CHAP1_HUMAN - dbPTM
CHAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHAP1_HUMAN
UniProt AC Q96JM3
Protein Name Chromosome alignment-maintaining phosphoprotein 1
Gene Name CHAMP1
Organism Homo sapiens (Human).
Sequence Length 812
Subcellular Localization Nucleus . Chromosome . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle .
Protein Description Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore..
Protein Sequence MEAFQELRKPSARLECDHCSFRGTDYENVQIHMGTIHPEFCDEMDAGGLGKMIFYQKSAKLFHCHKCFFTSKMYSNVYYHITSKHASPDKWNDKPKNQLNKETDPVKSPPLPEHQKIPCNSAEPKSIPALSMETQKLGSVLSPESPKPTPLTPLEPQKPGSVVSPELQTPLPSPEPSKPASVSSPEPPKSVPVCESQKLAPVPSPEPQKPAPVSPESVKATLSNPKPQKQSHFPETLGPPSASSPESPVLAASPEPWGPSPAASPESRKSARTTSPEPRKPSPSESPEPWKPFPAVSPEPRRPAPAVSPGSWKPGPPGSPRPWKSNPSASSGPWKPAKPAPSVSPGPWKPIPSVSPGPWKPTPSVSSASWKSSSVSPSSWKSPPASPESWKSGPPELRKTAPTLSPEHWKAVPPVSPELRKPGPPLSPEIRSPAGSPELRKPSGSPDLWKLSPDQRKTSPASLDFPESQKSSRGGSPDLWKSSFFIEPQKPVFPETRKPGPSGPSESPKAASDIWKPVLSIDTEPRKPALFPEPAKTAPPASPEARKRALFPEPRKHALFPELPKSALFSESQKAVELGDELQIDAIDDQKCDILVQEELLASPKKLLEDTLFPSSKKLKKDNQESSDAELSSSEYIKTDLDAMDIKGQESSSDQEQVDVESIDFSKENKMDMTSPEQSRNVLQFTEEKEAFISEEEIAKYMKRGKGKYYCKICCCRAMKKGAVLHHLVNKHNVHSPYKCTICGKAFLLESLLKNHVAAHGQSLLKCPRCNFESNFPRGFKKHLTHCQSRHNEEANKKLMEALEPPLEEQQI
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-------MEAFQELR
-------CHHHHHHH		8.2722814378
20PhosphorylationRLECDHCSFRGTDYE
CEECCCCCCCCCCHH		17.9828348404
35PhosphorylationNVQIHMGTIHPEFCD
CEEEEEECCCHHHCC		14.45-
60UbiquitinationIFYQKSAKLFHCHKC
HEHHHCCCEEECEEC		59.7929967540
66UbiquitinationAKLFHCHKCFFTSKM
CCEEECEECCCCCCC		37.8222817900
87PhosphorylationHITSKHASPDKWNDK
EECCCCCCCCCCCCC		33.0923401153
90UbiquitinationSKHASPDKWNDKPKN
CCCCCCCCCCCCCCH		51.8129967540
103PhosphorylationKNQLNKETDPVKSPP
CHHCCCCCCCCCCCC		47.4123927012
107UbiquitinationNKETDPVKSPPLPEH
CCCCCCCCCCCCCHH		63.7329967540
107AcetylationNKETDPVKSPPLPEH
CCCCCCCCCCCCCHH		63.7325953088
108PhosphorylationKETDPVKSPPLPEHQ
CCCCCCCCCCCCHHC		31.8029255136
116UbiquitinationPPLPEHQKIPCNSAE
CCCCHHCCCCCCCCC		50.9929967540
116AcetylationPPLPEHQKIPCNSAE
CCCCHHCCCCCCCCC		50.9925953088
121PhosphorylationHQKIPCNSAEPKSIP
HCCCCCCCCCCCCCC		40.5028985074
126PhosphorylationCNSAEPKSIPALSME
CCCCCCCCCCCCCCC		44.5127251275
131PhosphorylationPKSIPALSMETQKLG
CCCCCCCCCCCHHCC		19.3727251275
134PhosphorylationIPALSMETQKLGSVL
CCCCCCCCHHCCCCC		23.5126074081
136UbiquitinationALSMETQKLGSVLSP
CCCCCCHHCCCCCCC		63.3329967540
139PhosphorylationMETQKLGSVLSPESP
CCCHHCCCCCCCCCC		30.2623898821
142PhosphorylationQKLGSVLSPESPKPT
HHCCCCCCCCCCCCC		25.1925159151
145PhosphorylationGSVLSPESPKPTPLT
