NU133_HUMAN - dbPTM
NU133_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NU133_HUMAN
UniProt AC Q8WUM0
Protein Name Nuclear pore complex protein Nup133
Gene Name NUP133
Organism Homo sapiens (Human).
Sequence Length 1156
Subcellular Localization Nucleus, nuclear pore complex . Chromosome, centromere, kinetochore . Located on both the cytoplasmic and nuclear sides of the nuclear pore (PubMed:11564755). During mitosis, localizes to the kinetochores (PubMed:11564755).
Protein Description Involved in poly(A)+ RNA transport..
Protein Sequence MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYDVKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSYSSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKIHQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENITDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSEDLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVSILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRAVTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLLCEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIEWAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNIVTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTDNQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI
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-------MFPAAPSP
-------CCCCCCCC
40.3922223895
7Phosphorylation-MFPAAPSPRTPGTG
-CCCCCCCCCCCCCC
23.4523401153
9MethylationFPAAPSPRTPGTGSR
CCCCCCCCCCCCCCC
58.87115387851
10PhosphorylationPAAPSPRTPGTGSRR
CCCCCCCCCCCCCCC
29.4725159151
13PhosphorylationPSPRTPGTGSRRGPL
CCCCCCCCCCCCCCC
32.9425159151
15PhosphorylationPRTPGTGSRRGPLAG
CCCCCCCCCCCCCCC
20.7422115753
17MethylationTPGTGSRRGPLAGLG
CCCCCCCCCCCCCCC
53.4224129315
27PhosphorylationLAGLGPGSTPRTASR
CCCCCCCCCCCCCCC
38.0722167270
28PhosphorylationAGLGPGSTPRTASRK
CCCCCCCCCCCCCCC
23.7822167270
30MethylationLGPGSTPRTASRKGL
CCCCCCCCCCCCCCC
42.91-
31PhosphorylationGPGSTPRTASRKGLP
CCCCCCCCCCCCCCC
30.1325159151
33PhosphorylationGSTPRTASRKGLPLG
CCCCCCCCCCCCCCC
33.6321712546
35AcetylationTPRTASRKGLPLGSA
CCCCCCCCCCCCCCC
63.4026051181
35UbiquitinationTPRTASRKGLPLGSA
CCCCCCCCCCCCCCC
63.4023000965
41PhosphorylationRKGLPLGSAVSSPVL
CCCCCCCCCCCCCEE
32.9330266825
44PhosphorylationLPLGSAVSSPVLFSP
CCCCCCCCCCEEECC
28.7429255136
45PhosphorylationPLGSAVSSPVLFSPV
CCCCCCCCCEEECCC
16.6629255136
50PhosphorylationVSSPVLFSPVGRRSS
CCCCEEECCCCCCCC
17.9529255136
56PhosphorylationFSPVGRRSSLSSRGT
ECCCCCCCCCCCCCC
33.9826055452
57PhosphorylationSPVGRRSSLSSRGTP
CCCCCCCCCCCCCCC
30.3823401153
59PhosphorylationVGRRSSLSSRGTPTR
CCCCCCCCCCCCCCC
21.6722115753
