GWL_HUMAN - dbPTM
GWL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GWL_HUMAN
UniProt AC Q96GX5
Protein Name Serine/threonine-protein kinase greatwall
Gene Name MASTL
Organism Homo sapiens (Human).
Sequence Length 879
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus . Cleavage furrow . During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. Upon mitotic exit
Protein Description Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation..
Protein Sequence MDPTAGSKKEPGGGAATEEGVNRIAVPKPPSIEEFSIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFNTPIAEKNQDPANILSACLSETSQLSQGLVCPMSVDQKDTTPYSSKLLKSCLETVASNPGMPVKCLTSNLLQSRKRLATSSASSQSHTFISSVESECHSSPKWEKDCQESDEALGPTMMSWNAVEKLCAKSANAIETKGFNKKDLELALSPIHNSSALPTTGRSCVNLAKKCFSGEVSWEAVELDVNNINMDTDTSQLGFHQSNQWAVDSGGISEEHLGKRSLKRNFELVDSSPCKKIIQNKKTCVEYKHNEMTNCYTNQNTGLTVEVQDLKLSVHKSQQNDCANKENIVNSFTDKQQTPEKLPIPMIAKNLMCELDEDCEKNSKRDYLSSSFLCSDDDRASKNISMNSDSSFPGISIMESPLESQPLDSDRSIKESSFEESNIEDPLIVTPDCQEKTSPKGVENPAVQESNQKMLGPPLEVLKTLASKRNAVAFRSFNSHINASNNSEPSRMNMTSLDAMDISCAYSGSYPMAITPTQKRRSCMPHQQTPNQIKSGTPYRTPKSVRRGVAPVDDGRILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVEILLTIDDTKRAGMKELKRHPLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNTAQHLTVSGFSL
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-------MDPTAGSK
-------CCCCCCCC
14.5522814378
8AcetylationMDPTAGSKKEPGGGA
CCCCCCCCCCCCCCC
61.3026051181
8UbiquitinationMDPTAGSKKEPGGGA
CCCCCCCCCCCCCCC
61.30-
9AcetylationDPTAGSKKEPGGGAA
CCCCCCCCCCCCCCC
71.4926051181
9UbiquitinationDPTAGSKKEPGGGAA
CCCCCCCCCCCCCCC
71.49-
17PhosphorylationEPGGGAATEEGVNRI
CCCCCCCCCCCCCCC
33.7522210691
18UbiquitinationPGGGAATEEGVNRIA
CCCCCCCCCCCCCCC
48.2932015554
28UbiquitinationVNRIAVPKPPSIEEF
CCCCCCCCCCCCHHC
64.0629967540
31PhosphorylationIAVPKPPSIEEFSIV
CCCCCCCCCHHCEEE
51.68-
39UbiquitinationIEEFSIVKPISRGAF
CHHCEEEEEECCCCC
34.6623000965
39 (in isoform 1)Ubiquitination-34.6621890473
39 (in isoform 2)Ubiquitination-34.6621890473
39 (in isoform 3)Ubiquitination-34.6621890473
48UbiquitinationISRGAFGKVYLGQKG
ECCCCCCEEEECCCC
22.6629967540
54UbiquitinationGKVYLGQKGGKLYAV
CEEEECCCCCEEEEE
68.7629967540
57AcetylationYLGQKGGKLYAVKVV
EECCCCCEEEEEEEE
47.1725953088
57UbiquitinationYLGQKGGKLYAVKVV
EECCCCCEEEEEEEE
47.1729967540
62UbiquitinationGGKLYAVKVVKKADM
CCEEEEEEEEEHHHH
32.8922817900
65UbiquitinationLYAVKVVKKADMINK
EEEEEEEEHHHHCCC
45.2722817900
66UbiquitinationYAVKVVKKADMINKN
EEEEEEEHHHHCCCC
37.7022817900
66 (in isoform 1)Ubiquitination-37.7021890473
66 (in isoform 2)Ubiquitination-37.7021890473
66 (in isoform 3)Ubiquitination-37.7021890473
72UbiquitinationKKADMINKNMTHQVQ
EHHHHCCCCCHHHHH
36.8529967540
75PhosphorylationDMINKNMTHQVQAER
HHCCCCCHHHHHHHH
20.67-
108UbiquitinationQSANNVYLVMEYLIG
CCCCCEEEEEEHHHC
2.2932015554
109UbiquitinationSANNVYLVMEYLIGG
CCCCEEEEEEHHHCC
