KIF4A_HUMAN - dbPTM
KIF4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF4A_HUMAN
UniProt AC O95239
Protein Name Chromosome-associated kinesin KIF4A
Gene Name KIF4A
Organism Homo sapiens (Human).
Sequence Length 1232
Subcellular Localization Nucleus matrix. Cytoplasm, cytoskeleton, spindle. Midbody. Chromosome. Not present in the nucleolus. In early mitosis, associated with the mitotic spindle, in anaphase, localized to the spindle midzone and, in telophase and cytokinesis, to the midbod
Protein Description Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization..
Protein Sequence MKEEVKGIPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVNIDPQTAELNHLKQQVQQLQVLLLQAHGGTLPGSITVEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEKFLEQSMDIEDLKYCSEHSVNEHEDGDGDDDEGDDEEWKPTKLVKVSRKNIQGCSCKGWCGNKQCGCRKQKSDCGVDCCCDPTKCRNRQQGKDSLGTVERTQDSEGSFKLEDPTEVTPGLSFFNPVCATPNSKILKEMCDVEQVLSKKTPPAPSPFDLPELKHVATEYQENKAPGKKKKRALASNTSFFSGCSPIEEEAH
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
78AcetylationPLIKGVFKGYNATVL
HHHHHHHCCCCEEEE
59.0726051181
129UbiquitinationLFKEIDKKSDFEFTL
HHHHHCCCCCCEEEE
52.05-
158UbiquitinationLLCPSREKAQINIRE
HHCCCHHHHCCCCCC
44.47-
172UbiquitinationEDPKEGIKIVGLTEK
CCCCCCEEEEECCCC
42.04-
180PhosphorylationIVGLTEKTVLVALDT
EEECCCCEEEEEEEH
16.9130377224
187PhosphorylationTVLVALDTVSCLEQG
EEEEEEEHHHHHHCC
18.3730377224
189PhosphorylationLVALDTVSCLEQGNN
EEEEEHHHHHHCCCC
18.3130377224
197PhosphorylationCLEQGNNSRTVASTA
HHHCCCCCHHHHHHH
33.0730377224
199PhosphorylationEQGNNSRTVASTAMN
HCCCCCHHHHHHHCC
21.9030377224
203PhosphorylationNSRTVASTAMNSQSS
CCHHHHHHHCCCCCC
21.86-
207PhosphorylationVASTAMNSQSSRSHA
HHHHHCCCCCCCCEE
20.5327732954
209PhosphorylationSTAMNSQSSRSHAIF
HHHCCCCCCCCEEEE
27.7827732954
210PhosphorylationTAMNSQSSRSHAIFT
HHCCCCCCCCEEEEE
30.1127732954
234PhosphorylationDKNSSFRSKLHLVDL
CCCCCHHHHHHHHHH
37.2424719451
235UbiquitinationKNSSFRSKLHLVDLA
CCCCHHHHHHHHHHC
35.35-
244PhosphorylationHLVDLAGSERQKKTK
HHHHHCCCHHHHCCC
24.81-
250PhosphorylationGSERQKKTKAEGDRL
CCHHHHCCCCCCCHH
42.3923403867
251UbiquitinationSERQKKTKAEGDRLK
CHHHHCCCCCCCHHH
54.01-
258UbiquitinationKAEGDRLKEGININR
CCCCCHHHHCCCCCC
55.58-
269GlutathionylationNINRGLLCLGNVISA
CCCCHHHHHHHHHHH
5.7122555962
281AcetylationISALGDDKKGGFVPY
HHHCCCCCCCCCCCC
59.0425953088
282AcetylationSALGDDKKGGFVPYR
HHCCCCCCCCCCCCC
71.8626051181
288PhosphorylationKKGGFVPYRDSKLTR
CCCCCCCCCCCHHHH
23.0420068231
291PhosphorylationGFVPYRDSKLTRLLQ
CCCCCCCCHHHHHHH
22.1420068231
292UbiquitinationFVPYRDSKLTRLLQD
CCCCCCCHHHHHHHH
59.16-
294PhosphorylationPYRDSKLTRLLQDSL
CCCCCHHHHHHHHHC
24.0220068231
339AcetylationRARKIKNKPIVNIDP
HHHHHCCCCCCCCCH
30.9926051181
394PhosphorylationSLMEKNQSLVEENEK
HHHHHCHHHHHHHHH
43.7229255136
401SumoylationSLVEENEKLSRGLSE
HHHHHHHHHHHHHHH
64.44-
401AcetylationSLVEENEKLSRGLSE
HHHHHHHHHHHHHHH
64.4426051181
401SumoylationSLVEENEKLSRGLSE
HHHHHHHHHHHHHHH
64.44-
401UbiquitinationSLVEENEKLSRGLSE
