CTRO_HUMAN - dbPTM
CTRO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTRO_HUMAN
UniProt AC O14578
Protein Name Citron Rho-interacting kinase
Gene Name CIT
Organism Homo sapiens (Human).
Sequence Length 2027
Subcellular Localization Cytoplasm.
Protein Description Plays a role in cytokinesis. Required for KIF14 localization to the central spindle and midbody. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Displays serine/threonine protein kinase activity. Plays an important role in the regulation of cytokinesis and the development of the central nervous system. Phosphorylates MYL9/MLC2..
Protein Sequence MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFEECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATGDIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGGDLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDFGSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGRSPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFFSKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPNIFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGTPARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
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-------MLKFKYGA
-------CCCCCCCC
40.7322814378
13 (in isoform 3)Phosphorylation-44.1825849741
39PhosphorylationQGKPPFMTQQQMSPL
CCCCCCCCHHHCCCC
24.4929523821
44PhosphorylationFMTQQQMSPLSREGI
CCCHHHCCCCCHHHH
20.5324719451
47PhosphorylationQQQMSPLSREGILDA
HHHCCCCCHHHHHHH
31.5029523821
71UbiquitinationQPALMKIKHVSNFVR
CCHHHHHHHHHHHHH
32.2229967540
71 (in isoform 4)Ubiquitination-32.22-
79UbiquitinationHVSNFVRKYSDTIAE
HHHHHHHHHHHHHHH
43.7529967540
81PhosphorylationSNFVRKYSDTIAELQ
HHHHHHHHHHHHHHH
31.1728348404
83PhosphorylationFVRKYSDTIAELQEL
HHHHHHHHHHHHHHH
19.0228348404
95UbiquitinationQELQPSAKDFEVRSL
HHHCCCCCCCCHHHH
68.2521906983
95 (in isoform 1)Ubiquitination-68.2521906983
95 (in isoform 2)Ubiquitination-68.2521906983
117AcetylationEVQVVREKATGDIYA
EEEEEEHHCCCCCHH
40.467695767
126UbiquitinationTGDIYAMKVMKKKAL
CCCCHHHHHHHHHHH
30.88-
126 (in isoform 4)Ubiquitination-30.88-
140PhosphorylationLLAQEQVSFFEEERN
HHHHHHHHHHHHHHC
24.7430266825
223UbiquitinationGYVHRDIKPENILVD
HHHCCCCCHHHEEEC
51.0424816145
232PhosphorylationENILVDRTGHIKLVD
HHEEECCCCCEEEEE
28.75-
236UbiquitinationVDRTGHIKLVDFGSA
ECCCCCEEEEECCCC
36.46-
236 (in isoform 4)Ubiquitination-36.46-
245UbiquitinationVDFGSAAKMNSNKMV
EECCCCCCCCCCCCC
38.0329967540
245 (in isoform 4)Ubiquitination-38.03-
250UbiquitinationAAKMNSNKMVNAKLP
