RERE_HUMAN - dbPTM
RERE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RERE_HUMAN
UniProt AC Q9P2R6
Protein Name Arginine-glutamic acid dipeptide repeats protein
Gene Name RERE
Organism Homo sapiens (Human).
Sequence Length 1566
Subcellular Localization Nucleus . Localized in nuclear bodies of variables size. Colocalized with PML and BAX in nuclear PODs.
Protein Description Plays a role as a transcriptional repressor during development. May play a role in the control of cell survival. Overexpression of RERE recruits BAX to the nucleus particularly to POD and triggers caspase-3 activation, leading to cell death..
Protein Sequence MTADKDKDKDKEKDRDRDRDREREKRDKARESENSRPRRSCTLEGGAKNYAESDHSEDEDNDNNSATAEESTKKNKKKPPKKKSRYERTDTGEITSYITEDDVVYRPGDCVYIESRRPNTPYFICSIQDFKLVHNSQACCRSPTPALCDPPACSLPVASQPPQHLSEAGRGPVGSKRDHLLMNVKWYYRQSEVPDSVYQHLVQDRHNENDSGRELVITDPVIKNRELFISDYVDTYHAAALRGKCNISHFSDIFAAREFKARVDSFFYILGYNPETRRLNSTQGEIRVGPSHQAKLPDLQPFPSPDGDTVTQHEELVWMPGVNDCDLLMYLRAARSMAAFAGMCDGGSTEDGCVAASRDDTTLNALNTLHESGYDAGKALQRLVKKPVPKLIEKCWTEDEVKRFVKGLRQYGKNFFRIRKELLPNKETGELITFYYYWKKTPEAASSRAHRRHRRQAVFRRIKTRTASTPVNTPSRPPSSEFLDLSSASEDDFDSEDSEQELKGYACRHCFTTTSKDWHHGGRENILLCTDCRIHFKKYGELPPIEKPVDPPPFMFKPVKEEDDGLSGKHSMRTRRSRGSMSTLRSGRKKQPASPDGRTSPINEDIRSSGRNSPSAASTSSNDSKAETVKKSAKKVKEEASSPLKSNKRQREKVASDTEEADRTSSKKTKTQEISRPNSPSEGEGESSDSRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQMLQAQPPALQAPTGVTPAPSSAPPGTPQLPTPGPTPSATAVPPQGSPTASQAPNQPQAPTAPVPHTHIQQAPALHPQRPPSPHPPPHPSPHPPLQPLTGSAGQPSAPSHAQPPLHGQGPPGPHSLQAGPLLQHPGPPQPFGLPPQASQGQAPLGTSPAAAYPHTSLQLPASQSALQSQQPPREQPLPPAPLAMPHIKPPPTTPIPQLPAPQAHKHPPHLSGPSPFSMNANLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQPLPSSPAQPPGLTQSQNLPPPPASHPPTGLHQVAPQPPFAQHPFVPGGPPPITPPTCPSTSTPPAGPGTSAQPPCSGAAASGGSIAGGSSCPLPTVQIKEEALDDAEEPESPPPPPRSPSPEPTVVDTPSHASQSARFYKHLDRGYNSCARTDLYFMPLAGSKLAKKREEAIEKAKREAEQKAREEREREKEKEKEREREREREREAERAAKASSSAHEGRLSDPQLSGPGHMRPSFEPPPTTIAAVPPYIGPDTPALRTLSEYARPHVMSPTNRNHPFYMPLNPTDPLLAYHMPGLYNVDPTIRERELREREIREREIRERELRERMKPGFEVKPPELDPLHPAANPMEHFARHSALTIPPTAGPHPFASFHPGLNPLERERLALAGPQLRPEMSYPDRLAAERIHAERMASLTSDPLARLQMFNVTPHHHQHSHIHSHLHLHQQDPLHQGSAGPVHPLVDPLTAGPHLARFPYPPGTLPNPLLGQPPHEHEMLRHPVFGTPYPRDLPGAIPPPMSAAHQLQAMHAQSAELQRLAMEQQWLHGHPHMHGGHLPSQEDYYSRLKKEGDKQL
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
52-Hydroxyisobutyrylation---MTADKDKDKDKE
---CCCCCCCHHHHH
65.30-
35PhosphorylationKARESENSRPRRSCT
HHHHCHHCCCCCCEE
39.3429214152
36UbiquitinationARESENSRPRRSCTL
HHHCHHCCCCCCEEC
40.0833845483
40PhosphorylationENSRPRRSCTLEGGA
HHCCCCCCEECCCCH
16.8433259812
40 (in isoform 2)Phosphorylation-16.84-
42PhosphorylationSRPRRSCTLEGGAKN
CCCCCCEECCCCHHC
29.1429396449
45 (in isoform 2)Phosphorylation-44.46-
