TPX2_HUMAN - dbPTM
TPX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPX2_HUMAN
UniProt AC Q9ULW0
Protein Name Targeting protein for Xklp2
Gene Name TPX2
Organism Homo sapiens (Human).
Sequence Length 747
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, it is diffusely distributed throughout the nucl
Protein Description Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. [PubMed: 18663142]
Protein Sequence MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQAIVTPLKPVDNTYYKEAEKENLVEQSIPSNACSSLEVEAAISRKTPAQPQRRSLRLSAQKDLEQKEKHHVKMKAKRCATPVIIDEILPSKKMKVSNNKKKPEEEGSAHQDTAEKNASSPEKAKGRHTVPCMPPAKQKFLKSTEEQELEKSMKMQQEVVEMRKKNEEFKKLALAGIGQPVKKSVSQVTKSVDFHFRTDERIKQHPKNQEEYKEVNFTSELRKHPSSPARVTKGCTIVKPFNLSQGKKRTFDETVSTYVPLAQQVEDFHKRTPNRYHLRSKKDDINLLPSKSSVTKICRDPQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERESKKKTEDEHFEFHSRPCPTKILEDVVGVPEKKVLPITVPKSPAFALKNRIRMPTKEDEEEDEPVVIKAQPVPHYGVPFKPQIPEARTVEICPFSFDSRDKERQLQKEKKIKELQKGEVPKFKALPLPHFDTINLPEKKVKNVTQIEPFCLETDRRGALKAQTWKHQLEEELRQQKEAACFKARPNTVISQEPFVPKKEKKSVAEGLSGSLVQEPFQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQPLTVPVSPKFSTRFHC
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
6Phosphorylation--MSQVKSSYSYDAP
--CCCCCCCCCCCCC		35.3328102081
7Phosphorylation-MSQVKSSYSYDAPS
-CCCCCCCCCCCCCC		16.6328102081
8PhosphorylationMSQVKSSYSYDAPSD
CCCCCCCCCCCCCCC		20.5228102081
9PhosphorylationSQVKSSYSYDAPSDF
CCCCCCCCCCCCCCC		20.6328102081
10PhosphorylationQVKSSYSYDAPSDFI
CCCCCCCCCCCCCCC		14.1128102081
14PhosphorylationSYSYDAPSDFINFSS
CCCCCCCCCCCCHHH		47.0428102081
20PhosphorylationPSDFINFSSLDDEGD
CCCCCCHHHCCCCCC		26.0419007248
21PhosphorylationSDFINFSSLDDEGDT
CCCCCHHHCCCCCCC		31.5119007248
28PhosphorylationSLDDEGDTQNIDSWF
HCCCCCCCCCHHHHH		34.0819007248
33PhosphorylationGDTQNIDSWFEEKAN
CCCCCHHHHHHHHHC		29.8419007248
44UbiquitinationEKANLENKLLGKNGT
HHHCCCHHHCCCCCC		35.4021890473
48SumoylationLENKLLGKNGTGGLF
CCHHHCCCCCCCCCC		52.77-
48SumoylationLENKLLGKNGTGGLF
CCHHHCCCCCCCCCC		52.77-
48UbiquitinationLENKLLGKNGTGGLF
CCHHHCCCCCCCCCC		52.7721890473
51PhosphorylationKLLGKNGTGGLFQGK
HHCCCCCCCCCCCCC		37.1521712546
58AcetylationTGGLFQGKTPLRKAN
CCCCCCCCCCCCCCC		35.87-
58UbiquitinationTGGLFQGKTPLRKAN
CCCCCCCCCCCCCCC		35.87-
58AcetylationTGGLFQGKTPLRKAN
CCCCCCCCCCCCCCC		35.8723749302
58UbiquitinationTGGLFQGKTPLRKAN
CCCCCCCCCCCCCCC		35.87-
59PhosphorylationGGLFQGKTPLRKANL
CCCCCCCCCCCCCCC		34.0925159151
63UbiquitinationQGKTPLRKANLQQAI