CCCCCCCCCCCCCCC
44.0129967540
307PhosphorylationRSPFAEGTSARTFNN
CCCCCCCCCCHHHHH
15.6619691289
308PhosphorylationSPFAEGTSARTFNNI
CCCCCCCCCHHHHHH
26.9819691289
323UbiquitinationMNFQRFLKFPDDPKV
HCHHHHCCCCCCCCC
52.73-
323 (in isoform 4)Ubiquitination-52.73-
350UbiquitinationCGQKERLKFEGLCCH
CCCHHHCCCCCEECC
47.8229967540
350 (in isoform 4)Ubiquitination-47.82-
362AcetylationCCHPFFSKIDWNNIR
ECCCCCCCCCHHHCC
39.26129615
371PhosphorylationDWNNIRNSPPPFVPT
CHHHCCCCCCCCCCC
29.0025159151
380UbiquitinationPPFVPTLKSDDDTSN
CCCCCCCCCCCCCCC
55.082190698
380 (in isoform 1)Ubiquitination-55.0821906983
380 (in isoform 2)Ubiquitination-55.0821906983
398PhosphorylationPEKNSWVSSSPCQLS
CCCCCCCCCCCCCCC
20.8825627689
400PhosphorylationKNSWVSSSPCQLSPS
CCCCCCCCCCCCCCC
23.3722210691
403UbiquitinationWVSSSPCQLSPSGFS
CCCCCCCCCCCCCCC
48.6521890473
407UbiquitinationSPCQLSPSGFSGEEL
CCCCCCCCCCCCCCC
49.4421890473
431PhosphorylationALGILGRSESVVSGL
HHCCCCCCHHHHCCC
32.2125159151
433PhosphorylationGILGRSESVVSGLDS
CCCCCCHHHHCCCCC
29.1225159151
436PhosphorylationGRSESVVSGLDSPAK
CCCHHHHCCCCCCCC
31.3330266825
440PhosphorylationSVVSGLDSPAKTSSM
HHHCCCCCCCCCCHH
31.6219664994
444PhosphorylationGLDSPAKTSSMEKKL
CCCCCCCCCHHHHHH
28.3026074081
445PhosphorylationLDSPAKTSSMEKKLL
CCCCCCCCHHHHHHH
27.2924114839
445UbiquitinationLDSPAKTSSMEKKLL
CCCCCCCCHHHHHHH
27.2921890473
446PhosphorylationDSPAKTSSMEKKLLI
CCCCCCCHHHHHHHH
35.8728122231
449UbiquitinationAKTSSMEKKLLIKSK
CCCCHHHHHHHHHCH
39.8321890473
465UbiquitinationLQDSQDKCHKMEQEM
HHCCHHHHHHHHHHH
5.1221890473
467UbiquitinationDSQDKCHKMEQEMTR
CCHHHHHHHHHHHHH
54.3129967540
469UbiquitinationQDKCHKMEQEMTRLH
HHHHHHHHHHHHHHH
48.4721890473
473PhosphorylationHKMEQEMTRLHRRVS
HHHHHHHHHHHHHHH
29.3520068231
480PhosphorylationTRLHRRVSEVEAVLS
HHHHHHHHHHHHHHC
33.8330266825
487PhosphorylationSEVEAVLSQKEVELK
HHHHHHHCHHHHHHC
32.3823927012
489UbiquitinationVEAVLSQKEVELKAS
HHHHHCHHHHHHCCC
61.4229967540
518UbiquitinationITECSSLKRSLEQAR
HHHHHHHHHHHHHHH
41.7232015554
518AcetylationITECSSLKRSLEQAR
HHHHHHHHHHHHHHH
41.7226051181
529PhosphorylationEQARMEVSQEDDKAL
HHHHHHCCHHHHHHH
17.9724719451
553UbiquitinationSRKLQEIKEQEYQAQ
HHHHHHHHHHHHHHH
53.2229967540
582PhosphorylationLVSARRRSDLYESEL
HHHHHHHHHHHHHHH
30.1030266825
585PhosphorylationARRRSDLYESELRES
HHHHHHHHHHHHHHH
23.5423927012
587PhosphorylationRRSDLYESELRESRL
HHHHHHHHHHHHHHH
28.5123186163
600UbiquitinationRLAAEEFKRKATECQ
HHHHHHHHHHHHHHH
57.1629967540
652PhosphorylationLEKAVKASTEATELL
HHHHHHHHHHHHHHH
22.5118452278
