55-
660UbiquitinationGLEGLVLKDVKGTYE
HHCCCEEECCCCCCC
53.6629967540
663AcetylationGLVLKDVKGTYEPGK
CCEEECCCCCCCCCC
56.5225953088
663MalonylationGLVLKDVKGTYEPGK
CCEEECCCCCCCCCC
56.5226320211
663UbiquitinationGLVLKDVKGTYEPGK
CCEEECCCCCCCCCC
56.52-
665PhosphorylationVLKDVKGTYEPGKRH
EEECCCCCCCCCCCE
20.99-
666PhosphorylationLKDVKGTYEPGKRHW
EECCCCCCCCCCCEE
28.88-
720PhosphorylationMGCYDPGSQKWCTVT
EECCCCCCCCEEEEE
33.69-
728UbiquitinationQKWCTVTKCAGGHDD
CCEEEEEEECCCCCH
20.11-
728AcetylationQKWCTVTKCAGGHDD
CCEEEEEEECCCCCH
20.1125953088
728UbiquitinationQKWCTVTKCAGGHDD
CCEEEEEEECCCCCH
20.1121963094
728 (in isoform 1)Ubiquitination-20.1121890473
728 (in isoform 2)Ubiquitination-20.1121890473
737UbiquitinationAGGHDDATLARLQNE
CCCCCHHHHHHHHHH
28.1321890473
749UbiquitinationQNELDMVKISKDPSK
HHHHCCEEECCCHHH
34.3329967540
756UbiquitinationKISKDPSKIPSWLKV
EECCCHHHCCCHHCC
65.1129967540
762UbiquitinationSKIPSWLKVNKIYYP
HHCCCHHCCCEEECC
37.1922817900
765UbiquitinationPSWLKVNKIYYPDFI
CCHHCCCEEECCCCC
34.76-
765UbiquitinationPSWLKVNKIYYPDFI
CCHHCCCEEECCCCC
34.7622817900
765 (in isoform 1)Ubiquitination-34.7621890473
765 (in isoform 2)Ubiquitination-34.7621890473
766PhosphorylationSWLKVNKIYYPDFIV
CHHCCCEEECCCCCC
3.1718669648
767PhosphorylationWLKVNKIYYPDFIVP
HHCCCEEECCCCCCC
15.5628152594
768PhosphorylationLKVNKIYYPDFIVPD
HCCCEEECCCCCCCC
10.3728152594
771UbiquitinationNKIYYPDFIVPDPKK
CEEECCCCCCCCHHH
5.3922817900
774UbiquitinationYYPDFIVPDPKKAAV
ECCCCCCCCHHHHEE
47.5821890473
792PhosphorylationTGAEFSKSEAHTADG
ECCEECCCCCCCCCC
38.5321406692
796PhosphorylationFSKSEAHTADGISIR
ECCCCCCCCCCEEEE
33.2321406692
801PhosphorylationAHTADGISIRFPRCT
CCCCCCEEEECCCCC
17.1521406692
817SumoylationIRDDKDWKSATNLPQ
ECCCCCHHHCCCHHH
40.10-
817MethylationIRDDKDWKSATNLPQ
ECCCCCHHHCCCHHH
40.10110867271
817SumoylationIRDDKDWKSATNLPQ
ECCCCCHHHCCCHHH
40.10-
817UbiquitinationIRDDKDWKSATNLPQ
ECCCCCHHHCCCHHH
40.1029967540
818PhosphorylationRDDKDWKSATNLPQL
CCCCCHHHCCCHHHH
35.7520860994
820PhosphorylationDKDWKSATNLPQLKE
CCCHHHCCCHHHHHH
44.3621406692
826UbiquitinationATNLPQLKELYQLSK
CCCHHHHHHHHHHHH
40.1929967540
829PhosphorylationLPQLKELYQLSKEKA
HHHHHHHHHHHHHHC
14.4326437602
833UbiquitinationKELYQLSKEKADFTV
HHHHHHHHHHCCEEE
72.3532015554
839PhosphorylationSKEKADFTVVAGDEG
HHHHCCEEEEECCCC
18.0230576142
847PhosphorylationVVAGDEGSSTTGGSS
EEECCCCCCCCCCCC
23.5925159151
848PhosphorylationVAGDEGSSTTGGSSE
EECCCCCCCCCCCCC
40.6225159151
849PhosphorylationAGDEGSSTTGGSSEE
ECCCCCCCCCCCCCC
31.0228102081
850PhosphorylationGDEGSSTTGGSSEEN
CCCCCCCCCCCCCCC
41.3028102081
853PhosphorylationGSSTTGGSSEENKGP
CCCCCCCCCCCCCCC
35.6030278072
853 (in isoform 2)Phosphorylation-35.60-
854PhosphorylationSSTTGGSSEENKGPS
CCCCCCCCCCCCCCC
52.8025159151
861PhosphorylationSEENKGPSGSAVSRK
CCCCCCCCCCCCCCC
54.7928450419
863PhosphorylationENKGPSGSAVSRKAP
CCCCCCCCCCCCCCC
29.8128450419
866PhosphorylationGPSGSAVSRKAPSKP
CCCCCCCCCCCCCCC
27.9928450419
871PhosphorylationAVSRKAPSKPSASTK
CCCCCCCCCCCCCCH
63.1621406692
874PhosphorylationRKAPSKPSASTKKAE
CCCCCCCCCCCHHCC
38.2921406692
876PhosphorylationAPSKPSASTKKAEGK
CCCCCCCCCHHCCCC
45.1321406692
877PhosphorylationPSKPSASTKKAEGKL
CCCCCCCCHHCCCCC
35.9621406692
883AcetylationSTKKAEGKLSNSNSK
CCHHCCCCCCCCCCC
40.007910587
885PhosphorylationKKAEGKLSNSNSKDG
HHCCCCCCCCCCCCC
41.5228348404
887PhosphorylationAEGKLSNSNSKDGNM
CCCCCCCCCCCCCCC
38.8221712546
889PhosphorylationGKLSNSNSKDGNMQT
CCCCCCCCCCCCCCC
31.7621712546
890AcetylationKLSNSNSKDGNMQTA
CCCCCCCCCCCCCCC
74.1126051181
898AcetylationDGNMQTAKPSAMKVG
CCCCCCCCHHHHHHH
42.7826822725
900PhosphorylationNMQTAKPSAMKVGEK
CCCCCCHHHHHHHHH
40.04-
903AcetylationTAKPSAMKVGEKLAT
CCCHHHHHHHHHHCC
46.9725953088
907AcetylationSAMKVGEKLATKSSP
HHHHHHHHHCCCCCC
37.1825953088
910PhosphorylationKVGEKLATKSSPVKV
HHHHHHCCCCCCCCC
41.7330266825
911AcetylationVGEKLATKSSPVKVG
HHHHHCCCCCCCCCC
43.2425953088
912PhosphorylationGEKLATKSSPVKVGE
HHHHCCCCCCCCCCC
35.2030266825
913PhosphorylationEKLATKSSPVKVGEK
HHHCCCCCCCCCCCH
34.9623927012
913 (in isoform 2)Phosphorylation-34.96-

