CD11A_HUMAN - dbPTM
CD11A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD11A_HUMAN
UniProt AC Q9UQ88
Protein Name Cyclin-dependent kinase 11A
Gene Name CDK11A
Organism Homo sapiens (Human).
Sequence Length 783
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression..
Protein Sequence MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHCMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKVHHRKDEKRKEKWKHARVKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEETGSNSEEASEQSAEEVSEEEMSEDEERENENHLLVVPESRFDRDSGESEEAEEEVGEGTPQSSALTEGDYVPDSPALLPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTQWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGNSEIDQINKVFKELGTPSEKIWPGYSELPVVKKMTFSEHPYNNLRKRFGALLSDQGFDLMNKFLTYFPGRRISAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF
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
8 (in isoform 5)Phosphorylation-21.4220068231
8 (in isoform 9)Phosphorylation-21.4229116813
9 (in isoform 5)Phosphorylation-37.4920068231
10 (in isoform 5)Phosphorylation-4.6920068231
10 (in isoform 9)Phosphorylation-4.6929116813
11SumoylationEKDSWKVKTLDEILQ
HHHHHHHCCHHHHHH
39.38-
11SumoylationEKDSWKVKTLDEILQ
HHHHHHHCCHHHHHH
39.38-
11UbiquitinationEKDSWKVKTLDEILQ
HHHHHHHCCHHHHHH
39.38-
12PhosphorylationKDSWKVKTLDEILQE
HHHHHHCCHHHHHHH
42.2921815630
15 (in isoform 5)Phosphorylation-49.0320068231
15 (in isoform 9)Phosphorylation-49.0325159151
18 (in isoform 5)Phosphorylation-67.1520068231
19 (in isoform 5)Phosphorylation-58.0420068231
20SumoylationLDEILQEKKRRKEQE
HHHHHHHHHHHHHHH
38.32-
20SumoylationLDEILQEKKRRKEQE
HHHHHHHHHHHHHHH
38.32-
20UbiquitinationLDEILQEKKRRKEQE
HHHHHHHHHHHHHHH
38.32-
20 (in isoform 1)Ubiquitination-38.3221906983
20 (in isoform 10)Ubiquitination-38.3221906983
20 (in isoform 2)Ubiquitination-38.3221906983
20 (in isoform 3)Ubiquitination-38.3221906983
20 (in isoform 4)Ubiquitination-38.3221906983
29SumoylationRRKEQEEKAEIKRLK
HHHHHHHHHHHHHHH
51.04-
29SumoylationRRKEQEEKAEIKRLK
HHHHHHHHHHHHHHH
51.04-
38PhosphorylationEIKRLKNSDDRDSKR
HHHHHHCCCCCHHHH
39.0220068231
43PhosphorylationKNSDDRDSKRDSLEE
HCCCCCHHHHHHHHH
30.4030108239
47PhosphorylationDRDSKRDSLEEGELR
CCHHHHHHHHHHHHH
41.5329255136
61PhosphorylationRDHCMEITIRNSPYR
HHHHEEEEECCCCCC
10.6923927012
65PhosphorylationMEITIRNSPYRREDS
EEEEECCCCCCCCCC
17.2922167270
67PhosphorylationITIRNSPYRREDSME
EEECCCCCCCCCCCC
23.3223927012
69 (in isoform 5)Ubiquitination-46.3521906983
72O-linked_GlycosylationSPYRREDSMEDRGEE
CCCCCCCCCCCCCCC
21.2230379171
72PhosphorylationSPYRREDSMEDRGEE
CCCCCCCCCCCCCCC
21.2229255136
82PhosphorylationDRGEEDDSLAIKPPQ
CCCCCCCCCCCCCHH
31.8323403867
91 (in isoform 8)Ubiquitination-3.3521906983
92PhosphorylationIKPPQQMSRKEKVHH
CCCHHHCCCHHHCCC
35.5423403867
101AcetylationKEKVHHRKDEKRKEK
HHHCCCHHHHHHHHH
66.9230585411
113 (in isoform 8)Ubiquitination-39.5021906983
