P66A_HUMAN - dbPTM
P66A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P66A_HUMAN
UniProt AC Q86YP4
Protein Name Transcriptional repressor p66-alpha
Gene Name GATAD2A
Organism Homo sapiens (Human).
Sequence Length 633
Subcellular Localization Nucleus speckle . Speckled nuclear localization requires both CR1 and CR2 regions.
Protein Description Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B..
Protein Sequence MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALKETSTEALMKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTGSVGSTVTTPPPLVRGTQNIPAGKPSLQTSSARMPGSVIPPPLVRGGQQASSKLGPQASSQVVMPPLVRGAQQIHSIRQHSSTGPPPLLLAPRASVPSVQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTPASLKGTTATSAQANSTPTSVASVVTSAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQGRMSAATVLSREPYMCAQCKTDFTCRWREEKSGAIMCENCMTTNQKKALKVEHTSRLKAAFVKALQQEQEIEQRLLQQGTAPAQAKAEPTAAPHPVLKQVIKPRRKLAFRSGEARDWSNGAVLQASSQLSRGSATTPRGVLHTFSPSPKLQNSASATALVSRTGRHSERTVSAGKGSATSNWKKTPLSTGGTLAFVSPSLAVHKSSSAVDRQREYLLDMIPPRSIPQSATWK
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
20PhosphorylationRALERDPTEDDVESK
HHHHCCCCHHHHHHH
57.2323917254
26PhosphorylationPTEDDVESKKIKMER
CCHHHHHHHHHHHHC
38.8122985185
27AcetylationTEDDVESKKIKMERG
CHHHHHHHHHHHHCC
45.0425953088
30SumoylationDVESKKIKMERGLLA
HHHHHHHHHHCCCCH
43.52-
30SumoylationDVESKKIKMERGLLA
HHHHHHHHHHCCCCH
43.52-
38PhosphorylationMERGLLASDLNTDGD
HHCCCCHHHCCCCCC
42.4729978859
42PhosphorylationLLASDLNTDGDMRVT
CCHHHCCCCCCCCCC
48.9729255136
46SulfoxidationDLNTDGDMRVTPEPG
HCCCCCCCCCCCCCC
4.5521406390
49PhosphorylationTDGDMRVTPEPGAGP
CCCCCCCCCCCCCCC
16.1519664994
57PhosphorylationPEPGAGPTQGLLRAT
CCCCCCCCHHHHHHH
34.0629978859
64PhosphorylationTQGLLRATEATAMAM
CHHHHHHHHHHHHHC
21.5127251275
67PhosphorylationLLRATEATAMAMGRG
HHHHHHHHHHHCCCC
15.6727251275
73MethylationATAMAMGRGEGLVGD
HHHHHCCCCCCCCCC
27.23-
85SulfoxidationVGDGPVDMRTSHSDM
CCCCCCCCCCCHHHC
5.2521406390
87PhosphorylationDGPVDMRTSHSDMKS
CCCCCCCCCHHHCCC
24.9324719451
88PhosphorylationGPVDMRTSHSDMKSE
CCCCCCCCHHHCCCC
15.6124719451
90PhosphorylationVDMRTSHSDMKSERR
CCCCCCHHHCCCCCC
38.8827251275
93SumoylationRTSHSDMKSERRPPS
CCCHHHCCCCCCCCC
54.90-
93SumoylationRTSHSDMKSERRPPS
CCCHHHCCCCCCCCC
54.9028112733
94PhosphorylationTSHSDMKSERRPPSP
CCHHHCCCCCCCCCC
29.6921406692
100PhosphorylationKSERRPPSPDVIVLS
CCCCCCCCCCEEEEC
36.0929255136
107PhosphorylationSPDVIVLSDNEQPSS
CCCEEEECCCCCCCC
27.7429255136
113PhosphorylationLSDNEQPSSPRVNGL
ECCCCCCCCCCCCCE
53.3129255136
114PhosphorylationSDNEQPSSPRVNGLT
CCCCCCCCCCCCCEE
24.3329255136
121PhosphorylationSPRVNGLTTVALKET
CCCCCCEEEEEEEEC
22.1822115753
122PhosphorylationPRVNGLTTVALKETS
CCCCCEEEEEEEECC
14.6122115753
128PhosphorylationTTVALKETSTEALMK
EEEEEEECCHHHHHH
39.0824732914
129PhosphorylationTVALKETSTEALMKS
EEEEEECCHHHHHHC
25.9121815630
