OTUD4_HUMAN - dbPTM
OTUD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTUD4_HUMAN
UniProt AC Q01804
Protein Name OTU domain-containing protein 4
Gene Name OTUD4 {ECO:0000312|HGNC:HGNC:24949}
Organism Homo sapiens (Human).
Sequence Length 1114
Subcellular Localization Cytoplasm . Nucleus . Primarily cytoplasmic.
Protein Description Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. [PubMed: 23827681]
Protein Sequence MEAAVGVPDGGDQGGAGPREDATPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIHYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYPIKYKESSAMCQSLLYELLYEKVFKTDVSKIVMELDTLEVADEDNSEISDSEDDSCKSKTAAAAADVNGFKPLSGNEQLKNNGNSTSLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLVEELGKKHTSKNLKAPPPESWNTVSGKKMKKPSTSGQNFHSDVDYRGPKNPSKPIKAPSALPPRLQHPSGVRQHAFSSHSSGSQSQKFSSEHKNLSRTPSQIIRKPDRERVEDFDHTSRESNYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVNQSASQSSNPCVQRKSSHVGDRKGSRRRMDTEERKDKDSIHGHSQLDKRPEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAPIPVLSVTQTLTTGPDSAVSQAHLTPSPVPVSIQAVNQPLMPLPQTLSLYQDPLYPGFPCNEKGDRAIVPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVPVYPHNPWFQEAPAAQNESDCTCTDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKNMFPQPSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDEKGELDLSLENLDLSKDCGSVSTVDEFPEARGEHVHSLPEASVSSKPDEGRTEQSSQTRKADTALASIPPVAEGKAHPPTQILNRERETVPVELEPKRTIQSLKEKTEKVKDPKTAADVVSPGANSVDSRVQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGYSGRGGYQHVRSEESWKGQPSRSRDEGYQYHRNVRGRPFRGDRRRSGMGDGHRGQHT
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
1Acetylation-------MEAAVGVP
-------CCCCCCCC
36.3022223895
41AcetylationLYRKLVAKDGSCLFR
HHHHHHCCCCCHHHH
55.9623749302
41UbiquitinationLYRKLVAKDGSCLFR
HHHHHHCCCCCHHHH
55.9633845483
55PhosphorylationRAVAEQVLHSQSRHV
HHHHHHHHHCCCCCH
3.0027251275
120PhosphorylationYRKDFIIYREPNVSP
HCCCEEEEECCCCCH
12.2429395066
126PhosphorylationIYREPNVSPSQVTEN
EEECCCCCHHHCCCC
26.0229395066
128PhosphorylationREPNVSPSQVTENNF
ECCCCCHHHCCCCCC
29.7629395066
131PhosphorylationNVSPSQVTENNFPEK
CCCHHHCCCCCCCCE
25.9229395066
144PhosphorylationEKVLLCFSNGNHYDI
CEEEEEEECCCEEEE
42.7127251275
147UbiquitinationLLCFSNGNHYDIVYP
EEEEECCCEEEEEEE
34.4927667366
154UbiquitinationNHYDIVYPIKYKESS
CEEEEEEEEECCHHH
13.0027667366
160PhosphorylationYPIKYKESSAMCQSL
EEEECCHHHHHHHHH
21.17-
161PhosphorylationPIKYKESSAMCQSLL
EEECCHHHHHHHHHH
22.55-
166PhosphorylationESSAMCQSLLYELLY
HHHHHHHHHHHHHHH
18.5329395066
169PhosphorylationAMCQSLLYELLYEKV
HHHHHHHHHHHHHHH
15.15-
190PhosphorylationKIVMELDTLEVADED
HHHHHHCCEEECCCC
37.1329514088
199PhosphorylationEVADEDNSEISDSED
EECCCCCCCCCCCCC
48.9429514088
202PhosphorylationDEDNSEISDSEDDSC
CCCCCCCCCCCCCCH
30.9129395066
204PhosphorylationDNSEISDSEDDSCKS