CCCCCCCCCCCCHHE		49.67-
63SumoylationQGKTPLRKANLQQAI
CCCCCCCCCCCCHHE		49.67-
63SumoylationQGKTPLRKANLQQAI
CCCCCCCCCCCCHHE		49.67-
63UbiquitinationQGKTPLRKANLQQAI
CCCCCCCCCCCCHHE		49.67-
72PhosphorylationNLQQAIVTPLKPVDN
CCCHHEECCCCCCCC		19.4520201521
75AcetylationQAIVTPLKPVDNTYY
HHEECCCCCCCCCCC		44.17-
75SumoylationQAIVTPLKPVDNTYY
HHEECCCCCCCCCCC		44.17-
75AcetylationQAIVTPLKPVDNTYY
HHEECCCCCCCCCCC		44.1721339330
75SumoylationQAIVTPLKPVDNTYY
HHEECCCCCCCCCCC		44.17-
75UbiquitinationQAIVTPLKPVDNTYY
HHEECCCCCCCCCCC		44.1721890473
80PhosphorylationPLKPVDNTYYKEAEK
CCCCCCCCCCHHHHH		24.6224732914
81PhosphorylationLKPVDNTYYKEAEKE
CCCCCCCCCHHHHHC		20.8524732914
82PhosphorylationKPVDNTYYKEAEKEN
CCCCCCCCHHHHHCC		10.5824732914
94PhosphorylationKENLVEQSIPSNACS
HCCCCCCCCCCCHHH		23.9819007248
101PhosphorylationSIPSNACSSLEVEAA
CCCCCHHHCCHHHHH		35.2325159151
102PhosphorylationIPSNACSSLEVEAAI
CCCCHHHCCHHHHHH		28.5625159151
110PhosphorylationLEVEAAISRKTPAQP
CHHHHHHCCCCCCCC		24.0127282143
113PhosphorylationEAAISRKTPAQPQRR
HHHHCCCCCCCCCHH		23.8128985074
121PhosphorylationPAQPQRRSLRLSAQK
CCCCCHHHHHHHHHH		21.7423401153
125PhosphorylationQRRSLRLSAQKDLEQ
CHHHHHHHHHHHHHH		23.4023401153
128AcetylationSLRLSAQKDLEQKEK
HHHHHHHHHHHHHHH		65.09-
128AcetylationSLRLSAQKDLEQKEK
HHHHHHHHHHHHHHH		65.0923749302
147PhosphorylationMKAKRCATPVIIDEI
HHHHHCCCCCHHHHH		23.0129255136
157PhosphorylationIIDEILPSKKMKVSN
HHHHHCCCCCCCCCC		41.2722199227
158AcetylationIDEILPSKKMKVSNN
HHHHCCCCCCCCCCC		55.7525953088
163PhosphorylationPSKKMKVSNNKKKPE
CCCCCCCCCCCCCHH		29.2122496350
174PhosphorylationKKPEEEGSAHQDTAE
CCHHHCCCCCHHHHH		26.3424732914
179PhosphorylationEGSAHQDTAEKNASS
CCCCCHHHHHHHCCC		30.1024732914
185PhosphorylationDTAEKNASSPEKAKG
HHHHHHCCCHHHHCC		56.6828176443
186PhosphorylationTAEKNASSPEKAKGR
HHHHHCCCHHHHCCC		34.3728176443
195PhosphorylationEKAKGRHTVPCMPPA
HHHCCCCCCCCCCHH		25.4528555341
203UbiquitinationVPCMPPAKQKFLKST
CCCCCHHHHHHHCCH		60.85-
208SumoylationPAKQKFLKSTEEQEL
HHHHHHHCCHHHHHH		59.47-
208AcetylationPAKQKFLKSTEEQEL
HHHHHHHCCHHHHHH		59.4726051181
208SumoylationPAKQKFLKSTEEQEL
HHHHHHHCCHHHHHH		59.47-
209PhosphorylationAKQKFLKSTEEQELE
HHHHHHCCHHHHHHH		43.1025159151
210PhosphorylationKQKFLKSTEEQELEK
HHHHHCCHHHHHHHH		41.7920068231
218PhosphorylationEEQELEKSMKMQQEV
HHHHHHHHHHHHHHH		17.7929214152
220SumoylationQELEKSMKMQQEVVE
HHHHHHHHHHHHHHH		40.42-
220SumoylationQELEKSMKMQQEVVE
HHHHHHHHHHHHHHH		40.42-