123AcetylationEREHERRKRHREEQD
HHHHHHHHHHHHHHH
59.7922368469
179 (in isoform 5)Ubiquitination-55.9121906983
200PhosphorylationREARREVSAHHRTMR
HHHHHHHHHHHHHHC
19.6818212344
204 (in isoform 9)Phosphorylation-21.9825849741
210PhosphorylationHRTMREDYSDKVKAS
HHHHCHHCCHHHHHH
17.6426074081
211PhosphorylationRTMREDYSDKVKASH
HHHCHHCCHHHHHHH
43.1920068231
2132-HydroxyisobutyrylationMREDYSDKVKASHWS
HCHHCCHHHHHHHCC
39.43-
213AcetylationMREDYSDKVKASHWS
HCHHCCHHHHHHHCC
39.43-
217PhosphorylationYSDKVKASHWSRSPP
CCHHHHHHHCCCCCC
21.5528348404
220PhosphorylationKVKASHWSRSPPRPP
HHHHHHCCCCCCCCC
19.9123401153
222PhosphorylationKASHWSRSPPRPPRE
HHHHCCCCCCCCCHH
33.4723401153
252 (in isoform 4)Phosphorylation-62.6925849741
254SumoylationAQKPAQLKEEKMEER
CCCCHHHHHHHHHHH
52.31-
254SumoylationAQKPAQLKEEKMEER
CCCCHHHHHHHHHHH
52.31-
261 (in isoform 3)Phosphorylation-26.9425849741
262 (in isoform 2)Phosphorylation-56.0625849741
262 (in isoform 5)Ubiquitination-56.0621906983
265PhosphorylationMEERDLLSDLQDISD
HHHHHHHHHHHHCCH
43.5025463755
271PhosphorylationLSDLQDISDSERKTS
HHHHHHCCHHHHCCC
43.2919664994
273PhosphorylationDLQDISDSERKTSSA
HHHHCCHHHHCCCCC
32.2929255136
283PhosphorylationKTSSAESSSAESGSG
CCCCCCCCCCCCCCC
25.6920068231
308PhosphorylationEEEEGSTSEESEEEE
HHHCCCCCHHHHHHH
40.8520068231
321 (in isoform 5)Ubiquitination-74.1821906983
325PhosphorylationEEEEEEETGSNSEEA
HHHHHHHHCCCCHHH
49.5418452278
343 (in isoform 5)Ubiquitination-52.0421906983
346PhosphorylationEVSEEEMSEDEEREN
HHCHHHHCHHHHHHH
45.2130177828
363PhosphorylationHLLVVPESRFDRDSG
CEEEEEHHHCCCCCC
31.9818669648
369PhosphorylationESRFDRDSGESEEAE
HHHCCCCCCCCHHHH
45.4125849741
372PhosphorylationFDRDSGESEEAEEEV
CCCCCCCCHHHHHHH
44.2418669648
383PhosphorylationEEEVGEGTPQSSALT
HHHHCCCCCCCCCCC
17.5318669648
386PhosphorylationVGEGTPQSSALTEGD
HCCCCCCCCCCCCCC
20.8426074081
387PhosphorylationGEGTPQSSALTEGDY
CCCCCCCCCCCCCCC
23.2726074081
390PhosphorylationTPQSSALTEGDYVPD
CCCCCCCCCCCCCCC
37.3226074081
391 (in isoform 9)Ubiquitination-51.4121906983
394PhosphorylationSALTEGDYVPDSPAL
CCCCCCCCCCCCCCC
25.4126074081
398PhosphorylationEGDYVPDSPALLPIE
CCCCCCCCCCCCCCC
13.1526074081
407SumoylationALLPIELKQELPKYL
CCCCCCHHHHHHHHH
29.01-
412UbiquitinationELKQELPKYLPALQG
CHHHHHHHHHHHHCC
72.54-
422PhosphorylationPALQGCRSVEEFQCL
HHHCCCCCHHHHHHH
37.6523401153
436PhosphorylationLNRIEEGTYGVVYRA
HHCCCCCCCEEEEEE
22.0020860994
437PhosphorylationNRIEEGTYGVVYRAK
HCCCCCCCEEEEEEC
20.8422322096
439 (in isoform 4)Ubiquitination-2.1121906983
441PhosphorylationEGTYGVVYRAKDKKT
CCCCEEEEEECCCCC
11.4917360941
442 (in isoform 10)Ubiquitination-24.4521906983
444AcetylationYGVVYRAKDKKTDEI
CEEEEEECCCCCCHH
62.1711002155
446AcetylationVVYRAKDKKTDEIVA
EEEEECCCCCCHHHH
57.7911002163
447SumoylationVYRAKDKKTDEIVAL
EEEECCCCCCHHHHH
71.93-
447AcetylationVYRAKDKKTDEIVAL
EEEECCCCCCHHHHH
71.9311002171
447SumoylationVYRAKDKKTDEIVAL
