TCPQ_MOUSE - dbPTM
TCPQ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPQ_MOUSE
UniProt AC P42932
Protein Name T-complex protein 1 subunit theta
Gene Name Cct8
Organism Mus musculus (Mouse).
Sequence Length 548
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body .
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 (By similarity)..
Protein Sequence MALHVPKAPGFAQMLKDGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINRLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVISGYEIACKKAHEILPELVCCSAKNLRDVDEVSSLLRTSIMSKQYGSETFLAKLIAQACVSIFPDSGNFNVDNIRVCKILGSGIYSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKTAEELMNFSKGEENLMDAQVKAIAGTGANVIVTGGKVADIALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPKLTPPVQEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYSVHQEGNKNVGLDIEAEVPAVKDMLEASILDTYLGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGKKDWDDDQND
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------MALHVPKAP
------CCCCCCCCC
13.33-
7Acetylation-MALHVPKAPGFAQM
-CCCCCCCCCCHHHH
67.1522826441
7Ubiquitination-MALHVPKAPGFAQM
-CCCCCCCCCCHHHH
67.15-
16AcetylationPGFAQMLKDGAKHFS
CCHHHHHHHHHHHCC
49.0923806337
16UbiquitinationPGFAQMLKDGAKHFS
CCHHHHHHHHHHHCC
49.09-
16MalonylationPGFAQMLKDGAKHFS
CCHHHHHHHHHHHCC
49.0926320211
20UbiquitinationQMLKDGAKHFSGLEE
HHHHHHHHHCCCHHH
51.19-
20AcetylationQMLKDGAKHFSGLEE
HHHHHHHHHCCCHHH
51.1922826441
20MalonylationQMLKDGAKHFSGLEE
HHHHHHHHHCCCHHH
51.1926320211
23PhosphorylationKDGAKHFSGLEEAVY
HHHHHHCCCHHHHHH
42.0321082442
30PhosphorylationSGLEEAVYRNIQACK
CCHHHHHHHHHHHHH
12.6525263469
36GlutathionylationVYRNIQACKELAQTT
HHHHHHHHHHHHHHH
1.7024333276
37AcetylationYRNIQACKELAQTTR
HHHHHHHHHHHHHHC
59.8022826441
45PhosphorylationELAQTTRTAYGPNGM
HHHHHHCHHHCCCHH
23.3422817900
47PhosphorylationAQTTRTAYGPNGMNK
HHHHCHHHCCCHHHH
32.2822817900
62AcetylationMVINRLEKLFVTNDA
HHHHHHHHHHCCCCH
52.3923236377
62UbiquitinationMVINRLEKLFVTNDA
HHHHHHHHHHCCCCH
52.39-
148GlutathionylationEILPELVCCSAKNLR
HHHHHHHHCCCCCCC
2.0724333276
148S-nitrosylationEILPELVCCSAKNLR
HHHHHHHHCCCCCCC
2.0720925432
148S-nitrosocysteineEILPELVCCSAKNLR
HHHHHHHHCCCCCCC
2.07-
149GlutathionylationILPELVCCSAKNLRD
HHHHHHHCCCCCCCC
3.2724333276
161PhosphorylationLRDVDEVSSLLRTSI
CCCHHHHHHHHHHHH
17.1421743459
162PhosphorylationRDVDEVSSLLRTSIM
CCHHHHHHHHHHHHH
36.2821743459
171AcetylationLRTSIMSKQYGSETF
HHHHHHHCCCCCHHH
30.1122826441
175PhosphorylationIMSKQYGSETFLAKL
HHHCCCCCHHHHHHH
28.6429514104
206AcetylationVDNIRVCKILGSGIY
CCCEEEEEEECCCCC
37.8022826441
210PhosphorylationRVCKILGSGIYSSSV
EEEEEECCCCCCCCC
20.6922345495
213PhosphorylationKILGSGIYSSSVLHG
EEECCCCCCCCCEEE
13.1622345495
214PhosphorylationILGSGIYSSSVLHGM
EECCCCCCCCCEEEE
17.7622345495
215PhosphorylationLGSGIYSSSVLHGMV
ECCCCCCCCCEEEEE
13.9022345495
216PhosphorylationGSGIYSSSVLHGMVF
CCCCCCCCCEEEEEE
23.8222345495
224AcetylationVLHGMVFKKETEGDV
CEEEEEEECCCCCCC
37.9922826441
233PhosphorylationETEGDVTSVKDAKIA
CCCCCCCCCCCCEEE
27.3326824392
235UbiquitinationEGDVTSVKDAKIAVY
CCCCCCCCCCEEEEE
52.30-
235SuccinylationEGDVTSVKDAKIAVY
CCCCCCCCCCEEEEE
52.3023954790
244GlutathionylationAKIAVYSCPFDGMIT
CEEEEEECCCCCCEE
1.8224333276
244S-nitrosylationAKIAVYSCPFDGMIT
CEEEEEECCCCCCEE
1.8224926564
244S-palmitoylationAKIAVYSCPFDGMIT
CEEEEEECCCCCCEE
1.8228526873
254UbiquitinationDGMITETKGTVLIKT
CCCEECCCCEEEEEC
46.48-
260AcetylationTKGTVLIKTAEELMN
CCCEEEEECHHHHHC
37.2122826441
260UbiquitinationTKGTVLIKTAEELMN
CCCEEEEECHHHHHC
37.21-
269PhosphorylationAEELMNFSKGEENLM
HHHHHCCCCCCCCHH
34.4427841257
270UbiquitinationEELMNFSKGEENLMD
HHHHCCCCCCCCHHH
67.23-
281UbiquitinationNLMDAQVKAIAGTGA
CHHHHHHHHHHCCCC
23.22-
296UbiquitinationNVIVTGGKVADIALH
EEEEECCCHHHHHHH
35.28-
304PhosphorylationVADIALHYANKYNIM
HHHHHHHHHHHCCEE
16.8425367039
317PhosphorylationIMLVRLNSKWDLRRL
EEEEECCCHHHHHHH
39.4530372032
318MalonylationMLVRLNSKWDLRRLC
EEEECCCHHHHHHHH
43.5926320211
318AcetylationMLVRLNSKWDLRRLC
EEEECCCHHHHHHHH
43.5923864654
326AcetylationWDLRRLCKTVGATAL
HHHHHHHHHHCCCCC
51.3323806337
326SuccinylationWDLRRLCKTVGATAL
HHHHHHHHHHCCCCC
51.3323806337
326MalonylationWDLRRLCKTVGATAL
HHHHHHHHHHCCCCC
51.3326320211
327PhosphorylationDLRRLCKTVGATALP
HHHHHHHHHCCCCCC
24.15-
367AcetylationVVVFKHEKEDGAIST
EEEEEEECCCCCEEE
61.9123806337
367UbiquitinationVVVFKHEKEDGAIST
EEEEEEECCCCCEEE
61.91-
380PhosphorylationSTIVLRGSTDNLMDD
EEEEEECCCCCHHHH
26.5922006019
381PhosphorylationTIVLRGSTDNLMDDI
EEEEECCCCCHHHHH
31.5628066266
400UbiquitinationDDGVNTFKVLTRDKR
HCCCCEEEEEECCCC
34.01-
400MalonylationDDGVNTFKVLTRDKR
HCCCCEEEEEECCCC
34.0126320211
400AcetylationDDGVNTFKVLTRDKR
HCCCCEEEEEECCCC
34.0123806337
400SuccinylationDDGVNTFKVLTRDKR
HCCCCEEEEEECCCC
34.0123806337
421UbiquitinationATEIELAKQITSYGE
HHHHHHHHHHHHCCC
55.66-
430GlutathionylationITSYGETCPGLEQYA
HHHCCCCCCCHHHHH
1.8824333276
430S-nitrosylationITSYGETCPGLEQYA
HHHCCCCCCCHHHHH
1.8824926564
440UbiquitinationLEQYAIKKFAEAFEA
HHHHHHHHHHHHHHH
43.63-
459SuccinylationLAENSGVKANEVISK
HHHCCCCCHHHHHHH
49.3623954790
459UbiquitinationLAENSGVKANEVISK
HHHCCCCCHHHHHHH
49.36-
466AcetylationKANEVISKLYSVHQE
CHHHHHHHHHHHHHC
40.0822826441
505PhosphorylationLDTYLGKYWAIKLAT
HHHHHHHHHHHHHHH
9.77-
528MalonylationVDQIIMAKPAGGPKP
ECEEEEECCCCCCCC
20.3026320211
528UbiquitinationVDQIIMAKPAGGPKP
ECEEEEECCCCCCCC
20.30-
534MalonylationAKPAGGPKPPSGKKD
ECCCCCCCCCCCCCC
73.2226320211
534UbiquitinationAKPAGGPKPPSGKKD
ECCCCCCCCCCCCCC
73.22-
537PhosphorylationAGGPKPPSGKKDWDD
CCCCCCCCCCCCCCC
72.3026824392
539UbiquitinationGPKPPSGKKDWDDDQ
CCCCCCCCCCCCCCC
52.47-
540UbiquitinationPKPPSGKKDWDDDQN
CCCCCCCCCCCCCCC
68.52-

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 TCPQ_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPQ_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 TCPQ_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPZ_HUMANCCT6Aphysical
26496610
CSTF1_HUMANCSTF1physical
26496610
DHX15_HUMANDHX15physical
26496610
TNPO1_HUMANTNPO1physical
26496610
PHLP_HUMANPDCLphysical
26496610
PFD2_HUMANPFDN2physical
26496610
PPP6_HUMANPPP6Cphysical
26496610
GTR1_HUMANSLC2A1physical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
EIF3I_HUMANEIF3Iphysical
26496610
PDCD5_HUMANPDCD5physical
26496610
ARP2_HUMANACTR2physical
26496610
TXND9_HUMANTXNDC9physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPE_HUMANCCT5physical
26496610
AT132_HUMANATP13A2physical
26496610
NDUAD_HUMANNDUFA13physical
26496610
HGH1_HUMANHGH1physical
26496610
DTL_HUMANDTLphysical
26496610
TMCO1_HUMANTMCO1physical
26496610
RFWD3_HUMANRFWD3physical
26496610
NCLN_HUMANNCLNphysical
26496610
LST8_HUMANMLST8physical
26496610
PDCL3_HUMANPDCL3physical
26496610
ACTL8_HUMANACTL8physical
26496610
K2013_HUMANKIAA2013physical
26496610
ESCO1_HUMANESCO1physical
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 TCPQ_MOUSE

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Related Literatures of Post-Translational Modification

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