CCCCCCCCCCCCCCC		41.4225159151
149PhosphorylationSPESPKPTPLTPLEP
CCCCCCCCCCCCCCC		36.7425159151
152PhosphorylationSPKPTPLTPLEPQKP
CCCCCCCCCCCCCCC		27.3425159151
161PhosphorylationLEPQKPGSVVSPELQ
CCCCCCCCCCCCCCC		28.0730576142
164PhosphorylationQKPGSVVSPELQTPL
CCCCCCCCCCCCCCC		15.5325159151
169PhosphorylationVVSPELQTPLPSPEP
CCCCCCCCCCCCCCC		39.1425159151
173PhosphorylationELQTPLPSPEPSKPA
CCCCCCCCCCCCCCC		49.9725159151
177PhosphorylationPLPSPEPSKPASVSS
CCCCCCCCCCCCCCC		50.0030576142
181PhosphorylationPEPSKPASVSSPEPP
CCCCCCCCCCCCCCC		30.9330576142
183PhosphorylationPSKPASVSSPEPPKS
CCCCCCCCCCCCCCC		37.3725159151
184PhosphorylationSKPASVSSPEPPKSV
CCCCCCCCCCCCCCC		31.0025159151
190PhosphorylationSSPEPPKSVPVCESQ
CCCCCCCCCCCCCCC		37.1125159151
196PhosphorylationKSVPVCESQKLAPVP
CCCCCCCCCCCCCCC		27.7326074081
204PhosphorylationQKLAPVPSPEPQKPA
CCCCCCCCCCCCCCC		41.9729255136
214PhosphorylationPQKPAPVSPESVKAT
CCCCCCCCHHHHHHH		23.1429255136
217PhosphorylationPAPVSPESVKATLSN
CCCCCHHHHHHHHCC		32.1029255136
221PhosphorylationSPESVKATLSNPKPQ
CHHHHHHHHCCCCCC		25.6330266825
223PhosphorylationESVKATLSNPKPQKQ
HHHHHHHCCCCCCCC		46.8930266825
226AcetylationKATLSNPKPQKQSHF
HHHHCCCCCCCCCCC		65.4225953088
231PhosphorylationNPKPQKQSHFPETLG
CCCCCCCCCCCCCCC		33.8530108239
236PhosphorylationKQSHFPETLGPPSAS
CCCCCCCCCCCCCCC		36.9330266825
241PhosphorylationPETLGPPSASSPESP
CCCCCCCCCCCCCCC		43.8726657352
243PhosphorylationTLGPPSASSPESPVL
CCCCCCCCCCCCCCE		51.2530266825
244PhosphorylationLGPPSASSPESPVLA
CCCCCCCCCCCCCEE		32.1930266825
247PhosphorylationPSASSPESPVLAASP
CCCCCCCCCCEECCC		24.5623401153
253PhosphorylationESPVLAASPEPWGPS
CCCCEECCCCCCCCC		24.9630266825
260PhosphorylationSPEPWGPSPAASPES
CCCCCCCCCCCCHHH		24.1930266825
264PhosphorylationWGPSPAASPESRKSA
CCCCCCCCHHHHHCC		31.1630266825
267PhosphorylationSPAASPESRKSARTT
CCCCCHHHHHCCCCC		48.6820363803
270PhosphorylationASPESRKSARTTSPE
CCHHHHHCCCCCCCC		23.1330177828
273PhosphorylationESRKSARTTSPEPRK
HHHHCCCCCCCCCCC		31.2030266825
274PhosphorylationSRKSARTTSPEPRKP
HHHCCCCCCCCCCCC		36.4130266825
275PhosphorylationRKSARTTSPEPRKPS
HHCCCCCCCCCCCCC		27.0130266825
282PhosphorylationSPEPRKPSPSESPEP
CCCCCCCCCCCCCCC		44.0622167270
284PhosphorylationEPRKPSPSESPEPWK
CCCCCCCCCCCCCCC		55.8522167270
286PhosphorylationRKPSPSESPEPWKPF
CCCCCCCCCCCCCCC		38.6122167270
297PhosphorylationWKPFPAVSPEPRRPA
CCCCCCCCCCCCCCC		26.1720201521
301MethylationPAVSPEPRRPAPAVS
CCCCCCCCCCCCCCC		56.40115920653
308PhosphorylationRRPAPAVSPGSWKPG
CCCCCCCCCCCCCCC		26.1619664994
311PhosphorylationAPAVSPGSWKPGPPG
CCCCCCCCCCCCCCC		35.0030266825