CCCCCCCCCCCCHHH
35.8129395066
208PhosphorylationISDSEDDSCKSKTAA
CCCCCCCCHHHHHHH
35.4529514088
212UbiquitinationEDDSCKSKTAAAAAD
CCCCHHHHHHHHHHC
27.9027667366
219UbiquitinationKTAAAAADVNGFKPL
HHHHHHHCCCCCCCC
29.6827667366
234UbiquitinationSGNEQLKNNGNSTSL
CCCHHHHHCCCCCCC
49.8129967540
257UbiquitinationSLNPAVYRNVEYEIW
HCCHHHHCCCEEEEE
17.1829967540
266MethylationVEYEIWLKSKQAQQK
CEEEEEECCHHHHHH
28.03115974523
278UbiquitinationQQKRDYSIAAGLQYE
HHHCCCCHHHCCEEE
6.9129967540
282UbiquitinationDYSIAAGLQYEVGDK
CCCHHHCCEEEECCE
31.2729967540
284PhosphorylationSIAAGLQYEVGDKCQ
CHHHCCEEEECCEEE
27.3621945579
299AcetylationVRLDHNGKFLNADVQ
EEECCCCCCCCEEEE
7.2426051181
329UbiquitinationKKHTSKNLKAPPPES
CCCCCCCCCCCCCHH
69.142190698
330 (in isoform 1)Ubiquitination-25.6221906983
341PhosphorylationPESWNTVSGKKMKKP
CHHCCCCCCCCCCCC
29.3025159151
343AcetylationSWNTVSGKKMKKPST
HCCCCCCCCCCCCCC
60.5225953088
344AcetylationWNTVSGKKMKKPSTS
CCCCCCCCCCCCCCC
8.437298789
344UbiquitinationWNTVSGKKMKKPSTS
CCCCCCCCCCCCCCC
8.4329967540
349PhosphorylationGKKMKKPSTSGQNFH
CCCCCCCCCCCCCCC
45.4629978859
350PhosphorylationKKMKKPSTSGQNFHS
CCCCCCCCCCCCCCC
42.6025159151
351PhosphorylationKMKKPSTSGQNFHSD
CCCCCCCCCCCCCCC
26.9224719451
361PhosphorylationNFHSDVDYRGPKNPS
CCCCCCCCCCCCCCC
50.93-
368PhosphorylationYRGPKNPSKPIKAPS
CCCCCCCCCCCCCCC
52.6027470641
375PhosphorylationSKPIKAPSALPPRLQ
CCCCCCCCCCCCCCC
24.0320068231
378PhosphorylationIKAPSALPPRLQHPS
CCCCCCCCCCCCCCC
50.9224719451
380MethylationAPSALPPRLQHPSGV
CCCCCCCCCCCCCCC
7.27115486099
385PhosphorylationPPRLQHPSGVRQHAF
CCCCCCCCCCCCCCC
24.0720068231
393PhosphorylationGVRQHAFSSHSSGSQ
CCCCCCCCCCCCCCC
22.4230576142
394PhosphorylationVRQHAFSSHSSGSQS
CCCCCCCCCCCCCCC
25.4530576142
396PhosphorylationQHAFSSHSSGSQSQK
CCCCCCCCCCCCCHH
36.7230576142
399PhosphorylationFSSHSSGSQSQKFSS
CCCCCCCCCCHHCCH
54.1030576142
401PhosphorylationSHSSGSQSQKFSSEH
CCCCCCCCHHCCHHC
43.08-
412PhosphorylationSSEHKNLSRTPSQII
CHHCCCCCCCHHHHH
54.5525159151
414PhosphorylationEHKNLSRTPSQIIRK
HCCCCCCCHHHHHCC
24.1130266825
416PhosphorylationKNLSRTPSQIIRKPD
CCCCCCHHHHHCCCC
36.0123401153
434PhosphorylationVEDFDHTSRESNYFG
HHCCCCCCHHHCCCC
53.1421712546
437PhosphorylationFDHTSRESNYFGLSP
CCCCCHHHCCCCCCH
31.2528796482
438PhosphorylationDHTSRESNYFGLSPE
CCCCHHHCCCCCCHH
14.3317389395
439PhosphorylationHTSRESNYFGLSPEE
CCCHHHCCCCCCHHH
10.4423927012
443PhosphorylationESNYFGLSPEERREK
HHCCCCCCHHHHHHH
53.1319664994
452PhosphorylationEERREKQAIEESRLL
HHHHHHHHHHHHHHH
5.8227251275
460PhosphorylationIEESRLLYEIQNRDE
HHHHHHHHHHHCCCC
37.7621945579
474PhosphorylationEQAFPALSSSSVNQS
CCHHHHCCCCCCCCC
27.7326074081
475PhosphorylationQAFPALSSSSVNQSA
CHHHHCCCCCCCCCC
34.6221945579
476PhosphorylationAFPALSSSSVNQSAS