60PhosphorylationGRRSSLSSRGTPTRM
CCCCCCCCCCCCCCC
39.7723401153
61MethylationRRSSLSSRGTPTRMF
CCCCCCCCCCCCCCC
50.0254557731
63PhosphorylationSSLSSRGTPTRMFPH
CCCCCCCCCCCCCCC
22.0025159151
65PhosphorylationLSSRGTPTRMFPHHS
CCCCCCCCCCCCCCC
34.3022115753
72PhosphorylationTRMFPHHSITESVNY
CCCCCCCCCCCCCCC
28.3325159151
74PhosphorylationMFPHHSITESVNYDV
CCCCCCCCCCCCCEE
25.8130108239
76PhosphorylationPHHSITESVNYDVKT
CCCCCCCCCCCEECC
13.6530108239
82AcetylationESVNYDVKTFGSSLP
CCCCCEECCCCCCCC
34.9326051181
82SumoylationESVNYDVKTFGSSLP
CCCCCEECCCCCCCC
34.93-
82UbiquitinationESVNYDVKTFGSSLP
CCCCCEECCCCCCCC
34.9321963094
122AcetylationACLVCKEKLIIWKIA
EEEEECCEEEEEEHH
30.4026051181
131PhosphorylationIIWKIALSPITKLSV
EEEEHHCCCCCCHHH
12.7730266825
134PhosphorylationKIALSPITKLSVCKE
EHHCCCCCCHHHHHH
29.3530266825
135AcetylationIALSPITKLSVCKEL
HHCCCCCCHHHHHHC
39.2125953088
135UbiquitinationIALSPITKLSVCKEL
HHCCCCCCHHHHHHC
39.2123000965
140UbiquitinationITKLSVCKELQLPPS
CCCHHHHHHCCCCCH
60.3423000965
197PhosphorylationLAGEDTYTEAFVDSG
CCCCCEEEEEEECCC
23.95-
213PhosphorylationDKTYSFLTAVQGGSF
CCEEEEEEEECCCEE
23.8328985074
219PhosphorylationLTAVQGGSFILSSSG
EEEECCCEEEECCCC
18.8828985074
223PhosphorylationQGGSFILSSSGSQLI
CCCEEEECCCCHHHE
20.03-
227PhosphorylationFILSSSGSQLIRLIP
EEECCCCHHHEEECC
24.6228985074
239UbiquitinationLIPESSGKIHQHILP
ECCCCCCCEEECCCC
38.67-
253PhosphorylationPQGQGMLSGIGRKVS
CCCCCCCCCHHHHHH
21.3328555341
258UbiquitinationMLSGIGRKVSSLFGI
CCCCHHHHHHHHHCC
41.05-
260PhosphorylationSGIGRKVSSLFGILS
CCHHHHHHHHHCCCC
25.1022199227
261PhosphorylationGIGRKVSSLFGILSP
CHHHHHHHHHCCCCC
30.6122199227
267PhosphorylationSSLFGILSPSSDLTL
HHHHCCCCCCCCCCH
22.3322199227
269PhosphorylationLFGILSPSSDLTLSS
HHCCCCCCCCCCHHH
32.8622199227
270PhosphorylationFGILSPSSDLTLSSV
HCCCCCCCCCCHHHH
39.7722199227
273PhosphorylationLSPSSDLTLSSVLWD
CCCCCCCCHHHHCCC
29.5922199227
275PhosphorylationPSSDLTLSSVLWDRE
CCCCCCHHHHCCCCC
17.1122199227
276PhosphorylationSSDLTLSSVLWDRER
CCCCCHHHHCCCCCC
25.0922199227
285PhosphorylationLWDRERSSFYSLTSS
CCCCCCCCCEEECCC
34.1320860994
287PhosphorylationDRERSSFYSLTSSNI
CCCCCCCEEECCCCC
12.5220860994
288PhosphorylationRERSSFYSLTSSNIS
CCCCCCEEECCCCCC
24.1420860994
290PhosphorylationRSSFYSLTSSNISKW
CCCCEEECCCCCCCE
24.9520860994
291PhosphorylationSSFYSLTSSNISKWE
CCCEEECCCCCCCEE
27.0420860994
292PhosphorylationSFYSLTSSNISKWEL
CCEEECCCCCCCEEC
32.7120860994
295PhosphorylationSLTSSNISKWELDDS
EECCCCCCCEECCCC
35.6520860994
296UbiquitinationLTSSNISKWELDDSS
ECCCCCCCEECCCCC
40.67-
303PhosphorylationKWELDDSSEKHAYSW
CEECCCCCCCCCHHH
58.62-
305AcetylationELDDSSEKHAYSWDI