313AcetylationAVSPGSWKPGPPGSP
CCCCCCCCCCCCCCC		41.6226051181
319PhosphorylationWKPGPPGSPRPWKSN
CCCCCCCCCCCCCCC		24.4122167270
325PhosphorylationGSPRPWKSNPSASSG
CCCCCCCCCCCCCCC		50.5325159151
325O-linked_GlycosylationGSPRPWKSNPSASSG
CCCCCCCCCCCCCCC		50.5332574038
328PhosphorylationRPWKSNPSASSGPWK
CCCCCCCCCCCCCCC		45.0623927012
330PhosphorylationWKSNPSASSGPWKPA
CCCCCCCCCCCCCCC		39.9223927012
331PhosphorylationKSNPSASSGPWKPAK
CCCCCCCCCCCCCCC		48.9025159151
342PhosphorylationKPAKPAPSVSPGPWK
CCCCCCCCCCCCCCC		37.0223927012
344PhosphorylationAKPAPSVSPGPWKPI
CCCCCCCCCCCCCCC		28.6028355574
344O-linked_GlycosylationAKPAPSVSPGPWKPI
CCCCCCCCCCCCCCC		28.6032574038
349AcetylationSVSPGPWKPIPSVSP
CCCCCCCCCCCCCCC		35.8823236377
349UbiquitinationSVSPGPWKPIPSVSP
CCCCCCCCCCCCCCC		35.8829967540
353PhosphorylationGPWKPIPSVSPGPWK
CCCCCCCCCCCCCCC		35.6325159151
355PhosphorylationWKPIPSVSPGPWKPT
CCCCCCCCCCCCCCC		28.6023927012
362PhosphorylationSPGPWKPTPSVSSAS
CCCCCCCCCCCCCCC		25.1922115753
362O-linked_GlycosylationSPGPWKPTPSVSSAS
CCCCCCCCCCCCCCC		25.1932574038
364PhosphorylationGPWKPTPSVSSASWK
CCCCCCCCCCCCCCC		36.7930576142
364O-linked_GlycosylationGPWKPTPSVSSASWK
CCCCCCCCCCCCCCC		36.7932574038
366PhosphorylationWKPTPSVSSASWKSS
CCCCCCCCCCCCCCC		25.2325627689
366O-linked_GlycosylationWKPTPSVSSASWKSS
CCCCCCCCCCCCCCC		25.2332574038
367PhosphorylationKPTPSVSSASWKSSS
CCCCCCCCCCCCCCC		24.9422199227
367O-linked_GlycosylationKPTPSVSSASWKSSS
CCCCCCCCCCCCCCC		24.9432574038
369PhosphorylationTPSVSSASWKSSSVS
CCCCCCCCCCCCCCC		36.6625627689
369O-linked_GlycosylationTPSVSSASWKSSSVS
CCCCCCCCCCCCCCC		36.6632574038
371MethylationSVSSASWKSSSVSPS
CCCCCCCCCCCCCCC		37.65115978091
372PhosphorylationVSSASWKSSSVSPSS
CCCCCCCCCCCCCCC		22.9123927012
373PhosphorylationSSASWKSSSVSPSSW
CCCCCCCCCCCCCCC		30.9123927012
374PhosphorylationSASWKSSSVSPSSWK
CCCCCCCCCCCCCCC		33.4330266825
376PhosphorylationSWKSSSVSPSSWKSP
CCCCCCCCCCCCCCC		22.4725159151
378PhosphorylationKSSSVSPSSWKSPPA
CCCCCCCCCCCCCCC		41.1330266825
379PhosphorylationSSSVSPSSWKSPPAS
CCCCCCCCCCCCCCC		41.7430266825
382PhosphorylationVSPSSWKSPPASPES
CCCCCCCCCCCCHHH		29.8322167270
386PhosphorylationSWKSPPASPESWKSG
CCCCCCCCHHHHHCC		34.6719664994
389PhosphorylationSPPASPESWKSGPPE
CCCCCHHHHHCCCHH		43.0930266825
391UbiquitinationPASPESWKSGPPELR
CCCHHHHHCCCHHHH		55.6129967540
392PhosphorylationASPESWKSGPPELRK
CCHHHHHCCCHHHHH		50.7230266825
398MethylationKSGPPELRKTAPTLS
HCCCHHHHHCCCCCC		32.3981441485
399UbiquitinationSGPPELRKTAPTLSP
CCCHHHHHCCCCCCH		62.7629967540
400PhosphorylationGPPELRKTAPTLSPE
CCHHHHHCCCCCCHH		31.2823927012
403PhosphorylationELRKTAPTLSPEHWK