130PhosphorylationVALKETSTEALMKSS
EEEEECCHHHHHHCC
32.4730624053
135UbiquitinationTSTEALMKSSPEERE
CCHHHHHHCCHHHHH
48.94-
135UbiquitinationTSTEALMKSSPEERE
CCHHHHHHCCHHHHH
48.94-
136PhosphorylationSTEALMKSSPEERER
CHHHHHHCCHHHHHH
36.8424732914
137PhosphorylationTEALMKSSPEERERM
HHHHHHCCHHHHHHH
30.7124732914
153MethylationKQLKEELRLEEAKLV
HHHHHHHCHHHHHHH
43.25-
158UbiquitinationELRLEEAKLVLLKKL
HHCHHHHHHHHHHHH
42.27-
172AcetylationLRQSQIQKEATAQKP
HHHHHHHHHHHCCCC
51.447366045
175PhosphorylationSQIQKEATAQKPTGS
HHHHHHHHCCCCCCC
30.6121712546
178UbiquitinationQKEATAQKPTGSVGS
HHHHHCCCCCCCCCC
41.92-
178SumoylationQKEATAQKPTGSVGS
HHHHHCCCCCCCCCC
41.9228112733
178UbiquitinationQKEATAQKPTGSVGS
HHHHHCCCCCCCCCC
41.92-
180PhosphorylationEATAQKPTGSVGSTV
HHHCCCCCCCCCCEE
49.4722115753
182O-linked_GlycosylationTAQKPTGSVGSTVTT
HCCCCCCCCCCEECC
26.2830059200
182PhosphorylationTAQKPTGSVGSTVTT
HCCCCCCCCCCEECC
26.2822115753
185PhosphorylationKPTGSVGSTVTTPPP
CCCCCCCCEECCCCC
19.9730266825
186PhosphorylationPTGSVGSTVTTPPPL
CCCCCCCEECCCCCC
18.8830266825
188PhosphorylationGSVGSTVTTPPPLVR
CCCCCEECCCCCCCC
33.4030266825
189PhosphorylationSVGSTVTTPPPLVRG
CCCCEECCCCCCCCC
29.4825159151
204UbiquitinationTQNIPAGKPSLQTSS
CCCCCCCCCCCCCCC
33.27-
204AcetylationTQNIPAGKPSLQTSS
CCCCCCCCCCCCCCC
33.2726051181
204SumoylationTQNIPAGKPSLQTSS
CCCCCCCCCCCCCCC
33.2728112733
204UbiquitinationTQNIPAGKPSLQTSS
CCCCCCCCCCCCCCC
33.27-
206PhosphorylationNIPAGKPSLQTSSAR
CCCCCCCCCCCCCCC
36.2728555341
209O-linked_GlycosylationAGKPSLQTSSARMPG
CCCCCCCCCCCCCCC
29.9130059200
210O-linked_GlycosylationGKPSLQTSSARMPGS
CCCCCCCCCCCCCCC
14.7230059200
211PhosphorylationKPSLQTSSARMPGSV
CCCCCCCCCCCCCCC
24.2320068231
213MethylationSLQTSSARMPGSVIP
CCCCCCCCCCCCCCC
33.50-
214SulfoxidationLQTSSARMPGSVIPP
CCCCCCCCCCCCCCC
4.3921406390
217PhosphorylationSSARMPGSVIPPPLV
CCCCCCCCCCCCCEE
15.8222210691
225MethylationVIPPPLVRGGQQASS
CCCCCEECCCCCCHH
51.73-
233UbiquitinationGGQQASSKLGPQASS
CCCCCHHCCCCCCCC
55.77-
233AcetylationGGQQASSKLGPQASS
CCCCCHHCCCCCCCC
55.7725953088
233SumoylationGGQQASSKLGPQASS
CCCCCHHCCCCCCCC
55.7728112733
233UbiquitinationGGQQASSKLGPQASS
CCCCCHHCCCCCCCC
55.77-
239PhosphorylationSKLGPQASSQVVMPP
HCCCCCCCCCCCCCC
18.9626714015
240PhosphorylationKLGPQASSQVVMPPL
CCCCCCCCCCCCCCC
29.9726714015
244SulfoxidationQASSQVVMPPLVRGA
CCCCCCCCCCCCCCH
2.7321406390
249DimethylationVVMPPLVRGAQQIHS
CCCCCCCCCHHHHHH
42.27-
249MethylationVVMPPLVRGAQQIHS
CCCCCCCCCHHHHHH
42.2724129315
256PhosphorylationRGAQQIHSIRQHSST
CCHHHHHHHHHCCCC
22.5423401153
258DimethylationAQQIHSIRQHSSTGP
HHHHHHHHHCCCCCC
31.04-
258MethylationAQQIHSIRQHSSTGP
HHHHHHHHHCCCCCC
31.0424129315
261PhosphorylationIHSIRQHSSTGPPPL
HHHHHHCCCCCCCCE
22.6623312004
262PhosphorylationHSIRQHSSTGPPPLL
HHHHHCCCCCCCCEE
34.9523312004
263PhosphorylationSIRQHSSTGPPPLLL
HHHHCCCCCCCCEEE
