INCE_HUMAN - dbPTM
INCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INCE_HUMAN
UniProt AC Q9NQS7
Protein Name Inner centromere protein
Gene Name INCENP
Organism Homo sapiens (Human).
Sequence Length 918
Subcellular Localization Nucleus . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle . Midbody . Chromosome, centromere, kinetochore . Colocalized at synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromat
Protein Description Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules. [PubMed: 15316025]
Protein Sequence MGTTAPGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEAERMFTREFSKEPELMPKTPSQKNRRKKRRISYVQDENRDPIRRRLSRRKSRSSQLSSRRLRSKDSVEKLATVVGENGSVLRRVTRAAAAAAAATMALAAPSSPTPESPTMLTKKPEDNHTQCQLVPVVEIGISERQNAEQHVTQLMSTEPLPRTLSPTPASATAPTSQGIPTSDEESTPKKSKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPGPRDSPAFPDSPWRERVLAPILPDNFSTPTGSRTDSQSVRHSPIAPSSPSPQVLAQKYSLVAKQESVVRRASRRLAKKTAEEPAASGRIICHSYLERLLNVEVPQKVGSEQKEPPEEAEPVAAAEPEVPENNGNNSWPHNDTEIANSTPNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQHLEDEELQPPRSKTPSSPCPASKVVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLRMDPKCSFVEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKALNVTVDVQSPACTSYQMTPQGHRAPPKINPDNYGMDLNSDDSTDDEAHPRKPIPTWARGTPLSQAIIHQYYHPPNLLELFGTILPLDLEDIFKKSKPRYHKRTSSAVWNSPPLQGARVPSSLAYSLKKH
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
3Phosphorylation-----MGTTAPGPIH
-----CCCCCCCCCH		20.6320068231
50PhosphorylationRMFTREFSKEPELMP
HHHHHHHHCCCCCCC		31.2120860994
51UbiquitinationMFTREFSKEPELMPK
HHHHHHHCCCCCCCC		80.6722817900
51 (in isoform 1)Ubiquitination-80.6721890473
51 (in isoform 2)Ubiquitination-80.6721890473
59PhosphorylationEPELMPKTPSQKNRR
CCCCCCCCCCHHCHH		23.4627273156
61PhosphorylationELMPKTPSQKNRRKK
CCCCCCCCHHCHHHH		60.0428450419
72PhosphorylationRRKKRRISYVQDENR
HHHHHHCCHHCCCCC		19.8930266825
73PhosphorylationRKKRRISYVQDENRD
HHHHHCCHHCCCCCH		10.3523927012
91PhosphorylationRRLSRRKSRSSQLSS
HHHHHHHHHHHHHHH		35.2725159151
93PhosphorylationLSRRKSRSSQLSSRR
HHHHHHHHHHHHHHH		29.5325159151
94PhosphorylationSRRKSRSSQLSSRRL
HHHHHHHHHHHHHHH		33.7526055452
97O-linked_GlycosylationKSRSSQLSSRRLRSK
HHHHHHHHHHHHCCH		17.7330379171
97PhosphorylationKSRSSQLSSRRLRSK
HHHHHHHHHHHHCCH		17.7329052541
98PhosphorylationSRSSQLSSRRLRSKD
HHHHHHHHHHHCCHH		29.9729052541
103PhosphorylationLSSRRLRSKDSVEKL
HHHHHHCCHHHHHHH		45.4617192257
104UbiquitinationSSRRLRSKDSVEKLA
HHHHHCCHHHHHHHH		47.8133845483
106PhosphorylationRRLRSKDSVEKLATV
HHHCCHHHHHHHHHH		35.5928985074
109UbiquitinationRSKDSVEKLATVVGE
CCHHHHHHHHHHHCC		41.0629967540
112PhosphorylationDSVEKLATVVGENGS
HHHHHHHHHHCCCCH		26.5920860994
119PhosphorylationTVVGENGSVLRRVTR
HHHCCCCHHHHHHHH		29.5630266825