237SumoylationKKNEEFKKLALAGIG
HCCHHHHHHHHCCCC		44.29-
237SumoylationKKNEEFKKLALAGIG
HCCHHHHHHHHCCCC		44.29-
248AcetylationAGIGQPVKKSVSQVT
CCCCCCCHHCHHHHH		46.1125953088
249AcetylationGIGQPVKKSVSQVTK
CCCCCCHHCHHHHHH		57.2226051181
249SuccinylationGIGQPVKKSVSQVTK
CCCCCCHHCHHHHHH		57.2227452117
250PhosphorylationIGQPVKKSVSQVTKS
CCCCCHHCHHHHHHC		22.6829214152
252PhosphorylationQPVKKSVSQVTKSVD
CCCHHCHHHHHHCCE		26.4829214152
255PhosphorylationKKSVSQVTKSVDFHF
HHCHHHHHHCCEEEC		15.2329214152
256SumoylationKSVSQVTKSVDFHFR
HCHHHHHHCCEEECC		50.02-
256AcetylationKSVSQVTKSVDFHFR
HCHHHHHHCCEEECC		50.0225953088
256SumoylationKSVSQVTKSVDFHFR
HCHHHHHHCCEEECC		50.02-
257PhosphorylationSVSQVTKSVDFHFRT
CHHHHHHCCEEECCC		19.9722617229
264PhosphorylationSVDFHFRTDERIKQH
CCEEECCCHHHHHHC		41.0725159151
278PhosphorylationHPKNQEEYKEVNFTS
CCCCHHHHHHCCCCH		16.2328796482
279SumoylationPKNQEEYKEVNFTSE
CCCHHHHHHCCCCHH		59.47-
279SumoylationPKNQEEYKEVNFTSE
CCCHHHHHHCCCCHH		59.47-
279UbiquitinationPKNQEEYKEVNFTSE
CCCHHHHHHCCCCHH		59.47-
284PhosphorylationEYKEVNFTSELRKHP
HHHHCCCCHHHHHCC		18.9826074081
285PhosphorylationYKEVNFTSELRKHPS
HHHCCCCHHHHHCCC		30.4225159151
288MethylationVNFTSELRKHPSSPA
CCCCHHHHHCCCCCC		31.05115918865
292PhosphorylationSELRKHPSSPARVTK
HHHHHCCCCCCCCCC		48.9930266825
293PhosphorylationELRKHPSSPARVTKG
HHHHCCCCCCCCCCC		27.3430266825
298PhosphorylationPSSPARVTKGCTIVK
CCCCCCCCCCCEEEE		19.0326074081
302PhosphorylationARVTKGCTIVKPFNL
CCCCCCCEEEECCCC		37.1628555341
305AcetylationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.79-
305UbiquitinationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.79-
305SumoylationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.79-
305AcetylationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.7919608861
305SumoylationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.7919608861
305UbiquitinationTKGCTIVKPFNLSQG
CCCCEEEECCCCCCC		39.7919608861
310PhosphorylationIVKPFNLSQGKKRTF
EEECCCCCCCCCCCC		37.6825159151
313AcetylationPFNLSQGKKRTFDET
CCCCCCCCCCCCCCH		31.2925953088
313UbiquitinationPFNLSQGKKRTFDET
CCCCCCCCCCCCCCH		31.29-
314AcetylationFNLSQGKKRTFDETV
CCCCCCCCCCCCCHH		64.5930586073
316PhosphorylationLSQGKKRTFDETVST
CCCCCCCCCCCHHHH		44.3024732914
320PhosphorylationKKRTFDETVSTYVPL
CCCCCCCHHHHHHHH		22.9224732914
322PhosphorylationRTFDETVSTYVPLAQ
CCCCCHHHHHHHHHH		22.8028796482
323PhosphorylationTFDETVSTYVPLAQQ
CCCCHHHHHHHHHHH		24.9728796482