57.6423312004
273DimethylationPPLLLAPRASVPSVQ
CCEEECCCCCCCCEE
33.61-
273MethylationPPLLLAPRASVPSVQ
CCEEECCCCCCCCEE
33.6124129315
275PhosphorylationLLLAPRASVPSVQIQ
EEECCCCCCCCEEEC
35.5229978859
278PhosphorylationAPRASVPSVQIQGQR
CCCCCCCCEEECCEE
25.2123186163
285MethylationSVQIQGQRIIQQGLI
CEEECCEEHHHCCCE
34.5024129315
293MethylationIIQQGLIRVANVPNT
HHHCCCEEEECCCCC
26.91-
300PhosphorylationRVANVPNTSLLVNIP
EEECCCCCEEEEECC
18.0628122231
301PhosphorylationVANVPNTSLLVNIPQ
EECCCCCEEEEECCC
26.7528122231
310PhosphorylationLVNIPQPTPASLKGT
EEECCCCCCCCCCCC
26.6628122231
313PhosphorylationIPQPTPASLKGTTAT
CCCCCCCCCCCCCCC
31.6420068231
317O-linked_GlycosylationTPASLKGTTATSAQA
CCCCCCCCCCCCCCC
16.2130059200
317PhosphorylationTPASLKGTTATSAQA
CCCCCCCCCCCCCCC
16.2124732914
318O-linked_GlycosylationPASLKGTTATSAQAN
CCCCCCCCCCCCCCC
36.2830059200
318PhosphorylationPASLKGTTATSAQAN
CCCCCCCCCCCCCCC
36.2824732914
320PhosphorylationSLKGTTATSAQANST
CCCCCCCCCCCCCCC
23.6224732914
321O-linked_GlycosylationLKGTTATSAQANSTP
CCCCCCCCCCCCCCC
18.8730059200
321PhosphorylationLKGTTATSAQANSTP
CCCCCCCCCCCCCCC
18.8724732914
326O-linked_GlycosylationATSAQANSTPTSVAS
CCCCCCCCCCCCHHH
38.4930059200
326PhosphorylationATSAQANSTPTSVAS
CCCCCCCCCCCCHHH
38.4924732914
327O-linked_GlycosylationTSAQANSTPTSVASV
CCCCCCCCCCCHHHH
30.3230059200
327PhosphorylationTSAQANSTPTSVASV
CCCCCCCCCCCHHHH
30.3225159151
329O-linked_GlycosylationAQANSTPTSVASVVT
CCCCCCCCCHHHHHH
35.6030059200
329PhosphorylationAQANSTPTSVASVVT
CCCCCCCCCHHHHHH
35.6028176443
330O-linked_GlycosylationQANSTPTSVASVVTS
CCCCCCCCHHHHHHC
19.5230059200
330PhosphorylationQANSTPTSVASVVTS
CCCCCCCCHHHHHHC
19.5229255136
333O-linked_GlycosylationSTPTSVASVVTSAES
CCCCCHHHHHHCCCC
18.2430059200
333PhosphorylationSTPTSVASVVTSAES
CCCCCHHHHHHCCCC
18.2429255136
336O-linked_GlycosylationTSVASVVTSAESPAS
CCHHHHHHCCCCHHH
21.7730059200
336PhosphorylationTSVASVVTSAESPAS
CCHHHHHHCCCCHHH
21.7729255136
337PhosphorylationSVASVVTSAESPASR
CHHHHHHCCCCHHHH
20.5929255136
340PhosphorylationSVVTSAESPASRQAA
HHHHCCCCHHHHHHH
26.0329255136
343O-linked_GlycosylationTSAESPASRQAAAKL
HCCCCHHHHHHHHHH
28.4530059200
343PhosphorylationTSAESPASRQAAAKL
HCCCCHHHHHHHHHH
28.4529255136
349UbiquitinationASRQAAAKLALRKQL
HHHHHHHHHHHHHHH
29.57-
404SulfoxidationLLETQGRMSAATVLS
HHHHCCCCCHHHHHC
4.0121406390
405PhosphorylationLETQGRMSAATVLSR
HHHCCCCCHHHHHCC
17.2520068231
411PhosphorylationMSAATVLSREPYMCA
CCHHHHHCCCCEEEC
30.2020068230
421UbiquitinationPYMCAQCKTDFTCRW
CEEECCCCCCCCCCC
38.76-
422UbiquitinationYMCAQCKTDFTCRWR
EEECCCCCCCCCCCC
43.93-
432AcetylationTCRWREEKSGAIMCE
CCCCCHHCCCCEEEE
49.8126051181
432UbiquitinationTCRWREEKSGAIMCE
CCCCCHHCCCCEEEE
49.81-
451SumoylationTNQKKALKVEHTSRL
CCHHHCCCCHHHHHH
50.89-
451SumoylationTNQKKALKVEHTSRL
CCHHHCCCCHHHHHH
50.89-
452UbiquitinationNQKKALKVEHTSRLK