653PhosphorylationEKAVKASTEATELLQ
HHHHHHHHHHHHHHH
34.2018452278
656PhosphorylationVKASTEATELLQNIR
HHHHHHHHHHHHHHH
22.4218452278
699 (in isoform 4)Phosphorylation-38.2930266825
709 (in isoform 4)Phosphorylation-24.55-
741PhosphorylationKDLADKETLENMMQR
HHHCCHHHHHHHHHH
45.1520363803
772PhosphorylationAMINAMDSKIRSLEQ
HHHHHHHHHHHHHHH
19.5224043423
776PhosphorylationAMDSKIRSLEQRIVE
HHHHHHHHHHHHHHH
39.4725599653
794PhosphorylationANKLAANSSLFTQRN
HHHHHHCCCHHHHHH
24.5628857561
795PhosphorylationNKLAANSSLFTQRNM
HHHHHCCCHHHHHHH
27.5823312004
810PhosphorylationKAQEEMISELRQQKF
HHHHHHHHHHHHHHH
29.3024719451
825UbiquitinationYLETQAGKLEAQNRK
HHHHHHHHHHHHHHH
46.2829967540
841PhosphorylationEEQLEKISHQDHSDK
HHHHHHHCCCCCCCH
26.6022673903
846PhosphorylationKISHQDHSDKNRLLE
HHCCCCCCCHHHHHH
59.5822673903
8482-HydroxyisobutyrylationSHQDHSDKNRLLELE
CCCCCCCHHHHHHHH
47.16-
867UbiquitinationEVSLEHEEQKLELKR
HHCCHHHHHHHHHHH
55.7329967540
869UbiquitinationSLEHEEQKLELKRQL
CCHHHHHHHHHHHHH
47.4021890473
873UbiquitinationEEQKLELKRQLTELQ
HHHHHHHHHHHHHHH
28.8221890473
882PhosphorylationQLTELQLSLQERESQ
HHHHHHHHHHHHHHH
18.2919413330
911UbiquitinationLRQAKTELEETTAEA
HHHHHHHHHHHHHHH
9.7321890473
915UbiquitinationKTELEETTAEAEEEI
HHHHHHHHHHHHHHH
26.2721890473
969PhosphorylationELNNQNFYLSKQLDE
HHHHCCEEHHHHHHH
20.02-
999PhosphorylationDHLRREITEREMQLT
HHHHHHHHHHHHHHH
25.0026437602
1054UbiquitinationRSVLGDEKSQFECRV
HHHHCCHHHHHHHHH
55.0630230243
1072UbiquitinationQRMLDTEKQSRARAD
HHHHCHHHHHHHHHH
56.5230230243
1085PhosphorylationADQRITESRQVVELA
HHHHHHHHHHHHHHH
21.2525599653
1096UbiquitinationVELAVKEHKAEILAL
HHHHHHHHHHHHHHH
28.9830230243
1108UbiquitinationLALQQALKEQKLKAE
HHHHHHHHHHCHHHH
62.2032015554
1111UbiquitinationQQALKEQKLKAESLS
HHHHHHHCHHHHHHH
53.7130230243
1114UbiquitinationLKEQKLKAESLSDKL
HHHHCHHHHHHHHHH
23.2630230243
1137PhosphorylationMLEMNARSLQQKLET
HHHHHHHHHHHHHHH
28.2822673903
1141UbiquitinationNARSLQQKLETEREL
HHHHHHHHHHHHHHH
35.0229967540
1150UbiquitinationETERELKQRLLEEQA
HHHHHHHHHHHHHHH
54.6132015554
1153UbiquitinationRELKQRLLEEQAKLQ
HHHHHHHHHHHHHHH
8.0930230243
1158UbiquitinationRLLEEQAKLQQQMDL
HHHHHHHHHHHHHHH
46.6629967540
1167UbiquitinationQQQMDLQKNHIFRLT
HHHHHHHHHHHHHHH
58.7629967540
1183UbiquitinationGLQEALDRADLLKTE
HHHHHHHHHHHHHHH
30.7429967540
1196PhosphorylationTERSDLEYQLENIQV
HHHHHHHHHHHHHEE
26.20-
1200UbiquitinationDLEYQLENIQVLYSH
HHHHHHHHHEEEEEC
38.2929967540
1209UbiquitinationQVLYSHEKVKMEGTI
EEEEECCCCCCEEEC
41.5529967540
1229UbiquitinationLIDFLQAKMDQPAKK
HHHHHHHHCCCCHHH