135PhosphorylationAAAAAAATMALAAPS
HHHHHHHHHHHHCCC		9.7629255136
142PhosphorylationTMALAAPSSPTPESP
HHHHHCCCCCCCCCC		44.1930266825
143PhosphorylationMALAAPSSPTPESPT
HHHHCCCCCCCCCCC		31.5629255136
145PhosphorylationLAAPSSPTPESPTML
HHCCCCCCCCCCCCC		41.4530266825
148PhosphorylationPSSPTPESPTMLTKK
CCCCCCCCCCCCCCC		27.2028176443
150PhosphorylationSPTPESPTMLTKKPE
CCCCCCCCCCCCCCC		33.8130266825
153PhosphorylationPESPTMLTKKPEDNH
CCCCCCCCCCCCCCC		26.6326055452
184PhosphorylationQNAEQHVTQLMSTEP
CCHHHHHHHHHCCCC		17.5426074081
188PhosphorylationQHVTQLMSTEPLPRT
HHHHHHHCCCCCCCC		37.9126074081
189PhosphorylationHVTQLMSTEPLPRTL
HHHHHHCCCCCCCCC		27.8826074081
195PhosphorylationSTEPLPRTLSPTPAS
CCCCCCCCCCCCCCC		29.6423927012
197PhosphorylationEPLPRTLSPTPASAT
CCCCCCCCCCCCCCC		26.5625159151
199PhosphorylationLPRTLSPTPASATAP
CCCCCCCCCCCCCCC		28.2823927012
202PhosphorylationTLSPTPASATAPTSQ
CCCCCCCCCCCCCCC		27.6230266825
204PhosphorylationSPTPASATAPTSQGI
CCCCCCCCCCCCCCC		30.5823927012
207PhosphorylationPASATAPTSQGIPTS
CCCCCCCCCCCCCCC		31.0830266825
208PhosphorylationASATAPTSQGIPTSD
CCCCCCCCCCCCCCC		25.9230266825
213PhosphorylationPTSQGIPTSDEESTP
CCCCCCCCCCCCCCC		47.0625159151
214PhosphorylationTSQGIPTSDEESTPK
CCCCCCCCCCCCCCC		37.3625159151
218PhosphorylationIPTSDEESTPKKSKA
CCCCCCCCCCCHHHH		48.2225159151
219PhosphorylationPTSDEESTPKKSKAR
CCCCCCCCCCHHHHH		42.2723927012
223PhosphorylationEESTPKKSKARILES
CCCCCCHHHHHHHHH		37.3630576142
230PhosphorylationSKARILESITVSSLM
HHHHHHHHCCHHHHH		21.8026055452
232PhosphorylationARILESITVSSLMAT
HHHHHHCCHHHHHCC		24.5021712546
234PhosphorylationILESITVSSLMATPQ
HHHHCCHHHHHCCCC		14.7626055452
235PhosphorylationLESITVSSLMATPQD
HHHCCHHHHHCCCCC		20.1629255136
239PhosphorylationTVSSLMATPQDPKGQ
CHHHHHCCCCCCCCC		13.9129255136
250PhosphorylationPKGQGVGTGRSASKL
CCCCCCCCCCCCCCE		27.3224732914
253PhosphorylationQGVGTGRSASKLRIA
CCCCCCCCCCCEEEE		37.9325849741
255PhosphorylationVGTGRSASKLRIAQV
CCCCCCCCCEEEEEE		33.2121712546
263PhosphorylationKLRIAQVSPGPRDSP
CEEEEEECCCCCCCC		16.4429255136
269PhosphorylationVSPGPRDSPAFPDSP
ECCCCCCCCCCCCCC		21.2925159151
275PhosphorylationDSPAFPDSPWRERVL
CCCCCCCCCHHHHCC		26.9722167270
291PhosphorylationPILPDNFSTPTGSRT
CCCCCCCCCCCCCCC		39.4729255136
292PhosphorylationILPDNFSTPTGSRTD
CCCCCCCCCCCCCCC		22.2629255136
294PhosphorylationPDNFSTPTGSRTDSQ
CCCCCCCCCCCCCCC		48.1330266825
296PhosphorylationNFSTPTGSRTDSQSV
CCCCCCCCCCCCCCC		34.1930266825
298PhosphorylationSTPTGSRTDSQSVRH
CCCCCCCCCCCCCCC		41.5223927012
300PhosphorylationPTGSRTDSQSVRHSP
CCCCCCCCCCCCCCC		24.6023401153
302PhosphorylationGSRTDSQSVRHSPIA
CCCCCCCCCCCCCCC		25.6830278072
306PhosphorylationDSQSVRHSPIAPSSP
CCCCCCCCCCCCCCC		13.8729255136
311PhosphorylationRHSPIAPSSPSPQVL
CCCCCCCCCCCHHHH		45.9529255136