EEEECCCCCCHHHHH
71.93-
447UbiquitinationVYRAKDKKTDEIVAL
EEEECCCCCCHHHHH
71.93-
448 (in isoform 3)Ubiquitination-44.6021906983
449 (in isoform 2)Ubiquitination-53.1321906983
452 (in isoform 1)Ubiquitination-4.8621906983
455SumoylationTDEIVALKRLKMEKE
CCHHHHHHHHHCHHH
46.04-
4552-HydroxyisobutyrylationTDEIVALKRLKMEKE
CCHHHHHHHHHCHHH
46.04-
455AcetylationTDEIVALKRLKMEKE
CCHHHHHHHHHCHHH
46.047214019
455SumoylationTDEIVALKRLKMEKE
CCHHHHHHHHHCHHH
46.04-
455UbiquitinationTDEIVALKRLKMEKE
CCHHHHHHHHHCHHH
46.0421906983
463UbiquitinationRLKMEKEKEGFPITS
HHHCHHHHCCCCCCC
74.36-
470PhosphorylationKEGFPITSLREINTI
HCCCCCCCHHHHHHH
26.5816327805
476PhosphorylationTSLREINTILKAQHP
CCHHHHHHHHHCCCC
33.0916327805
479SumoylationREINTILKAQHPNIV
HHHHHHHHCCCCCEE
41.99-
479SumoylationREINTILKAQHPNIV
HHHHHHHHCCCCCEE
41.99-
479UbiquitinationREINTILKAQHPNIV
HHHHHHHHCCCCCEE
41.99-
501PhosphorylationGSNMDKIYIVMNYVE
CCCCCEEEEEEHHHH
8.0020068231
506PhosphorylationKIYIVMNYVEHDLKS
EEEEEEHHHHHHHHH
6.7920068231
513PhosphorylationYVEHDLKSLMETMKQ
HHHHHHHHHHHHHHC
40.0020068231
517PhosphorylationDLKSLMETMKQPFLP
HHHHHHHHHHCCCCC
18.7220068231
519UbiquitinationKSLMETMKQPFLPGE
HHHHHHHHCCCCCHH
63.34-
529PhosphorylationFLPGEVKTLMIQLLR
CCCHHHHHHHHHHHH
27.0820068231
539UbiquitinationIQLLRGVKHLHDNWI
HHHHHCCCCHHHCEE
43.18-
549 (in isoform 4)Ubiquitination-47.7321906983
552SumoylationWILHRDLKTSNLLLS
EECCCCHHHHCCCHH
54.95-
552SumoylationWILHRDLKTSNLLLS
EECCCCHHHHCCCHH
54.95-
552UbiquitinationWILHRDLKTSNLLLS
EECCCCHHHHCCCHH
54.95-
552 (in isoform 10)Ubiquitination-54.9521906983
558 (in isoform 3)Ubiquitination-3.8821906983
559 (in isoform 2)Ubiquitination-15.9721906983
562 (in isoform 1)Ubiquitination-21.9721906983
565UbiquitinationLSHAGILKVGDFGLA
HHHCCEEEECCCCHH
42.1021906983
574PhosphorylationGDFGLAREYGSPLKA
CCCCHHHHHCCCCCC
48.9518669648
575PhosphorylationDFGLAREYGSPLKAY
CCCHHHHHCCCCCCC
19.8322617229
577PhosphorylationGLAREYGSPLKAYTP
CHHHHHCCCCCCCCC
26.5922167270
579PhosphorylationAREYGSPLKAYTPVV
HHHHCCCCCCCCCEE
5.4818669648
580PhosphorylationREYGSPLKAYTPVVV
HHHCCCCCCCCCEEE
42.6118669648
582PhosphorylationYGSPLKAYTPVVVTQ
HCCCCCCCCCEEEEE
15.2530266825
583PhosphorylationGSPLKAYTPVVVTQW
CCCCCCCCCEEEEEE
17.9223927012
588PhosphorylationAYTPVVVTQWYRAPE
CCCCEEEEEEEECHH
11.1930266825
591PhosphorylationPVVVTQWYRAPELLL
CEEEEEEEECHHHHH
6.2530266825
603PhosphorylationLLLGAKEYSTAVDMW
HHHCCCCCCCHHHHH
15.6020860994
604PhosphorylationLLGAKEYSTAVDMWS
HHCCCCCCCHHHHHH
15.8120860994
611PhosphorylationSTAVDMWSVGCIFGE
CCHHHHHHHHHHHHH
11.2920860994
630PhosphorylationKPLFPGNSEIDQINK
CCCCCCCCHHHHHHH
41.6725599653
632 (in isoform 4)Ubiquitination-4.7921906983
635 (in isoform 10)Ubiquitination-4.8321906983
637SumoylationSEIDQINKVFKELGT
CHHHHHHHHHHHHCC
51.15-
637SumoylationSEIDQINKVFKELGT
CHHHHHHHHHHHHCC
51.15-
637UbiquitinationSEIDQINKVFKELGT
