TCPE_HUMAN - dbPTM
TCPE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPE_HUMAN
UniProt AC P48643
Protein Name T-complex protein 1 subunit epsilon
Gene Name CCT5
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin..
Protein Sequence MASMGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE
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
2Acetylation------MASMGTLAF
------CCCCCCEEE		14.2819413330
3Phosphorylation-----MASMGTLAFD
-----CCCCCCEEEC		19.2220068231
4Sulfoxidation----MASMGTLAFDE
----CCCCCCEEECC		3.2728183972
6Phosphorylation--MASMGTLAFDEYG
--CCCCCCEEECCCC		13.2820068231
12PhosphorylationGTLAFDEYGRPFLII
CCEEECCCCCEEEEE		21.9320068231
20SumoylationGRPFLIIKDQDRKSR
CCEEEEEECCCHHHH		42.2028112733
20UbiquitinationGRPFLIIKDQDRKSR
CCEEEEEECCCHHHH		42.20-
25UbiquitinationIIKDQDRKSRLMGLE
EEECCCHHHHHCCHH		48.49-
26PhosphorylationIKDQDRKSRLMGLEA
EECCCHHHHHCCHHH		31.3830266825
27MethylationKDQDRKSRLMGLEAL
ECCCHHHHHCCHHHH		31.56-
29SulfoxidationQDRKSRLMGLEALKS
CCHHHHHCCHHHHHH		5.8321406390
35UbiquitinationLMGLEALKSHIMAAK
HCCHHHHHHHHHHHH		47.2221890473
35UbiquitinationLMGLEALKSHIMAAK
HCCHHHHHHHHHHHH		47.2221890473
35AcetylationLMGLEALKSHIMAAK
HCCHHHHHHHHHHHH		47.2225953088
35UbiquitinationLMGLEALKSHIMAAK
HCCHHHHHHHHHHHH		47.2221890473
39SulfoxidationEALKSHIMAAKAVAN
HHHHHHHHHHHHHHH		2.1930846556
42SumoylationKSHIMAAKAVANTMR
HHHHHHHHHHHHHHH		33.58-
42SumoylationKSHIMAAKAVANTMR
HHHHHHHHHHHHHHH		33.58-
42UbiquitinationKSHIMAAKAVANTMR
HHHHHHHHHHHHHHH		33.5821906983
49MethylationKAVANTMRTSLGPNG
HHHHHHHHHCCCCCC		21.08-
50PhosphorylationAVANTMRTSLGPNGL
HHHHHHHHCCCCCCH		19.9229449344
51PhosphorylationVANTMRTSLGPNGLD
HHHHHHHCCCCCCHH		22.4425159151
57UbiquitinationTSLGPNGLDKMMVDK
HCCCCCCHHCEEECC		7.90-
59AcetylationLGPNGLDKMMVDKDG
CCCCCHHCEEECCCC		33.6627452117
59UbiquitinationLGPNGLDKMMVDKDG
CCCCCHHCEEECCCC		33.66-
64AcetylationLDKMMVDKDGDVTVT
HHCEEECCCCCEEEE		52.8012649881
64UbiquitinationLDKMMVDKDGDVTVT
HHCEEECCCCCEEEE		52.80-
67AcetylationMMVDKDGDVTVTNDG
EEECCCCCEEEECCC		42.94-
67UbiquitinationMMVDKDGDVTVTNDG
EEECCCCCEEEECCC		42.94-
69PhosphorylationVDKDGDVTVTNDGAT
ECCCCCEEEECCCCE		26.7621406692
71PhosphorylationKDGDVTVTNDGATIL
CCCCEEEECCCCEEE		20.4421406692
76PhosphorylationTVTNDGATILSMMDV
EEECCCCEEEEECCH		28.1621406692
77UbiquitinationVTNDGATILSMMDVD
EECCCCEEEEECCHH		2.38-
79PhosphorylationNDGATILSMMDVDHQ
CCCCEEEEECCHHHH		14.2821406692
83UbiquitinationTILSMMDVDHQIAKL
EEEEECCHHHHHHHH		3.73-
117UbiquitinationVVLAGALLEEAEQLL
HHHCHHHHHHHHHHH		5.76-
121UbiquitinationGALLEEAEQLLDRGI
HHHHHHHHHHHHCCC		45.07-
130AcetylationLLDRGIHPIRIADGY
HHHCCCCCEEECCCH		18.68-