312PhosphorylationHSPIAPSSPSPQVLA
CCCCCCCCCCHHHHH		28.4729255136
314PhosphorylationPIAPSSPSPQVLAQK
CCCCCCCCHHHHHHH		29.8829255136
321AcetylationSPQVLAQKYSLVAKQ
CHHHHHHHHHHHHHH		31.0625953088
321UbiquitinationSPQVLAQKYSLVAKQ
CHHHHHHHHHHHHHH		31.0622817900
321 (in isoform 1)Ubiquitination-31.0621890473
321 (in isoform 2)Ubiquitination-31.0621890473
322PhosphorylationPQVLAQKYSLVAKQE
HHHHHHHHHHHHHHH		8.6524732914
323PhosphorylationQVLAQKYSLVAKQES
HHHHHHHHHHHHHHH		24.3324732914
327SumoylationQKYSLVAKQESVVRR
HHHHHHHHHHHHHHH		47.31-
327AcetylationQKYSLVAKQESVVRR
HHHHHHHHHHHHHHH		47.3125953088
327SumoylationQKYSLVAKQESVVRR
HHHHHHHHHHHHHHH		47.31-
327UbiquitinationQKYSLVAKQESVVRR
HHHHHHHHHHHHHHH		47.3133845483
330PhosphorylationSLVAKQESVVRRASR
HHHHHHHHHHHHHHH		24.3421712546
336PhosphorylationESVVRRASRRLAKKT
HHHHHHHHHHHHHHH		19.0022817900
341MethylationRASRRLAKKTAEEPA
HHHHHHHHHHCCCCC		56.07116253813
343PhosphorylationSRRLAKKTAEEPAAS
HHHHHHHHCCCCCCC		38.30-
350PhosphorylationTAEEPAASGRIICHS
HCCCCCCCCCEEEHH		30.6120860994
357PhosphorylationSGRIICHSYLERLLN
CCCEEEHHHHHHHHC		27.3125159151
358PhosphorylationGRIICHSYLERLLNV
CCEEEHHHHHHHHCC		6.7429396449
370UbiquitinationLNVEVPQKVGSEQKE
HCCCCCCCCCCCCCC		42.3633845483
373PhosphorylationEVPQKVGSEQKEPPE
CCCCCCCCCCCCCCH		39.5820860994
400PhosphorylationPENNGNNSWPHNDTE
CCCCCCCCCCCCCCH		46.0817192257
406PhosphorylationNSWPHNDTEIANSTP
CCCCCCCCHHCCCCC		34.3117192257
411PhosphorylationNDTEIANSTPNPKPA
CCCHHCCCCCCCCCC		35.9017192257
412PhosphorylationDTEIANSTPNPKPAA
CCHHCCCCCCCCCCC		27.2225159151
420PhosphorylationPNPKPAASSPETPSA
CCCCCCCCCCCCCCC		48.8325159151
421PhosphorylationNPKPAASSPETPSAG
CCCCCCCCCCCCCCC		23.2529255136
424PhosphorylationPAASSPETPSAGQQE
CCCCCCCCCCCCCCC		26.4029255136
426PhosphorylationASSPETPSAGQQEAK
CCCCCCCCCCCCCCC		53.0729255136
434PhosphorylationAGQQEAKTDQADGPR
CCCCCCCCCCCCCCC		40.1523186163
446PhosphorylationGPREPPQSARRKRSY
CCCCCCHHHHHHHHH		29.5325159151
452PhosphorylationQSARRKRSYKQAVSE
HHHHHHHHHHHHHHH		39.4523401153
453PhosphorylationSARRKRSYKQAVSEL
HHHHHHHHHHHHHHC		15.9127134283
454AcetylationARRKRSYKQAVSELD
HHHHHHHHHHHHHCC		32.7825953088
458PhosphorylationRSYKQAVSELDEEQH
HHHHHHHHHCCHHHC		35.1421082442
476PhosphorylationEELQPPRSKTPSSPC
CCCCCCCCCCCCCCC		46.8125159151
478PhosphorylationLQPPRSKTPSSPCPA
CCCCCCCCCCCCCCH		29.6523401153
480PhosphorylationPPRSKTPSSPCPASK
CCCCCCCCCCCCHHH		52.7430266825
481PhosphorylationPRSKTPSSPCPASKV
CCCCCCCCCCCHHHH		31.5523401153
486PhosphorylationPSSPCPASKVVRPLR
CCCCCCHHHHHHCHH		15.8922115753
487AcetylationSSPCPASKVVRPLRT
CCCCCHHHHHHCHHH		47.027308167
494PhosphorylationKVVRPLRTFLHTVQR
HHHHCHHHHHHHHHH		37.93-
498PhosphorylationPLRTFLHTVQRNQML
CHHHHHHHHHHCCCC		22.0823312004