HHHHHHHHHHHHHHH
64.44-
407PhosphorylationEKLSRGLSEAAGQTA
HHHHHHHHHHHHHHH
28.1922067460
423PhosphorylationMLERIILTEQANEKM
HHHHHHHHHHHHHHH
18.68-
429UbiquitinationLTEQANEKMNAKLEE
HHHHHHHHHHHHHHH
36.94-
433UbiquitinationANEKMNAKLEELRQH
HHHHHHHHHHHHHHH
51.97-
444UbiquitinationLRQHAACKLDLQKLV
HHHHHHHHHHHHHHH
40.07-
449UbiquitinationACKLDLQKLVETLED
HHHHHHHHHHHHHCH
62.89-
460SumoylationTLEDQELKENVEIIC
HHCHHHHHHHHHHHH
46.63-
474PhosphorylationCNLQQLITQLSDETV
HHHHHHHHHCCHHHH
31.8617081983
490PhosphorylationCMAAAIDTAVEQEAQ
HHHHHHHHHHHHHHH
26.8717081983
500PhosphorylationEQEAQVETSPETSRS
HHHHHHCCCCCCCCC
51.2126074081
501PhosphorylationQEAQVETSPETSRSS
HHHHHCCCCCCCCCC
13.7726074081
504PhosphorylationQVETSPETSRSSDAF
HHCCCCCCCCCCCCH
32.5926074081
505PhosphorylationVETSPETSRSSDAFT
HCCCCCCCCCCCCHH
28.6226074081
507PhosphorylationTSPETSRSSDAFTTQ
CCCCCCCCCCCHHHH
32.1330266825
508PhosphorylationSPETSRSSDAFTTQH
CCCCCCCCCCHHHHH
31.6730266825
512PhosphorylationSRSSDAFTTQHALRQ
CCCCCCHHHHHHHHH
27.5426074081
513PhosphorylationRSSDAFTTQHALRQA
CCCCCHHHHHHHHHH
16.3526074081
523PhosphorylationALRQAQMSKELVELN
HHHHHHHHHHHHHHH
15.7626074081
542SumoylationLKEALARKMTQNDSQ
HHHHHHHHHCCCCHH
40.46-
542SumoylationLKEALARKMTQNDSQ
HHHHHHHHHCCCCHH
40.46-
542UbiquitinationLKEALARKMTQNDSQ
HHHHHHHHHCCCCHH
40.46-
544PhosphorylationEALARKMTQNDSQLQ
HHHHHHHCCCCHHCC
27.5322817900
548PhosphorylationRKMTQNDSQLQPIQY
HHHCCCCHHCCCCEE
40.1027282143
593AcetylationKKDANQAKLSERRRK
HHHHHHHHHHHHHHH
42.6623236377
595PhosphorylationDANQAKLSERRRKRL
HHHHHHHHHHHHHHH
28.4923532336
624AcetylationNEQSKLLKLKESTER
HHHHHHHHHHHHHHH
68.872402993
632PhosphorylationLKESTERTVSKLNQE
HHHHHHHHHHHHHHH
23.9322617229
634PhosphorylationESTERTVSKLNQEIR
HHHHHHHHHHHHHHH
30.7122617229
635AcetylationSTERTVSKLNQEIRM
HHHHHHHHHHHHHHH
47.3125953088
635UbiquitinationSTERTVSKLNQEIRM
HHHHHHHHHHHHHHH
47.31-
670UbiquitinationQWKQKKDKEVIQLKE
HHHHHCCHHHHHHHH
63.86-
676UbiquitinationDKEVIQLKERDRKRQ
CHHHHHHHHHHHHHH
34.04-
684PhosphorylationERDRKRQYELLKLER
HHHHHHHHHHHHHHH
16.7528152594
688UbiquitinationKRQYELLKLERNFQK
HHHHHHHHHHHHHHH
62.01-
715UbiquitinationAAANKRLKDALQKQR
HHHHHHHHHHHHHHH
45.01-
772SumoylationNDLLEDRKILAQDVA
HHHHHHHHHHHHHHH
55.16-
772SumoylationNDLLEDRKILAQDVA
HHHHHHHHHHHHHHH
55.16-
782UbiquitinationAQDVAQLKEKKESGE
HHHHHHHHHHHHCCC
56.24-
787PhosphorylationQLKEKKESGENPPPK
HHHHHHHCCCCCCCH
61.3522985185
799PhosphorylationPPKLRRRTFSLTEVR
CCHHHHHEEEEEEEE
18.7622167270
801PhosphorylationKLRRRTFSLTEVRGQ
HHHHHEEEEEEEECC
33.4919664994
803PhosphorylationRRRTFSLTEVRGQVS
HHHEEEEEEEECCCC
31.1030266825
810PhosphorylationTEVRGQVSESEDSIT
EEEECCCCCCHHHHH
27.7622167270
812PhosphorylationVRGQVSESEDSITKQ
EECCCCCCHHHHHHH
38.9222167270
815PhosphorylationQVSESEDSITKQIES
CCCCCHHHHHHHHHH
28.2729255136
817PhosphorylationSESEDSITKQIESLE
CCCHHHHHHHHHHHH
22.3529255136
822PhosphorylationSITKQIESLETEMEF
HHHHHHHHHHHHHHH
32.8927174698
825PhosphorylationKQIESLETEMEFRSA
HHHHHHHHHHHHHHH
