U5S1_HUMAN - dbPTM
U5S1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U5S1_HUMAN
UniProt AC Q15029
Protein Name 116 kDa U5 small nuclear ribonucleoprotein component
Gene Name EFTUD2
Organism Homo sapiens (Human).
Sequence Length 972
Subcellular Localization Nucleus .
Protein Description Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP..
Protein Sequence MDTDLYDEFGNYIGPELDSDEDDDELGRETKDLDEMDDDDDDDDVGDHDDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERGVGIKSTPVTVVLPDTKGKSYLFNIMDTPGHVNFSDEVTAGLRISDGVVLFIDAAEGVMLNTERLIKHAVQERLAVTVCINKIDRLILELKLPPTDAYYKLRHIVDEVNGLISMYSTDENLILSPLLGNVCFSSSQYSICFTLGSFAKIYADTFGDINYQEFAKRLWGDIYFNPKTRKFTKKAPTSSSQRSFVEFILEPLYKILAQVVGDVDTSLPRTLDELGIHLTKEELKLNIRPLLRLVCKKFFGEFTGFVDMCVQHIPSPKVGAKPKIEHTYTGGVDSDLGEAMSDCDPDGPLMCHTTKMYSTDDGVQFHAFGRVLSGTIHAGQPVKVLGENYTLEDEEDSQICTVGRLWISVARYHIEVNRVPAGNWVLIEGVDQPIVKTATITEPRGNEEAQIFRPLKFNTTSVIKIAVEPVNPSELPKMLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRKKLGEFFQTKYDWDLLAARSIWAFGPDATGPNILVDDTLPSEVDKALLGSVKDSIVQGFQWGTREGPLCDELIRNVKFKILDAVVAQEPLHRGGGQIIPTARRVVYSAFLMATPRLMEPYYFVEVQAPADCVSAVYTVLARRRGHVTQDAPIPGSPLYTIKAFIPAIDSFGFETDLRTHTQGQAFSLSVFHHWQIVPGDPLDKSIVIRPLEPQPAPHLAREFMIKTRRRKGLSEDVSISKFFDDPMLLELAKQDVVLNYPM
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-------MDTDLYDE
-------CCCHHHHH
12.9720068231
3Phosphorylation-----MDTDLYDEFG
-----CCCHHHHHCC
26.9717081983
6Phosphorylation--MDTDLYDEFGNYI
--CCCHHHHHCCCCC
19.0824732914
12PhosphorylationLYDEFGNYIGPELDS
HHHHCCCCCCCCCCC
13.9724043423
19PhosphorylationYIGPELDSDEDDDEL
CCCCCCCCCCCCCHH
56.3728355574
30PhosphorylationDDELGRETKDLDEMD
CCHHCCCCCCHHHCC
28.6222617229
63AcetylationEVVLHEDKKYYPTAE
EEEEECCCCCCCCHH
39.4226051181
64SumoylationVVLHEDKKYYPTAEE
EEEECCCCCCCCHHH
63.4425114211
64UbiquitinationVVLHEDKKYYPTAEE
EEEECCCCCCCCHHH
63.44-
65PhosphorylationVLHEDKKYYPTAEEV
EEECCCCCCCCHHHH
22.0323186163
66PhosphorylationLHEDKKYYPTAEEVY
EECCCCCCCCHHHHH
11.7323186163
68PhosphorylationEDKKYYPTAEEVYGP
CCCCCCCCHHHHHCC
30.4929116813
73PhosphorylationYPTAEEVYGPEVETI
CCCHHHHHCCCCEEE
30.1823663014
79PhosphorylationVYGPEVETIVQEEDT
HHCCCCEEEEECCCC
31.4623898821
86PhosphorylationTIVQEEDTQPLTEPI
EEEECCCCCCCCCCC
35.0517525332
90PhosphorylationEEDTQPLTEPIIKPV
CCCCCCCCCCCCCCC
46.5319276368
95UbiquitinationPLTEPIIKPVKTKKF
CCCCCCCCCCCCCCE
44.4721906983
103PhosphorylationPVKTKKFTLMEQTLP
CCCCCCEEECEEECC
33.7924043423
108PhosphorylationKFTLMEQTLPVTVYE
CEEECEEECCEEEEE
21.5224043423
112PhosphorylationMEQTLPVTVYEMDFL
CEEECCEEEEEHHHH
18.5424043423
114PhosphorylationQTLPVTVYEMDFLAD
EECCEEEEEHHHHHH
9.0024043423
126PhosphorylationLADLMDNSELIRNVT