507PhosphorylationQRNQMLMTPTSAPRS
HHCCCCCCCCCCCHH		21.3226055452
509PhosphorylationNQMLMTPTSAPRSVM
CCCCCCCCCCCHHHH		28.4926055452
510PhosphorylationQMLMTPTSAPRSVMK
CCCCCCCCCCHHHHH		37.1626055452
514PhosphorylationTPTSAPRSVMKSFIK
CCCCCCHHHHHHHHH		26.0418669648
517AcetylationSAPRSVMKSFIKRNT
CCCHHHHHHHHHCCC		39.8125953088
518PhosphorylationAPRSVMKSFIKRNTP
CCHHHHHHHHHCCCC		17.7020860994
521UbiquitinationSVMKSFIKRNTPLRM
HHHHHHHHCCCCCCC		37.2732015554
524PhosphorylationKSFIKRNTPLRMDPK
HHHHHCCCCCCCCCC		27.9430576142
548UbiquitinationRLENLRRKEEAEQLR
HHHHHHHHHHHHHHH		54.1729967540
592UbiquitinationRERVEQMKEEKKKQI
HHHHHHHHHHHHHHH		63.5223000965
593UbiquitinationERVEQMKEEKKKQIE
HHHHHHHHHHHHHHH		70.4823000965
596UbiquitinationEQMKEEKKKQIEQKF
HHHHHHHHHHHHHHH		53.8723000965
597UbiquitinationQMKEEKKKQIEQKFA
HHHHHHHHHHHHHHH		68.5223000965
598UbiquitinationMKEEKKKQIEQKFAQ
HHHHHHHHHHHHHHH		54.0221890473
598 (in isoform 2)Ubiquitination-54.0221890473
602AcetylationKKKQIEQKFAQIDEK
HHHHHHHHHHHHHHH		29.8520167786
602UbiquitinationKKKQIEQKFAQIDEK
HHHHHHHHHHHHHHH		29.8523000965
602 (in isoform 1)Ubiquitination-29.8521890473
609AcetylationKFAQIDEKTEKAKEE
HHHHHHHHHHHHHHH		59.2320167786
610PhosphorylationFAQIDEKTEKAKEER
HHHHHHHHHHHHHHH		40.4420068231
630"N6,N6-dimethyllysine"AKKKAAAKKMEEVEA
HHHHHHHHHHHHHHH		48.18-
630AcetylationAKKKAAAKKMEEVEA
HHHHHHHHHHHHHHH		48.1812437563
630MethylationAKKKAAAKKMEEVEA
HHHHHHHHHHHHHHH		48.18-
631"N6,N6-dimethyllysine"KKKAAAKKMEEVEAR
HHHHHHHHHHHHHHH		46.98-
631AcetylationKKKAAAKKMEEVEAR
HHHHHHHHHHHHHHH		46.9812437571
631MethylationKKKAAAKKMEEVEAR
HHHHHHHHHHHHHHH		46.98-
744UbiquitinationLQEREKALRLQKEQL
HHHHHHHHHHHHHHH		9.2229967540
748UbiquitinationEKALRLQKEQLQREL
HHHHHHHHHHHHHHH		52.6129967540
793PhosphorylationASKALNVTVDVQSPA
CCHHCCCEEEECCCC		15.2024732914
798PhosphorylationNVTVDVQSPACTSYQ
CCEEEECCCCCCCEE		17.8225159151
802PhosphorylationDVQSPACTSYQMTPQ
EECCCCCCCEEECCC		32.3524732914
803PhosphorylationVQSPACTSYQMTPQG
ECCCCCCCEEECCCC		17.1625159151
804PhosphorylationQSPACTSYQMTPQGH
CCCCCCCEEECCCCC		5.5524732914
807PhosphorylationACTSYQMTPQGHRAP
CCCCEEECCCCCCCC		9.2725159151
808PhosphorylationCTSYQMTPQGHRAPP
CCCEEECCCCCCCCC		32.5818669648
822PhosphorylationPKINPDNYGMDLNSD
CCCCCCCCCCCCCCC		22.6223927012
828PhosphorylationNYGMDLNSDDSTDDE
CCCCCCCCCCCCCCC		50.5223927012
831PhosphorylationMDLNSDDSTDDEAHP
CCCCCCCCCCCCCCC		38.4323927012
832PhosphorylationDLNSDDSTDDEAHPR
CCCCCCCCCCCCCCC		55.2323927012
833PhosphorylationLNSDDSTDDEAHPRK
CCCCCCCCCCCCCCC		56.5622067460
836PhosphorylationDDSTDDEAHPRKPIP
CCCCCCCCCCCCCCC		25.6122067460
837PhosphorylationDSTDDEAHPRKPIPT
CCCCCCCCCCCCCCC		22.2022067460
844PhosphorylationHPRKPIPTWARGTPL
CCCCCCCCCCCCCCH		32.2620068231
