PHC3_HUMAN - dbPTM
PHC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHC3_HUMAN
UniProt AC Q8NDX5
Protein Name Polyhomeotic-like protein 3
Gene Name PHC3
Organism Homo sapiens (Human).
Sequence Length 983
Subcellular Localization Nucleus .
Protein Description Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility..
Protein Sequence MDTEPNPGTSSVSTTTSSTTTTTITTSSSRMQQPQISVYSGSDRHAVQVIQQALHRPPSSAAQYLQQMYAAQQQHLMLHTAALQQQHLSSSQLQSLAAVQASLSSGRPSTSPTGSVTQQSSMSQTSINLSTSPTPAQLISRSQASSSTSGSITQQTMLLGSTSPTLTASQAQMYLRAQMLIFTPATTVAAVQSDIPVVSSSSSSSCQSAATQVQNLTLRSQKLGVLSSSQNGPPKSTSQTQSLTICHNKTTVTSSKISQRDPSPESNKKGESPSLESRSTAVTRTSSIHQLIAPASYSPIQPHSLIKHQQIPLHSPPSKVSHHQLILQQQQQQIQPITLQNSTQDPPPSQHCIPLQNHGLPPAPSNAQSQHCSPIQSHPSPLTVSPNQSQSAQQSVVVSPPPPHSPSQSPTIIIHPQALIQPHPLVSSALQPGPNLQQSTANQVQATAQLNLPSHLPLPASPVVHIGPVQQSALVSPGQQIVSPSHQQYSSLQSSPIPIASPPQMSTSPPAQIPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPVVYQVEDVCEEEMPEESDECVRMDRTPPPPTLSPAAITVGRGEDLTSEHPLLEQVELPAVASVSASVIKSPSDPSHVSVPPPPLLLPAATTRSNSTSMHSSIPSIENKPPQAIVKPQILTHVIEGFVIQEGLEPFPVSRSSLLIEQPVKKRPLLDNQVINSVCVQPELQNNTKHADNSSDTEMEDMIAEETLEEMDSELLKCEFCGKMGYANEFLRSKRFCTMSCAKRYNVSCSKKFALSRWNRKPDNQSLGHRGRRPSGPDGAAREHILRQLPITYPSAEEDLASHEDSVPSAMTTRLRRQSERERERELRDVRIRKMPENSDLLPVAQTEPSIWTVDDVWAFIHSLPGCQDIADEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICARINSLKES
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
37O-linked_GlycosylationRMQQPQISVYSGSDR
CCCCCEEEEECCCCH
15.1220068230
37PhosphorylationRMQQPQISVYSGSDR
CCCCCEEEEECCCCH
15.1220068231
39PhosphorylationQQPQISVYSGSDRHA
CCCEEEEECCCCHHH
10.6720068231
40PhosphorylationQPQISVYSGSDRHAV
CCEEEEECCCCHHHH
29.6620068231
42PhosphorylationQISVYSGSDRHAVQV
EEEEECCCCHHHHHH
26.0720068231
59O-linked_GlycosylationQALHRPPSSAAQYLQ
HHHCCCCCHHHHHHH
34.9820068230
60O-linked_GlycosylationALHRPPSSAAQYLQQ
HHCCCCCHHHHHHHH
33.1420068230
113PhosphorylationGRPSTSPTGSVTQQS
CCCCCCCCCCCCCCC
41.6830576142
113 (in isoform 2)Phosphorylation-41.6822210691
117PhosphorylationTSPTGSVTQQSSMSQ
CCCCCCCCCCCCCCC
23.6930576142
120PhosphorylationTGSVTQQSSMSQTSI
CCCCCCCCCCCCEEE
20.4230576142
125PhosphorylationQQSSMSQTSINLSTS
CCCCCCCEEEECCCC
25.0330576142
131PhosphorylationQTSINLSTSPTPAQL
CEEEECCCCCCHHHH
41.7230576142
146 (in isoform 2)Phosphorylation-40.4222210691
147PhosphorylationSRSQASSSTSGSITQ
HHHHCCCCCCCCEEH
24.8922210691
155 (in isoform 2)Phosphorylation-21.8922210691
161PhosphorylationQQTMLLGSTSPTLTA
HHEEECCCCCCCCCH
26.1926074081
162PhosphorylationQTMLLGSTSPTLTAS
HEEECCCCCCCCCHH
36.6126074081
163PhosphorylationTMLLGSTSPTLTASQ
EEECCCCCCCCCHHH
19.9926074081
165PhosphorylationLLGSTSPTLTASQAQ