HHHHCCCHHHHHHEE
29.5224043423
133PhosphorylationSELIRNVTLCGHLHH
HHHHHHEEECCCCCC
21.6324043423
142AcetylationCGHLHHGKTCFVDCL
CCCCCCCCCCHHHHH
37.4526051181
144GlutathionylationHLHHGKTCFVDCLIE
CCCCCCCCHHHHHHH
3.4022555962
159UbiquitinationQTHPEIRKRYDQDLC
CCCHHHHHHCCCCCC
62.05-
161PhosphorylationHPEIRKRYDQDLCYT
CHHHHHHCCCCCCEE
22.4628796482
166GlutathionylationKRYDQDLCYTDILFT
HHCCCCCCEECEEEC
4.6522555962
167PhosphorylationRYDQDLCYTDILFTE
HCCCCCCEECEEECC
18.1028796482
168PhosphorylationYDQDLCYTDILFTEQ
CCCCCCEECEEECCC
18.6328796482
172UbiquitinationLCYTDILFTEQERGV
CCEECEEECCCCCCC
7.84-
173PhosphorylationCYTDILFTEQERGVG
CEECEEECCCCCCCC
33.0628258704
1822-HydroxyisobutyrylationQERGVGIKSTPVTVV
CCCCCCCCCCCEEEE
42.20-
182UbiquitinationQERGVGIKSTPVTVV
CCCCCCCCCCCEEEE
42.2021906983
184PhosphorylationRGVGIKSTPVTVVLP
CCCCCCCCCEEEECC
19.4423911959
234UbiquitinationLFIDAAEGVMLNTER
EEEECCCCCCCCHHH
12.86-
244UbiquitinationLNTERLIKHAVQERL
CCHHHHHHHHHHHHH
30.06-
259AcetylationAVTVCINKIDRLILE
CCEEHHHHHCHHHHC
26.5226051181
272PhosphorylationLELKLPPTDAYYKLR
HCCCCCCCHHHHHHH
31.1828634298
275PhosphorylationKLPPTDAYYKLRHIV
CCCCCHHHHHHHHHH
12.1628634298
276PhosphorylationLPPTDAYYKLRHIVD
CCCCHHHHHHHHHHH
12.7928634298
277AcetylationPPTDAYYKLRHIVDE
CCCHHHHHHHHHHHH
26.7726822725
277UbiquitinationPPTDAYYKLRHIVDE
CCCHHHHHHHHHHHH
26.77-
317UbiquitinationSSSQYSICFTLGSFA
CCCCEEEEEEHHHHH
1.4321890473
331UbiquitinationAKIYADTFGDINYQE
HHHHHHCCCCCCHHH
9.47-
336PhosphorylationDTFGDINYQEFAKRL
HCCCCCCHHHHHHHH
15.11-
341AcetylationINYQEFAKRLWGDIY
CCHHHHHHHHHCCEE
54.0326051181
341UbiquitinationINYQEFAKRLWGDIY
CCHHHHHHHHHCCEE
54.0321906983
342UbiquitinationNYQEFAKRLWGDIYF
CHHHHHHHHHCCEEC
32.04-
348PhosphorylationKRLWGDIYFNPKTRK
HHHHCCEECCCCCCC
11.31-
352UbiquitinationGDIYFNPKTRKFTKK
CCEECCCCCCCCCCC
63.1621890473
352UbiquitinationGDIYFNPKTRKFTKK
CCEECCCCCCCCCCC
63.1621890473
353PhosphorylationDIYFNPKTRKFTKKA
CEECCCCCCCCCCCC
40.1118452278
370UbiquitinationSSSQRSFVEFILEPL
CCHHHHHHHHHHHHH
6.5621890473
374UbiquitinationRSFVEFILEPLYKIL
HHHHHHHHHHHHHHH
7.2321890473
395UbiquitinationVDTSLPRTLDELGIH
CCCCCCCHHHHHCCC
36.30-
399UbiquitinationLPRTLDELGIHLTKE
CCCHHHHHCCCCCHH
8.56-
405UbiquitinationELGIHLTKEELKLNI
HHCCCCCHHHHHCCH
56.4021890473
405AcetylationELGIHLTKEELKLNI
HHCCCCCHHHHHCCH
56.4026822725
405UbiquitinationELGIHLTKEELKLNI
HHCCCCCHHHHHCCH
56.4021890473
409UbiquitinationHLTKEELKLNIRPLL
CCCHHHHHCCHHHHH
42.6521890473
409AcetylationHLTKEELKLNIRPLL
CCCHHHHHCCHHHHH
42.6526822725
409UbiquitinationHLTKEELKLNIRPLL
CCCHHHHHCCHHHHH
42.6521890473
452PhosphorylationAKPKIEHTYTGGVDS
CCCCCEEEEECCCCC
15.2528122231