130UbiquitinationLLDRGIHPIRIADGY
HHHCCCCCEEECCCH		18.68-
130AcetylationLLDRGIHPIRIADGY
HHHCCCCCEEECCCH		18.6819608861
130UbiquitinationLLDRGIHPIRIADGY
HHHCCCCCEEECCCH		18.6819608861
132MethylationDRGIHPIRIADGYEQ
HCCCCCEEECCCHHH		23.61-
133UbiquitinationRGIHPIRIADGYEQA
CCCCCEEECCCHHHH		4.19-
137PhosphorylationPIRIADGYEQAARVA
CEEECCCHHHHHHHH		12.8628152594
139AcetylationRIADGYEQAARVAIE
EECCCHHHHHHHHHH		31.66-
139UbiquitinationRIADGYEQAARVAIE
EECCCHHHHHHHHHH		31.66-
139AcetylationRIADGYEQAARVAIE
EECCCHHHHHHHHHH		31.6619608861
139UbiquitinationRIADGYEQAARVAIE
EECCCHHHHHHHHHH		31.6619608861
149UbiquitinationRVAIEHLDKISDSVL
HHHHHHHHHCCCEEE		48.42-
1502-HydroxyisobutyrylationVAIEHLDKISDSVLV
HHHHHHHHCCCEEEE		50.93-
150UbiquitinationVAIEHLDKISDSVLV
HHHHHHHHCCCEEEE		50.9321906983
152PhosphorylationIEHLDKISDSVLVDI
HHHHHHCCCEEEEEC		29.5830266825
154UbiquitinationHLDKISDSVLVDIKD
HHHHCCCEEEEECCC		15.57-
154PhosphorylationHLDKISDSVLVDIKD
HHHHCCCEEEEECCC		15.5730266825
160SumoylationDSVLVDIKDTEPLIQ
CEEEEECCCCHHHHH		54.88-
1602-HydroxyisobutyrylationDSVLVDIKDTEPLIQ
CEEEEECCCCHHHHH		54.88-
160AcetylationDSVLVDIKDTEPLIQ
CEEEEECCCCHHHHH		54.8823954790
160SumoylationDSVLVDIKDTEPLIQ
CEEEEECCCCHHHHH		54.88-
160UbiquitinationDSVLVDIKDTEPLIQ
CEEEEECCCCHHHHH		54.8821906983
168UbiquitinationDTEPLIQTAKTTLGS
CCHHHHHHHHHHHCH		24.11-
168PhosphorylationDTEPLIQTAKTTLGS
CCHHHHHHHHHHHCH		24.11-
170UbiquitinationEPLIQTAKTTLGSKV
HHHHHHHHHHHCHHH		45.49-
1702-HydroxyisobutyrylationEPLIQTAKTTLGSKV
HHHHHHHHHHHCHHH		45.49-
170AcetylationEPLIQTAKTTLGSKV
HHHHHHHHHHHCHHH		45.4925953088
170MalonylationEPLIQTAKTTLGSKV
HHHHHHHHHHHCHHH		45.4926320211
170UbiquitinationEPLIQTAKTTLGSKV
HHHHHHHHHHHCHHH		45.49-
171UbiquitinationPLIQTAKTTLGSKVV
HHHHHHHHHHCHHHH		25.4521890473
172AcetylationLIQTAKTTLGSKVVN
HHHHHHHHHCHHHHH		28.54-
172UbiquitinationLIQTAKTTLGSKVVN
HHHHHHHHHCHHHHH		28.54-
176SumoylationAKTTLGSKVVNSCHR
HHHHHCHHHHHHHHH		48.69-
1762-HydroxyisobutyrylationAKTTLGSKVVNSCHR
HHHHHCHHHHHHHHH		48.69-
176AcetylationAKTTLGSKVVNSCHR
HHHHHCHHHHHHHHH		48.6926051181
176SumoylationAKTTLGSKVVNSCHR
HHHHHCHHHHHHHHH		48.69-
176UbiquitinationAKTTLGSKVVNSCHR
HHHHHCHHHHHHHHH		48.69-
177UbiquitinationKTTLGSKVVNSCHRQ
HHHHCHHHHHHHHHH		5.4421890473
181S-nitrosocysteineGSKVVNSCHRQMAEI
CHHHHHHHHHHHHHH		2.30-
181S-nitrosylationGSKVVNSCHRQMAEI
CHHHHHHHHHHHHHH		2.3019483679
182AcetylationSKVVNSCHRQMAEIA
HHHHHHHHHHHHHHH		23.87-
182UbiquitinationSKVVNSCHRQMAEIA
HHHHHHHHHHHHHHH		23.87-
186AcetylationNSCHRQMAEIAVNAV
HHHHHHHHHHHHHHH		9.19-
189UbiquitinationHRQMAEIAVNAVLTV
HHHHHHHHHHHHEHH		4.68-
191UbiquitinationQMAEIAVNAVLTVAD
HHHHHHHHHHEHHHH		18.47-
210UbiquitinationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.0221890473
210SumoylationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.02-
2102-HydroxyisobutyrylationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.02-
210AcetylationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.0226051181
210SumoylationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.0228112733
210UbiquitinationDVDFELIKVEGKVGG
CCCEEEEEEECEECC		47.0221906983
214SumoylationELIKVEGKVGGRLED
EEEEEECEECCCCCC		24.9728112733
214UbiquitinationELIKVEGKVGGRLED
EEEEEECEECCCCCC		24.9721906983
220UbiquitinationGKVGGRLEDTKLIKG
CEECCCCCCCEEEEE		63.3721890473
2232-HydroxyisobutyrylationGGRLEDTKLIKGVIV
CCCCCCCEEEEEEEE		61.61-
223AcetylationGGRLEDTKLIKGVIV
CCCCCCCEEEEEEEE		61.6123749302
223MalonylationGGRLEDTKLIKGVIV
CCCCCCCEEEEEEEE		61.6126320211
223UbiquitinationGGRLEDTKLIKGVIV
CCCCCCCEEEEEEEE		61.6119608861
226UbiquitinationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.5221890473
226SumoylationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.52-
2262-HydroxyisobutyrylationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.52-
226AcetylationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.5227452117
226MalonylationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.5226320211
226SumoylationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.52-
226UbiquitinationLEDTKLIKGVIVDKD
CCCCEEEEEEEECCC		58.5221890473
229UbiquitinationTKLIKGVIVDKDFSH
CEEEEEEEECCCCCC		4.5221890473
232UbiquitinationIKGVIVDKDFSHPQM
EEEEEECCCCCCCCC		50.1821890473
2322-HydroxyisobutyrylationIKGVIVDKDFSHPQM
EEEEEECCCCCCCCC		50.18-
232AcetylationIKGVIVDKDFSHPQM
EEEEEECCCCCCCCC		50.1823749302
232UbiquitinationIKGVIVDKDFSHPQM
EEEEEECCCCCCCCC		50.1821890473
235PhosphorylationVIVDKDFSHPQMPKK
EEECCCCCCCCCCCC		44.3720860994
239SulfoxidationKDFSHPQMPKKVEDA
CCCCCCCCCCCHHCC		6.5630846556
2412-HydroxyisobutyrylationFSHPQMPKKVEDAKI
CCCCCCCCCHHCCEE		65.20-
242AcetylationSHPQMPKKVEDAKIA
CCCCCCCCHHCCEEE		45.017379973
2472-HydroxyisobutyrylationPKKVEDAKIAILTCP
CCCHHCCEEEEEECC		45.02-
247UbiquitinationPKKVEDAKIAILTCP
CCCHHCCEEEEEECC		45.02-
253GlutathionylationAKIAILTCPFEPPKP
CEEEEEECCCCCCCC		3.0522555962
253S-palmitoylationAKIAILTCPFEPPKP
CEEEEEECCCCCCCC		3.0529575903
259UbiquitinationTCPFEPPKPKTKHKL
ECCCCCCCCCCCCCC		70.62-
259AcetylationTCPFEPPKPKTKHKL
ECCCCCCCCCCCCCC		70.6226051181
259MalonylationTCPFEPPKPKTKHKL
ECCCCCCCCCCCCCC		70.6226320211
259UbiquitinationTCPFEPPKPKTKHKL
ECCCCCCCCCCCCCC		70.62-
261AcetylationPFEPPKPKTKHKLDV
CCCCCCCCCCCCCCC		76.0811789789
261MalonylationPFEPPKPKTKHKLDV