ECCCCCCCCCHHHHH
36.1926074081
167PhosphorylationGSTSPTLTASQAQMY
CCCCCCCCHHHHHHH
27.0926074081
169PhosphorylationTSPTLTASQAQMYLR
CCCCCCHHHHHHHHH
22.3322210691
175PhosphorylationASQAQMYLRAQMLIF
HHHHHHHHHHCEECC
2.8427251275
217PhosphorylationATQVQNLTLRSQKLG
HHHHHHHHHHHHHHC
27.8924719451
222SumoylationNLTLRSQKLGVLSSS
HHHHHHHHHCCCCCC
48.75-
222AcetylationNLTLRSQKLGVLSSS
HHHHHHHHHCCCCCC
48.7525953088
222SumoylationNLTLRSQKLGVLSSS
HHHHHHHHHCCCCCC
48.75-
222UbiquitinationNLTLRSQKLGVLSSS
HHHHHHHHHCCCCCC
48.75-
227PhosphorylationSQKLGVLSSSQNGPP
HHHHCCCCCCCCCCC
26.0723186163
228PhosphorylationQKLGVLSSSQNGPPK
HHHCCCCCCCCCCCC
31.6125159151
229PhosphorylationKLGVLSSSQNGPPKS
HHCCCCCCCCCCCCC
25.0417525332
234 (in isoform 7)Ubiquitination-44.63-
235UbiquitinationSSQNGPPKSTSQTQS
CCCCCCCCCCCCCEE
70.29-
236O-linked_GlycosylationSQNGPPKSTSQTQSL
CCCCCCCCCCCCEEE
38.7820068230
236PhosphorylationSQNGPPKSTSQTQSL
CCCCCCCCCCCCEEE
38.7829083192
237O-linked_GlycosylationQNGPPKSTSQTQSLT
CCCCCCCCCCCEEEE
30.8620068230
237PhosphorylationQNGPPKSTSQTQSLT
CCCCCCCCCCCEEEE
30.8629083192
238O-linked_GlycosylationNGPPKSTSQTQSLTI
CCCCCCCCCCEEEEE
38.0220068230
238PhosphorylationNGPPKSTSQTQSLTI
CCCCCCCCCCEEEEE
38.0229083192
240O-linked_GlycosylationPPKSTSQTQSLTICH
CCCCCCCCEEEEEEE
21.6420068230
240PhosphorylationPPKSTSQTQSLTICH
CCCCCCCCEEEEEEE
21.6429083192
242O-linked_GlycosylationKSTSQTQSLTICHNK
CCCCCCEEEEEEECC
30.7620068230
242PhosphorylationKSTSQTQSLTICHNK
CCCCCCEEEEEEECC
30.7629083192
244O-linked_GlycosylationTSQTQSLTICHNKTT
CCCCEEEEEEECCCE
27.1420068230
244PhosphorylationTSQTQSLTICHNKTT
CCCCEEEEEEECCCE
27.1429083192
250O-linked_GlycosylationLTICHNKTTVTSSKI
EEEEECCCEECCCCC
31.6420068230
250PhosphorylationLTICHNKTTVTSSKI
EEEEECCCEECCCCC
31.6428060719
251PhosphorylationTICHNKTTVTSSKIS
EEEECCCEECCCCCC
24.3228060719
253O-linked_GlycosylationCHNKTTVTSSKISQR
EECCCEECCCCCCCC
25.7820068230
253PhosphorylationCHNKTTVTSSKISQR
EECCCEECCCCCCCC
25.7828060719
254O-linked_GlycosylationHNKTTVTSSKISQRD
ECCCEECCCCCCCCC
25.8720068230
254PhosphorylationHNKTTVTSSKISQRD
ECCCEECCCCCCCCC
25.8728060719
255PhosphorylationNKTTVTSSKISQRDP
CCCEECCCCCCCCCC
25.3328060719
256AcetylationKTTVTSSKISQRDPS
CCEECCCCCCCCCCC
46.2525953088
256UbiquitinationKTTVTSSKISQRDPS
CCEECCCCCCCCCCC
46.25-
258PhosphorylationTVTSSKISQRDPSPE
EECCCCCCCCCCCCC
23.9328176443
263PhosphorylationKISQRDPSPESNKKG
CCCCCCCCCCCCCCC
45.6625159151
266PhosphorylationQRDPSPESNKKGESP
CCCCCCCCCCCCCCC
58.2828176443
269UbiquitinationPSPESNKKGESPSLE
CCCCCCCCCCCCCHH
72.64-
272PhosphorylationESNKKGESPSLESRS
CCCCCCCCCCHHHHC
28.5823401153
274PhosphorylationNKKGESPSLESRSTA
