TCPB_HUMAN - dbPTM
TCPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPB_HUMAN
UniProt AC P78371
Protein Name T-complex protein 1 subunit beta
Gene Name CCT2
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Cytoplasm .
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 MASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
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
1 (in isoform 2)Acetylation-5.2922814378
2Acetylation------MASLSLAPV
------CCCCCCCCH
21.1220068231
3Phosphorylation-----MASLSLAPVN
-----CCCCCCCCHH
19.7229255136
5Phosphorylation---MASLSLAPVNIF
---CCCCCCCCHHEE
21.7129255136
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
132-HydroxyisobutyrylationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.96-
13AcetylationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9619608861
13UbiquitinationLAPVNIFKAGADEER
CCCHHEECCCCCHHH
41.9621890473
13 (in isoform 2)Phosphorylation-41.9629507054
23PhosphorylationADEERAETARLTSFI
CCHHHHHHHHHHHHH
18.98-
27PhosphorylationRAETARLTSFIGAIA
HHHHHHHHHHHHHHH
18.9527273156
28PhosphorylationAETARLTSFIGAIAI
HHHHHHHHHHHHHHH
21.3221601212
40UbiquitinationIAIGDLVKSTLGPKG
HHHHHHHHHCCCCCC
45.0521906983
46UbiquitinationVKSTLGPKGMDKILL
HHHCCCCCCCCEEEE
66.13-
50UbiquitinationLGPKGMDKILLSSGR
CCCCCCCEEEECCCC
26.7621890473
54PhosphorylationGMDKILLSSGRDASL
CCCEEEECCCCCCEE
27.5723403867
55PhosphorylationMDKILLSSGRDASLM
CCEEEECCCCCCEEE
37.5023403867
60PhosphorylationLSSGRDASLMVTNDG
ECCCCCCEEEEECCC
22.6830266825
62SulfoxidationSGRDASLMVTNDGAT
CCCCCEEEEECCCCH
3.0221406390
64PhosphorylationRDASLMVTNDGATIL
CCCEEEEECCCCHHH
17.3930266825
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHCCCCCH
42.5421890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
82UbiquitinationGVDNPAAKVLVDMSR
CCCCHHHEEEEEHHH
37.9021890473
99PhosphorylationDDEVGDGTTSVTVLA
CCCCCCCHHHHHHHH
22.1930622161
100PhosphorylationDEVGDGTTSVTVLAA
CCCCCCHHHHHHHHH
27.0830622161
101PhosphorylationEVGDGTTSVTVLAAE
CCCCCHHHHHHHHHH
18.6730622161
103PhosphorylationGDGTTSVTVLAAELL
CCCHHHHHHHHHHHH
15.0130622161
107AcetylationTSVTVLAAELLREAE
HHHHHHHHHHHHHHH
12.1019608861
107UbiquitinationTSVTVLAAELLREAE
HHHHHHHHHHHHHHH
12.1019608861
115PhosphorylationELLREAESLIAKKIH
HHHHHHHHHHHHHHC
31.9321815630
119AcetylationEAESLIAKKIHPQTI
HHHHHHHHHHCHHHE
45.3125953088
119SuccinylationEAESLIAKKIHPQTI
HHHHHHHHHHCHHHE
45.3123954790
119UbiquitinationEAESLIAKKIHPQTI
HHHHHHHHHHCHHHE
45.31-
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121890473
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121890473
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121890473
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121890473
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121890473
120UbiquitinationAESLIAKKIHPQTII
HHHHHHHHHCHHHEE
36.9121906983
134AcetylationIAGWREATKAAREAL
ECCHHHHHHHHHHHH
19.2319608861
134PhosphorylationIAGWREATKAAREAL
ECCHHHHHHHHHHHH
19.2322210691
143PhosphorylationAAREALLSSAVDHGS
HHHHHHHHHHHHCCC
19.6620068231
144PhosphorylationAREALLSSAVDHGSD
HHHHHHHHHHHCCCC
32.0820068231
150PhosphorylationSSAVDHGSDEVKFRQ
HHHHHCCCCCHHHHH
27.4620068231
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5521890473
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5521890473