1.1822817900
130UbiquitinationHIYGYFDEEMAVKYI
HHHCCCCHHHHHHHH
39.5121963094
150UbiquitinationALDYLHRHGIIHRDL
HHHHHHHCCCCCCCC
22.5122817900
158UbiquitinationGIIHRDLKPDNMLIS
CCCCCCCCCCCEEEC
55.4022817900
158 (in isoform 1)Ubiquitination-55.4021890473
158 (in isoform 2)Ubiquitination-55.4021890473
158 (in isoform 3)Ubiquitination-55.4021890473
173PhosphorylationNEGHIKLTDFGLSKV
CCCCEEECCCCCCEE
25.0422210691
178PhosphorylationKLTDFGLSKVTLNRD
EECCCCCCEEEECCC
26.0122210691
179UbiquitinationLTDFGLSKVTLNRDI
ECCCCCCEEEECCCC
44.2621906983
179 (in isoform 1)Ubiquitination-44.2621890473
179 (in isoform 2)Ubiquitination-44.2621890473
179 (in isoform 3)Ubiquitination-44.2621890473
181PhosphorylationDFGLSKVTLNRDINM
CCCCCEEEECCCCCC
23.2724260401
189UbiquitinationLNRDINMMDILTTPS
ECCCCCCHHHHCCCC
2.2132015554
193PhosphorylationINMMDILTTPSMAKP
CCCHHHHCCCCCCCC
36.6720068231
194PhosphorylationNMMDILTTPSMAKPR
CCHHHHCCCCCCCCC
15.2121712546
196PhosphorylationMDILTTPSMAKPRQD
HHHHCCCCCCCCCCC
29.3128122231
199UbiquitinationLTTPSMAKPRQDYSR
HCCCCCCCCCCCCCC
31.9022817900
199 (in isoform 1)Ubiquitination-31.9021890473
199 (in isoform 2)Ubiquitination-31.9021890473
199 (in isoform 3)Ubiquitination-31.9021890473
204PhosphorylationMAKPRQDYSRTPGQV
CCCCCCCCCCCHHHH
7.5422199227
205PhosphorylationAKPRQDYSRTPGQVL
CCCCCCCCCCHHHHH
37.6622199227
207PhosphorylationPRQDYSRTPGQVLSL
CCCCCCCCHHHHHHH
26.3225159151
213PhosphorylationRTPGQVLSLISSLGF
CCHHHHHHHHHHCCC
25.4622199227
216PhosphorylationGQVLSLISSLGFNTP
HHHHHHHHHCCCCCC
25.4622199227
217PhosphorylationQVLSLISSLGFNTPI
HHHHHHHHCCCCCCH
26.0522199227
222PhosphorylationISSLGFNTPIAEKNQ
HHHCCCCCCHHHHCC
17.5125159151
258SumoylationCPMSVDQKDTTPYSS
CCCCCCCCCCCCCCH
53.21-
260PhosphorylationMSVDQKDTTPYSSKL
CCCCCCCCCCCCHHH
36.3830576142
261PhosphorylationSVDQKDTTPYSSKLL
CCCCCCCCCCCHHHH
30.2929396449
263PhosphorylationDQKDTTPYSSKLLKS
CCCCCCCCCHHHHHH
24.3928985074
264PhosphorylationQKDTTPYSSKLLKSC
CCCCCCCCHHHHHHH
23.3821712546
265PhosphorylationKDTTPYSSKLLKSCL
CCCCCCCHHHHHHHH
22.83-
266AcetylationDTTPYSSKLLKSCLE
CCCCCCHHHHHHHHH
52.4725953088
266UbiquitinationDTTPYSSKLLKSCLE
CCCCCCHHHHHHHHH
52.4729967540
269MethylationPYSSKLLKSCLETVA
CCCHHHHHHHHHHHH
49.94115972827
269UbiquitinationPYSSKLLKSCLETVA
CCCHHHHHHHHHHHH
49.9432015554
270PhosphorylationYSSKLLKSCLETVAS
CCHHHHHHHHHHHHH
24.7321712546
274PhosphorylationLLKSCLETVASNPGM
HHHHHHHHHHHCCCC
14.3929214152
277PhosphorylationSCLETVASNPGMPVK
HHHHHHHHCCCCCHH
38.9421815630
284UbiquitinationSNPGMPVKCLTSNLL
HCCCCCHHHHHHHHH
20.0429967540
288PhosphorylationMPVKCLTSNLLQSRK
CCHHHHHHHHHHHHH
16.7221712546
292PhosphorylationCLTSNLLQSRKRLAT
HHHHHHHHHHHHHHH
44.3432645325
293PhosphorylationLTSNLLQSRKRLATS
HHHHHHHHHHHHHHC
39.4725159151
295UbiquitinationSNLLQSRKRLATSSA
HHHHHHHHHHHHCCC
57.9432015554
299PhosphorylationQSRKRLATSSASSQS