HHHHCCCCCCCCCCC
27.3426074081
477PhosphorylationFPALSSSSVNQSASQ
HHHCCCCCCCCCCCC
9.0321945579
480PhosphorylationLSSSSVNQSASQSSN
CCCCCCCCCCCCCCC
25.3727251275
481PhosphorylationSSSSVNQSASQSSNP
CCCCCCCCCCCCCCC
11.2224719451
483PhosphorylationSSVNQSASQSSNPCV
CCCCCCCCCCCCCCC
51.0726074081
485PhosphorylationVNQSASQSSNPCVQR
CCCCCCCCCCCCCHH
36.8321945579
486PhosphorylationNQSASQSSNPCVQRK
CCCCCCCCCCCCHHC
38.9621945579
492PhosphorylationSSNPCVQRKSSHVGD
CCCCCCHHCCCCCCC
38.9427251275
494PhosphorylationNPCVQRKSSHVGDRK
CCCCHHCCCCCCCCC
25.8123882029
495PhosphorylationPCVQRKSSHVGDRKG
CCCHHCCCCCCCCCC
34.3726074081
503PhosphorylationHVGDRKGSRRRMDTE
CCCCCCCCCCCCCHH
38.6023882029
517PhosphorylationEERKDKDSIHGHSQL
HHHCCCCCCCCCCCC
6.9128555341
531PhosphorylationLDKRPEPSTLENITD
CCCCCCCCCCCCCCC
49.1320873877
532PhosphorylationDKRPEPSTLENITDD
CCCCCCCCCCCCCCC
5.7920873877
537PhosphorylationPSTLENITDDKYATV
CCCCCCCCCCCCCCC
46.7520873877
541PhosphorylationENITDDKYATVSSPS
CCCCCCCCCCCCCCC
13.7823927012
543PhosphorylationITDDKYATVSSPSKS
CCCCCCCCCCCCCCC
3.9830266825
544PhosphorylationTDDKYATVSSPSKSK
CCCCCCCCCCCCCCC
31.9821406692
545PhosphorylationDDKYATVSSPSKSKK
CCCCCCCCCCCCCCC
28.9323401153
546PhosphorylationDKYATVSSPSKSKKL
CCCCCCCCCCCCCCC
37.9722167270
547PhosphorylationKYATVSSPSKSKKLE
CCCCCCCCCCCCCCC
52.0521406692
548PhosphorylationYATVSSPSKSKKLEC
CCCCCCCCCCCCCCC
70.4530266825
550PhosphorylationTVSSPSKSKKLECPS
CCCCCCCCCCCCCCC
66.1826074081
557PhosphorylationSKKLECPSPAEQKPA
CCCCCCCCCCCCCCC
25.5925849741
568PhosphorylationQKPAEHVSLSNPAPL
CCCCCCCCCCCCCCE
5.8026074081
578PhosphorylationNPAPLLVSPEVHLTP
CCCCEEECCCCCCCC
39.9026074081
607O-linked_GlycosylationEPTTFGPTGVPAPIP
CCCCCCCCCCCCCCC
26.9223301498
617O-linked_GlycosylationPAPIPVLSVTQTLTT
CCCCCEEEEEEEEEC
3.9323301498
619O-linked_GlycosylationPIPVLSVTQTLTTGP
CCCEEEEEEEEECCC
32.1523301498
621O-linked_GlycosylationPVLSVTQTLTTGPDS
CEEEEEEEEECCCCC
2.6523301498
629UbiquitinationLTTGPDSAVSQAHLT
EECCCCCCCCCCCCC
5.1629967540
657O-linked_GlycosylationPLMPLPQTLSLYQDP
CCCCCCCCEECCCCC
2.5323301498
710PhosphorylationFNLGVKAYSCPMWAP
HHCCCCCCCCCCCCC
19.32-
720PhosphorylationPMWAPHSYLYPLHQA
CCCCCCCHHHHHHHH
3.88-
827PhosphorylationGQLLHADYEESLSGK
CCEEECCHHHHCCCC
41.4819651622
828PhosphorylationQLLHADYEESLSGKN
CEEECCHHHHCCCCC
51.2332142685
835PhosphorylationEESLSGKNMFPQPSF
HHHCCCCCCCCCCCC
6.2127251275
840PhosphorylationGKNMFPQPSFGPNPF
CCCCCCCCCCCCCCC
37.2727251275
857PhosphorylationPVPIAPPFFPHVWYG
CCCCCCCCCCCEECC
5.1527251275
878PhosphorylationIENPVMRQNIVLPSD
CCCCCCCCCEEECCC
18.9027251275
892PhosphorylationDEKGELDLSLENLDL
CCCCCCCEEEECCCC
33.0521406692
893PhosphorylationEKGELDLSLENLDLS
CCCCCCEEEECCCCC
7.0419664994