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5521890473
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5521890473
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5521890473
154AcetylationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5519608861
154MalonylationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5526320211
154UbiquitinationDHGSDEVKFRQDLMN
HCCCCCHHHHHHHHH
32.5520639865
160SulfoxidationVKFRQDLMNIAGTTL
HHHHHHHHHHHCCCH
4.6021406390
165PhosphorylationDLMNIAGTTLSSKLL
HHHHHHCCCHHHHHH
18.6223403867
166PhosphorylationLMNIAGTTLSSKLLT
HHHHHCCCHHHHHHH
24.5923403867
168PhosphorylationNIAGTTLSSKLLTHH
HHHCCCHHHHHHHCC
24.2823403867
169PhosphorylationIAGTTLSSKLLTHHK
HHCCCHHHHHHHCCH
30.3621815630
1702-HydroxyisobutyrylationAGTTLSSKLLTHHKD
HCCCHHHHHHHCCHH
44.11-
170AcetylationAGTTLSSKLLTHHKD
HCCCHHHHHHHCCHH
44.1125953088
170UbiquitinationAGTTLSSKLLTHHKD
HCCCHHHHHHHCCHH
44.11-
176AcetylationSKLLTHHKDHFTKLA
HHHHHCCHHHHHHHH
45.3426051181
176UbiquitinationSKLLTHHKDHFTKLA
HHHHHCCHHHHHHHH
45.34-
181AcetylationHHKDHFTKLAVEAVL
CCHHHHHHHHHHHHH
33.2419608861
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
1912-HydroxyisobutyrylationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.59-
191AcetylationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5923749302
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5921890473
193PhosphorylationAVLRLKGSGNLEAIH
HHHHHCCCCCHHHHH
23.9523312004
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
2032-HydroxyisobutyrylationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.14-
203AcetylationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1425953088
203UbiquitinationLEAIHIIKKLGGSLA
HHHHHHHHHHCCCCH
41.1421890473
2042-HydroxyisobutyrylationEAIHIIKKLGGSLAD
HHHHHHHHHCCCCHH
41.79-
204UbiquitinationEAIHIIKKLGGSLAD
HHHHHHHHHCCCCHH
41.7921906983
208PhosphorylationIIKKLGGSLADSYLD
HHHHHCCCCHHHHHC
20.7028152594
212PhosphorylationLGGSLADSYLDEGFL
HCCCCHHHHHCCCCC
23.2228152594
213NitrationGGSLADSYLDEGFLL
CCCCHHHHHCCCCCC
20.79-
213PhosphorylationGGSLADSYLDEGFLL
CCCCHHHHHCCCCCC
20.7928152594
222AcetylationDEGFLLDKKIGVNQP
CCCCCCCCCCCCCCC
46.3823236377
222UbiquitinationDEGFLLDKKIGVNQP
CCCCCCCCCCCCCCC
46.3821906983
223SumoylationEGFLLDKKIGVNQPK
CCCCCCCCCCCCCCC
44.34-
2232-HydroxyisobutyrylationEGFLLDKKIGVNQPK
CCCCCCCCCCCCCCC
44.34-
223SumoylationEGFLLDKKIGVNQPK
CCCCCCCCCCCCCCC
44.34-
223UbiquitinationEGFLLDKKIGVNQPK
CCCCCCCCCCCCCCC
44.34-
230UbiquitinationKIGVNQPKRIENAKI
CCCCCCCCHHHCCEE
57.13-
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221890473
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221890473
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221890473
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221890473
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221890473
2362-HydroxyisobutyrylationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.02-
236AcetylationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0225953088
236UbiquitinationPKRIENAKILIANTG
CCHHHCCEEEEECCC
50.0221906983
242PhosphorylationAKILIANTGMDTDKI
CEEEEECCCCCHHHE
25.5120860994
244SulfoxidationILIANTGMDTDKIKI
EEEECCCCCHHHEEE
4.7621406390
246PhosphorylationIANTGMDTDKIKIFG
EECCCCCHHHEEECC