ECCCCCCCCCHHHHH
35.1726051181
305UbiquitinationELDDSSEKHAYSWDI
ECCCCCCCCCHHHHH
35.1729967540
308PhosphorylationDSSEKHAYSWDINRA
CCCCCCCHHHHHHHH
15.2620068231
309PhosphorylationSSEKHAYSWDINRAL
CCCCCCHHHHHHHHH
21.0320068231
317UbiquitinationWDINRALKENITDAI
HHHHHHHHHCCCHHH
47.9721906983
321PhosphorylationRALKENITDAIWGSE
HHHHHCCCHHHHCCC
30.8424114839
329PhosphorylationDAIWGSESNYEAIKE
HHHHCCCCHHHHHHC
46.5428796482
331PhosphorylationIWGSESNYEAIKEGV
HHCCCCHHHHHHCCC
18.9328796482
335UbiquitinationESNYEAIKEGVNIRY
CCHHHHHHCCCCCEE
56.3021906983
450PhosphorylationVFNAQGDSVLGAGAC
EEECCCCCEECCCCC
26.5120068231
465PhosphorylationGGVPIIFSRNSGLVS
CCCEEEEECCCCCEE
21.8320068231
474PhosphorylationNSGLVSITSRENVSI
CCCCEEEECCCCEEE
17.7726471730
475PhosphorylationSGLVSITSRENVSIL
CCCEEEECCCCEEEE
35.6126471730
480PhosphorylationITSRENVSILAEDLE
EECCCCEEEEEEHHC
24.3822817900
489PhosphorylationLAEDLEGSLASSVAG
EEEHHCCCHHHHCCC
16.0430108239
492PhosphorylationDLEGSLASSVAGPNS
HHCCCHHHHCCCCCC
30.5530108239
493PhosphorylationLEGSLASSVAGPNSE
HCCCHHHHCCCCCCC
15.4730108239
499PhosphorylationSSVAGPNSESMIFET
HHCCCCCCCCCEEEE
33.8926074081
501PhosphorylationVAGPNSESMIFETTT
CCCCCCCCCEEEECC
19.5926074081
506PhosphorylationSESMIFETTTKNETI
CCCCEEEECCCCCCC
29.0828102081
507PhosphorylationESMIFETTTKNETIA
CCCEEEECCCCCCCC
28.6828102081
508PhosphorylationSMIFETTTKNETIAQ
CCEEEECCCCCCCCH
39.0128102081
512PhosphorylationETTTKNETIAQEDKI
EECCCCCCCCHHHHH
30.8929255136
518AcetylationETIAQEDKIKLLKAA
CCCCHHHHHHHHHHH
40.7726051181
518UbiquitinationETIAQEDKIKLLKAA
CCCCHHHHHHHHHHH
40.77-
523UbiquitinationEDKIKLLKAAFLQYC
HHHHHHHHHHHHHHH
48.37-
546PhosphorylationMVVDELFSSHSDLDS
HHHHHHHHCCCCCCC
39.5020068231
547PhosphorylationVVDELFSSHSDLDSD
HHHHHHHCCCCCCCH
21.4820068231
549PhosphorylationDELFSSHSDLDSDSE
HHHHHCCCCCCCHHH
41.6420068231
553PhosphorylationSSHSDLDSDSELDRA
HCCCCCCCHHHHHHH
50.7829116813
555PhosphorylationHSDLDSDSELDRAVT
CCCCCCHHHHHHHHH
43.9720068231
575PhosphorylationLMDDYPASDPRWAES
CCCCCCCCCCHHHHC
43.5820860994
582PhosphorylationSDPRWAESVPEEAPG
CCCHHHHCCCCCCCC
34.9128348404
591PhosphorylationPEEAPGFSNTSLIIL
CCCCCCCCCCEEEEE
45.1528348404
593PhosphorylationEAPGFSNTSLIILHQ
CCCCCCCCEEEEEEE
24.5824719451
594PhosphorylationAPGFSNTSLIILHQL
CCCCCCCEEEEEEEC
23.0928348404
604UbiquitinationILHQLEDKMKAHSFL
EEEECHHHHHHHHHH
32.69-
606UbiquitinationHQLEDKMKAHSFLMD
EECHHHHHHHHHHHH
49.00-
626PhosphorylationGLFGRLGSFPVRGTP
CCCCCCCCCCCCCCC
30.8525278378
632PhosphorylationGSFPVRGTPMATRLL
CCCCCCCCCHHHHHH
10.1825278378
636PhosphorylationVRGTPMATRLLLCEH
CCCCCHHHHHHHHHH
18.6525278378