900PhosphorylationSLENLDLSKDCGSVS
EEECCCCCCCCCCCC
65.4222617229
905PhosphorylationDLSKDCGSVSTVDEF
CCCCCCCCCCCHHCC
3.1830576142
907PhosphorylationSKDCGSVSTVDEFPE
CCCCCCCCCHHCCHH
29.8030576142
908PhosphorylationKDCGSVSTVDEFPEA
CCCCCCCCHHCCHHH
5.31-
917UbiquitinationDEFPEARGEHVHSLP
HCCHHHCCCCCCCCC
36.8624816145
922PhosphorylationARGEHVHSLPEASVS
HCCCCCCCCCCCCCC
2.4130266825
924UbiquitinationGEHVHSLPEASVSSK
CCCCCCCCCCCCCCC
59.8924816145
927PhosphorylationVHSLPEASVSSKPDE
CCCCCCCCCCCCCCC
10.9030266825
929PhosphorylationSLPEASVSSKPDEGR
CCCCCCCCCCCCCCC
46.1630183078
930PhosphorylationLPEASVSSKPDEGRT
CCCCCCCCCCCCCCC
49.3230183078
937PhosphorylationSKPDEGRTEQSSQTR
CCCCCCCCCCCCCCH
47.2927251275
940PhosphorylationDEGRTEQSSQTRKAD
CCCCCCCCCCCHHHC
34.9519664995
941PhosphorylationEGRTEQSSQTRKADT
CCCCCCCCCCHHHCH
51.0416964243
943PhosphorylationRTEQSSQTRKADTAL
CCCCCCCCHHHCHHH
25.2427251275
946PhosphorylationQSSQTRKADTALASI
CCCCCHHHCHHHHCC
35.2327251275
952PhosphorylationKADTALASIPPVAEG
HHCHHHHCCCCCCCC
3.5828555341
958PhosphorylationASIPPVAEGKAHPPT
HCCCCCCCCCCCCCC
23.7824719451
959PhosphorylationSIPPVAEGKAHPPTQ
CCCCCCCCCCCCCCC
34.7224719451
975UbiquitinationLNRERETVPVELEPK
CCCCCCCCCCCCCCH
22.6823000965
981PhosphorylationTVPVELEPKRTIQSL
CCCCCCCCHHHHHHH
53.4424719451
982UbiquitinationVPVELEPKRTIQSLK
CCCCCCCHHHHHHHH
48.0223000965
984PhosphorylationVELEPKRTIQSLKEK
CCCCCHHHHHHHHHH
2.8028555341
988UbiquitinationPKRTIQSLKEKTEKV
CHHHHHHHHHHHHCC
63.5124816145
989UbiquitinationKRTIQSLKEKTEKVK
HHHHHHHHHHHHCCC
71.1924816145
1000O-linked_GlycosylationEKVKDPKTAADVVSP
HCCCCCCCHHHHCCC
14.0623301498
1000PhosphorylationEKVKDPKTAADVVSP
HCCCCCCCHHHHCCC
14.0628985074
1005PhosphorylationPKTAADVVSPGANSV
CCCHHHHCCCCCCCH
19.9121406692
1006PhosphorylationKTAADVVSPGANSVD
CCHHHHCCCCCCCHH
34.0119664994
1011PhosphorylationVVSPGANSVDSRVQR
HCCCCCCCHHHHCCC
8.5323927012
1014PhosphorylationPGANSVDSRVQRPKE
CCCCCHHHHCCCCCC
24.9123927012
1020AcetylationDSRVQRPKEESSEDE
HHHCCCCCCCCCCCH
66.837683203
1022PhosphorylationRVQRPKEESSEDENE
HCCCCCCCCCCCHHH
39.8721406692
1023PhosphorylationVQRPKEESSEDENEV
CCCCCCCCCCCHHHH
52.9619664994
1024PhosphorylationQRPKEESSEDENEVS
CCCCCCCCCCHHHHH
77.8419664994
1031PhosphorylationSEDENEVSNILRSGR
CCCHHHHHHHHHHCC
42.3522167270
1040MethylationILRSGRSKQFYNQTY
HHHHCCCHHHHHCCC
47.50-
1040UbiquitinationILRSGRSKQFYNQTY
HHHHCCCHHHHHCCC
47.5023000965
1046PhosphorylationSKQFYNQTYGSRKYK
CHHHHHCCCCCCCCC
11.8829978859
1046UbiquitinationSKQFYNQTYGSRKYK
CHHHHHCCCCCCCCC
11.8823000965
1047PhosphorylationKQFYNQTYGSRKYKS
HHHHHCCCCCCCCCC
25.1029978859
1047UbiquitinationKQFYNQTYGSRKYKS
HHHHHCCCCCCCCCC
25.1023000965
1049PhosphorylationFYNQTYGSRKYKSDW
HHHCCCCCCCCCCCC
41.7928348404
1050MethylationYNQTYGSRKYKSDWG