CCCCCCCCCCCCCCC		76.0826320211
261UbiquitinationPFEPPKPKTKHKLDV
CCCCCCCCCCCCCCC		76.08-
263AcetylationEPPKPKTKHKLDVTS
CCCCCCCCCCCCCCC		44.8911789799
263UbiquitinationEPPKPKTKHKLDVTS
CCCCCCCCCCCCCCC		44.89-
265UbiquitinationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.1921890473
265SumoylationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.19-
2652-HydroxyisobutyrylationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.19-
265AcetylationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.1923954790
265SumoylationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.1928112733
265UbiquitinationPKPKTKHKLDVTSVE
CCCCCCCCCCCCCHH		48.1921890473
269PhosphorylationTKHKLDVTSVEDYKA
CCCCCCCCCHHHHHH		27.0729978859
270PhosphorylationKHKLDVTSVEDYKAL
CCCCCCCCHHHHHHH		24.2921815630
274PhosphorylationDVTSVEDYKALQKYE
CCCCHHHHHHHHHHH		5.6726074081
275UbiquitinationVTSVEDYKALQKYEK
CCCHHHHHHHHHHHH		55.7521890473
275UbiquitinationVTSVEDYKALQKYEK
CCCHHHHHHHHHHHH		55.75-
275AcetylationVTSVEDYKALQKYEK
CCCHHHHHHHHHHHH		55.7523236377
275SumoylationVTSVEDYKALQKYEK
CCCHHHHHHHHHHHH		55.7528112733
275UbiquitinationVTSVEDYKALQKYEK
CCCHHHHHHHHHHHH		55.7521890473
277UbiquitinationSVEDYKALQKYEKEK
CHHHHHHHHHHHHHH		3.84-
279SumoylationEDYKALQKYEKEKFE
HHHHHHHHHHHHHHH		57.11-
2792-HydroxyisobutyrylationEDYKALQKYEKEKFE
HHHHHHHHHHHHHHH		57.11-
279AcetylationEDYKALQKYEKEKFE
HHHHHHHHHHHHHHH		57.1123749302
279SumoylationEDYKALQKYEKEKFE
HHHHHHHHHHHHHHH		57.1128112733
279UbiquitinationEDYKALQKYEKEKFE
HHHHHHHHHHHHHHH		57.11-
280PhosphorylationDYKALQKYEKEKFEE
HHHHHHHHHHHHHHH		21.1926074081
282AcetylationKALQKYEKEKFEEMI
HHHHHHHHHHHHHHH		64.2125953088
282UbiquitinationKALQKYEKEKFEEMI
HHHHHHHHHHHHHHH		64.21-
284UbiquitinationLQKYEKEKFEEMIQQ
HHHHHHHHHHHHHHH		69.9721890473
284AcetylationLQKYEKEKFEEMIQQ
HHHHHHHHHHHHHHH		69.9725953088
284UbiquitinationLQKYEKEKFEEMIQQ
HHHHHHHHHHHHHHH		69.9721906983
285UbiquitinationQKYEKEKFEEMIQQI
HHHHHHHHHHHHHHH		11.44-
288SulfoxidationEKEKFEEMIQQIKET
HHHHHHHHHHHHHHH		2.3621406390
299UbiquitinationIKETGANLAICQWGF
HHHHCCCEEEEECCC		3.18-
306UbiquitinationLAICQWGFDDEANHL
EEEEECCCCHHHHHH		11.03-
306AcetylationLAICQWGFDDEANHL
EEEEECCCCHHHHHH		11.0319608861
306UbiquitinationLAICQWGFDDEANHL
EEEEECCCCHHHHHH		11.0319608861
346UbiquitinationGRIVPRFSELTAEKL
CCEECCHHHHHHHHH		32.73-
346PhosphorylationGRIVPRFSELTAEKL
CCEECCHHHHHHHHH		32.7325850435
352UbiquitinationFSELTAEKLGFAGLV
HHHHHHHHHCCCCEE		51.99-
363PhosphorylationAGLVQEISFGTTKDK
CCEEEEECCCCCCCC		19.5128348404
368UbiquitinationEISFGTTKDKMLVIE
EECCCCCCCCEEEEE		56.0121906983
3702-HydroxyisobutyrylationSFGTTKDKMLVIEQC
CCCCCCCCEEEEEEC		35.37-