453PhosphorylationKPKIEHTYTGGVDSD
CCCCEEEEECCCCCC
12.8027732954
454PhosphorylationPKIEHTYTGGVDSDL
CCCEEEEECCCCCCH
28.7227732954
459PhosphorylationTYTGGVDSDLGEAMS
EEECCCCCCHHHHHH
32.1230576142
466PhosphorylationSDLGEAMSDCDPDGP
CCHHHHHHCCCCCCC
41.9830576142
478PhosphorylationDGPLMCHTTKMYSTD
CCCEEEEECCEEECC
24.1620873877
479PhosphorylationGPLMCHTTKMYSTDD
CCEEEEECCEEECCC
7.0820873877
498UbiquitinationHAFGRVLSGTIHAGQ
EEEEEEECCEEECCC
30.91-
498PhosphorylationHAFGRVLSGTIHAGQ
EEEEEEECCEEECCC
30.91-
508UbiquitinationIHAGQPVKVLGENYT
EECCCEEEEEEECCC
38.12-
533PhosphorylationTVGRLWISVARYHIE
EHHHHEEEEEEEEEE
9.7221406692
546UbiquitinationIEVNRVPAGNWVLIE
EEECCCCCCCEEEEE
22.5421890473
551UbiquitinationVPAGNWVLIEGVDQP
CCCCCEEEEECCCCC
1.92-
561UbiquitinationGVDQPIVKTATITEP
CCCCCEEEEEEEECC
32.9121906983
562PhosphorylationVDQPIVKTATITEPR
CCCCEEEEEEEECCC
20.3821406692
564PhosphorylationQPIVKTATITEPRGN
CCEEEEEEEECCCCC
33.3921406692
566PhosphorylationIVKTATITEPRGNEE
EEEEEEEECCCCCCC
35.2721406692
567UbiquitinationVKTATITEPRGNEEA
EEEEEEECCCCCCCE
29.2021890473
569MethylationTATITEPRGNEEAQI
EEEEECCCCCCCEEE
55.10-
571UbiquitinationTITEPRGNEEAQIFR
EEECCCCCCCEEEEE
45.26-
579UbiquitinationEEAQIFRPLKFNTTS
CCEEEEEEECCCCCE
29.20-
581UbiquitinationAQIFRPLKFNTTSVI
EEEEEEECCCCCEEE
38.9721890473
581AcetylationAQIFRPLKFNTTSVI
EEEEEEECCCCCEEE
38.9726051181
581UbiquitinationAQIFRPLKFNTTSVI
EEEEEEECCCCCEEE
38.9721906983
589UbiquitinationFNTTSVIKIAVEPVN
CCCCEEEEEEEECCC
23.58-
592UbiquitinationTSVIKIAVEPVNPSE
CEEEEEEEECCCHHH
11.00-
598PhosphorylationAVEPVNPSELPKMLD
EEECCCHHHHHHHHH
46.7025850435
599UbiquitinationVEPVNPSELPKMLDG
EECCCHHHHHHHHHH
71.05-
602UbiquitinationVNPSELPKMLDGLRK
CCHHHHHHHHHHHHH
65.8021890473
602UbiquitinationVNPSELPKMLDGLRK
CCHHHHHHHHHHHHH
65.8021890473
609UbiquitinationKMLDGLRKVNKSYPS
HHHHHHHHHHHCCCC
56.02-
612UbiquitinationDGLRKVNKSYPSLTT
HHHHHHHHCCCCCEE
55.12-
614PhosphorylationLRKVNKSYPSLTTKV
HHHHHHCCCCCEEEE
9.8430631047
616PhosphorylationKVNKSYPSLTTKVEE
HHHHCCCCCEEEEEE
30.0720068231
618PhosphorylationNKSYPSLTTKVEESG
HHCCCCCEEEEEECC
28.9830631047
619PhosphorylationKSYPSLTTKVEESGE
HCCCCCEEEEEECCC
38.0830631047
636UbiquitinationILGTGELYLDCVMHD
EECCCCHHHHHHHHH
9.01-
646UbiquitinationCVMHDLRKMYSEIDI
HHHHHHHHHHHHCCE
49.87-
649PhosphorylationHDLRKMYSEIDIKVA
HHHHHHHHHCCEEEC
25.2829978859
663UbiquitinationADPVVTFCETVVETS
CCCCEEEEEEEEECC
2.90-
663GlutathionylationADPVVTFCETVVETS
CCCCEEEEEEEEECC
2.9022555962
673UbiquitinationVVETSSLKCFAETPN
EEECCCCEEEECCCC
29.29-
674UbiquitinationVETSSLKCFAETPNK
EECCCCEEEECCCCC
4.79-
681AcetylationCFAETPNKKNKITMI
EEECCCCCCCCEEEE
59.9525953088