852PhosphorylationWARGTPLSQAIIHQY
CCCCCCHHHHHHHHH		20.8325332170
859PhosphorylationSQAIIHQYYHPPNLL
HHHHHHHHCCCCCHH		6.9225332170
887 (in isoform 2)Methylation-50.34-
892PhosphorylationKPRYHKRTSSAVWNS
CCCCCCCCCCCCCCC		31.6623401153
893PhosphorylationPRYHKRTSSAVWNSP
CCCCCCCCCCCCCCC		21.9730266825
894PhosphorylationRYHKRTSSAVWNSPP
CCCCCCCCCCCCCCC		26.6522024163
897PhosphorylationKRTSSAVWNSPPLQG
CCCCCCCCCCCCCCC		10.1712925766
898PhosphorylationRTSSAVWNSPPLQGA
CCCCCCCCCCCCCCC		37.7322067460
899PhosphorylationTSSAVWNSPPLQGAR
CCCCCCCCCCCCCCC		16.5125159151
904PhosphorylationWNSPPLQGARVPSSL
CCCCCCCCCCCCHHH		24.0422067460
909PhosphorylationLQGARVPSSLAYSLK
CCCCCCCHHHHHHHH		34.8218691976
910O-linked_GlycosylationQGARVPSSLAYSLKK
CCCCCCHHHHHHHHC		15.7930379171
910PhosphorylationQGARVPSSLAYSLKK
CCCCCCHHHHHHHHC		15.7918669648
913PhosphorylationRVPSSLAYSLKKH--
CCCHHHHHHHHCC--		21.5925159151
914PhosphorylationVPSSLAYSLKKH---
CCHHHHHHHHCC---		28.2723401153
916AcetylationSSLAYSLKKH-----
HHHHHHHHCC-----		42.7525953088
916MethylationSSLAYSLKKH-----
HHHHHHHHCC-----		42.75115971431
917MethylationSLAYSLKKH------
HHHHHHHCC------		60.90115971435
919PhosphorylationAYSLKKH--------
HHHHHCC--------		22067460
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
59TPhosphorylationKinaseAURKBQ96GD4
GPS
72SPhosphorylationKinaseAURKBQ96GD4
GPS
494TPhosphorylationKinaseAURKBQ96GD4
GPS
518SPhosphorylationKinaseAURKBQ96GD4
GPS
892TPhosphorylationKinaseAURBQ96GD4
PSP
892TPhosphorylationKinaseAURCQ9UQB9
PSP
893SPhosphorylationKinaseAURBQ96GD4
PSP
893SPhosphorylationKinaseAURCQ9UQB9
PSP
894SPhosphorylationKinaseAURBQ96GD4
PSP
894SPhosphorylationKinaseAURCQ9UQB9
PSP
894SPhosphorylationKinaseLATS1O95835
PSP
894SPhosphorylationKinaseLATS2Q9NRM7
PSP
897TPhosphorylationKinaseAURKBQ96GD4
PhosphoELM
898SPhosphorylationKinaseAURKBQ96GD4
PhosphoELM
899SPhosphorylationKinaseAURKBQ96GD4
PhosphoELM
899SPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INCE_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 INCE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIRC5_HUMANBIRC5physical
19951914
BOREA_HUMANCDCA8physical
19951914
AURKB_HUMANAURKBphysical
19951914
AURKA_HUMANAURKAphysical
18773538
AURKB_HUMANAURKBphysical
18773538
AURKA_HUMANAURKAphysical
11050385
AURKB_HUMANAURKBphysical
11050385
BIRC5_HUMANBIRC5physical
16239925
AURKB_HUMANAURKBphysical
16239925
BOREA_HUMANCDCA8physical
16239925
AURKB_HUMANAURKBphysical
12925766
CBX5_HUMANCBX5physical
20562864
AURKB_HUMANAURKBphysical
20562864
BOREA_HUMANCDCA8physical
17956729
BIRC5_HUMANBIRC5physical
17956729
AURKB_HUMANAURKBphysical
17956729
BIRC5_HUMANBIRC5physical
16571674
BOREA_HUMANCDCA8physical
16571674
AURKB_HUMANAURKBphysical
16571674