HHCCCCCCCCCCCCC
59.7480702183
1051MethylationNQTYGSRKYKSDWGY
HCCCCCCCCCCCCCC
18.02115974507
1053MethylationTYGSRKYKSDWGYSG
CCCCCCCCCCCCCCC
35.19115974515
1058PhosphorylationKYKSDWGYSGRGGYQ
CCCCCCCCCCCCCCC
20.34-
1059PhosphorylationYKSDWGYSGRGGYQH
CCCCCCCCCCCCCCC
24.62-
1061MethylationSDWGYSGRGGYQHVR
CCCCCCCCCCCCCCC
42.5630760013
1068MethylationRGGYQHVRSEESWKG
CCCCCCCCCCCCCCC
44.63115367967
1072PhosphorylationQHVRSEESWKGQPSR
CCCCCCCCCCCCCCC
16.4528857561
1080PhosphorylationWKGQPSRSRDEGYQY
CCCCCCCCHHHCCCC
44.9128348404
1085PhosphorylationSRSRDEGYQYHRNVR
CCCHHHCCCCCCCCC
38.11-
1087PhosphorylationSRDEGYQYHRNVRGR
CHHHCCCCCCCCCCC
10.1821552520
1089MethylationDEGYQYHRNVRGRPF
HHCCCCCCCCCCCCC
17.9681450765

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 OTUD4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
63Kubiquitylation

29395066
202SPhosphorylation

29395066
204SPhosphorylation

29395066

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 OTUD4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DSG1_HUMANDSG1physical
19615732
FLNC_HUMANFLNCphysical
19615732
GALK1_HUMANGALK1physical
19615732
AGAL_HUMANGLAphysical
19615732
DNJB1_HUMANDNAJB1physical
19615732
K2C8_HUMANKRT8physical
19615732
K1H1_HUMANKRT31physical
19615732
KT33B_HUMANKRT33Bphysical
19615732
KRT85_HUMANKRT85physical
19615732
MOG_HUMANMOGphysical
19615732
OAT_HUMANOATphysical
19615732
TBA1A_HUMANTUBA1Aphysical
19615732
KRT36_HUMANKRT36physical
19615732
FXR2_HUMANFXR2physical
19615732
PSA_HUMANNPEPPSphysical
19615732
BAG5_HUMANBAG5physical
19615732
GEPH_HUMANGPHNphysical
19615732
MYCBP_HUMANMYCBPphysical
19615732
NMD3_HUMANNMD3physical
19615732
PAR11_HUMANPARP11physical
19615732
RPTN_HUMANRPTNphysical
19615732
UBC_HUMANUBCphysical
23827681
ALKB3_HUMANALKBH3physical
25944111
UBC_HUMANUBCphysical
25944111
UBP7_HUMANUSP7physical
25944111
USP9X_HUMANUSP9Xphysical
25944111

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 OTUD4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-442; SER-556 AND SER-1005, AND MASSSPECTROMETRY.
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-442; SER-1005; SER-1022AND SER-1023, AND MASS SPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-442; SER-556 AND SER-1005, 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-442; SER-1005; SER-1022AND SER-1023, AND MASS SPECTROMETRY.
"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-940, 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-1022 AND SER-1023, ANDMASS SPECTROMETRY.
"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-438, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-438, AND MASSSPECTROMETRY.

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