HHHHHHHHCCCCCCC
28.0123663014
300O-linked_GlycosylationSRKRLATSSASSQSH
HHHHHHHCCCCCCCC
20.4923301498
300PhosphorylationSRKRLATSSASSQSH
HHHHHHHCCCCCCCC
20.4923663014
301PhosphorylationRKRLATSSASSQSHT
HHHHHHCCCCCCCCE
28.0223663014
301UbiquitinationRKRLATSSASSQSHT
HHHHHHCCCCCCCCE
28.0230230243
303PhosphorylationRLATSSASSQSHTFI
HHHHCCCCCCCCEEH
30.7523663014
304PhosphorylationLATSSASSQSHTFIS
HHHCCCCCCCCEEHH
35.1023663014
306PhosphorylationTSSASSQSHTFISSV
HCCCCCCCCEEHHHH
26.8323663014
308PhosphorylationSASSQSHTFISSVES
CCCCCCCEEHHHHHH
28.1023663014
311PhosphorylationSQSHTFISSVESECH
CCCCEEHHHHHHHHH
24.9230108239
312PhosphorylationQSHTFISSVESECHS
CCCEEHHHHHHHHHC
25.7023663014
315PhosphorylationTFISSVESECHSSPK
EEHHHHHHHHHCCCC
43.2823663014
319PhosphorylationSVESECHSSPKWEKD
HHHHHHHCCCCCHHH
61.0525159151
320PhosphorylationVESECHSSPKWEKDC
HHHHHHCCCCCHHHH
13.5625159151
322UbiquitinationSECHSSPKWEKDCQE
HHHHCCCCCHHHHHH
70.6829967540
330PhosphorylationWEKDCQESDEALGPT
CHHHHHHCHHHHCCC
18.1825159151
331UbiquitinationEKDCQESDEALGPTM
HHHHHHCHHHHCCCH
44.4232015554
350UbiquitinationAVEKLCAKSANAIET
HHHHHHHHHCCCCCC
49.4532015554
355UbiquitinationCAKSANAIETKGFNK
HHHHCCCCCCCCCCH
7.4833845483
358UbiquitinationSANAIETKGFNKKDL
HCCCCCCCCCCHHHH
49.0329967540
362UbiquitinationIETKGFNKKDLELAL
CCCCCCCHHHHHHHC
45.46-
363UbiquitinationETKGFNKKDLELALS
CCCCCCHHHHHHHCC
69.5229967540
370PhosphorylationKDLELALSPIHNSSA
HHHHHHCCCCCCCCC
19.0529255136
375PhosphorylationALSPIHNSSALPTTG
HCCCCCCCCCCCCCC
11.6530278072
376PhosphorylationLSPIHNSSALPTTGR
CCCCCCCCCCCCCCC
38.8625159151
380PhosphorylationHNSSALPTTGRSCVN
CCCCCCCCCCCHHHH
42.6128176443
381PhosphorylationNSSALPTTGRSCVNL
CCCCCCCCCCHHHHH
28.7625159151
381UbiquitinationNSSALPTTGRSCVNL
CCCCCCCCCCHHHHH
28.7632015554
384PhosphorylationALPTTGRSCVNLAKK
CCCCCCCHHHHHHHH
24.6221712546
390UbiquitinationRSCVNLAKKCFSGEV
CHHHHHHHHHHCCCC
53.9229967540
442PhosphorylationEEHLGKRSLKRNFEL
HHHHCHHHHHHCCEE
41.55-
452PhosphorylationRNFELVDSSPCKKII
HCCEECCCCHHHHHH
28.8030266825
453PhosphorylationNFELVDSSPCKKIIQ
CCEECCCCHHHHHHC
29.8319664994
456AcetylationLVDSSPCKKIIQNKK
ECCCCHHHHHHCCCC
50.8425953088
456UbiquitinationLVDSSPCKKIIQNKK
ECCCCHHHHHHCCCC
50.8432015554
457UbiquitinationVDSSPCKKIIQNKKT
CCCCHHHHHHCCCCC
52.32-
462UbiquitinationCKKIIQNKKTCVEYK
HHHHHCCCCCEEEEE
32.8430230243
464PhosphorylationKIIQNKKTCVEYKHN
HHHCCCCCEEEEECC
24.3226074081
483UbiquitinationCYTNQNTGLTVEVQD
CEECCCCCCEEEEEE
27.2232015554
492UbiquitinationTVEVQDLKLSVHKSQ
EEEEEEEEEEEEHHH
47.1832015554
497UbiquitinationDLKLSVHKSQQNDCA
EEEEEEEHHHCCCCC
48.0529967540
498PhosphorylationLKLSVHKSQQNDCAN
EEEEEEHHHCCCCCC
23.3223312004
506UbiquitinationQQNDCANKENIVNSF
HCCCCCCCHHHHHHC
33.3429967540
512PhosphorylationNKENIVNSFTDKQQT
CCHHHHHHCCCCCCC
20.7329255136
514PhosphorylationENIVNSFTDKQQTPE
HHHHHHCCCCCCCCC