370AcetylationSFGTTKDKMLVIEQC
CCCCCCCCEEEEEEC		35.3727452117
370UbiquitinationSFGTTKDKMLVIEQC
CCCCCCCCEEEEEEC		35.37-
371SulfoxidationFGTTKDKMLVIEQCK
CCCCCCCEEEEEECC		5.3221406390
377GlutathionylationKMLVIEQCKNSRAVT
CEEEEEECCCCCEEE		2.6722555962
377S-nitrosylationKMLVIEQCKNSRAVT
CEEEEEECCCCCEEE		2.672212679
3782-HydroxyisobutyrylationMLVIEQCKNSRAVTI
EEEEEECCCCCEEEE		58.62-
378AcetylationMLVIEQCKNSRAVTI
EEEEEECCCCCEEEE		58.6225953088
378UbiquitinationMLVIEQCKNSRAVTI
EEEEEECCCCCEEEE		58.6221906983
390UbiquitinationVTIFIRGGNKMIIEE
EEEEEECCCEEHHHH		22.27-
3922-HydroxyisobutyrylationIFIRGGNKMIIEEAK
EEEECCCEEHHHHHH		34.45-
392AcetylationIFIRGGNKMIIEEAK
EEEECCCEEHHHHHH		34.4525953088
392SumoylationIFIRGGNKMIIEEAK
EEEECCCEEHHHHHH		34.4528112733
392UbiquitinationIFIRGGNKMIIEEAK
EEEECCCEEHHHHHH		34.4521906983
393SulfoxidationFIRGGNKMIIEEAKR
EEECCCEEHHHHHHH		4.2921406390
399AcetylationKMIIEEAKRSLHDAL
EEHHHHHHHHHHHHH		45.8819608861
399UbiquitinationKMIIEEAKRSLHDAL
EEHHHHHHHHHHHHH		45.8819608861
403AcetylationEEAKRSLHDALCVIR
HHHHHHHHHHHHHHH		21.39-
403UbiquitinationEEAKRSLHDALCVIR
HHHHHHHHHHHHHHH		21.39-
407S-nitrosocysteineRSLHDALCVIRNLIR
HHHHHHHHHHHHHHC		2.28-
407S-nitrosylationRSLHDALCVIRNLIR
HHHHHHHHHHHHHHC		2.2819483679
409UbiquitinationLHDALCVIRNLIRDN
HHHHHHHHHHHHCCC		2.06-
420UbiquitinationIRDNRVVYGGGAAEI
HCCCCEEECCCHHHH		13.75-
421UbiquitinationRDNRVVYGGGAAEIS
CCCCEEECCCHHHHH		19.22-
428UbiquitinationGGGAAEISCALAVSQ
CCCHHHHHHHHHHCC		5.7121890473
436UbiquitinationCALAVSQEADKCPTL
HHHHHCCCHHCCCHH		51.86-
439UbiquitinationAVSQEADKCPTLEQY
HHCCCHHCCCHHHHH		49.51-
440GlutathionylationVSQEADKCPTLEQYA
HCCCHHCCCHHHHHH		2.9922555962
442UbiquitinationQEADKCPTLEQYAMR
CCHHCCCHHHHHHHH		53.01-
459UbiquitinationADALEVIPMALSENS
HHHHHHHHHHHHCCC		13.7321890473
463PhosphorylationEVIPMALSENSGMNP
HHHHHHHHCCCCCCC		25.79-
466PhosphorylationPMALSENSGMNPIQT
HHHHHCCCCCCCCCH		35.05-
473PhosphorylationSGMNPIQTMTEVRAR
CCCCCCCHHHHHHHH		27.12-
474UbiquitinationGMNPIQTMTEVRARQ
CCCCCCHHHHHHHHH		1.4021890473
483UbiquitinationEVRARQVKEMNPALG
HHHHHHHHHHCHHCC		42.8021890473
483AcetylationEVRARQVKEMNPALG
HHHHHHHHHHCHHCC		42.8026051181
483UbiquitinationEVRARQVKEMNPALG
HHHHHHHHHHCHHCC		42.8021890473
485SulfoxidationRARQVKEMNPALGID
HHHHHHHHCHHCCCC		6.3621406390
493GlutathionylationNPALGIDCLHKGTND
CHHCCCCCCCCCCCH		3.9722555962
496AcetylationLGIDCLHKGTNDMKQ
CCCCCCCCCCCHHHH		55.2523749302
496UbiquitinationLGIDCLHKGTNDMKQ
CCCCCCCCCCCHHHH		55.25-
502SumoylationHKGTNDMKQQHVIET
CCCCCHHHHHHHHHH		50.06-
502AcetylationHKGTNDMKQQHVIET
CCCCCHHHHHHHHHH		50.0626822725
502SumoylationHKGTNDMKQQHVIET
CCCCCHHHHHHHHHH		50.06-