30.0129967540
1242PhosphorylationKKKKGLFSRRKEDPA
HHCCCCCCCCCCCCC
35.9028674151
1251UbiquitinationRKEDPALPTQVPLQY
CCCCCCCCCCCCCCH
23.9229967540
1262UbiquitinationPLQYNELKLALEKEK
CCCHHHHHHHHHHHH
26.0729967540
1271UbiquitinationALEKEKARCAELEEA
HHHHHHHHHHHHHHH
31.1129967540
1282PhosphorylationLEEALQKTRIELRSA
HHHHHHHHHHHHHHH
24.7430622161
1304UbiquitinationKATDHPHPSTPATAR
HCCCCCCCCCCHHHH
44.3329967540
1305PhosphorylationATDHPHPSTPATARQ
CCCCCCCCCCHHHHH
43.9425159151
1306PhosphorylationTDHPHPSTPATARQQ
CCCCCCCCCHHHHHH
22.7627422710
1309PhosphorylationPHPSTPATARQQIAM
CCCCCCHHHHHHHHH
24.4727732954
1317PhosphorylationARQQIAMSAIVRSPE
HHHHHHHHHHHCCCC
13.0628464451
1322PhosphorylationAMSAIVRSPEHQPSA
HHHHHHCCCCCCCCH
24.6023401153
1328PhosphorylationRSPEHQPSAMSLLAP
CCCCCCCCHHHHCCC
29.9930266825
1331PhosphorylationEHQPSAMSLLAPPSS
CCCCCHHHHCCCCCC
21.6820873877
1343PhosphorylationPSSRRKESSTPEEFS
CCCCCCCCCCHHHHH
42.4119691289
1344PhosphorylationSSRRKESSTPEEFSR
CCCCCCCCCHHHHHH
49.4219691289
1345PhosphorylationSRRKESSTPEEFSRR
CCCCCCCCHHHHHHH
43.9619691289
1350PhosphorylationSSTPEEFSRRLKERM
CCCHHHHHHHHHHHH
21.5519691289
1382PhosphorylationKCAVCLDTVHFGRQA
CEEEEECHHHCCCHH
11.70-
1410PhosphorylationCSTCLPATCGLPAEY
CCCCCCCCCCCCHHH
12.74-
1417PhosphorylationTCGLPAEYATHFTEA
CCCCCHHHHHHHHHH
20.93-
1419PhosphorylationGLPAEYATHFTEAFC
CCCHHHHHHHHHHHH
19.34-
1432PhosphorylationFCRDKMNSPGLQTKE
HHHHHCCCCCCCCCC
19.4925159151
1433 (in isoform 3)Phosphorylation-42.3721406692
1434 (in isoform 3)Phosphorylation-30.1821406692
1435 (in isoform 3)Phosphorylation-7.1121406692
1437PhosphorylationMNSPGLQTKEPSSSL
CCCCCCCCCCCCCCC
42.2824732914
1437 (in isoform 3)Phosphorylation-42.2825849741
1467PhosphorylationQQGWDRKYIVLEGSK
CCCCCCEEEEEECCE
9.35-
1473PhosphorylationKYIVLEGSKVLIYDN
EEEEEECCEEEEECH
15.37-
1571UbiquitinationGGRVSREKAEADAKL
CCCCCHHHHHHHHHH
50.87-
1582PhosphorylationDAKLLGNSLLKLEGD
HHHHHCCCHHHCCCC
33.0322199227
1613 (in isoform 4)Ubiquitination-2.27-
1720PhosphorylationLRYNENLSKYCIRKE
EECCCCHHHHHHHHH
32.9128102081
1721AcetylationRYNENLSKYCIRKEI
ECCCCHHHHHHHHHC
47.5119608861
1759PhosphorylationYEIDMKQYTLEEFLD
EEEECHHHCHHHHHC
14.05-
1760PhosphorylationEIDMKQYTLEEFLDK
EEECHHHCHHHHHCC
25.79-
1763AcetylationMKQYTLEEFLDKNDH
CHHHCHHHHHCCCCC
55.4019608861
1899AcetylationKLRVICCKGNLVKES
CEEEEEECCCEECCC
46.5525953088
1917PhosphorylationHHRGPSTSRSSPNKR
CCCCCCCCCCCCCCC
34.2128102081
1919PhosphorylationRGPSTSRSSPNKRGP
CCCCCCCCCCCCCCC
50.3326699800
1920PhosphorylationGPSTSRSSPNKRGPP
CCCCCCCCCCCCCCC