324PhosphorylationFDETVSTYVPLAQQV
CCCHHHHHHHHHHHH		7.8028796482
336UbiquitinationQQVEDFHKRTPNRYH
HHHHHHHHHCCCCCC		58.94-
338PhosphorylationVEDFHKRTPNRYHLR
HHHHHHHCCCCCCCC		29.7123401153
342PhosphorylationHKRTPNRYHLRSKKD
HHHCCCCCCCCCCCC		16.3120860994
346PhosphorylationPNRYHLRSKKDDINL
CCCCCCCCCCCCCCC		50.8720860994
348UbiquitinationRYHLRSKKDDINLLP
CCCCCCCCCCCCCCC		62.98-
356PhosphorylationDDINLLPSKSSVTKI
CCCCCCCCCCCHHHH		45.1826055452
357AcetylationDINLLPSKSSVTKIC
CCCCCCCCCCHHHHH		44.8225953088
357UbiquitinationDINLLPSKSSVTKIC
CCCCCCCCCCHHHHH		44.82-
358PhosphorylationINLLPSKSSVTKICR
CCCCCCCCCHHHHHC		34.0925159151
359PhosphorylationNLLPSKSSVTKICRD
CCCCCCCCHHHHHCC		37.2325159151
361PhosphorylationLPSKSSVTKICRDPQ
CCCCCCHHHHHCCCC		19.3524732914
362AcetylationPSKSSVTKICRDPQT
CCCCCHHHHHCCCCC		37.3425953088
369PhosphorylationKICRDPQTPVLQTKH
HHHCCCCCCCCCCCH		22.2829255136
370 (in isoform 2)Phosphorylation-21.4120860994
374PhosphorylationPQTPVLQTKHRARAV
CCCCCCCCCHHCCCC		25.3423927012
375AcetylationQTPVLQTKHRARAVT
CCCCCCCCHHCCCCC		20.3823749302
375UbiquitinationQTPVLQTKHRARAVT
CCCCCCCCHHCCCCC		20.38-
375 (in isoform 2)Phosphorylation-20.3821712546
382PhosphorylationKHRARAVTCKSTAEL
CHHCCCCCCCCCCHH		17.15-
384SumoylationRARAVTCKSTAELEA
HCCCCCCCCCCHHCH		41.28-
384AcetylationRARAVTCKSTAELEA
HCCCCCCCCCCHHCH		41.2825953088
384SumoylationRARAVTCKSTAELEA
HCCCCCCCCCCHHCH		41.28-
385PhosphorylationARAVTCKSTAELEAE
CCCCCCCCCCHHCHH		34.6919691289
386PhosphorylationRAVTCKSTAELEAEE
CCCCCCCCCHHCHHH		15.0519691289
396UbiquitinationLEAEELEKLQQYKFK
HCHHHHHHHHHHCCH		65.31-
401SumoylationLEKLQQYKFKARELD
HHHHHHHCCHHHCCC		35.73-
401AcetylationLEKLQQYKFKARELD
HHHHHHHCCHHHCCC		35.7326051181
401SumoylationLEKLQQYKFKARELD
HHHHHHHCCHHHCCC		35.73-
411AcetylationARELDPRILEGGPIL
HHCCCHHHHCCCCCC		5.10-
420UbiquitinationEGGPILPKKPPVKPP
CCCCCCCCCCCCCCC		74.58-
421UbiquitinationGGPILPKKPPVKPPT
CCCCCCCCCCCCCCC		53.25-
428PhosphorylationKPPVKPPTEPIGFDL
CCCCCCCCCCCCCCH		64.0220068231
439AcetylationGFDLEIEKRIQERES
CCCHHHHHHHHHHHH		61.5426051181
450PhosphorylationERESKKKTEDEHFEF
HHHHCCCCCCHHCCH		58.5128555341
465UbiquitinationHSRPCPTKILEDVVG
HCCCCCCCHHHHHCC		30.36-
476SumoylationDVVGVPEKKVLPITV
HHCCCCCCCEEEEEC		41.95-
476AcetylationDVVGVPEKKVLPITV
HHCCCCCCCEEEEEC		41.9523749302
476SumoylationDVVGVPEKKVLPITV
HHCCCCCCCEEEEEC		41.95-
477SumoylationVVGVPEKKVLPITVP
HCCCCCCCEEEEECC		47.55-
477SumoylationVVGVPEKKVLPITVP
HCCCCCCCEEEEECC		47.5528112733