46 (in isoform 2)Phosphorylation-24.81-
50PhosphorylationLEGGAKNYAESDHSE
CCCCHHCCCCCCCCC
15.8423927012
53PhosphorylationGAKNYAESDHSEDED
CHHCCCCCCCCCCCC
32.2426503892
56PhosphorylationNYAESDHSEDEDNDN
CCCCCCCCCCCCCCC
52.3026503892
65PhosphorylationDEDNDNNSATAEEST
CCCCCCCCCCHHHHH
33.0023403867
67PhosphorylationDNDNNSATAEESTKK
CCCCCCCCHHHHHHH
34.1323403867
71PhosphorylationNSATAEESTKKNKKK
CCCCHHHHHHHCCCC
36.7123403867
72PhosphorylationSATAEESTKKNKKKP
CCCHHHHHHHCCCCC
49.6823403867
87 (in isoform 2)Phosphorylation-48.25-
88 (in isoform 2)Phosphorylation-29.03-
102PhosphorylationTSYITEDDVVYRPGD
EEEECCCCEEECCCC
26.0832645325
102 (in isoform 2)Phosphorylation-26.08-
110UbiquitinationVVYRPGDCVYIESRR
EEECCCCEEEEECCC
2.8721890473
110 (in isoform 2)Ubiquitination-2.8721890473
120PhosphorylationIESRRPNTPYFICSI
EECCCCCCCEEEEEE
23.2725159151
122PhosphorylationSRRPNTPYFICSIQD
CCCCCCCEEEEEECC
11.9728450419
125 (in isoform 2)Phosphorylation-1.78-
126PhosphorylationNTPYFICSIQDFKLV
CCCEEEEEECCEEEE
20.6123186163
136PhosphorylationDFKLVHNSQACCRSP
CEEEECCCCCCCCCC
12.3223401153
142PhosphorylationNSQACCRSPTPALCD
CCCCCCCCCCCCCCC
21.1523401153
144PhosphorylationQACCRSPTPALCDPP
CCCCCCCCCCCCCCC
23.5730266825
154PhosphorylationLCDPPACSLPVASQP
CCCCCCCCCCCCCCC
37.5023663014
159PhosphorylationACSLPVASQPPQHLS
CCCCCCCCCCCHHHH
43.3830266825
166PhosphorylationSQPPQHLSEAGRGPV
CCCCHHHHHCCCCCC
24.2320873877
191PhosphorylationVKWYYRQSEVPDSVY
EEEEECHHCCCHHHH
31.4027732954
196PhosphorylationRQSEVPDSVYQHLVQ
CHHCCCHHHHHHHHH
19.3627732954
198PhosphorylationSEVPDSVYQHLVQDR
HCCCHHHHHHHHHCC
8.3127732954
223UbiquitinationVITDPVIKNRELFIS
EEECCEECCCEEEHH
50.6229967540
265PhosphorylationEFKARVDSFFYILGY
HHHHHHHHEEHHHCC
17.8825278378
268PhosphorylationARVDSFFYILGYNPE
HHHHHEEHHHCCCHH
8.0125278378
272PhosphorylationSFFYILGYNPETRRL
HEEHHHCCCHHHCCC
24.8925278378
276PhosphorylationILGYNPETRRLNSTQ
HHCCCHHHCCCCCCC
23.5025278378
281PhosphorylationPETRRLNSTQGEIRV
HHHCCCCCCCCEEEE
27.05-
282PhosphorylationETRRLNSTQGEIRVG
HHCCCCCCCCEEEEC
39.25-
304PhosphorylationPDLQPFPSPDGDTVT
CCCCCCCCCCCCCCC
35.6826074081
309PhosphorylationFPSPDGDTVTQHEEL
CCCCCCCCCCCCCEE
30.8626074081
311PhosphorylationSPDGDTVTQHEELVW
CCCCCCCCCCCEEEE
26.7126074081
336PhosphorylationMYLRAARSMAAFAGM
HHHHHHHHHHHHHCC
14.19-
336UbiquitinationMYLRAARSMAAFAGM
HHHHHHHHHHHHHCC
14.1921890473
348PhosphorylationAGMCDGGSTEDGCVA
HCCCCCCCCCCCCEE
33.87-
349PhosphorylationGMCDGGSTEDGCVAA
CCCCCCCCCCCCEEE
41.17-
357PhosphorylationEDGCVAASRDDTTLN
CCCCEEECCCCCHHH
26.89-
378UbiquitinationESGYDAGKALQRLVK
HHCCCHHHHHHHHHH
47.8722817900
378 (in isoform 1)Ubiquitination-47.8721890473
394UbiquitinationPVPKLIEKCWTEDEV
CHHHHHHHHCCHHHH
28.2529967540
441PhosphorylationFYYYWKKTPEAASSR
EEEEHHHCHHHHHHH
23.7225072903