661PhosphorylationKNHHSRLSDLVNTAI
HCCHHHHHHHHHHHH
27.9928188228
666PhosphorylationRLSDLVNTAILIALN
HHHHHHHHHHHHHHH
13.9528188228
674UbiquitinationAILIALNKREYEIPS
HHHHHHHCCCCCCCC
47.6721906983
677PhosphorylationIALNKREYEIPSNLT
HHHHCCCCCCCCCCC
24.1628796482
681PhosphorylationKREYEIPSNLTPADV
CCCCCCCCCCCHHHH
50.5725159151
684PhosphorylationYEIPSNLTPADVFFR
CCCCCCCCHHHHHHH
22.2327732954
740PhosphorylationKDMLQAASHYRQNRN
HHHHHHHHHHHHHHH
24.8620068231
755PhosphorylationSLYRREESLEKEPEY
HHHHCHHHHCCCCCC
36.7630108239
758AcetylationRREESLEKEPEYVPW
HCHHHHCCCCCCCCC
81.5025953088
758UbiquitinationRREESLEKEPEYVPW
HCHHHHCCCCCCCCC
81.5021906983
762PhosphorylationSLEKEPEYVPWTATS
HHCCCCCCCCCCCCC
23.6423186163
766PhosphorylationEPEYVPWTATSGPGG
CCCCCCCCCCCCCCC
17.6223186163
768PhosphorylationEYVPWTATSGPGGIR
CCCCCCCCCCCCCEE
27.1723186163
769PhosphorylationYVPWTATSGPGGIRT
CCCCCCCCCCCCEEE
40.2923186163
787AcetylationRQHEIVLKVAYPQAD
ECCEEEEEEECCCCC
17.5825953088
787UbiquitinationRQHEIVLKVAYPQAD
ECCEEEEEEECCCCC
17.5821906983
832PhosphorylationKSSNRERYDNLEMEY
CCCCHHHHHHHHHHH
12.39-
8422-HydroxyisobutyrylationLEMEYLQKRSDLLSP
HHHHHHHHHHHHHHH
51.80-
842UbiquitinationLEMEYLQKRSDLLSP
HHHHHHHHHHHHHHH
51.8023000965
908UbiquitinationLFRWYLEKGKRGKLL
HHHHHHHCCCCCCCC
68.11-
913UbiquitinationLEKGKRGKLLSQPIS
HHCCCCCCCCCCCHH
50.7329967540
961PhosphorylationLGLANMETRYFAKKK
HHHCCCCHHHHHHHH
21.65-
967UbiquitinationETRYFAKKKTLLGLS
CHHHHHHHHHHHHHH
47.7829967540
968UbiquitinationTRYFAKKKTLLGLSK
HHHHHHHHHHHHHHH
43.6429967540
969PhosphorylationRYFAKKKTLLGLSKL
HHHHHHHHHHHHHHH
35.77-
975UbiquitinationKTLLGLSKLAALASD
HHHHHHHHHHHHHCC
47.3832015554
981PhosphorylationSKLAALASDFSEDML
HHHHHHHCCCCHHHH
39.7820860994
991UbiquitinationSEDMLQEKIEEMAEQ
CHHHHHHHHHHHHHH
42.3229967540
1007PhosphorylationRFLLHQETLPEQLLA
HHHHCCCCCHHHHHH
40.8328348404
1021PhosphorylationAEKQLNLSAMPVLTA
HHHCCCCCCCCCCCH
22.8125159151
1027PhosphorylationLSAMPVLTAPQLIGL
CCCCCCCCHHHHHEE
36.20-
1046PhosphorylationENRRANEYDFKKALD
CCCCCCCCCHHHHHH
26.8728152594
1049UbiquitinationRANEYDFKKALDLLE
CCCCCCHHHHHHHHH
33.9529967540
1076UbiquitinationLKLEILCKALQRDNW
HHHHHHHHHHHCCCC
49.0032015554
1084PhosphorylationALQRDNWSSSDGKDD
HHHCCCCCCCCCCCC
26.64-
1085PhosphorylationLQRDNWSSSDGKDDP
HHCCCCCCCCCCCCC
24.86-
1086PhosphorylationQRDNWSSSDGKDDPI
HCCCCCCCCCCCCCC
44.88-
1089AcetylationNWSSSDGKDDPIEVS
CCCCCCCCCCCCCCC
65.0426051181
1089UbiquitinationNWSSSDGKDDPIEVS
CCCCCCCCCCCCCCC
65.0421906983
1097AcetylationDDPIEVSKDSIFVKI
CCCCCCCHHHHHHHH
61.7526051181
1097UbiquitinationDDPIEVSKDSIFVKI
CCCCCCCHHHHHHHH
61.7529967540