482PhosphorylationEKKVLPITVPKSPAF
CCCEEEEECCCCHHH		28.9023927012
485UbiquitinationVLPITVPKSPAFALK
EEEEECCCCHHHHHH		65.81-
486PhosphorylationLPITVPKSPAFALKN
EEEECCCCHHHHHHC		18.5222167270
492SumoylationKSPAFALKNRIRMPT
CCHHHHHHCCCCCCC		40.53-
492AcetylationKSPAFALKNRIRMPT
CCHHHHHHCCCCCCC		40.5325953088
492SumoylationKSPAFALKNRIRMPT
CCHHHHHHCCCCCCC		40.53-
492UbiquitinationKSPAFALKNRIRMPT
CCHHHHHHCCCCCCC		40.53-
499PhosphorylationKNRIRMPTKEDEEED
HCCCCCCCCCCCCCC		37.4127273156
500SumoylationNRIRMPTKEDEEEDE
CCCCCCCCCCCCCCC		58.24-
500AcetylationNRIRMPTKEDEEEDE
CCCCCCCCCCCCCCC		58.2426051181
500SumoylationNRIRMPTKEDEEEDE
CCCCCCCCCCCCCCC		58.2428112733
512AcetylationEDEPVVIKAQPVPHY
CCCCEEEECEECCCC		29.38-
512UbiquitinationEDEPVVIKAQPVPHY
CCCCEEEECEECCCC		29.38-
519PhosphorylationKAQPVPHYGVPFKPQ
ECEECCCCCCCCCCC		17.4728796482
524AcetylationPHYGVPFKPQIPEAR
CCCCCCCCCCCCCCC		29.9123749302
524UbiquitinationPHYGVPFKPQIPEAR
CCCCCCCCCCCCCCC		29.9121890473
536GlutathionylationEARTVEICPFSFDSR
CCCEEEECCCCCCCH		1.4422555962
539PhosphorylationTVEICPFSFDSRDKE
EEEECCCCCCCHHHH		17.1824732914
542PhosphorylationICPFSFDSRDKERQL
ECCCCCCCHHHHHHH		40.1325159151
560AcetylationKKIKELQKGEVPKFK
HHHHHHHCCCCCCCC		70.44-
560SumoylationKKIKELQKGEVPKFK
HHHHHHHCCCCCCCC		70.44-
560SumoylationKKIKELQKGEVPKFK
HHHHHHHCCCCCCCC		70.44-
560UbiquitinationKKIKELQKGEVPKFK
HHHHHHHCCCCCCCC		70.44-
565SumoylationLQKGEVPKFKALPLP
HHCCCCCCCCCCCCC		65.75-
565SumoylationLQKGEVPKFKALPLP
HHCCCCCCCCCCCCC		65.75-
567SumoylationKGEVPKFKALPLPHF
CCCCCCCCCCCCCCC		55.96-
567SumoylationKGEVPKFKALPLPHF
CCCCCCCCCCCCCCC		55.96-
567UbiquitinationKGEVPKFKALPLPHF
CCCCCCCCCCCCCCC		55.9621890473
576PhosphorylationLPLPHFDTINLPEKK
CCCCCCCCCCCCHHH		15.7228555341
582AcetylationDTINLPEKKVKNVTQ
CCCCCCHHHCCCCCE		62.0123749302
585SumoylationNLPEKKVKNVTQIEP
CCCHHHCCCCCEECC		55.36-
585SumoylationNLPEKKVKNVTQIEP
CCCHHHCCCCCEECC		55.36-
585UbiquitinationNLPEKKVKNVTQIEP
CCCHHHCCCCCEECC		55.36-
588PhosphorylationEKKVKNVTQIEPFCL
HHHCCCCCEECCEEE		32.9728555341
604SumoylationTDRRGALKAQTWKHQ
CCCCCHHHHHHHHHH		37.60-
604AcetylationTDRRGALKAQTWKHQ
CCCCCHHHHHHHHHH		37.6025953088
604MethylationTDRRGALKAQTWKHQ
CCCCCHHHHHHHHHH		37.60110879389
604SumoylationTDRRGALKAQTWKHQ
CCCCCHHHHHHHHHH		37.60-
604UbiquitinationTDRRGALKAQTWKHQ
CCCCCHHHHHHHHHH		37.60-
609AcetylationALKAQTWKHQLEEEL
HHHHHHHHHHHHHHH		25.5125953088
609UbiquitinationALKAQTWKHQLEEEL
HHHHHHHHHHHHHHH		25.51-