30.2421815630
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521890473
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521890473
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521890473
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521890473
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521890473
2482-HydroxyisobutyrylationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.25-
248AcetylationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2523954790
248SumoylationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2528112733
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2521906983
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121890473
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121890473
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121890473
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121890473
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121890473
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4121906983
254PhosphorylationDKIKIFGSRVRVDST
HHEEECCCCEEECCC
19.4925056879
260PhosphorylationGSRVRVDSTAKVAEI
CCCEEECCCCHHHHH
27.6627273156
261PhosphorylationSRVRVDSTAKVAEIE
CCEEECCCCHHHHHH
26.4928176443
2632-HydroxyisobutyrylationVRVDSTAKVAEIEHA
EEECCCCHHHHHHHH
41.91-
263UbiquitinationVRVDSTAKVAEIEHA
EEECCCCHHHHHHHH
41.9121906983
272AcetylationAEIEHAEKEKMKEKV
HHHHHHHHHHHHHHH
64.5223749302
272SuccinylationAEIEHAEKEKMKEKV
HHHHHHHHHHHHHHH
64.5223954790
272UbiquitinationAEIEHAEKEKMKEKV
HHHHHHHHHHHHHHH
64.52-
274UbiquitinationIEHAEKEKMKEKVER
HHHHHHHHHHHHHHH
67.36-
278UbiquitinationEKEKMKEKVERILKH
HHHHHHHHHHHHHHH
43.83-
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021890473
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021890473
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021890473
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021890473
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021890473
284AcetylationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1025953088
284MethylationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.10-
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1021906983
297PhosphorylationFINRQLIYNYPEQLF
EECCHHHHCCHHHHH
19.7522817900
3422-HydroxyisobutyrylationFDHPELVKLGSCKLI
CCCHHHHCCCCCCEE
60.81-
342AcetylationFDHPELVKLGSCKLI
CCCHHHHCCCCCCEE
60.8125953088
342UbiquitinationFDHPELVKLGSCKLI
CCCHHHHCCCCCCEE
60.8121906983
347UbiquitinationLVKLGSCKLIEEVMI
HHCCCCCCEEEEEEE
54.95-
353SulfoxidationCKLIEEVMIGEDKLI
CCEEEEEEECCCCEE
3.5421406390
379PhosphorylationTIVLRGATQQILDEA
HHHHCHHHHHHHHHH
24.6721406692
389PhosphorylationILDEAERSLHDALCV
HHHHHHHHHHHHHHH
22.8928450419
395GlutathionylationRSLHDALCVLAQTVK
HHHHHHHHHHHHHHC
2.2422555962
395S-palmitoylationRSLHDALCVLAQTVK
HHHHHHHHHHHHHHC
2.2429575903
402AcetylationCVLAQTVKDSRTVYG
HHHHHHHCCCCCEEC
54.0625953088
402UbiquitinationCVLAQTVKDSRTVYG
HHHHHHHCCCCCEEC
54.0621906983
404PhosphorylationLAQTVKDSRTVYGGG
HHHHHCCCCCEECCC
24.9222210691
406PhosphorylationQTVKDSRTVYGGGCS
HHHCCCCCEECCCHH
23.2523403867
408PhosphorylationVKDSRTVYGGGCSEM
HCCCCCEECCCHHHH
14.9422210691
413PhosphorylationTVYGGGCSEMLMAHA
CEECCCHHHHHHHHH
29.3422210691
415SulfoxidationYGGGCSEMLMAHAVT
ECCCHHHHHHHHHHH
1.4630846556