HHHHCCCCCCHHHHH		37.0922322096
405PhosphorylationRKTAPTLSPEHWKAV
HHCCCCCCHHHHHCC		30.6222322096
416PhosphorylationWKAVPPVSPELRKPG
HHCCCCCCHHHCCCC		20.5929255136
421UbiquitinationPVSPELRKPGPPLSP
CCCHHHCCCCCCCCH		67.9329967540
427PhosphorylationRKPGPPLSPEIRSPA
CCCCCCCCHHHCCCC		26.6829255136
431MethylationPPLSPEIRSPAGSPE
CCCCHHHCCCCCCCH		34.62115920657
432PhosphorylationPLSPEIRSPAGSPEL
CCCHHHCCCCCCCHH		25.4329255136
436PhosphorylationEIRSPAGSPELRKPS
HHCCCCCCCHHCCCC		19.8029255136
443PhosphorylationSPELRKPSGSPDLWK
CCHHCCCCCCCCHHH		55.7422167270
445PhosphorylationELRKPSGSPDLWKLS
HHCCCCCCCCHHHCC		21.4122167270
452PhosphorylationSPDLWKLSPDQRKTS
CCCHHHCCCCCCCCC		23.7822167270
457UbiquitinationKLSPDQRKTSPASLD
HCCCCCCCCCCCCCC		47.9624816145
458PhosphorylationLSPDQRKTSPASLDF
CCCCCCCCCCCCCCC		41.9719664994
459PhosphorylationSPDQRKTSPASLDFP
CCCCCCCCCCCCCCC		22.8529255136
462PhosphorylationQRKTSPASLDFPESQ
CCCCCCCCCCCCHHH		31.6829255136
468PhosphorylationASLDFPESQKSSRGG
CCCCCCHHHHCCCCC		43.0530266825
470UbiquitinationLDFPESQKSSRGGSP
CCCCHHHHCCCCCCC		60.7332015554
471PhosphorylationDFPESQKSSRGGSPD
CCCHHHHCCCCCCCC		20.0323401153
472PhosphorylationFPESQKSSRGGSPDL
CCHHHHCCCCCCCCH		41.8230266825
473MethylationPESQKSSRGGSPDLW
CHHHHCCCCCCCCHH		61.66115920661
476PhosphorylationQKSSRGGSPDLWKSS
HHCCCCCCCCHHHHC		20.3319664994
482PhosphorylationGSPDLWKSSFFIEPQ
CCCCHHHHCEEECCC		22.3126074081
483PhosphorylationSPDLWKSSFFIEPQK
CCCHHHHCEEECCCC		22.0526074081
490AcetylationSFFIEPQKPVFPETR
CEEECCCCCCCCCCC		54.5919608861
490SumoylationSFFIEPQKPVFPETR
CEEECCCCCCCCCCC		54.59-
490SumoylationSFFIEPQKPVFPETR
CEEECCCCCCCCCCC		54.5928112733
490UbiquitinationSFFIEPQKPVFPETR
CEEECCCCCCCCCCC		54.5923000965
496PhosphorylationQKPVFPETRKPGPSG
CCCCCCCCCCCCCCC		44.2025159151
502PhosphorylationETRKPGPSGPSESPK
CCCCCCCCCCCCCCC		70.0630266825
505PhosphorylationKPGPSGPSESPKAAS
CCCCCCCCCCCCHHH		54.9930266825
507PhosphorylationGPSGPSESPKAASDI
CCCCCCCCCCHHHHH		35.7229255136
512PhosphorylationSESPKAASDIWKPVL
CCCCCHHHHHCCCCC		34.1930266825
516UbiquitinationKAASDIWKPVLSIDT
CHHHHHCCCCCCCCC		26.1129967540
516AcetylationKAASDIWKPVLSIDT
CHHHHHCCCCCCCCC		26.1125953088
520PhosphorylationDIWKPVLSIDTEPRK
HHCCCCCCCCCCCCC		20.7430266825
523PhosphorylationKPVLSIDTEPRKPAL
CCCCCCCCCCCCCCC		46.3430266825
537PhosphorylationLFPEPAKTAPPASPE
CCCCCCCCCCCCCHH		46.6423927012
542PhosphorylationAKTAPPASPEARKRA
CCCCCCCCHHHHHHH		29.1029255136
556MethylationALFPEPRKHALFPEL
HCCCCCCHHHCCCCC		43.90115978099
556UbiquitinationALFPEPRKHALFPEL
HCCCCCCHHHCCCCC		43.9029967540
556AcetylationALFPEPRKHALFPEL