31.2325849741
1928PhosphorylationPNKRGPPTYNEHITK
CCCCCCCCCCHHHHH
41.9523312004
1929PhosphorylationNKRGPPTYNEHITKR
CCCCCCCCCHHHHHH
25.0725159151
1934PhosphorylationPTYNEHITKRVASSP
CCCCHHHHHHHHCCC
18.08-
1939PhosphorylationHITKRVASSPAPPEG
HHHHHHHCCCCCCCC
33.7230266825
1940PhosphorylationITKRVASSPAPPEGP
HHHHHHCCCCCCCCC
18.4930266825
1948PhosphorylationPAPPEGPSHPREPST
CCCCCCCCCCCCCCC
57.9124732914
1954PhosphorylationPSHPREPSTPHRYRE
CCCCCCCCCCCCCCC
50.2224732914
1955PhosphorylationSHPREPSTPHRYREG
CCCCCCCCCCCCCCC
33.5528258704
1971PhosphorylationTELRRDKSPGRPLER
CHHCCCCCCCCCCCC
36.5529255136
1981PhosphorylationRPLEREKSPGRMLST
CCCCCCCCCCCCCCC
28.0327251275
1987PhosphorylationKSPGRMLSTRRERSP
CCCCCCCCCCCCCCC
15.5518691976
1988PhosphorylationSPGRMLSTRRERSPG
CCCCCCCCCCCCCCC
29.7727251275
1993PhosphorylationLSTRRERSPGRLFED
CCCCCCCCCCCCCCC
27.2723401153
2001PhosphorylationPGRLFEDSSRGRLPA
CCCCCCCCCCCCCCC
18.1023927012
2002PhosphorylationGRLFEDSSRGRLPAG
CCCCCCCCCCCCCCC
51.5923927012
2003MethylationRLFEDSSRGRLPAGA
CCCCCCCCCCCCCCC
37.90-
2013PhosphorylationLPAGAVRTPLSQVNK
CCCCCCCCCHHHHCC
23.2228985074
2016PhosphorylationGAVRTPLSQVNKVWD
CCCCCCHHHHCCHHC
33.0328857561
2025PhosphorylationVNKVWDQSSV-----
HCCHHCCCCC-----
30.5120044836
2026PhosphorylationNKVWDQSSV------
CCHHCCCCC------
26.6422199227

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 CTRO_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTRO_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 CTRO_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHOA_HUMANRHOAphysical
8543060
RHOB_HUMANRHOBphysical
8543060
RAC1_HUMANRAC1physical
8543060
HGS_HUMANHGSphysical
21748597
ZN706_HUMANZNF706physical
22939629
UBP28_HUMANUSP28physical
22939629
GAG_HV1H2gagphysical
27339686

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 CTRO_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1721, 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-433 AND SER-440, ANDMASS 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-440, AND MASSSPECTROMETRY.
"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-440, AND MASSSPECTROMETRY.
"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-440, 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-440, AND MASSSPECTROMETRY.
"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-440, AND MASSSPECTROMETRY.
"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-1971 AND SER-1993, ANDMASS SPECTROMETRY.

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