502UbiquitinationHKGTNDMKQQHVIET
CCCCCHHHHHHHHHH		50.0621906983
509PhosphorylationKQQHVIETLIGKKQQ
HHHHHHHHHHCHHHH		16.7320068231
5132-HydroxyisobutyrylationVIETLIGKKQQISLA
HHHHHHCHHHHHHHH		40.18-
513AcetylationVIETLIGKKQQISLA
HHHHHHCHHHHHHHH		40.1825953088
513UbiquitinationVIETLIGKKQQISLA
HHHHHHCHHHHHHHH		40.1821906983
514UbiquitinationIETLIGKKQQISLAT
HHHHHCHHHHHHHHH		42.0721890473
5142-HydroxyisobutyrylationIETLIGKKQQISLAT
HHHHHCHHHHHHHHH		42.07-
514UbiquitinationIETLIGKKQQISLAT
HHHHHCHHHHHHHHH		42.0721890473
518PhosphorylationIGKKQQISLATQMVR
HCHHHHHHHHHHHHH		13.9628258704
521PhosphorylationKQQISLATQMVRMIL
HHHHHHHHHHHHHHH		23.6121406692
523SulfoxidationQISLATQMVRMILKI
HHHHHHHHHHHHHCH		1.4728465586
529UbiquitinationQMVRMILKIDDIRKP
HHHHHHHCHHHCCCC		32.9121890473
5292-HydroxyisobutyrylationQMVRMILKIDDIRKP
HHHHHHHCHHHCCCC		32.91-
529AcetylationQMVRMILKIDDIRKP
HHHHHHHCHHHCCCC		32.9127452117
529UbiquitinationQMVRMILKIDDIRKP
HHHHHHHCHHHCCCC		32.9121890473
534MethylationILKIDDIRKPGESEE
HHCHHHCCCCCCCCC		46.22-
535AcetylationLKIDDIRKPGESEE-
HCHHHCCCCCCCCC-		58.6826051181
535UbiquitinationLKIDDIRKPGESEE-
HCHHHCCCCCCCCC-		58.682190698
539PhosphorylationDIRKPGESEE-----
HCCCCCCCCC-----		53.6025159151
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 TCPE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPE_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 TCPE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBC17_HUMANTBC1D17physical
16169070
ELP1_HUMANIKBKAPphysical
16169070
MIC60_HUMANIMMTphysical
16169070
P53_HUMANTP53physical
16169070
THEG_HUMANTHEGphysical
10747865
GNB5_HUMANGNB5physical
19376773
GBB1_HUMANGNB1physical
19376773
RGS7_HUMANRGS7physical
19376773
TCPG_HUMANCCT3physical
22939629
TCPQ_HUMANCCT8physical
22939629
TCPZ_HUMANCCT6Aphysical
22939629
TCPH_HUMANCCT7physical
22939629
TCPW_HUMANCCT6Bphysical
22939629
TERA_HUMANVCPphysical
22939629
XPO1_HUMANXPO1physical
22939629
TXNL1_HUMANTXNL1physical
22939629
TIF1B_HUMANTRIM28physical
22939629
TCPB_HUMANCCT2physical
22863883
TCPQ_HUMANCCT8physical
22863883
ARP2_HUMANACTR2physical
26344197
TCPB_HUMANCCT2physical
26344197
TCPG_HUMANCCT3physical
26344197
TCPD_HUMANCCT4physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
TCPW_HUMANCCT6Bphysical
26344197
TCPH_HUMANCCT7physical
26344197
TCPQ_HUMANCCT8physical
26344197
TCPA_HUMANTCP1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
256840Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCPE_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-223; LYS-232 AND LYS-399,AND MASS SPECTROMETRY.

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