681UbiquitinationCFAETPNKKNKITMI
EEECCCCCCCCEEEE
59.95-
6842-HydroxyisobutyrylationETPNKKNKITMIAEP
CCCCCCCCEEEEECC
48.73-
684UbiquitinationETPNKKNKITMIAEP
CCCCCCCCEEEEECC
48.73-
687SulfoxidationNKKNKITMIAEPLEK
CCCCCEEEEECCHHC
2.8821406390
694UbiquitinationMIAEPLEKGLAEDIE
EEECCHHCCCHHHHH
67.89-
702UbiquitinationGLAEDIENEVVQITW
CCHHHHHCCEEEEEE
47.93-
703UbiquitinationLAEDIENEVVQITWN
CHHHHHCCEEEEEEC
31.13-
711UbiquitinationVVQITWNRKKLGEFF
EEEEEECHHHHHHHH
29.10-
712UbiquitinationVQITWNRKKLGEFFQ
EEEEECHHHHHHHHH
49.49-
713AcetylationQITWNRKKLGEFFQT
EEEECHHHHHHHHHC
59.4925953088
713UbiquitinationQITWNRKKLGEFFQT
EEEECHHHHHHHHHC
59.4921906983
721UbiquitinationLGEFFQTKYDWDLLA
HHHHHHCCCCHHHHH
30.3521906983
722PhosphorylationGEFFQTKYDWDLLAA
HHHHHCCCCHHHHHH
26.1728152594
740PhosphorylationWAFGPDATGPNILVD
EEECCCCCCCCEECC
61.63-
749PhosphorylationPNILVDDTLPSEVDK
CCEECCCCCCHHHHH
35.78-
752PhosphorylationLVDDTLPSEVDKALL
ECCCCCCHHHHHHHH
54.05-
755UbiquitinationDTLPSEVDKALLGSV
CCCCHHHHHHHHHHH
26.8521890473
756UbiquitinationTLPSEVDKALLGSVK
CCCHHHHHHHHHHHH
46.22-
763UbiquitinationKALLGSVKDSIVQGF
HHHHHHHHHHHHHHC
47.6721906983
780GlutathionylationGTREGPLCDELIRNV
CCCCCCCHHHHHHHC
4.2622555962
788UbiquitinationDELIRNVKFKILDAV
HHHHHHCCHHHHCHH
44.48-
790UbiquitinationLIRNVKFKILDAVVA
HHHHCCHHHHCHHHH
36.3221890473
7902-HydroxyisobutyrylationLIRNVKFKILDAVVA
HHHHCCHHHHCHHHH
36.32-
790AcetylationLIRNVKFKILDAVVA
HHHHCCHHHHCHHHH
36.3225825284
790UbiquitinationLIRNVKFKILDAVVA
HHHHCCHHHHCHHHH
36.3221906983
803MethylationVAQEPLHRGGGQIIP
HHCCCCCCCCCCCCC
53.81-
811PhosphorylationGGGQIIPTARRVVYS
CCCCCCCCHHHHHHH
23.5320068231
813MethylationGQIIPTARRVVYSAF
CCCCCCHHHHHHHHH
34.11-
817PhosphorylationPTARRVVYSAFLMAT
CCHHHHHHHHHHHHC
7.4521406692
818PhosphorylationTARRVVYSAFLMATP
CHHHHHHHHHHHHCC
10.8421406692
824PhosphorylationYSAFLMATPRLMEPY
HHHHHHHCCCCCCCE
8.5820068231
858PhosphorylationARRRGHVTQDAPIPG
HHHCCCCCCCCCCCC
18.3023663014
866PhosphorylationQDAPIPGSPLYTIKA
CCCCCCCCCCEEEEE
13.3323663014
869PhosphorylationPIPGSPLYTIKAFIP
CCCCCCCEEEEEEHH
15.1423663014
870PhosphorylationIPGSPLYTIKAFIPA
CCCCCCEEEEEEHHH
24.5523663014
880PhosphorylationAFIPAIDSFGFETDL
EEHHHHHHCCCCCCC
22.5827307780
885PhosphorylationIDSFGFETDLRTHTQ
HHHCCCCCCCCCCCC
37.7627307780
889PhosphorylationGFETDLRTHTQGQAF
CCCCCCCCCCCCCCE
36.2527307780
891PhosphorylationETDLRTHTQGQAFSL
CCCCCCCCCCCCEEE
33.5127307780
897PhosphorylationHTQGQAFSLSVFHHW
CCCCCCEEEEEEECE
23.8127307780
899PhosphorylationQGQAFSLSVFHHWQI
CCCCEEEEEEECEEE
22.8727307780
915PhosphorylationPGDPLDKSIVIRPLE
CCCCCCCCEEEEECC
23.0428555341
926UbiquitinationRPLEPQPAPHLAREF