46.0227174698
840UbiquitinationQIADLQQKLLDAESE
HHHHHHHHHHHCCCC
37.7521890473
840 (in isoform 1)Ubiquitination-37.7521890473
840 (in isoform 2)Ubiquitination-37.7521890473
851UbiquitinationAESEDRPKQRWENIA
CCCCCCHHHHHHHHH
54.08-
868AcetylationLEAKCALKYLIGELV
HHHHHHHHHHHHHHH
21.3419608861
869PhosphorylationEAKCALKYLIGELVS
HHHHHHHHHHHHHHH
12.3820068231
876PhosphorylationYLIGELVSSKIQVSK
HHHHHHHHCCHHHHH
38.2420068231
877PhosphorylationLIGELVSSKIQVSKL
HHHHHHHCCHHHHHH
26.7120068231
883AcetylationSSKIQVSKLESSLKQ
HCCHHHHHHHHHHHH
58.3723236377
883UbiquitinationSSKIQVSKLESSLKQ
HCCHHHHHHHHHHHH
58.37-
893PhosphorylationSSLKQSKTSCADMQK
HHHHHCCCCHHHHHH
33.99-
894PhosphorylationSLKQSKTSCADMQKM
HHHHCCCCHHHHHHH
15.85-
900AcetylationTSCADMQKMLFEERN
CCHHHHHHHHHHHHC
30.8225953088
930AcetylationMEQQHQEKVLYLLSQ
HHHHHHHHHHHHHHH
30.8526051181
941PhosphorylationLLSQLQQSQMAEKQL
HHHHHHHHHHHHHHH
14.6827050516
946UbiquitinationQQSQMAEKQLEESVS
HHHHHHHHHHHHHHH
51.12-
951PhosphorylationAEKQLEESVSEKEQQ
HHHHHHHHHHHHHHH
22.9030266825
953PhosphorylationKQLEESVSEKEQQLL
HHHHHHHHHHHHHHH
52.8330266825
955AcetylationLEESVSEKEQQLLST
HHHHHHHHHHHHHHH
54.0026051181
955UbiquitinationLEESVSEKEQQLLST
HHHHHHHHHHHHHHH
54.0021890473
955 (in isoform 1)Ubiquitination-54.0021890473
955 (in isoform 2)Ubiquitination-54.0021890473
961PhosphorylationEKEQQLLSTLKCQDE
HHHHHHHHHHCCCHH
40.0421712546
962PhosphorylationKEQQLLSTLKCQDEE
HHHHHHHHHCCCHHH
30.1524732914
964UbiquitinationQQLLSTLKCQDEELE
HHHHHHHCCCHHHHH
29.91-
993AcetylationENEIIKQKLTLLQVA
HCHHHHHHHHHHHHH
38.1425953088
993UbiquitinationENEIIKQKLTLLQVA
HCHHHHHHHHHHHHH
38.14-
995PhosphorylationEIIKQKLTLLQVASR
HHHHHHHHHHHHHHH
32.2418318008
1001PhosphorylationLTLLQVASRQKHLPK
HHHHHHHHHCCCCCC
36.0725159151
1010PhosphorylationQKHLPKDTLLSPDSS
CCCCCCCCCCCCCCC
35.4117081983
1013PhosphorylationLPKDTLLSPDSSFEY
CCCCCCCCCCCCCCC
29.7625159151
1016PhosphorylationDTLLSPDSSFEYVPP
CCCCCCCCCCCCCCC
40.0725159151
1017PhosphorylationTLLSPDSSFEYVPPK
CCCCCCCCCCCCCCC
29.4925159151
1020PhosphorylationSPDSSFEYVPPKPKP
CCCCCCCCCCCCCCC
19.0821712546
1028PhosphorylationVPPKPKPSRVKEKFL
CCCCCCCCHHHHHHH
56.6930108239
1031AcetylationKPKPSRVKEKFLEQS
CCCCCHHHHHHHHHC
54.8225953088
1038PhosphorylationKEKFLEQSMDIEDLK
HHHHHHHCCCHHHHH
14.7329255136
1039SulfoxidationEKFLEQSMDIEDLKY
HHHHHHCCCHHHHHH
6.3421406390
1046PhosphorylationMDIEDLKYCSEHSVN
CCHHHHHHHHHCCCC
14.4323663014
1048PhosphorylationIEDLKYCSEHSVNEH
HHHHHHHHHCCCCCC
34.9422617229
1051PhosphorylationLKYCSEHSVNEHEDG
HHHHHHCCCCCCCCC
23.6822617229
1071SumoylationEGDDEEWKPTKLVKV
CCCCCCCCCEEEEEE
46.20-
1095UbiquitinationCKGWCGNKQCGCRKQ
CCCCCCCCCCCCCCC
32.05-
1104PhosphorylationCGCRKQKSDCGVDCC
CCCCCCCCCCCCCCC
35.3228258704
1115PhosphorylationVDCCCDPTKCRNRQQ
CCCCCCCHHHCCCCC
29.5328258704
1126PhosphorylationNRQQGKDSLGTVERT
CCCCCCCCCCCCEEC
31.9825159151
1129PhosphorylationQGKDSLGTVERTQDS
CCCCCCCCCEECCCC
25.2024732914
1133PhosphorylationSLGTVERTQDSEGSF
CCCCCEECCCCCCCE