CCCCCCCCHHHHCCC
54.7930108239
275PhosphorylationKKGESPSLESRSTAV
CCCCCCCHHHHCCCC
8.6524719451
277PhosphorylationGESPSLESRSTAVTR
CCCCCHHHHCCCCCC
36.5024702127
279O-linked_GlycosylationSPSLESRSTAVTRTS
CCCHHHHCCCCCCCC
29.9620068230
281 (in isoform 7)Ubiquitination-11.26-
283O-linked_GlycosylationESRSTAVTRTSSIHQ
HHHCCCCCCCCCCHH
26.2620068230
283O-linked_GlycosylationESRSTAVTRTSSIHQ
HHHCCCCCCCCCCHH
26.2620068230
284PhosphorylationSRSTAVTRTSSIHQL
HHCCCCCCCCCCHHH
26.4724719451
285PhosphorylationRSTAVTRTSSIHQLI
HCCCCCCCCCCHHHH
19.9125159151
286PhosphorylationSTAVTRTSSIHQLIA
CCCCCCCCCCHHHHC
24.8125159151
287PhosphorylationTAVTRTSSIHQLIAP
CCCCCCCCCHHHHCC
24.3925159151
296PhosphorylationHQLIAPASYSPIQPH
HHHHCCCCCCCCCCC
25.6925159151
297PhosphorylationQLIAPASYSPIQPHS
HHHCCCCCCCCCCCC
22.1424732914
298PhosphorylationLIAPASYSPIQPHSL
HHCCCCCCCCCCCCC
17.0325159151
299PhosphorylationIAPASYSPIQPHSLI
HCCCCCCCCCCCCCC
22.4727251275
304PhosphorylationYSPIQPHSLIKHQQI
CCCCCCCCCCCCCCC
38.1724732914
308PhosphorylationQPHSLIKHQQIPLHS
CCCCCCCCCCCCCCC
20.1324719451
310PhosphorylationHSLIKHQQIPLHSPP
CCCCCCCCCCCCCCC
38.7027251275
315PhosphorylationHQQIPLHSPPSKVSH
CCCCCCCCCCCCCCH
46.3025159151
318PhosphorylationIPLHSPPSKVSHHQL
CCCCCCCCCCCHHHH
49.4230266825
327PhosphorylationVSHHQLILQQQQQQI
CCHHHHHHHHHHHHC
5.2424719451
383PhosphorylationQSHPSPLTVSPNQSQ
CCCCCCCCCCCCCCC
23.4826074081
385PhosphorylationHPSPLTVSPNQSQSA
CCCCCCCCCCCCCCC
16.9426074081
389PhosphorylationLTVSPNQSQSAQQSV
CCCCCCCCCCCCCCE
32.5126074081
391PhosphorylationVSPNQSQSAQQSVVV
CCCCCCCCCCCCEEE
33.0426074081
395PhosphorylationQSQSAQQSVVVSPPP
CCCCCCCCEEECCCC
12.5626074081
399PhosphorylationAQQSVVVSPPPPHSP
CCCCEEECCCCCCCC
21.7826074081
405PhosphorylationVSPPPPHSPSQSPTI
ECCCCCCCCCCCCEE
31.8326074081
407PhosphorylationPPPPHSPSQSPTIII
CCCCCCCCCCCEEEE
46.4326074081
409PhosphorylationPPHSPSQSPTIIIHP
CCCCCCCCCEEEECC
28.4826074081
411PhosphorylationHSPSQSPTIIIHPQA
CCCCCCCEEEECCCC
30.0126074081
609PhosphorylationECVRMDRTPPPPTLS
CCCCCCCCCCCCCCC
35.5622322096
614PhosphorylationDRTPPPPTLSPAAIT
CCCCCCCCCCCCEEE
45.7122322096
616PhosphorylationTPPPPTLSPAAITVG
CCCCCCCCCCEEEEC
18.2522322096
621PhosphorylationTLSPAAITVGRGEDL
CCCCCEEEECCCCCC
16.5130266825
626PhosphorylationAITVGRGEDLTSEHP
EEEECCCCCCCCCCC
48.7824719451
628PhosphorylationTVGRGEDLTSEHPLL
EECCCCCCCCCCCCH
5.0327251275
629PhosphorylationVGRGEDLTSEHPLLE
ECCCCCCCCCCCCHH
44.3726074081
630PhosphorylationGRGEDLTSEHPLLEQ
CCCCCCCCCCCCHHC
41.0026074081
645PhosphorylationVELPAVASVSASVIK
CCCCCEEEEEEECCC
15.2520068231
647PhosphorylationLPAVASVSASVIKSP
CCCEEEEEEECCCCC
16.6020068231