41.9529255136
516UbiquitinationIVNSFTDKQQTPEKL
HHHHCCCCCCCCCCC
41.0532015554
519PhosphorylationSFTDKQQTPEKLPIP
HCCCCCCCCCCCCCC
30.8125159151
542UbiquitinationELDEDCEKNSKRDYL
HCCHHHHHHCCCHHH
73.2332015554
548PhosphorylationEKNSKRDYLSSSFLC
HHHCCCHHHHHHCCC
16.7118691976
550PhosphorylationNSKRDYLSSSFLCSD
HCCCHHHHHHCCCCC
20.0829214152
551PhosphorylationSKRDYLSSSFLCSDD
CCCHHHHHHCCCCCC
23.6330576142
552PhosphorylationKRDYLSSSFLCSDDD
CCHHHHHHCCCCCCC
20.8925159151
556PhosphorylationLSSSFLCSDDDRASK
HHHHCCCCCCCHHCC
46.3425159151
566PhosphorylationDRASKNISMNSDSSF
CHHCCCCCCCCCCCC
22.7028674151
569PhosphorylationSKNISMNSDSSFPGI
CCCCCCCCCCCCCCC
30.1723532336
571PhosphorylationNISMNSDSSFPGISI
CCCCCCCCCCCCCEE
33.4328674151
572PhosphorylationISMNSDSSFPGISIM
CCCCCCCCCCCCEEE
40.2128674151
577PhosphorylationDSSFPGISIMESPLE
CCCCCCCEEECCCCC
23.0724719451
581PhosphorylationPGISIMESPLESQPL
CCCEEECCCCCCCCC
19.8729523821
585PhosphorylationIMESPLESQPLDSDR
EECCCCCCCCCCCCC
44.7929523821
590PhosphorylationLESQPLDSDRSIKES
CCCCCCCCCCCCCHH
42.4829523821
593PhosphorylationQPLDSDRSIKESSFE
CCCCCCCCCCHHHCC
42.9023186163
597PhosphorylationSDRSIKESSFEESNI
CCCCCCHHHCCCCCC
35.0130266825
598PhosphorylationDRSIKESSFEESNIE
CCCCCHHHCCCCCCC
37.4630266825
602PhosphorylationKESSFEESNIEDPLI
CHHHCCCCCCCCCEE
35.5928464451
611PhosphorylationIEDPLIVTPDCQEKT
CCCCEEECCCCCCCC
13.3530266825
618PhosphorylationTPDCQEKTSPKGVEN
CCCCCCCCCCCCCCC
49.8930266825
619PhosphorylationPDCQEKTSPKGVENP
CCCCCCCCCCCCCCH
35.3630266825
621UbiquitinationCQEKTSPKGVENPAV
CCCCCCCCCCCCHHH
75.3029967540
631PhosphorylationENPAVQESNQKMLGP
CCHHHHHHHHHHHCC
27.7225159151
634UbiquitinationAVQESNQKMLGPPLE
HHHHHHHHHHCCCHH
40.1029967540
644AcetylationGPPLEVLKTLASKRN
CCCHHHHHHHHHHCC
46.8218604563
644UbiquitinationGPPLEVLKTLASKRN
CCCHHHHHHHHHHCC
46.8232015554
657PhosphorylationRNAVAFRSFNSHINA
CCCEEEEHHHHCCCC
23.4825159151
660PhosphorylationVAFRSFNSHINASNN
EEEEHHHHCCCCCCC
24.5920068231
665PhosphorylationFNSHINASNNSEPSR
HHHCCCCCCCCCCCC
31.8625159151
668PhosphorylationHINASNNSEPSRMNM
CCCCCCCCCCCCCCC
55.9525159151
671PhosphorylationASNNSEPSRMNMTSL
CCCCCCCCCCCCCHH
39.8622199227
676PhosphorylationEPSRMNMTSLDAMDI
CCCCCCCCHHHHHCH
22.5728348404
677PhosphorylationPSRMNMTSLDAMDIS
CCCCCCCHHHHHCHH
17.3028348404
696PhosphorylationGSYPMAITPTQKRRS
CCCCCEECCCCCCCC
15.6724719451
703 (in isoform 2)Phosphorylation-20.85-
703 (in isoform 3)Phosphorylation-20.85-
709 (in isoform 2)Phosphorylation-56.7625159151
709 (in isoform 3)Phosphorylation-56.7625159151
710PhosphorylationSCMPHQQTPNQIKSG
CCCCCCCCCCCCCCC
20.0325159151
714UbiquitinationHQQTPNQIKSGTPYR
CCCCCCCCCCCCCCC
4.9529967540
715UbiquitinationQQTPNQIKSGTPYRT
CCCCCCCCCCCCCCC
32.8229967540
716PhosphorylationQTPNQIKSGTPYRTP
CCCCCCCCCCCCCCC
49.9121712546
717 (in isoform 2)Phosphorylation-26.2125159151