466PhosphorylationFRRIKTRTASTPVNT
HHHHHCCCCCCCCCC
30.1422817900
468PhosphorylationRIKTRTASTPVNTPS
HHHCCCCCCCCCCCC
32.4122817900
473PhosphorylationTASTPVNTPSRPPSS
CCCCCCCCCCCCCCH
23.9122817900
475PhosphorylationSTPVNTPSRPPSSEF
CCCCCCCCCCCCHHH
56.2117081983
479PhosphorylationNTPSRPPSSEFLDLS
CCCCCCCCHHHCCCC
45.22-
486PhosphorylationSSEFLDLSSASEDDF
CHHHCCCCCCCCCCC
24.4323909892
487PhosphorylationSEFLDLSSASEDDFD
HHHCCCCCCCCCCCC
43.0123909892
489PhosphorylationFLDLSSASEDDFDSE
HCCCCCCCCCCCCCC
43.4323909892
495PhosphorylationASEDDFDSEDSEQEL
CCCCCCCCCCHHHHH
43.2123909892
498PhosphorylationDDFDSEDSEQELKGY
CCCCCCCHHHHHHHE
36.8123909892
552 (in isoform 2)Phosphorylation-30.23-
559 (in isoform 2)Phosphorylation-14.54-
560SumoylationPFMFKPVKEEDDGLS
CCCCCCCCCCCCCCC
65.0128112733
561 (in isoform 2)Phosphorylation-67.88-
565 (in isoform 2)Phosphorylation-33.78-
577O-linked_GlycosylationHSMRTRRSRGSMSTL
CHHHCCCCCCCHHHH
37.3930379171
577PhosphorylationHSMRTRRSRGSMSTL
CHHHCCCCCCCHHHH
37.3920873877
578MethylationSMRTRRSRGSMSTLR
HHHCCCCCCCHHHHH
39.12115491123
580PhosphorylationRTRRSRGSMSTLRSG
HCCCCCCCHHHHHCC
14.4023401153
581UbiquitinationTRRSRGSMSTLRSGR
CCCCCCCHHHHHCCC
3.8521890473
582PhosphorylationRRSRGSMSTLRSGRK
CCCCCCHHHHHCCCC
26.4520873877
583PhosphorylationRSRGSMSTLRSGRKK
CCCCCHHHHHCCCCC
19.9726434776
590UbiquitinationTLRSGRKKQPASPDG
HHHCCCCCCCCCCCC
61.2233845483
594PhosphorylationGRKKQPASPDGRTSP
CCCCCCCCCCCCCCC
30.1520201521
599PhosphorylationPASPDGRTSPINEDI
CCCCCCCCCCCCHHH
44.3729255136
600PhosphorylationASPDGRTSPINEDIR
CCCCCCCCCCCHHHH
23.5629255136
608PhosphorylationPINEDIRSSGRNSPS
CCCHHHHHCCCCCCC
37.1623401153
609PhosphorylationINEDIRSSGRNSPSA
CCHHHHHCCCCCCCC
31.7423927012
613PhosphorylationIRSSGRNSPSAASTS
HHHCCCCCCCCCCCC
20.9029255136
615PhosphorylationSSGRNSPSAASTSSN
HCCCCCCCCCCCCCC
35.9725159151
618PhosphorylationRNSPSAASTSSNDSK
CCCCCCCCCCCCHHH
28.6523927012
619PhosphorylationNSPSAASTSSNDSKA
CCCCCCCCCCCHHHH
31.2923927012
620PhosphorylationSPSAASTSSNDSKAE
CCCCCCCCCCHHHHH
25.3423927012
621PhosphorylationPSAASTSSNDSKAET
CCCCCCCCCHHHHHH
44.7523927012
624PhosphorylationASTSSNDSKAETVKK
CCCCCCHHHHHHHHH
37.7123927012
635AcetylationTVKKSAKKVKEEASS
HHHHHHHHHHHHHCC
59.257707267
637SumoylationKKSAKKVKEEASSPL
HHHHHHHHHHHCCCC
59.73-
637SumoylationKKSAKKVKEEASSPL
HHHHHHHHHHHCCCC
59.7328112733
641PhosphorylationKKVKEEASSPLKSNK
HHHHHHHCCCCCCCH
35.4530266825
642PhosphorylationKVKEEASSPLKSNKR
HHHHHHCCCCCCCHH
41.1029255136
645AcetylationEEASSPLKSNKRQRE
HHHCCCCCCCHHHHH
56.207707279
646PhosphorylationEASSPLKSNKRQREK
HHCCCCCCCHHHHHH
56.0923312004
656PhosphorylationRQREKVASDTEEADR
HHHHHHCCCCHHHHH
48.3129255136
658PhosphorylationREKVASDTEEADRTS
HHHHCCCCHHHHHHC
32.9830278072
664PhosphorylationDTEEADRTSSKKTKT