417SulfoxidationGGCSEMLMAHAVTQL
CCHHHHHHHHHHHHH
2.1930846556
422PhosphorylationMLMAHAVTQLANRTP
HHHHHHHHHHHHCCC
20.7425627689
427MethylationAVTQLANRTPGKEAV
HHHHHHHCCCCCHHH
36.37-
428PhosphorylationVTQLANRTPGKEAVA
HHHHHHCCCCCHHHH
35.8825159151
431AcetylationLANRTPGKEAVAMES
HHHCCCCCHHHHHHH
43.6426051181
431UbiquitinationLANRTPGKEAVAMES
HHHCCCCCHHHHHHH
43.6421906983
436SulfoxidationPGKEAVAMESYAKAL
CCCHHHHHHHHHHHH
2.5630846556
438PhosphorylationKEAVAMESYAKALRM
CHHHHHHHHHHHHHH
19.8021712546
439PhosphorylationEAVAMESYAKALRML
HHHHHHHHHHHHHHH
9.9823403867
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
4412-HydroxyisobutyrylationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.46-
441AcetylationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4625953088
441UbiquitinationVAMESYAKALRMLPT
HHHHHHHHHHHHHCH
39.4621890473
445SulfoxidationSYAKALRMLPTIIAD
HHHHHHHHHCHHHHC
5.6730846556
448PhosphorylationKALRMLPTIIADNAG
HHHHHHCHHHHCCCC
22.51-
456PhosphorylationIIADNAGYDSADLVA
HHHCCCCCCHHHHHH
12.33-
458PhosphorylationADNAGYDSADLVAQL
HCCCCCCHHHHHHHH
18.39-
470PhosphorylationAQLRAAHSEGNTTAG
HHHHHHHHCCCCCCC
42.3328985074
480SulfoxidationNTTAGLDMREGTIGD
CCCCCCCCCCCCHHH
5.1621406390
500UbiquitinationITESFQVKRQVLLSA
CCCCHHHHHHHHHHH
26.74-
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
522AcetylationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4025953088
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4021890473
527UbiquitinationIIKAAPRKRVPDHHP
HHHHCCCCCCCCCCC
57.60-

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
260SPhosphorylationKinaseAKT1P31749
PSP
260SPhosphorylationKinaseRPS6KA1Q15418
GPS
260SPhosphorylationKinaseRPS6KB1P23443
GPS
260SPhosphorylationKinaseRSK-SUBFAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPB_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 TCPB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNE1_HUMANCCNE1physical
9819444
PACRG_HUMANPACRGphysical
14532270
TCPD_HUMANCCT4physical
22939629
TCPE_HUMANCCT5physical
22939629
TCPG_HUMANCCT3physical
22939629
TCPQ_HUMANCCT8physical
22939629
TCPZ_HUMANCCT6Aphysical
22939629
TCPH_HUMANCCT7physical
22939629
TCPW_HUMANCCT6Bphysical
22939629
TIF1B_HUMANTRIM28physical
22939629
TXNL1_HUMANTXNL1physical
22939629
ACTS_HUMANACTA1physical
23190606
TBA1B_HUMANTUBA1Bphysical
23190606
EF2_HUMANEEF2physical
23190606
RS3_HUMANRPS3physical
23190606
ENPL_HUMANHSP90B1physical
23190606
ERLN2_HUMANERLIN2physical
23190606
TERA_HUMANVCPphysical
23190606
PSMD2_HUMANPSMD2physical
23190606
XIAP_HUMANXIAPphysical
23190606
CASP7_HUMANCASP7physical
23190606
HS90B_HUMANHSP90AB1physical
23190606
PRS10_HUMANPSMC6physical
23190606
HS90A_HUMANHSP90AA1physical
23190606
TCPG_HUMANCCT3physical
22863883
TCPZ_HUMANCCT6Aphysical
22863883
TCPH_HUMANCCT7physical
22863883
EF1D_HUMANEEF1Dphysical
22863883
IQGA1_HUMANIQGAP1physical
22863883
PSB8_HUMANPSMB8physical
22863883
TCPA_HUMANTCP1physical
22863883
TCPQ_HUMANCCT8physical
26344197
CH10_HUMANHSPE1physical
26344197
IMA3_HUMANKPNA4physical
26344197

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 TCPB_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-13; LYS-154 AND LYS-181, ANDMASS SPECTROMETRY.

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