CHHHCCCCHHHHHHH
7.29-
455PhosphorylationKALKVEHTSRLKAAF
HCCCCHHHHHHHHHH
11.3120068231
456PhosphorylationALKVEHTSRLKAAFV
CCCCHHHHHHHHHHH
37.2120068231
464SumoylationRLKAAFVKALQQEQE
HHHHHHHHHHHHHHH
36.6028112733
464UbiquitinationRLKAAFVKALQQEQE
HHHHHHHHHHHHHHH
36.6021890473
464 (in isoform 1)Ubiquitination-36.6021890473
464 (in isoform 2)Ubiquitination-36.6021890473
465UbiquitinationLKAAFVKALQQEQEI
HHHHHHHHHHHHHHH
12.8021890473
487SumoylationGTAPAQAKAEPTAAP
CCCCHHHCCCCCCCC
41.00-
487AcetylationGTAPAQAKAEPTAAP
CCCCHHHCCCCCCCC
41.0026051181
487SumoylationGTAPAQAKAEPTAAP
CCCCHHHCCCCCCCC
41.0028112733
487UbiquitinationGTAPAQAKAEPTAAP
CCCCHHHCCCCCCCC
41.00-
488UbiquitinationTAPAQAKAEPTAAPH
CCCHHHCCCCCCCCC
30.89-
491O-linked_GlycosylationAQAKAEPTAAPHPVL
HHHCCCCCCCCCHHH
27.27OGP
499UbiquitinationAAPHPVLKQVIKPRR
CCCCHHHHHHHCCCH
42.63-
500UbiquitinationAPHPVLKQVIKPRRK
CCCHHHHHHHCCCHH
37.70-
512PhosphorylationRRKLAFRSGEARDWS
CHHHCCCCCCCCCCC
34.2325159151
527PhosphorylationNGAVLQASSQLSRGS
CCCEEEECCHHCCCC
12.9818776048
528PhosphorylationGAVLQASSQLSRGSA
CCEEEECCHHCCCCC
37.85-
531PhosphorylationLQASSQLSRGSATTP
EEECCHHCCCCCCCC
27.2718776048
532MethylationQASSQLSRGSATTPR
EECCHHCCCCCCCCC
52.24-
534PhosphorylationSSQLSRGSATTPRGV
CCHHCCCCCCCCCCE
22.7221955146
537PhosphorylationLSRGSATTPRGVLHT
HCCCCCCCCCCEEEE
15.6518776048
539Asymmetric dimethylarginineRGSATTPRGVLHTFS
CCCCCCCCCEEEECC
45.84-
539MethylationRGSATTPRGVLHTFS
CCCCCCCCCEEEECC
45.8424129315
544PhosphorylationTPRGVLHTFSPSPKL
CCCCEEEECCCCHHH
22.9629255136
546PhosphorylationRGVLHTFSPSPKLQN
CCEEEECCCCHHHCC
26.1429255136
548PhosphorylationVLHTFSPSPKLQNSA
EEEECCCCHHHCCCH
33.2129255136
550SumoylationHTFSPSPKLQNSASA
EECCCCHHHCCCHHC
68.02-
550AcetylationHTFSPSPKLQNSASA
EECCCCHHHCCCHHC
68.0226051181
550MethylationHTFSPSPKLQNSASA
EECCCCHHHCCCHHC
68.02-
550SumoylationHTFSPSPKLQNSASA
EECCCCHHHCCCHHC
68.0228112733
550UbiquitinationHTFSPSPKLQNSASA
EECCCCHHHCCCHHC
68.02-
551UbiquitinationTFSPSPKLQNSASAT
ECCCCHHHCCCHHCH
7.09-
554PhosphorylationPSPKLQNSASATALV
CCHHHCCCHHCHHHH
15.6125159151
556PhosphorylationPKLQNSASATALVSR
HHHCCCHHCHHHHCC
26.4430576142
558PhosphorylationLQNSASATALVSRTG
HCCCHHCHHHHCCCC
20.3023312004
568PhosphorylationVSRTGRHSERTVSAG
HCCCCCCCEEEEECC
27.6720068231
571PhosphorylationTGRHSERTVSAGKGS
CCCCCEEEEECCCCC
18.1120068231
573PhosphorylationRHSERTVSAGKGSAT
CCCEEEEECCCCCCC
30.5920068231
576SumoylationERTVSAGKGSATSNW
EEEEECCCCCCCCCC
49.78-
576AcetylationERTVSAGKGSATSNW
EEEEECCCCCCCCCC
49.7826051181
576SumoylationERTVSAGKGSATSNW
EEEEECCCCCCCCCC
49.78-
576UbiquitinationERTVSAGKGSATSNW
EEEEECCCCCCCCCC
49.78-
577UbiquitinationRTVSAGKGSATSNWK
EEEECCCCCCCCCCE
22.92-
578PhosphorylationTVSAGKGSATSNWKK
EEECCCCCCCCCCEE
31.6820068231
580PhosphorylationSAGKGSATSNWKKTP
ECCCCCCCCCCEECC
25.0420068231