617MethylationHQLEEELRQQKEAAC
HHHHHHHHHHHHHHH		39.91115918869
618AcetylationQLEEELRQQKEAACF
HHHHHHHHHHHHHHH		71.91-
620UbiquitinationEEELRQQKEAACFKA
HHHHHHHHHHHHHHC		40.77-
631PhosphorylationCFKARPNTVISQEPF
HHHCCCCCCCCCCCC		23.1526714015
634PhosphorylationARPNTVISQEPFVPK
CCCCCCCCCCCCCCH		24.9317525332
641SumoylationSQEPFVPKKEKKSVA
CCCCCCCHHHHCCHH		69.16-
641SumoylationSQEPFVPKKEKKSVA
CCCCCCCHHHHCCHH		69.1628112733
641UbiquitinationSQEPFVPKKEKKSVA
CCCCCCCHHHHCCHH		69.16-
645SumoylationFVPKKEKKSVAEGLS
CCCHHHHCCHHHHCC		51.78-
645SumoylationFVPKKEKKSVAEGLS
CCCHHHHCCHHHHCC		51.78-
645UbiquitinationFVPKKEKKSVAEGLS
CCCHHHHCCHHHHCC		51.78-
646PhosphorylationVPKKEKKSVAEGLSG
CCHHHHCCHHHHCCC		37.3121712546
652PhosphorylationKSVAEGLSGSLVQEP
CCHHHHCCCCHHHHH		36.8723401153
654PhosphorylationVAEGLSGSLVQEPFQ
HHHHCCCCHHHHHHH		23.2223401153
664PhosphorylationQEPFQLATEKRAKER
HHHHHHHHHHHHHHH		51.1127542207
666SumoylationPFQLATEKRAKERQE
HHHHHHHHHHHHHHH		53.99-
666AcetylationPFQLATEKRAKERQE
HHHHHHHHHHHHHHH		53.9926051181
666SumoylationPFQLATEKRAKERQE
HHHHHHHHHHHHHHH		53.99-
666UbiquitinationPFQLATEKRAKERQE
HHHHHHHHHHHHHHH		53.99-
685UbiquitinationMAEVEAQKAQQLEEA
HHHHHHHHHHHHHHH		56.03-
700AcetylationRLQEEEQKKEELARL
HHHHHHHHHHHHHHH		66.4926051181
714UbiquitinationLRRELVHKANPIRKY
HHHHHHHHHCCCHHC		42.24-
720SumoylationHKANPIRKYQGLEIK
HHHCCCHHCCCCEEC		42.52-
720SumoylationHKANPIRKYQGLEIK
HHHCCCHHCCCCEEC		42.52-
720UbiquitinationHKANPIRKYQGLEIK
HHHCCCHHCCCCEEC		42.52-
721PhosphorylationKANPIRKYQGLEIKS
HHCCCHHCCCCEECC		9.66-
727SumoylationKYQGLEIKSSDQPLT
HCCCCEECCCCCCCE		34.23-
727SumoylationKYQGLEIKSSDQPLT
HCCCCEECCCCCCCE		34.23-
727UbiquitinationKYQGLEIKSSDQPLT
HCCCCEECCCCCCCE		34.23-
728PhosphorylationYQGLEIKSSDQPLTV
CCCCEECCCCCCCEE		44.8223927012
729PhosphorylationQGLEIKSSDQPLTVP
CCCEECCCCCCCEEE		34.9523927012
734PhosphorylationKSSDQPLTVPVSPKF
CCCCCCCEEECCCCC		29.4630266825
738PhosphorylationQPLTVPVSPKFSTRF
CCCEEECCCCCCCCC		19.1219664994
740SumoylationLTVPVSPKFSTRFHC
CEEECCCCCCCCCCC		44.43-
740AcetylationLTVPVSPKFSTRFHC
CEEECCCCCCCCCCC		44.4325953088
740SumoylationLTVPVSPKFSTRFHC
CEEECCCCCCCCCCC		44.4328112733
740UbiquitinationLTVPVSPKFSTRFHC
CEEECCCCCCCCCCC		44.43-
742PhosphorylationVPVSPKFSTRFHC--
EECCCCCCCCCCC--		25.4624732914
743PhosphorylationPVSPKFSTRFHC---
ECCCCCCCCCCC---		40.2524732914
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
72TPhosphorylationKinaseCDK1P06493
PSP