649PhosphorylationAVASVSASVIKSPSD
CEEEEEEECCCCCCC
19.5020068231
653PhosphorylationVSASVIKSPSDPSHV
EEEECCCCCCCCCCC
20.6425159151
655PhosphorylationASVIKSPSDPSHVSV
EECCCCCCCCCCCCC
70.0625159151
658PhosphorylationIKSPSDPSHVSVPPP
CCCCCCCCCCCCCCC
41.3225159151
661PhosphorylationPSDPSHVSVPPPPLL
CCCCCCCCCCCCCCC
24.3925159151
665PhosphorylationSHVSVPPPPLLLPAA
CCCCCCCCCCCCCCC
26.5427251275
673O-linked_GlycosylationPLLLPAATTRSNSTS
CCCCCCCCCCCCCCC
25.5020068230
674O-linked_GlycosylationLLLPAATTRSNSTSM
CCCCCCCCCCCCCCC
27.6320068230
676PhosphorylationLPAATTRSNSTSMHS
CCCCCCCCCCCCCCC
32.8023090842
678PhosphorylationAATTRSNSTSMHSSI
CCCCCCCCCCCCCCC
24.0925849741
679PhosphorylationATTRSNSTSMHSSIP
CCCCCCCCCCCCCCC
34.0323090842
680PhosphorylationTTRSNSTSMHSSIPS
CCCCCCCCCCCCCCC
17.8323090842
683PhosphorylationSNSTSMHSSIPSIEN
CCCCCCCCCCCCCCC
22.7123090842
684PhosphorylationNSTSMHSSIPSIENK
CCCCCCCCCCCCCCC
24.6823090842
687PhosphorylationSMHSSIPSIENKPPQ
CCCCCCCCCCCCCCC
40.6423090842
691PhosphorylationSIPSIENKPPQAIVK
CCCCCCCCCCCCCCC
45.3327251275
691SumoylationSIPSIENKPPQAIVK
CCCCCCCCCCCCCCC
45.3328112733
721O-linked_GlycosylationGLEPFPVSRSSLLIE
CCCCCCCCHHHEEEE
27.0420068230
723PhosphorylationEPFPVSRSSLLIEQP
CCCCCCHHHEEEECC
20.1719691289
724PhosphorylationPFPVSRSSLLIEQPV
CCCCCHHHEEEECCC
26.5325159151
732AcetylationLLIEQPVKKRPLLDN
EEEECCCCCCCCCCC
50.1525953088
732SumoylationLLIEQPVKKRPLLDN
EEEECCCCCCCCCCC
50.1528112733
732UbiquitinationLLIEQPVKKRPLLDN
EEEECCCCCCCCCCC
50.15-
733UbiquitinationLIEQPVKKRPLLDNQ
EEECCCCCCCCCCCH
60.53-
736PhosphorylationQPVKKRPLLDNQVIN
CCCCCCCCCCCHHEE
12.4627251275
744O-linked_GlycosylationLDNQVINSVCVQPEL
CCCHHEEEEECCHHH
13.0320068230
761PhosphorylationNTKHADNSSDTEMED
CCCCCCCCCCHHHHH
30.0930278072
762PhosphorylationTKHADNSSDTEMEDM
CCCCCCCCCHHHHHH
55.6030278072
764PhosphorylationHADNSSDTEMEDMIA
CCCCCCCHHHHHHHH
38.9030278072
773PhosphorylationMEDMIAEETLEEMDS
HHHHHHHHHHHHHCH
50.0727251275
774PhosphorylationEDMIAEETLEEMDSE
HHHHHHHHHHHHCHH
30.8623403867
776PhosphorylationMIAEETLEEMDSELL
HHHHHHHHHHCHHHH
59.7127251275
780PhosphorylationETLEEMDSELLKCEF
HHHHHHCHHHHHCCC
28.9123403867
807PhosphorylationSKRFCTMSCAKRYNV
CCCCCCHHHHHHHCC
7.8625627689
810SumoylationFCTMSCAKRYNVSCS
CCCHHHHHHHCCCCC
60.7928112733
815PhosphorylationCAKRYNVSCSKKFAL
HHHHHCCCCCCCCHH
14.72-
817PhosphorylationKRYNVSCSKKFALSR
HHHCCCCCCCCHHHH
31.23-
828AcetylationALSRWNRKPDNQSLG
HHHHCCCCCCCCCCC
54.21155409
837MethylationDNQSLGHRGRRPSGP
CCCCCCCCCCCCCCC
38.2226493849
839MethylationQSLGHRGRRPSGPDG
CCCCCCCCCCCCCCH
47.49115487371
842PhosphorylationGHRGRRPSGPDGAAR
CCCCCCCCCCCHHHH
62.2327273156
854PhosphorylationAAREHILRQLPITYP