HCCCCCCHHHCCCCC		43.9026051181
565SumoylationALFPELPKSALFSES
HCCCCCCHHHHCCHH		62.07-
565SumoylationALFPELPKSALFSES
HCCCCCCHHHHCCHH		62.0728112733
565UbiquitinationALFPELPKSALFSES
HCCCCCCHHHHCCHH		62.0729967540
566PhosphorylationLFPELPKSALFSESQ
CCCCCCHHHHCCHHH		28.4120068231
570PhosphorylationLPKSALFSESQKAVE
CCHHHHCCHHHHHHH		36.8723663014
572PhosphorylationKSALFSESQKAVELG
HHHHCCHHHHHHHHC		35.4630266825
574UbiquitinationALFSESQKAVELGDE
HHCCHHHHHHHHCCC		64.7732015554
603PhosphorylationVQEELLASPKKLLED
HHHHHHHCHHHHHHH		36.9019664994
606SumoylationELLASPKKLLEDTLF
HHHHCHHHHHHHCCC		62.7828112733
611PhosphorylationPKKLLEDTLFPSSKK
HHHHHHHCCCCCCCC		22.4130266825
615PhosphorylationLEDTLFPSSKKLKKD
HHHCCCCCCCCCCCC		47.6730266825
616PhosphorylationEDTLFPSSKKLKKDN
HHCCCCCCCCCCCCC		33.7630266825
617AcetylationDTLFPSSKKLKKDNQ
HCCCCCCCCCCCCCC		67.4723236377
617UbiquitinationDTLFPSSKKLKKDNQ
HCCCCCCCCCCCCCC		67.4732142685
626PhosphorylationLKKDNQESSDAELSS
CCCCCCCCCCCCCCC		24.6122167270
627PhosphorylationKKDNQESSDAELSSS
CCCCCCCCCCCCCCH		39.8422167270
632PhosphorylationESSDAELSSSEYIKT
CCCCCCCCCHHHHCH		24.2722167270
633PhosphorylationSSDAELSSSEYIKTD
CCCCCCCCHHHHCHH		39.5522167270
634PhosphorylationSDAELSSSEYIKTDL
CCCCCCCHHHHCHHH		30.9222167270
636PhosphorylationAELSSSEYIKTDLDA
CCCCCHHHHCHHHHH		15.0722167270
638SumoylationLSSSEYIKTDLDAMD
CCCHHHHCHHHHHHC		34.7828112733
639PhosphorylationSSSEYIKTDLDAMDI
CCHHHHCHHHHHHCC		32.0325841592
651PhosphorylationMDIKGQESSSDQEQV
HCCCCCCCCCCHHCC		27.5322167270
652PhosphorylationDIKGQESSSDQEQVD
CCCCCCCCCCHHCCC		36.8622167270
653PhosphorylationIKGQESSSDQEQVDV
CCCCCCCCCHHCCCH		53.2222167270
662PhosphorylationQEQVDVESIDFSKEN
HHCCCHHHCCCCHHC		27.5730266825
666PhosphorylationDVESIDFSKENKMDM
CHHHCCCCHHCCCCC		35.0030266825
670SumoylationIDFSKENKMDMTSPE
CCCCHHCCCCCCCHH		37.05-
670SumoylationIDFSKENKMDMTSPE
CCCCHHCCCCCCCHH		37.0528112733
674PhosphorylationKENKMDMTSPEQSRN
HHCCCCCCCHHHHHH		36.5429255136
675PhosphorylationENKMDMTSPEQSRNV
HCCCCCCCHHHHHHH		21.5723401153
679PhosphorylationDMTSPEQSRNVLQFT
CCCCHHHHHHHHHHH		24.9422617229
686PhosphorylationSRNVLQFTEEKEAFI
HHHHHHHHHHHHHCC		30.2121815630
689UbiquitinationVLQFTEEKEAFISEE
HHHHHHHHHHCCCHH		48.3829967540
689SumoylationVLQFTEEKEAFISEE
HHHHHHHHHHCCCHH		48.3828112733
694PhosphorylationEEKEAFISEEEIAKY
HHHHHCCCHHHHHHH		32.2828348404
712AcetylationGKGKYYCKICCCRAM
CCCCEEEEHHEHHHH		23.7425953088
721UbiquitinationCCCRAMKKGAVLHHL
HEHHHHHCCHHHHHH		38.7329967540
736PhosphorylationVNKHNVHSPYKCTIC
HHHCCCCCCCCCCCC		26.1625159151
738PhosphorylationKHNVHSPYKCTICGK
HCCCCCCCCCCCCCH		23.0128985074