717 (in isoform 3)Phosphorylation-26.2125159151
718PhosphorylationPNQIKSGTPYRTPKS
CCCCCCCCCCCCCCH
25.0025159151
720PhosphorylationQIKSGTPYRTPKSVR
CCCCCCCCCCCCHHH
27.2718669648
721 (in isoform 2)Phosphorylation-45.8425159151
721 (in isoform 3)Phosphorylation-45.8425159151
722PhosphorylationKSGTPYRTPKSVRRG
CCCCCCCCCCHHHCC
29.2618669648
725PhosphorylationTPYRTPKSVRRGVAP
CCCCCCCHHHCCCCC
23.2718669648
741PhosphorylationDDGRILGTPDYLAPE
CCCCCCCCCCCCCHH
15.0022199227
860PhosphorylationQPDDETDTSYFEARN
CCCCCCCCCHHHHCH
32.52-
868PhosphorylationSYFEARNTAQHLTVS
CHHHHCHHCCCEEEE
23.34-
873PhosphorylationRNTAQHLTVSGFSL-
CHHCCCEEEECCCC-
15.5329396449
875PhosphorylationTAQHLTVSGFSL---
HCCCEEEECCCC---
28.9625159151
878PhosphorylationHLTVSGFSL------
CEEEECCCC------
36.3725159151

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
75TPhosphorylationKinasePLK1P70032
PSP
194TPhosphorylationKinaseCDK1P06493
PSP
194TPhosphorylationKinaseCDK2P24941
PSP
299TPhosphorylationKinaseAKT1P31749
PSP
512SPhosphorylationKinasePLK1P70032
PSP
552SPhosphorylationKinasePLK1P70032
PSP
597SPhosphorylationKinasePLK1P70032
PSP
598SPhosphorylationKinasePLK1P70032
PSP
860TPhosphorylationKinasePLK1P70032
PSP
873TPhosphorylationKinasePLK1P70032
PSP
875SPhosphorylationKinaseCDK1P06493
PSP
875SPhosphorylationKinasePLK1P70032
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
741TPhosphorylation

18669648

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 GWL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IGO1_YEASTIGO1physical
23861665
CDK18_HUMANCDK18physical
26496610
AAAT_HUMANSLC1A5physical
26496610
SSFA2_HUMANSSFA2physical
26496610
TAP2_HUMANTAP2physical
26496610
MED26_HUMANMED26physical
26496610
TELO2_HUMANTELO2physical
26496610
UBN1_HUMANUBN1physical
26496610
DERL2_HUMANDERL2physical
26496610
RM02_HUMANMRPL2physical
26496610
E41L5_HUMANEPB41L5physical
26496610
FAKD5_HUMANFASTKD5physical
26496610
CEP85_HUMANCEP85physical
26496610
PKHA8_HUMANPLEKHA8physical
26496610
TM263_HUMANTMEM263physical
26496610
ACBD5_HUMANACBD5physical
26496610

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188000Thrombocytopenia 2 (THC2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GWL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-452, ANDMASS 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-293; SER-370; SER-452;SER-453; SER-552; SER-556; SER-631; TYR-720; THR-722; SER-725;THR-741; SER-875 AND SER-878, 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-370; SER-512; SER-552;SER-657; SER-665; SER-668; SER-875 AND SER-878, 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-370, 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-631, AND MASSSPECTROMETRY.
"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-631, AND MASSSPECTROMETRY.

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