CHHHHHHHHHHHHCC
51.15-
640UbiquitinationDQINKVFKELGTPSE
HHHHHHHHHHCCCHH
55.83-
641 (in isoform 3)Ubiquitination-40.7521906983
642 (in isoform 2)Ubiquitination-10.7621906983
644PhosphorylationKVFKELGTPSEKIWP
HHHHHHCCCHHHCCC
35.9429116813
645 (in isoform 1)Ubiquitination-38.4021906983
646PhosphorylationFKELGTPSEKIWPGY
HHHHCCCHHHCCCCC
51.8929116813
648UbiquitinationELGTPSEKIWPGYSE
HHCCCHHHCCCCCCC
55.1721906983
653PhosphorylationSEKIWPGYSELPVVK
HHHCCCCCCCCCEEE
8.5629116813
654PhosphorylationEKIWPGYSELPVVKK
HHCCCCCCCCCEEEE
38.2729116813
660UbiquitinationYSELPVVKKMTFSEH
CCCCCEEEECCCCCC
36.74-
661SumoylationSELPVVKKMTFSEHP
CCCCEEEECCCCCCC
31.40-
661SumoylationSELPVVKKMTFSEHP
CCCCEEEECCCCCCC
31.40-
661UbiquitinationSELPVVKKMTFSEHP
CCCCEEEECCCCCCC
31.40-
663PhosphorylationLPVVKKMTFSEHPYN
CCEEEECCCCCCCCC
32.6528270605
665PhosphorylationVVKKMTFSEHPYNNL
EEEECCCCCCCCCHH
26.3228270605
669PhosphorylationMTFSEHPYNNLRKRF
CCCCCCCCCHHHHHH
20.7028270605
691 (in isoform 4)Ubiquitination-5.3821906983
694 (in isoform 10)Ubiquitination-15.2121906983
700 (in isoform 3)Ubiquitination-4.3921906983
701PhosphorylationYFPGRRISAEDGLKH
HCCCCCCCCCCCCCC
24.6430108239
701 (in isoform 2)Ubiquitination-24.6421906983
704 (in isoform 1)Ubiquitination-68.4021906983
707SumoylationISAEDGLKHEYFRET
CCCCCCCCCHHHCCC
39.66-
707SumoylationISAEDGLKHEYFRET
CCCCCCCCCHHHCCC
39.66-
707UbiquitinationISAEDGLKHEYFRET
CCCCCCCCCHHHCCC
39.6621906983
713 (in isoform 4)Ubiquitination-44.9021906983
714PhosphorylationKHEYFRETPLPIDPS
CCHHHCCCCCCCCHH
26.3524247654
716 (in isoform 10)Ubiquitination-8.2921906983
722 (in isoform 3)Ubiquitination-5.9221906983
723 (in isoform 2)Ubiquitination-5.9821906983
726 (in isoform 1)Ubiquitination-7.3521906983
729SumoylationMFPTWPAKSEQQRVK
HCCCCCCCCHHHHHH
50.90-
729SumoylationMFPTWPAKSEQQRVK
HCCCCCCCCHHHHHH
50.90-
729UbiquitinationMFPTWPAKSEQQRVK
HCCCCCCCCHHHHHH
50.902190698
736PhosphorylationKSEQQRVKRGTSPRP
CCHHHHHHCCCCCCC
47.5018669648
737PhosphorylationSEQQRVKRGTSPRPP
CHHHHHHCCCCCCCC
51.2518669648
739PhosphorylationQQRVKRGTSPRPPEG
HHHHHCCCCCCCCCC
39.3229255136
740PhosphorylationQRVKRGTSPRPPEGG
HHHHCCCCCCCCCCC
23.0329255136
750PhosphorylationPPEGGLGYSQLGDDD
CCCCCCCCHHCCCCC
9.7830266825
751PhosphorylationPEGGLGYSQLGDDDL
CCCCCCCHHCCCCCH
19.6829255136
758PhosphorylationSQLGDDDLKETGFHL
HHCCCCCHHHHCEEE
7.5018669648
761PhosphorylationGDDDLKETGFHLTTT
CCCCHHHHCEEEEEC
43.4921082442
763PhosphorylationDDLKETGFHLTTTNQ
CCHHHHCEEEEECCC
5.8018669648
766PhosphorylationKETGFHLTTTNQGAS
HHHCEEEEECCCCCC
24.0118669648
767PhosphorylationETGFHLTTTNQGASA
HHCEEEEECCCCCCC
30.0627174698
768PhosphorylationTGFHLTTTNQGASAA
HCEEEEECCCCCCCC
21.9527174698
773PhosphorylationTTTNQGASAAGPGFS
EECCCCCCCCCCCCC
26.0225849741
780PhosphorylationSAAGPGFSLKF----
CCCCCCCCCCC----
36.2425159151
782SumoylationAGPGFSLKF------
CCCCCCCCC------
48.07-
