TCPB_MOUSE - dbPTM
TCPB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPB_MOUSE
UniProt AC P80314
Protein Name T-complex protein 1 subunit beta
Gene Name Cct2
Organism Mus musculus (Mouse).
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 MASLSLAPVNIFKAGADEERAETARLSSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDAALMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIISGWREATKAAREALLSSAVDHGSDEARFWQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHVIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDPRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESFAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGHITAGLDMKEGTIGDMAVLGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
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------MASLSLAPV
------CCCCCCCCH
21.12-
3Phosphorylation-----MASLSLAPVN
-----CCCCCCCCHH
19.7226824392
5Phosphorylation---MASLSLAPVNIF
---CCCCCCCCHHHC
21.7130352176
13UbiquitinationLAPVNIFKAGADEER
CCCHHHCCCCCCHHH
41.9622790023
13AcetylationLAPVNIFKAGADEER
CCCHHHCCCCCCHHH
41.9622826441
28PhosphorylationAETARLSSFIGAIAI
HHHHHHHHHHHHHHH
26.0228059163
40UbiquitinationIAIGDLVKSTLGPKG
HHHHHHHHHCCCCCC
45.05-
50AcetylationLGPKGMDKILLSSGR
CCCCCCCEEEECCCC
26.7622826441
50UbiquitinationLGPKGMDKILLSSGR
CCCCCCCEEEECCCC
26.7622790023
69PhosphorylationMVTNDGATILKNIGV
EEECCCCHHHHHHCC
32.1620469934
72UbiquitinationNDGATILKNIGVDNP
CCCCHHHHHHCCCCH
42.5422790023
119SuccinylationEAESLIAKKIHPQTI
HHHHHHHHHHCHHHH
45.3123954790
134PhosphorylationISGWREATKAAREAL
HHCHHHHHHHHHHHH
19.2322871156
150PhosphorylationSSAVDHGSDEARFWQ
HHHHHCCCHHHHHHH
28.9425338131
181AcetylationHHKDHFTKLAVEAVL
CCHHHHHHHHHHHHH
33.24-
191UbiquitinationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5922790023
191AcetylationVEAVLRLKGSGNLEA
HHHHHHHCCCCCHHH
44.5922826441
203AcetylationLEAIHVIKKLGGSLA
HHHHHHHHHHCCCHH
40.6422826441
204UbiquitinationEAIHVIKKLGGSLAD
HHHHHHHHHCCCHHH
41.0422790023
208PhosphorylationVIKKLGGSLADSYLD
HHHHHCCCHHHHHHC
20.7023984901
212PhosphorylationLGGSLADSYLDEGFL
HCCCHHHHHHCCCCC
23.2223984901
213PhosphorylationGGSLADSYLDEGFLL
CCCHHHHHHCCCCCC
20.7923984901
222UbiquitinationDEGFLLDKKIGVNQP
CCCCCCCCCCCCCCC
46.3822790023
222AcetylationDEGFLLDKKIGVNQP
CCCCCCCCCCCCCCC
46.3823236377
223MalonylationEGFLLDKKIGVNQPK
CCCCCCCCCCCCCCC
44.3426320211
242PhosphorylationAKILIANTGMDTDKI
CEEEEECCCCCHHHE
25.5128066266
246PhosphorylationIANTGMDTDKIKIFG
EECCCCCHHHEEECC
30.2428066266
248AcetylationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2523236377
248UbiquitinationNTGMDTDKIKIFGSR
CCCCCHHHEEECCCC
48.2522790023
250AcetylationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4122826441
250UbiquitinationGMDTDKIKIFGSRVR
CCCHHHEEECCCCEE
37.4122790023
254PhosphorylationDKIKIFGSRVRVDST
HHEEECCCCEEECCC
19.4925338131
260PhosphorylationGSRVRVDSTAKVAEI
CCCEEECCCCHHHHH
27.6626824392
261PhosphorylationSRVRVDSTAKVAEIE
CCEEECCCCHHHHHH
26.4925266776
284AcetylationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1022826441