72TPhosphorylationKinaseCDK2P24941
PSP
121SPhosphorylationKinaseAURKAO14965
GPS
125SPhosphorylationKinaseAURKAO14965
GPS
486SPhosphorylationKinaseCDK5Q00535
PSP
738SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:16287863
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPX2_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 TPX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FZR1_HUMANFZR1physical
16287863
IMA5_HUMANKPNA1physical
14600264
IMB1_HUMANKPNB1physical
14600264
AURKA_HUMANAURKAphysical
14600264
HMMR_HUMANHMMRphysical
22110403
AURKA_HUMANAURKAphysical
22110403
BRCA1_HUMANBRCA1physical
22110403
ZN598_HUMANZNF598physical
22939629
UBE2S_HUMANUBE2Sphysical
22939629
TWF1_HUMANTWF1physical
22939629
IKKB_HUMANIKBKBphysical
17939994
IKKA_HUMANCHUKphysical
17939994
NEMO_HUMANIKBKGphysical
17939994
AFAP1_HUMANAFAP1physical
26496610
SP130_HUMANSAP130physical
26496610
AURKA_HUMANAURKAphysical
26831064
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 TPX2_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-305, 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 THR-72 AND SER-738, 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-738, AND MASSSPECTROMETRY.
"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-738, 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 THR-59; THR-72; SER-121;SER-125; SER-257; SER-310; THR-338; SER-486 AND SER-738, 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-121; SER-125; SER-185;SER-293; SER-486 AND SER-738, 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-20; SER-21; THR-28;SER-33; THR-51; THR-72; SER-94; THR-113; SER-121; SER-125; THR-179;SER-185; SER-186; SER-209; SER-218; SER-250; SER-293; THR-369;THR-374; SER-486; SER-652 AND SER-738, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, 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-121 AND SER-125, ANDMASS 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-486, 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 THR-51; THR-72; SER-121;SER-125; THR-147; SER-186; SER-293; THR-338; SER-359; THR-369;THR-374; SER-486; SER-542; SER-652; SER-654 AND SER-738, AND MASSSPECTROMETRY.
"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 THR-369; SER-486 ANDSER-738, 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-293, 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-738, AND MASSSPECTROMETRY.

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