782MethylationAGPGFSLKF------
CCCCCCCCC------
48.07-
782SumoylationAGPGFSLKF------
CCCCCCCCC------
48.07-
782UbiquitinationAGPGFSLKF------
CCCCCCCCC------
48.07-

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
470SPhosphorylationKinaseCDK7P50613
Uniprot
476TPhosphorylationKinaseCDK7P50613
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD11A_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 CD11A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNL2_HUMANCCNL2physical
14623875
CCNL1_HUMANCCNL1physical
14623875
PAK1_HUMANPAK1physical
12624090
B4GT1_HUMANB4GALT1physical
11506180
GA45A_HUMANGADD45Aphysical
21988832
CSK21_HUMANCSNK2A1physical
23602568
CSK22_HUMANCSNK2A2physical
23602568
CSK2B_HUMANCSNK2Bphysical
23602568
PR40A_HUMANPRPF40Aphysical
23602568
RBM25_HUMANRBM25physical
23602568
PSMD1_HUMANPSMD1physical
23602568
IMA1_HUMANKPNA2physical
23602568
CR025_HUMANC18orf25physical
23602568
A2MG_HUMANA2Mphysical
23602568
IMB1_HUMANKPNB1physical
23602568
HKR1_HUMANHKR1physical
23602568
ZN267_HUMANZNF267physical
23602568
ZN460_HUMANZNF460physical
23602568
ZN510_HUMANZNF510physical
23602568
ZFP14_HUMANZFP14physical
23602568
ZN33A_HUMANZNF33Aphysical
23602568
CDN2A_HUMANCDKN2Aphysical
23602568
ARF_HUMANCDKN2Aphysical
23602568
NOP58_HUMANNOP58physical
23602568
WDR47_HUMANWDR47physical
26186194
DDB2_HUMANDDB2physical
26186194
CD11B_HUMANCDK11Bphysical
26186194
ZG16B_HUMANZG16Bphysical
26186194
CL043_HUMANC12orf43physical
26186194
SPRR3_HUMANSPRR3physical
26186194
CRNN_HUMANCRNNphysical
26186194
AP3B1_HUMANAP3B1physical
26344197
CTR9_HUMANCTR9physical
26344197
REQU_HUMANDPF2physical
26344197
LEO1_HUMANLEO1physical
26344197
NOLC1_HUMANNOLC1physical
26344197
PELP1_HUMANPELP1physical
26344197
S30BP_HUMANSAP30BPphysical
26344197
SP16H_HUMANSUPT16Hphysical
26344197
CCNL2_HUMANCCNL2physical
28514442
FKBP5_HUMANFKBP5physical
28514442
CDC37_HUMANCDC37physical
28514442
HS90A_HUMANHSP90AA1physical
28514442
HS90B_HUMANHSP90AB1physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPD_HUMANCCT4physical
28514442
UBP15_HUMANUSP15physical
27173435
JIP4_HUMANSPAG9physical
27173435
MCM2_HUMANMCM2physical
27173435
MCM4_HUMANMCM4physical
27173435
MCM6_HUMANMCM6physical
27173435
NS1BP_HUMANIVNS1ABPphysical
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 CD11A_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 TYR-575; SER-577 ANDTHR-583, 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-47; SER-271; SER-577;THR-583; THR-739; SER-740 AND THR-761, 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-271; THR-583; THR-739AND SER-740, 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-222; SER-271; THR-739AND SER-740, AND MASS SPECTROMETRY.
"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-583, AND MASSSPECTROMETRY.

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