284UbiquitinationEKVERILKHGINCFI
HHHHHHHHHCCCCEE
37.1022790023
289S-palmitoylationILKHGINCFINRQLI
HHHHCCCCEECCHHH
3.2428526873
297PhosphorylationFINRQLIYNYPEQLF
EECCHHHHCCHHHHH
19.7522817900
299PhosphorylationNRQLIYNYPEQLFGA
CCHHHHCCHHHHHCC
7.3822345495
327PhosphorylationVERLALVTGGEIAST
CCEEEEEECCCHHHC
40.08-
342UbiquitinationFDHPELVKLGSCKLI
CCCHHHHCCCCCCEE
60.8122790023
389PhosphorylationILDEAERSLHDALCV
HHHHHHHHHHHHHHH
22.8925293948
395GlutathionylationRSLHDALCVLAQTVK
HHHHHHHHHHHCCCC
2.2424333276
395S-palmitoylationRSLHDALCVLAQTVK
HHHHHHHHHHHCCCC
2.2428526873
395S-nitrosylationRSLHDALCVLAQTVK
HHHHHHHHHHHCCCC
2.2420925432
395S-nitrosocysteineRSLHDALCVLAQTVK
HHHHHHHHHHHCCCC
2.24-
402AcetylationCVLAQTVKDPRTVYG
HHHHCCCCCCCCCCC
66.4622826441
408PhosphorylationVKDPRTVYGGGCSEM
CCCCCCCCCCCHHHH
14.9419854140
412S-palmitoylationRTVYGGGCSEMLMAH
CCCCCCCHHHHHHHH
3.3526165157
412GlutathionylationRTVYGGGCSEMLMAH
CCCCCCCHHHHHHHH
3.3524333276
413PhosphorylationTVYGGGCSEMLMAHA
CCCCCCHHHHHHHHH
29.3419854140
422PhosphorylationMLMAHAVTQLANRTP
HHHHHHHHHHHHCCC
20.7422817900
441AcetylationVAMESFAKALRMLPT
HHHHHHHHHHHHHCH
46.0422826441
441UbiquitinationVAMESFAKALRMLPT
HHHHHHHHHHHHHCH
46.0422790023
470PhosphorylationAQLRAAHSEGHITAG
HHHHHHHHCCCEEEC
40.3126824392
475PhosphorylationAHSEGHITAGLDMKE
HHHCCCEEECCCCCC
14.7028066266
522AcetylationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4022826441
522UbiquitinationLRVDNIIKAAPRKRV
HCHHHHHHHCCCCCC
34.4022790023
527UbiquitinationIIKAAPRKRVPDHHP
HHHHCCCCCCCCCCC
57.6022790023

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
260SPhosphorylationKinaseRPS6KB1Q8BSK8
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPB_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDCL3_HUMANPDCL3physical
20360068
TCPZ_HUMANCCT6Aphysical
26496610
CDC20_HUMANCDC20physical
26496610
CSTF1_HUMANCSTF1physical
26496610
GBB2_HUMANGNB2physical
26496610
IGBP1_HUMANIGBP1physical
26496610
PHLP_HUMANPDCLphysical
26496610
PDPK1_HUMANPDPK1physical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
RAE1L_HUMANRAE1physical
26496610
TNKS1_HUMANTNKSphysical
26496610
EIF3I_HUMANEIF3Iphysical
26496610
PDCD5_HUMANPDCD5physical
26496610
BUB3_HUMANBUB3physical
26496610
ARP2_HUMANACTR2physical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
TXND9_HUMANTXNDC9physical
26496610
DCAF7_HUMANDCAF7physical
26496610
SSA27_HUMANSSSCA1physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPQ_HUMANCCT8physical
26496610
TCPE_HUMANCCT5physical
26496610
HGH1_HUMANHGH1physical
26496610
KI21A_HUMANKIF21Aphysical
26496610
RPTOR_HUMANRPTORphysical
26496610
LST8_HUMANMLST8physical
26496610
PDCL3_HUMANPDCL3physical
26496610
ERI3_HUMANERI3physical
26496610
ACTL8_HUMANACTL8physical
26496610
OSBL9_HUMANOSBPL9physical
26496610
TIM14_HUMANDNAJC19physical
26496610
ESCO2_HUMANESCO2physical
26496610
TBB5_HUMANTUBBphysical
26496610
WDR92_HUMANWDR92physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCPB_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP