GAK_HUMAN - dbPTM
GAK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAK_HUMAN
UniProt AC O14976
Protein Name Cyclin-G-associated kinase
Gene Name GAK
Organism Homo sapiens (Human).
Sequence Length 1311
Subcellular Localization Cytoplasm, perinuclear region . Golgi apparatus, trans-Golgi network . Cell junction, focal adhesion . Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions.
Protein Description Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1..
Protein Sequence MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF
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------MSLLQSALD
------CCHHHHHHH
49.4419369195
2Phosphorylation------MSLLQSALD
------CCHHHHHHH
49.4428464451
6Phosphorylation--MSLLQSALDFLAG
--CCHHHHHHHHHHC
30.6728348404
16PhosphorylationDFLAGPGSLGGASGR
HHHHCCCCCCCCCCC
27.2924043423
21PhosphorylationPGSLGGASGRDQSDF
CCCCCCCCCCCCCCC
37.3230108239
26PhosphorylationGASGRDQSDFVGQTV
CCCCCCCCCCCCCEE
36.9927499020
73PhosphorylationYALKRLLSNEEEKNR
HHHHHHHCCHHHHHH
46.9525159151
78UbiquitinationLLSNEEEKNRAIIQE
HHCCHHHHHHHHHHH
55.82-
90AcetylationIQEVCFMKKLSGHPN
HHHHHHHHHHCCCCC
30.2525953088
90UbiquitinationIQEVCFMKKLSGHPN
HHHHHHHHHHCCCCC
30.25-
91UbiquitinationQEVCFMKKLSGHPNI
HHHHHHHHHCCCCCH
35.78-
112PhosphorylationASIGKEESDTGQAEF
HHCCCCCCCCCCHHH
41.3821082442
114PhosphorylationIGKEESDTGQAEFLL
CCCCCCCCCCHHHHH
40.2421082442
127UbiquitinationLLLTELCKGQLVEFL
HHHHHHHHHHHHHHH
63.42-
135UbiquitinationGQLVEFLKKMESRGP
HHHHHHHHHHHHCCC
56.23-
153PhosphorylationDTVLKIFYQTCRAVQ
HHHHHHHHHHHHHHH
13.34-
166UbiquitinationVQHMHRQKPPIIHRD
HHHHHHCCCCEECCC
53.36-
175UbiquitinationPIIHRDLKVENLLLS
CEECCCCCHHHEEEC
52.3621906983
182PhosphorylationKVENLLLSNQGTIKL
CHHHEEECCCCEEEE
27.3822210691
186PhosphorylationLLLSNQGTIKLCDFG
EEECCCCEEEECCCC
12.7427067055
201PhosphorylationSATTISHYPDYSWSA
CCCEECCCCCCCHHH
7.3322210691
204PhosphorylationTISHYPDYSWSAQRR
EECCCCCCCHHHHHH
13.9222817900
205PhosphorylationISHYPDYSWSAQRRA
ECCCCCCCHHHHHHH
23.1822210691
207PhosphorylationHYPDYSWSAQRRALV
CCCCCCHHHHHHHHH
14.4821082442
235PhosphorylationTPEIIDLYSNFPIGE
CHHHHHHHCCCCCCC
9.6021945579
276PhosphorylationLRIVNGKYSIPPHDT
EEEECCCEECCCCCC
17.15-
277PhosphorylationRIVNGKYSIPPHDTQ
EEECCCEECCCCCCH
31.91-
285PhosphorylationIPPHDTQYTVFHSLI
CCCCCCHHHHHHHHH
13.63-
290PhosphorylationTQYTVFHSLIRAMLQ
CHHHHHHHHHHHHHC
17.64-
325UbiquitinationAARNVNPKSPITELL
HHCCCCCCCHHHHHH
64.7621906983
326PhosphorylationARNVNPKSPITELLE
HCCCCCCCHHHHHHH
23.8528450419
329PhosphorylationVNPKSPITELLEQNG
CCCCCHHHHHHHHCC
24.7828450419
338PhosphorylationLLEQNGGYGSATLSR
HHHHCCCCCCCCCCC
14.87-
340PhosphorylationEQNGGYGSATLSRGP
HHCCCCCCCCCCCCC
15.0327251275
342PhosphorylationNGGYGSATLSRGPPP
CCCCCCCCCCCCCCC
27.2827251275
344PhosphorylationGYGSATLSRGPPPPV
CCCCCCCCCCCCCCC
30.7327251275
356PhosphorylationPPVGPAGSGYSGGLA
CCCCCCCCCCCCCEE
36.3428348404
359PhosphorylationGPAGSGYSGGLALAE
CCCCCCCCCCEEEEE
29.8824719451
367PhosphorylationGGLALAEYDQPYGGF
CCEEEEEECCCCCCH
17.8027642862
371PhosphorylationLAEYDQPYGGFLDIL
EEEECCCCCCHHHHH
25.0122817900
387PhosphorylationGGTERLFTNLKDTSS
CCHHHHHCCCCCCCH
44.2129978859
390UbiquitinationERLFTNLKDTSSKVI
HHHHCCCCCCCHHHH
62.11-
392PhosphorylationLFTNLKDTSSKVIQS
HHCCCCCCCHHHHHH
33.0628857561
393PhosphorylationFTNLKDTSSKVIQSV
HCCCCCCCHHHHHHH
37.9929978859
394PhosphorylationTNLKDTSSKVIQSVA
CCCCCCCHHHHHHHH
32.7929978859
395AcetylationNLKDTSSKVIQSVAN
CCCCCCHHHHHHHHH
43.037962549
395UbiquitinationNLKDTSSKVIQSVAN
CCCCCCHHHHHHHHH
43.03-
399PhosphorylationTSSKVIQSVANYAKG
CCHHHHHHHHHHHCC
16.4529978859
403PhosphorylationVIQSVANYAKGDLDI
HHHHHHHHHCCCCCH
10.4328152594
405UbiquitinationQSVANYAKGDLDISY
HHHHHHHCCCCCHHH
42.47-
412PhosphorylationKGDLDISYITSRIAV
CCCCCHHHHHCEEEE
14.46-
421PhosphorylationTSRIAVMSFPAEGVE
HCEEEEEECCHHHHH
22.83-
432UbiquitinationEGVESALKNNIEDVR
HHHHHHHHCCHHHEH
47.9021906983
439MethylationKNNIEDVRLFLDSKH
HCCHHHEHHHHCCCC
31.85-
445UbiquitinationVRLFLDSKHPGHYAV
EHHHHCCCCCCCEEE
54.18-
453PhosphorylationHPGHYAVYNLSPRTY
CCCCEEEEECCCCCC
11.3829214152
456PhosphorylationHYAVYNLSPRTYRPS
CEEEEECCCCCCCCC
14.5417192257
540PhosphorylationEAAVYMFSMKRCPPG
HHHHHHHHHCCCCCC
13.5824719451
555PhosphorylationIWPSHKRYIEYMCDM
CCHHHHHHHHHHHHH
11.6927050516
572PhosphorylationEEPITPHSKPILVRA
CCCCCCCCCCEEEEE
41.1327050516
583PhosphorylationLVRAVVMTPVPLFSK
EEEEEEECCCCCCCC
14.99-
589PhosphorylationMTPVPLFSKQRSGCR
ECCCCCCCCCCCCCC
35.2524719451
590UbiquitinationTPVPLFSKQRSGCRP
CCCCCCCCCCCCCCC
42.25-
593PhosphorylationPLFSKQRSGCRPFCE
CCCCCCCCCCCCCEE
39.4928348404
602PhosphorylationCRPFCEVYVGDERVA
CCCCEEEEECCEEEE
4.0429759185
610PhosphorylationVGDERVASTSQEYDK
ECCEEEECCCCHHHH
26.2429759185
612PhosphorylationDERVASTSQEYDKMR
CEEEECCCCHHHHHC
20.6529759185
615PhosphorylationVASTSQEYDKMRDFK
EECCCCHHHHHCCEE
17.1522817900
617UbiquitinationSTSQEYDKMRDFKIE
CCCCHHHHHCCEECC
34.63-
682UbiquitinationPRNATTVKFAKYDLD
CCCCCEEEEEEECCC
37.20-
685AcetylationATTVKFAKYDLDACD
CCEEEEEEECCCCCC
42.2925953088
685UbiquitinationATTVKFAKYDLDACD
CCEEEEEEECCCCCC
42.29-
733MalonylationSMRGLNPKILFSSRE
CCCCCCHHHCCCCHH
51.4732601280
748UbiquitinationEQQDILSKFGKPELP
HHHHHHHHHCCCCCC
55.48-
751UbiquitinationDILSKFGKPELPRQP
HHHHHHCCCCCCCCC
38.15-
760PhosphorylationELPRQPGSTAQYDAG
CCCCCCCCCCCCCCC
27.5328450419
761PhosphorylationLPRQPGSTAQYDAGA
CCCCCCCCCCCCCCC
24.5628450419
764PhosphorylationQPGSTAQYDAGAGSP
CCCCCCCCCCCCCCC
12.8028450419
770PhosphorylationQYDAGAGSPEAEPTD
CCCCCCCCCCCCCCC
21.0221712546
776PhosphorylationGSPEAEPTDSDSPPS
CCCCCCCCCCCCCCC
39.3730278072
778PhosphorylationPEAEPTDSDSPPSSS
CCCCCCCCCCCCCCH
42.3330278072
780PhosphorylationAEPTDSDSPPSSSAD
CCCCCCCCCCCCHHH
42.5430278072
783PhosphorylationTDSDSPPSSSADASR
CCCCCCCCCHHHHHH
40.0730278072
784PhosphorylationDSDSPPSSSADASRF
CCCCCCCCHHHHHHH
35.0130278072
785PhosphorylationSDSPPSSSADASRFL
CCCCCCCHHHHHHHH
34.2130278072
789PhosphorylationPSSSADASRFLHTLD
CCCHHHHHHHHHHCC
24.9024043423
794PhosphorylationDASRFLHTLDWQEEK
HHHHHHHHCCHHHHH
28.6723917254
801UbiquitinationTLDWQEEKEAETGAE
HCCHHHHHHHHHCCC
62.56-
805PhosphorylationQEEKEAETGAENASS
HHHHHHHHCCCCCCC
49.0618691976
811PhosphorylationETGAENASSKESESA
HHCCCCCCCHHHHHH
54.2318691976
812PhosphorylationTGAENASSKESESAL
HCCCCCCCHHHHHHH
37.7218691976
815PhosphorylationENASSKESESALMED
CCCCCHHHHHHHHCC
40.3623927012
817PhosphorylationASSKESESALMEDRD
CCCHHHHHHHHCCCC
35.6628355574
826PhosphorylationLMEDRDESEVSDEGG
HHCCCCCCCCCCCCC
47.8129255136
829PhosphorylationDRDESEVSDEGGSPI
CCCCCCCCCCCCCCC
26.3729255136
834PhosphorylationEVSDEGGSPISSEGQ
CCCCCCCCCCCCCCC
29.8921712546
837PhosphorylationDEGGSPISSEGQEPR
CCCCCCCCCCCCCCC
26.2221082442
838PhosphorylationEGGSPISSEGQEPRA
CCCCCCCCCCCCCCC
46.6021082442
905PhosphorylationPQACKAPSSNTDLLS
HHHCCCCCCCCCHHH
40.8728348404
906PhosphorylationQACKAPSSNTDLLSC
HHCCCCCCCCCHHHH
42.5628348404
908PhosphorylationCKAPSSNTDLLSCLL
CCCCCCCCCHHHHHH
29.9427251275
939O-linked_GlycosylationEDPLLLASPAPPLSV
CCCCEECCCCCCCCC
22.89OGP
939PhosphorylationEDPLLLASPAPPLSV
CCCCEECCCCCCCCC
22.8929496963
945PhosphorylationASPAPPLSVQSTPRG
CCCCCCCCCCCCCCC
24.7226074081
1027PhosphorylationEPSKMTASSSNPDLL
CCCCCCCCCCCCCCC
25.7328348404
1028PhosphorylationPSKMTASSSNPDLLG
CCCCCCCCCCCCCCC
31.5026074081
1029PhosphorylationSKMTASSSNPDLLGG
CCCCCCCCCCCCCCH
50.3026074081
1041PhosphorylationLGGWAAWTETAASAV
CCHHHHCCHHHHHHC
20.8028348404
1043PhosphorylationGWAAWTETAASAVAP
HHHHCCHHHHHHCCC
21.8328348404
1046PhosphorylationAWTETAASAVAPTPA
HCCHHHHHHCCCCCC
22.3228348404
1051PhosphorylationAASAVAPTPATEGPL
HHHHCCCCCCCCCCC
18.8028348404
1054PhosphorylationAVAPTPATEGPLFSP
HCCCCCCCCCCCCCC
42.5528348404
1060PhosphorylationATEGPLFSPGGQPAP
CCCCCCCCCCCCCCC
30.2528348404
1070PhosphorylationGQPAPCGSQASWTKS
CCCCCCCCCCCCCCC
29.3227251275
1073PhosphorylationAPCGSQASWTKSQNP
CCCCCCCCCCCCCCC
27.8627251275
1090PhosphorylationFADLGDLSSGLQGSP
CCCHHHHCCCCCCCC
27.4027251275
1091PhosphorylationADLGDLSSGLQGSPA
CCHHHHCCCCCCCCC
51.3127251275
1096PhosphorylationLSSGLQGSPAGFPPG
HCCCCCCCCCCCCCC
9.9017192257
1116PhosphorylationTATTPKGSSSWQTSR
CCCCCCCCCCCCCCC
27.5920068231
1118PhosphorylationTTPKGSSSWQTSRPP
CCCCCCCCCCCCCCC
25.54-
1123MethylationSSSWQTSRPPAQGAS
CCCCCCCCCCCCCCC
44.61-
1130O-linked_GlycosylationRPPAQGASWPPQAKP
CCCCCCCCCCCCCCC
47.1123301498
1130PhosphorylationRPPAQGASWPPQAKP
CCCCCCCCCCCCCCC
47.11-
1143PhosphorylationKPPPKACTQPRPNYA
CCCCCCCCCCCCCCC
46.6021945579
1149PhosphorylationCTQPRPNYASNFSVI
CCCCCCCCCCCCEEE
17.6821945579
1151PhosphorylationQPRPNYASNFSVIGA
CCCCCCCCCCEEEEC
28.2221945579
1154PhosphorylationPNYASNFSVIGAREE
CCCCCCCEEEECCHH
19.6421945579
1168PhosphorylationERGVRAPSFAQKPKV
HCCCCCCCHHCCCCC
32.0328857561
1172AcetylationRAPSFAQKPKVSEND
CCCCHHCCCCCCCCH
43.2925953088
1172UbiquitinationRAPSFAQKPKVSEND
CCCCHHCCCCCCCCH
43.29-
1176PhosphorylationFAQKPKVSENDFEDL
HHCCCCCCCCHHHHH
36.4926657352
1185PhosphorylationNDFEDLLSNQGFSSR
CHHHHHHHCCCCCCC
34.1120873877
1192MethylationSNQGFSSRSDKKGPK
HCCCCCCCCCCCCCH
47.91-
1213PhosphorylationKQDLAKDTDPLKLKL
HHHHHCCCCHHHHHH
38.52-
1217UbiquitinationAKDTDPLKLKLLDWI
HCCCCHHHHHHHHHH
49.30-
1219UbiquitinationDTDPLKLKLLDWIEG
CCCHHHHHHHHHHCC
45.47-
1265UbiquitinationVAPEQVKKHYRRAVL
CCHHHHHHHHHHHEE
47.19-
1278UbiquitinationVLAVHPDKAAGQPYE
EEECCCCCCCCCCHH
44.58-
1284NitrationDKAAGQPYEQHAKMI
CCCCCCCHHHHHHHH
21.97-

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
412YPhosphorylationKinaseSRCP12931
PSP
1149YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAK_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 GAK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USO1_HUMANUSO1physical
16189514
CDK5_HUMANCDK5physical
9013862
CCNG1_HUMANCCNG1physical
9013862
A4_HUMANAPPphysical
21832049
PPM1B_HUMANPPM1Bphysical
26344197
AP2A1_HUMANAP2A1physical
26496610
AP2A2_HUMANAP2A2physical
26496610
AP2B1_HUMANAP2B1physical
26496610
CALL3_HUMANCALML3physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
AP2M1_HUMANAP2M1physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
CLH1_HUMANCLTCphysical
26496610
CBPM_HUMANCPMphysical
26496610
DAB2_HUMANDAB2physical
26496610
DREB_HUMANDBN1physical
26496610
EPS15_HUMANEPS15physical
26496610
GOGB1_HUMANGOLGB1physical
26496610
HIP1_HUMANHIP1physical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
MYO6_HUMANMYO6physical
26496610
P3C2A_HUMANPIK3C2Aphysical
26496610
PSA5_HUMANPSMA5physical
26496610
SEC13_HUMANSEC13physical
26496610
SP1_HUMANSP1physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
CLH2_HUMANCLTCL1physical
26496610
PICAL_HUMANPICALMphysical
26496610
NUMB_HUMANNUMBphysical
26496610
TNK1_HUMANTNK1physical
26496610
HIP1R_HUMANHIP1Rphysical
26496610
XPR1_HUMANXPR1physical
26496610
SC24C_HUMANSEC24Cphysical
26496610
EPN4_HUMANCLINT1physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
FEM1B_HUMANFEM1Bphysical
26496610
ACK1_HUMANTNK2physical
26496610
RBM14_HUMANRBM14physical
26496610
KIF3A_HUMANKIF3Aphysical
26496610
SYNPO_HUMANSYNPOphysical
26496610
CE162_HUMANCEP162physical
26496610
AAK1_HUMANAAK1physical
26496610
EDRF1_HUMANEDRF1physical
26496610
SERA_HUMANPHGDHphysical
26496610
CHM4A_HUMANCHMP4Aphysical
26496610
LIMA1_HUMANLIMA1physical
26496610
GTSE1_HUMANGTSE1physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
BMP2K_HUMANBMP2Kphysical
26496610
KDIS_HUMANKIDINS220physical
26496610
STALP_HUMANSTAMBPL1physical
26496610
DEN1A_HUMANDENND1Aphysical
26496610
AFAP1_HUMANAFAP1physical
26496610
ZN106_HUMANZNF106physical
26496610
INF2_HUMANINF2physical
26496610
WNK1_HUMANWNK1physical
26496610
CPSF7_HUMANCPSF7physical
26496610
PUS7L_HUMANPUS7Lphysical
26496610
PAR10_HUMANPARP10physical
26496610
STON2_HUMANSTON2physical
26496610
MISP_HUMANMISPphysical
26496610
ACTT1_HUMANACTRT1physical
26496610
FA83B_HUMANFAM83Bphysical
26496610
FA83H_HUMANFAM83Hphysical
26496610

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 GAK_HUMAN

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Related Literatures of Post-Translational Modification
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-826 AND SER-829, ANDMASS SPECTROMETRY.
"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-16; SER-326; TYR-615;THR-776; SER-778; SER-780; THR-805; SER-815; SER-817; SER-826;SER-829; SER-834; SER-837; SER-838; SER-939; SER-1070; SER-1073;SER-1176 AND SER-1185, AND MASS SPECTROMETRY.
"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-826; SER-829 ANDSER-834, AND MASS 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-16; SER-456; SER-770;SER-780; SER-826; SER-829; SER-834 AND SER-1096, AND MASSSPECTROMETRY.

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