1107AcetylationIFVKILQKLLKDGIQ
HHHHHHHHHHHCCCC
52.9525953088
1107UbiquitinationIFVKILQKLLKDGIQ
HHHHHHHHHHHCCCC
52.9521890473
1110AcetylationKILQKLLKDGIQLSE
HHHHHHHHCCCCHHH
65.4326051181
1110UbiquitinationKILQKLLKDGIQLSE
HHHHHHHHCCCCHHH
65.4323000965
1123UbiquitinationSEYLPEVKDLLQADQ
HHHCHHHHHHHHHHH
40.7833845483
1133PhosphorylationLQADQLGSLKSNPYF
HHHHHCCCCCCCCCE
41.0130266825
1135UbiquitinationADQLGSLKSNPYFEF
HHHCCCCCCCCCEEE
50.3029967540
1150PhosphorylationVLKANYEYYVQGQI-
EEECCCEEEECCCC-
9.8922817900

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
50SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NU133_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 NU133_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU107_HUMANNUP107physical
11564755
NUP98_HUMANNUP98physical
11564755
NU107_HUMANNUP107physical
17363900
CENPF_HUMANCENPFphysical
17363900
SAP_HUMANPSAPphysical
22939629
NU107_HUMANNUP107physical
19674973
ELYS_HUMANAHCTF1physical
26344197
L10K_HUMANC19orf53physical
26344197
NU107_HUMANNUP107physical
26344197
ZMYM2_HUMANZMYM2physical
26344197
WWOX_HUMANWWOXphysical
24927568
P121A_HUMANPOM121physical
24927568
NUP50_HUMANNUP50physical
24927568
NU107_HUMANNUP107physical
24927568
RBP2_HUMANRANBP2physical
24927568
SENP2_HUMANSENP2physical
24927568
ELYS_HUMANAHCTF1physical
24927568
NUP98_HUMANNUP98physical
24927568
RL26L_HUMANRPL26L1physical
24927568
NU153_HUMANNUP153physical
24927568
LAP2A_HUMANTMPOphysical
24927568
LAP2B_HUMANTMPOphysical
24927568
RAF1_HUMANRAF1physical
27173435
NU107_HUMANNUP107physical
27173435
FTM_HUMANRPGRIP1Lphysical
27173435

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 NU133_HUMAN

loading...

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-7; THR-10; SER-27; THR-28; SER-45; SER-50 ANDSER-131, 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-45; SER-50 AND SER-480,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-7; THR-10; SER-27; THR-28; SER-45; SER-50 ANDSER-131, 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-27; THR-28; SER-41;SER-45 AND SER-50, 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-7; SER-45 AND SER-50,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-45 AND SER-50, AND MASSSPECTROMETRY.
"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-7; SER-57 AND SER-489,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-45 AND SER-50, AND MASSSPECTROMETRY.
"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 SER-27; THR-28 AND SER-45,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-45 AND SER-50, AND MASSSPECTROMETRY.

TOP