751PhosphorylationGKAFLLESLLKNHVA
CHHHHHHHHHHHCHH		38.6824719451
763PhosphorylationHVAAHGQSLLKCPRC
CHHHHCHHHHCCCCC		40.0224719451
766SumoylationAHGQSLLKCPRCNFE
HHCHHHHCCCCCCCC		47.70-
766SumoylationAHGQSLLKCPRCNFE
HHCHHHHCCCCCCCC		47.70-
778MethylationNFESNFPRGFKKHLT
CCCCCCCHHHHHHHH		60.0783108635
782UbiquitinationNFPRGFKKHLTHCQS
CCCHHHHHHHHHHHH		41.4029967540
785PhosphorylationRGFKKHLTHCQSRHN
HHHHHHHHHHHHHCC		21.96-
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 CHAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHAP1_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 CHAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POGZ_HUMANPOGZphysical
20850016
CBX3_HUMANCBX3physical
20850016
ZMYM4_HUMANZMYM4physical
26496610
MCA3_HUMANEEF1E1physical
26496610
GTPB1_HUMANGTPBP1physical
26496610
TBCD4_HUMANTBC1D4physical
26496610
CBX1_HUMANCBX1physical
26496610
CBX3_HUMANCBX3physical
26496610
POGZ_HUMANPOGZphysical
26496610
CBX5_HUMANCBX5physical
26496610
SOSSC_HUMANINIPphysical
26496610
HDGR2_HUMANHDGFRP2physical
26496610
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 CHAP1_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-490, 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-204; SER-214; SER-282;SER-286; SER-297; SER-382; SER-386; SER-427; SER-432; SER-436;SER-452; SER-507; SER-627; SER-651 AND SER-652, 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-204; SER-214; SER-217;SER-282; SER-286; SER-297; SER-376; SER-382; SER-386; SER-416;SER-445; THR-458; SER-459; SER-462; SER-476; SER-507; SER-542;SER-603; SER-627; SER-632; SER-633; SER-652 AND SER-653, 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-87; SER-204; SER-214;SER-282; SER-286; SER-297; SER-308; SER-319; SER-405; SER-416;SER-427; SER-432; SER-436; SER-445; SER-452; SER-459; SER-462;SER-476; SER-627; SER-651; SER-652 AND SER-653, 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-476, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-217; SER-427;SER-432; SER-436 AND SER-476, AND MASS SPECTROMETRY.
"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 SER-223; SER-616 ANDSER-736, 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-476, 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-108; SER-204; SER-217;SER-282; SER-286; SER-308; SER-319; SER-405; SER-427; SER-432;SER-436; SER-445; SER-459; SER-476; SER-507; SER-603; SER-651; SER-652AND SER-653, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-214; SER-275;SER-382; SER-386; SER-436; SER-476; SER-542 AND SER-653, AND MASSSPECTROMETRY.

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