HHHHHHHHHCCCCCC
35.0724719451
859PhosphorylationILRQLPITYPSAEED
HHHHCCCCCCCHHHH
27.6928450419
860PhosphorylationLRQLPITYPSAEEDL
HHHCCCCCCCHHHHH
8.9126074081
862PhosphorylationQLPITYPSAEEDLAS
HCCCCCCCHHHHHHC
37.5928450419
869PhosphorylationSAEEDLASHEDSVPS
CHHHHHHCCCCCCCH
34.4128450419
873PhosphorylationDLASHEDSVPSAMTT
HHHCCCCCCCHHHHH
32.7026074081
874PhosphorylationLASHEDSVPSAMTTR
HHCCCCCCCHHHHHH
7.2124719451
876PhosphorylationSHEDSVPSAMTTRLR
CCCCCCCHHHHHHHH
28.6326074081
879PhosphorylationDSVPSAMTTRLRRQS
CCCCHHHHHHHHHHH
14.4226074081
880PhosphorylationSVPSAMTTRLRRQSE
CCCHHHHHHHHHHHH
18.0226074081
881PhosphorylationVPSAMTTRLRRQSER
CCHHHHHHHHHHHHH
19.6127251275
886PhosphorylationTTRLRRQSERERERE
HHHHHHHHHHHHHHH
36.49-
906PhosphorylationIRKMPENSDLLPVAQ
HHCCCCCCCCCCCCC
28.1528787133
914PhosphorylationDLLPVAQTEPSIWTV
CCCCCCCCCCCCEEH
39.8828787133
917PhosphorylationPVAQTEPSIWTVDDV
CCCCCCCCCEEHHHH
25.2428787133
920PhosphorylationQTEPSIWTVDDVWAF
CCCCCCEEHHHHHHH
16.6428787133
966SumoylationLMSAMNIKLGPALKI
HHHHHCCCHHHHHHH
42.24-
966SumoylationLMSAMNIKLGPALKI
HHHHHCCCHHHHHHH
42.24-
979PhosphorylationKICARINSLKES---
HHHHHHHHHCCC---
38.1524719451
983PhosphorylationRINSLKES-------
HHHHHCCC-------
0.0027251275
991Phosphorylation---------------
---------------
24719451

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 PHC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHC3_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 PHC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RING2_HUMANRNF2physical
22325352
PCGF2_HUMANPCGF2physical
22325352
BMI1_HUMANBMI1physical
22325352
RING1_HUMANRING1physical
22325352
PHC1_HUMANPHC1physical
22325352
PHC2_HUMANPHC2physical
22325352
CBX2_HUMANCBX2physical
22325352
CBX4_HUMANCBX4physical
22325352
CBX6_HUMANCBX6physical
22325352
CBX8_HUMANCBX8physical
22325352
SCMH1_HUMANSCMH1physical
22325352
SCML1_HUMANSCML1physical
22325352

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 PHC3_HUMAN

loading...

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 THR-609; SER-616 ANDSER-762, 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-315; THR-609; SER-616;SER-761 AND SER-762, 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 THR-609; THR-614 ANDSER-616, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-274, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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-263; THR-609 ANDSER-616, AND MASS 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-263; THR-609 ANDSER-616, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609, AND MASSSPECTROMETRY.

TOP