CCHHHHHHCCCCCCC
37.5923403867
665PhosphorylationTEEADRTSSKKTKTQ
CHHHHHHCCCCCCCE
40.8423403867
666PhosphorylationEEADRTSSKKTKTQE
HHHHHHCCCCCCCEE
37.2423403867
671PhosphorylationTSSKKTKTQEISRPN
HCCCCCCCEECCCCC
36.3429255136
675PhosphorylationKTKTQEISRPNSPSE
CCCCEECCCCCCCCC
40.7229255136
679PhosphorylationQEISRPNSPSEGEGE
EECCCCCCCCCCCCC
32.2729255136
681PhosphorylationISRPNSPSEGEGESS
CCCCCCCCCCCCCCC
59.0430266825
687PhosphorylationPSEGEGESSDSRSVN
CCCCCCCCCCCCCCC
50.7530266825
688PhosphorylationSEGEGESSDSRSVND
CCCCCCCCCCCCCCC
34.9930266825
690PhosphorylationGEGESSDSRSVNDEG
CCCCCCCCCCCCCCC
28.5330266825
692PhosphorylationGESSDSRSVNDEGSS
CCCCCCCCCCCCCCC
29.2625849741
698PhosphorylationRSVNDEGSSDPKDID
CCCCCCCCCCHHHCC
29.5328348404
699PhosphorylationSVNDEGSSDPKDIDQ
CCCCCCCCCHHHCCC
69.6423532336
770UbiquitinationTPGPTPSATAVPPQG
CCCCCCCCCCCCCCC
10.7723000965
776UbiquitinationSATAVPPQGSPTASQ
CCCCCCCCCCCCHHH
59.9523000965
867UbiquitinationGPLLQHPGPPQPFGL
CCCCCCCCCCCCCCC
44.3821890473
867 (in isoform 2)Ubiquitination-44.3821890473
933PhosphorylationPHIKPPPTTPIPQLP
CCCCCCCCCCCCCCC
51.4827251275
934PhosphorylationHIKPPPTTPIPQLPA
CCCCCCCCCCCCCCC
25.6227251275
955PhosphorylationPPHLSGPSPFSMNAN
CCCCCCCCCCCCCCC
41.9425159151
1056UbiquitinationPPTCPSTSTPPAGPG
CCCCCCCCCCCCCCC
43.1621890473
1056 (in isoform 2)Ubiquitination-43.1621890473
1062UbiquitinationTSTPPAGPGTSAQPP
CCCCCCCCCCCCCCC
45.0223000965
1093UbiquitinationCPLPTVQIKEEALDD
CCCCCEEEEHHHHCC
5.4321890473
1106PhosphorylationDDAEEPESPPPPPRS
CCCCCCCCCCCCCCC
54.1230266825
1113PhosphorylationSPPPPPRSPSPEPTV
CCCCCCCCCCCCCEE
35.1930266825
1115PhosphorylationPPPPRSPSPEPTVVD
CCCCCCCCCCCEEEC
43.0430266825
1119PhosphorylationRSPSPEPTVVDTPSH
CCCCCCCEEECCCCC
31.3430266825
1123PhosphorylationPEPTVVDTPSHASQS
CCCEEECCCCCHHHH
18.3230266825
1125PhosphorylationPTVVDTPSHASQSAR
CEEECCCCCHHHHHH
33.5023663014
1128PhosphorylationVDTPSHASQSARFYK
ECCCCCHHHHHHHHH
21.1723663014
1130PhosphorylationTPSHASQSARFYKHL
CCCCHHHHHHHHHHH
20.9323663014
1134PhosphorylationASQSARFYKHLDRGY
HHHHHHHHHHHHCCC
7.6122468782
1135UbiquitinationSQSARFYKHLDRGYN
HHHHHHHHHHHCCCC
34.6721890473
1135 (in isoform 1)Ubiquitination-34.6721890473
1150PhosphorylationSCARTDLYFMPLAGS
CCCCCCEEECCCCCH
10.7117360941
1157PhosphorylationYFMPLAGSKLAKKRE
EECCCCCHHHHHHHH
20.91-
1158AcetylationFMPLAGSKLAKKREE
ECCCCCHHHHHHHHH
52.0925953088
1231O-linked_GlycosylationGPGHMRPSFEPPPTT
CCCCCCCCCCCCCCE
31.7030379171
1237O-linked_GlycosylationPSFEPPPTTIAAVPP
CCCCCCCCEEECCCC
36.2930379171
1238O-linked_GlycosylationSFEPPPTTIAAVPPY
CCCCCCCEEECCCCC
17.8830379171
1238PhosphorylationSFEPPPTTIAAVPPY
CCCCCCCEEECCCCC
17.8824719451
1250PhosphorylationPPYIGPDTPALRTLS
CCCCCCCCHHHHHHH
17.3724719451