EECCCCCCHHHHHHH
10.01-
931UbiquitinationQPAPHLAREFMIKTR
CCCHHHHHHHHHHHC
44.01-
936UbiquitinationLAREFMIKTRRRKGL
HHHHHHHHHCCCCCC
24.96-
941UbiquitinationMIKTRRRKGLSEDVS
HHHHCCCCCCCCCCC
63.49-
941UbiquitinationMIKTRRRKGLSEDVS
HHHHCCCCCCCCCCC
63.49-
944PhosphorylationTRRRKGLSEDVSISK
HCCCCCCCCCCCHHH
40.1830266825
948PhosphorylationKGLSEDVSISKFFDD
CCCCCCCCHHHHCCC
33.2021815630
950PhosphorylationLSEDVSISKFFDDPM
CCCCCCHHHHCCCHH
18.8629255136
951UbiquitinationSEDVSISKFFDDPML
CCCCCHHHHCCCHHH
48.672190698
957SulfoxidationSKFFDDPMLLELAKQ
HHHCCCHHHHHHHHC
9.5521406390
963UbiquitinationPMLLELAKQDVVLNY
HHHHHHHHCCCCCCC
60.70-

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 U5S1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U5S1_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 U5S1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARPC3_HUMANARPC3physical
16169070
U5S1_HUMANEFTUD2physical
16723661
U520_HUMANSNRNP200physical
16723661
PRP8_HUMANPRPF8physical
16723661
SNR40_HUMANSNRNP40physical
16723661
VIR_HUMANKIAA1429physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
ZN622_HUMANZNF622physical
22939629
UBR4_HUMANUBR4physical
22939629
SF3B3_HUMANSF3B3physical
22365833
SF3B4_HUMANSF3B4physical
22365833
SF01_HUMANSF1physical
22365833
LSM8_HUMANLSM8physical
22365833
RED_HUMANIKphysical
22365833
HSPB1_HUMANHSPB1physical
22365833
AASD1_HUMANAARSD1physical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SHLB2_HUMANSH3GLB2physical
22863883
SNF8_HUMANSNF8physical
22863883
PRP8_HUMANPRPF8physical
17317632
ZMY11_HUMANZMYND11physical
25263594
PRP8_HUMANPRPF8physical
25263594
U520_HUMANSNRNP200physical
25263594
CD2B2_HUMANCD2BP2physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
PRP4_HUMANPRPF4physical
26344197
RNPS1_HUMANRNPS1physical
26344197
SREK1_HUMANSREK1physical
26344197
HSF1_HUMANHSF1physical
27173435
U520_HUMANSNRNP200physical
27173435
SMU1_HUMANSMU1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610536Mandibulofacial dysostosis with microcephaly (MFDM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of U5S1_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-19 AND THR-30, 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-944, AND MASSSPECTROMETRY.
"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-19 AND THR-30, 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-19, AND MASSSPECTROMETRY.
"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 THR-86, AND MASSSPECTROMETRY.
"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 THR-86, AND MASSSPECTROMETRY.

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