AURKC_HUMANAURKCphysical
15316025
AURKB_HUMANAURKBphysical
15316025
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 INCE_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-197; THR-199; THR-213;SER-214; THR-239; SER-263; SER-269; SER-275; SER-306; SER-314;TYR-822; SER-828; SER-831; THR-832; SER-899 AND SER-914, AND MASSSPECTROMETRY.
"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-142; SER-143; THR-145;SER-148; THR-150; SER-197; THR-213; SER-214; SER-263; SER-291;THR-298; SER-311; SER-314; SER-421; SER-828; SER-831; THR-832; THR-892AND SER-899, 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 THR-195; THR-213; SER-214;SER-218; THR-219; SER-263; THR-292; SER-421 AND THR-424, 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-119; THR-145; SER-148;SER-197; THR-213; SER-218; SER-230; THR-239; SER-263; SER-269;SER-275; THR-292; SER-296; THR-298; SER-306; SER-312; SER-314;SER-446; THR-507; THR-509; SER-510; SER-514; SER-828; SER-831;THR-832; SER-893; SER-894; SER-899 AND SER-914, 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-72; TYR-73; SER-91;SER-93; SER-94; SER-103; SER-143; SER-148; SER-214; SER-218; THR-239;SER-263; SER-269; SER-275; THR-292; SER-296; SER-306; SER-312;SER-400; THR-406; SER-411; SER-420; SER-421; THR-424; SER-446;SER-458; SER-476; THR-478; SER-480; SER-481; SER-893; SER-894 ANDSER-899, 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-72; SER-263; SER-269;SER-275; THR-292 AND SER-296, 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-50; SER-72; TYR-73;SER-106; SER-119; THR-195; SER-197; THR-199; SER-214; SER-230;SER-235; THR-239; SER-263; SER-269; SER-275; THR-292; SER-306;SER-350; SER-373; THR-412; SER-420; SER-421; THR-424; SER-446;SER-481; THR-507; THR-509; SER-510; THR-793; SER-798 AND SER-899, ANDMASS 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 TYR-73; SER-119; SER-142;SER-143; SER-148; SER-197; THR-199; THR-213; SER-214; THR-219;SER-230; THR-239; SER-263; SER-269; SER-275; SER-291; THR-292;THR-294; SER-296; SER-306; SER-312; SER-314; SER-421; THR-424;SER-481; SER-828; SER-831; THR-832; THR-892; SER-893; SER-894 ANDSER-899, 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-263; SER-269; SER-275;THR-298; SER-312; SER-314 AND SER-421, AND MASS SPECTROMETRY.
"Exploring the functional interactions between Aurora B, INCENP, andsurvivin in mitosis.";
Honda R., Korner R., Nigg E.A.;
Mol. Biol. Cell 14:3325-3341(2003).
Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX,INDUCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-892;SER-893 AND SER-894.
"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 THR-292, AND MASSSPECTROMETRY.

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