1255PhosphorylationPDTPALRTLSEYARP
CCCHHHHHHHHHCCC
35.1723403867
1257PhosphorylationTPALRTLSEYARPHV
CHHHHHHHHHCCCCC
28.1323403867
1259PhosphorylationALRTLSEYARPHVMS
HHHHHHHHCCCCCCC
12.4423403867
1266PhosphorylationYARPHVMSPTNRNHP
HCCCCCCCCCCCCCC
27.7323401153
1268PhosphorylationRPHVMSPTNRNHPFY
CCCCCCCCCCCCCCC
39.2323927012
1282UbiquitinationYMPLNPTDPLLAYHM
CCCCCCCCCHHHHCC
32.8621890473
1287PhosphorylationPTDPLLAYHMPGLYN
CCCCHHHHCCCCCCC
9.91-
1288UbiquitinationTDPLLAYHMPGLYNV
CCCHHHHCCCCCCCC
15.4523000965
1324UbiquitinationRELRERMKPGFEVKP
HHHHHHCCCCCCCCC
48.4823000965
1324 (in isoform 1)Ubiquitination-48.4821890473
1330UbiquitinationMKPGFEVKPPELDPL
CCCCCCCCCCCCCCC
47.8923000965
1387MethylationALAGPQLRPEMSYPD
HHCCCCCCCCCCCCH
21.64115491099
1395MethylationPEMSYPDRLAAERIH
CCCCCCHHHHHHHHH
23.01115491107
1400MethylationPDRLAAERIHAERMA
CHHHHHHHHHHHHHH
22.67115491115
1405MethylationAERIHAERMASLTSD
HHHHHHHHHHHCCCC
27.10115491083
1408PhosphorylationIHAERMASLTSDPLA
HHHHHHHHCCCCHHH
23.8828555341
1416MethylationLTSDPLARLQMFNVT
CCCCHHHHHHHCCCC
32.89115491091

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 RERE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RERE_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 RERE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATN1_HUMANATN1physical
10814707
LZTR1_HUMANLZTR1physical
20211142
ACT1_DROMEAct5Cphysical
16481466
7UP1_DROMEsvpphysical
16481466
7UP2_DROMEsvpphysical
16481466
NR2E1_HUMANNR2E1physical
16481466
HDAC1_HUMANHDAC1physical
16481466
HDAC2_HUMANHDAC2physical
16481466
EHMT2_HUMANEHMT2physical
18451879
H32_HUMANHIST2H3Cphysical
18451879
KR412_HUMANKRTAP4-12physical
16713569
PLS1_HUMANPLSCR1physical
16713569
TRI22_HUMANTRIM22physical
16713569
ATN1_HUMANATN1physical
16713569
MTG8R_HUMANCBFA2T2physical
16713569
FBLN4_HUMANEFEMP2physical
16713569
PKCB1_HUMANZMYND8physical
16713569
PSA3_HUMANPSMA3physical
16713569
PRC2A_HUMANPRRC2Aphysical
16713569
ALG13_HUMANALG13physical
16713569
ECM1_HUMANECM1physical
16713569
FBLN3_HUMANEFEMP1physical
16713569
PRC2B_HUMANPRRC2Bphysical
16713569
KAT6A_HUMANKAT6Aphysical
16713569
RFOX2_HUMANRBFOX2physical
16713569
HDAC1_HUMANHDAC1physical
17150957
EP300_HUMANEP300physical
17150957

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 RERE_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-53; SER-56; SER-675 ANDSER-679, 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-53; SER-56 AND SER-642,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-1106; SER-1113AND SER-1115, 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-594 AND THR-599, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND SER-656, ANDMASS SPECTROMETRY.

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