24.1922617229
1136PhosphorylationTVERTQDSEGSFKLE
CCEECCCCCCCEECC
33.7621712546
1139PhosphorylationRTQDSEGSFKLEDPT
ECCCCCCCEECCCCC
18.3725159151
1146PhosphorylationSFKLEDPTEVTPGLS
CEECCCCCCCCCCCC
56.2423663014
1149PhosphorylationLEDPTEVTPGLSFFN
CCCCCCCCCCCCCCC
12.8523663014
1153PhosphorylationTEVTPGLSFFNPVCA
CCCCCCCCCCCCCCC
33.4429255136
1161PhosphorylationFFNPVCATPNSKILK
CCCCCCCCCCHHHHH
20.2029255136
1164PhosphorylationPVCATPNSKILKEMC
CCCCCCCHHHHHHHC
23.4429255136
1178PhosphorylationCDVEQVLSKKTPPAP
CCHHHHHCCCCCCCC
33.0021815630
1181PhosphorylationEQVLSKKTPPAPSPF
HHHHCCCCCCCCCCC
37.9429255136
1186PhosphorylationKKTPPAPSPFDLPEL
CCCCCCCCCCCCHHH
40.0622167270
1194SumoylationPFDLPELKHVATEYQ
CCCCHHHHHHHHHHH
34.0828112733
1198PhosphorylationPELKHVATEYQENKA
HHHHHHHHHHHHCCC
33.8526074081
1200PhosphorylationLKHVATEYQENKAPG
HHHHHHHHHHCCCCC
19.4426074081
1216PhosphorylationKKKRALASNTSFFSG
HHHHHHHCCCCCCCC
41.3022167270
1218PhosphorylationKRALASNTSFFSGCS
HHHHHCCCCCCCCCC
25.1522167270
1219PhosphorylationRALASNTSFFSGCSP
HHHHCCCCCCCCCCC
28.6622167270
1222PhosphorylationASNTSFFSGCSPIEE
HCCCCCCCCCCCCCC
36.5622167270
1225PhosphorylationTSFFSGCSPIEEEAH
CCCCCCCCCCCCCCC
32.2222167270

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
799TPhosphorylationKinaseAURAO14965
PSP
799TPhosphorylationKinaseAURKBQ96GD4
GPS
801SPhosphorylationKinasePRKAA1Q13131
GPS
801SPhosphorylationKinaseAURBQ96GD4
PSP
1161TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF4A_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 KIF4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HM20B_HUMANHMG20Bphysical
12809554
BRCA2_HUMANBRCA2physical
18604178
PRC1_HUMANPRC1physical
15297875
A4_HUMANAPPphysical
21832049
ARP6_HUMANACTR6physical
26344197
GBF1_HUMANGBF1physical
26344197
ZPR1_HUMANZPR1physical
26344197

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 KIF4A_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 SER-394; SER-801; SER-1001AND SER-1038, 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-801; THR-1161 ANDSER-1225, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995 AND SER-1001, 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 THR-799; SER-801; SER-951;SER-1001; SER-1013; SER-1016; SER-1017; TYR-1020; SER-1028; THR-1181;SER-1186 AND SER-1225, AND MASS SPECTROMETRY.
"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-394; SER-501; SER-810;SER-815; SER-1126 AND THR-1129, AND MASS SPECTROMETRY.
"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-507; SER-801; SER-810;SER-951; SER-1013; SER-1017; SER-1038; SER-1126; THR-1161; THR-1181;SER-1186 AND SER-1225, 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-801 AND THR-1181, ANDMASS 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-394; THR-544; THR-799;SER-801; THR-1010; SER-1013; SER-1016; SER-1038; SER-1048; SER-1051AND SER-1225, AND MASS SPECTROMETRY.

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