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
191TPhosphorylationKinaseCDK1P06493
PSP
191TPhosphorylationKinaseCDK2P24941
PSP
210SPhosphorylationKinaseCDK1P06493
PSP
210SPhosphorylationKinaseCDK2P24941
PSP
913SPhosphorylationKinaseCDK1P06493
PSP
913SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNLI3_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 DNLI3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEIL1_HUMANNEIL1physical
15260972
XRCC1_HUMANXRCC1physical
11352725
PNKP_HUMANPNKPphysical
11163244
PARP1_HUMANPARP1physical
12897160
XRCC5_HUMANXRCC5physical
12897160
XRCC6_HUMANXRCC6physical
12897160
A4_HUMANAPPphysical
21832049
TOP3A_HUMANTOP3Aphysical
26186194
PPCEL_HUMANPREPLphysical
26186194
JMJD4_HUMANJMJD4physical
26186194
CLPX_HUMANCLPXphysical
26186194
RSAD1_HUMANRSAD1physical
26186194
FMC1_HUMANC7orf55physical
26186194
PSME3_HUMANPSME3physical
26186194
NDUS6_HUMANNDUFS6physical
26186194
RGAP1_HUMANRACGAP1physical
26344197
JMJD4_HUMANJMJD4physical
28514442
FMC1_HUMANC7orf55physical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
PPCEL_HUMANPREPLphysical
28514442
NDUS6_HUMANNDUFS6physical
28514442
RSAD1_HUMANRSAD1physical
28514442
SYLM_HUMANLARS2physical
28514442

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
DB00290Bleomycin
Regulatory Network of DNLI3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-316, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-210, 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-227 AND SER-242, ANDMASS SPECTROMETRY.
"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-210, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, 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-210, AND MASSSPECTROMETRY.

TOP