581PhosphorylationAGKGSATSNWKKTPL
CCCCCCCCCCEECCC
40.1720068231
585SumoylationSATSNWKKTPLSTGG
CCCCCCEECCCCCCC
47.1728112733
586O-linked_GlycosylationATSNWKKTPLSTGGT
CCCCCEECCCCCCCE
26.2430059200
586PhosphorylationATSNWKKTPLSTGGT
CCCCCEECCCCCCCE
26.2424732914
589O-linked_GlycosylationNWKKTPLSTGGTLAF
CCEECCCCCCCEEEE
26.6430059200
589PhosphorylationNWKKTPLSTGGTLAF
CCEECCCCCCCEEEE
26.6424732914
590O-linked_GlycosylationWKKTPLSTGGTLAFV
CEECCCCCCCEEEEE
47.5230059200
590PhosphorylationWKKTPLSTGGTLAFV
CEECCCCCCCEEEEE
47.5224732914
593O-linked_GlycosylationTPLSTGGTLAFVSPS
CCCCCCCEEEEECHH
19.0930059200
593PhosphorylationTPLSTGGTLAFVSPS
CCCCCCCEEEEECHH
19.0924732914
598PhosphorylationGGTLAFVSPSLAVHK
CCEEEEECHHHCCCC
11.4325159151
600PhosphorylationTLAFVSPSLAVHKSS
EEEEECHHHCCCCCC
22.8125159151
605SumoylationSPSLAVHKSSSAVDR
CHHHCCCCCCCCHHH
45.4928112733
625O-linked_GlycosylationLDMIPPRSIPQSATW
HHHCCCCCCCCCCCC
44.3830059200
629PhosphorylationPPRSIPQSATWK---
CCCCCCCCCCCC---
23.4724719451
633MethylationIPQSATWK-------
CCCCCCCC-------
46.21-

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 P66A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P66A_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 P66A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP4_HUMANRBBP4physical
22939629
RBBP7_HUMANRBBP7physical
22939629
K1C40_HUMANKRT40physical
25416956
CHD3_HUMANCHD3physical
26344197
MBD2_HUMANMBD2physical
26344197
MBD3_HUMANMBD3physical
26344197
MTA1_HUMANMTA1physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
CHD5_HUMANCHD5physical
28514442
HDAC1_HUMANHDAC1physical
28514442
CHD3_HUMANCHD3physical
28514442
PKCB1_HUMANZMYND8physical
28514442
ZN592_HUMANZNF592physical
28514442
MBD2_HUMANMBD2physical
28514442
MTA3_HUMANMTA3physical
28514442
ZN687_HUMANZNF687physical
28514442
CHD4_HUMANCHD4physical
28514442
MBD3_HUMANMBD3physical
28514442
MTA1_HUMANMTA1physical
28514442
MTA2_HUMANMTA2physical
28514442
CDKA1_HUMANCDK2AP1physical
28514442
APBP2_HUMANAPPBP2physical
28514442
RBBP4_HUMANRBBP4physical
28514442

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 P66A_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 THR-49; SER-100; SER-107;SER-114; THR-189 AND SER-340, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-107; SER-114AND SER-340, 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 THR-49; SER-100; SER-107;SER-114; SER-340; SER-546; SER-548 AND SER-598, 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-49; SER-100; SER-107;SER-113 AND SER-114, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-598, ANDMASS 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-100; SER-107 ANDSER-114, 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 THR-189, AND MASSSPECTROMETRY.

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