TCPA_MOUSE - dbPTM
TCPA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPA_MOUSE
UniProt AC P11983
Protein Name T-complex protein 1 subunit alpha
Gene Name Tcp1
Organism Mus musculus (Mouse).
Sequence Length 556
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 (By similarity)..
Protein Sequence MEGPLSVFGDRSTGEAVRSQNVMAAASIANIVKSSFGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVAKASGASILSTLANLEGEETFEVTMLGQAEEVVQERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRVLELKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTLAVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLVHGKPRDNKQAGVFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKDDKHGSYENAVHSGALDD
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
1Acetylation-------MEGPLSVF
-------CCCCCEEC		14.00-
6Phosphorylation--MEGPLSVFGDRST
--CCCCCEECCCCCC		20.6628066266
12PhosphorylationLSVFGDRSTGEAVRS
CEECCCCCCCHHHHH		45.5729899451
27PhosphorylationQNVMAAASIANIVKS
HCHHHHHHHHHHHHH		19.9429899451
33UbiquitinationASIANIVKSSFGPVG
HHHHHHHHHCCCCCC		36.26-
43UbiquitinationFGPVGLDKMLVDDIG
CCCCCCCCEEECCCC		38.8922790023
53PhosphorylationVDDIGDVTITNDGAT
ECCCCCEEEECCCCH		27.1628066266
55PhosphorylationDIGDVTITNDGATIL
CCCCEEEECCCCHHH		20.2128066266
60PhosphorylationTITNDGATILKLLEV
EEECCCCHHHHHHCC		32.1628066266
76S-palmitoylationHPAAKVLCELADLQD
CHHHHHHHHHHCCCC		4.5128526873
90PhosphorylationDKEVGDGTTSVVIIA
CCCCCCCHHHHHHHH		22.1917203969
91PhosphorylationKEVGDGTTSVVIIAA
CCCCCCHHHHHHHHH		25.6717203969
92PhosphorylationEVGDGTTSVVIIAAE
CCCCCHHHHHHHHHH		17.7717203969
119PhosphorylationIHPTSVISGYRLACK
CCCCCHHCHHHHHHH		27.84-
126MalonylationSGYRLACKEAVRYIN
CHHHHHHHHHHHHHH		43.0026320211
126UbiquitinationSGYRLACKEAVRYIN
CHHHHHHHHHHHHHH		43.00-
131PhosphorylationACKEAVRYINENLII
HHHHHHHHHHCCCEE		11.0822802335
147GlutathionylationTDELGRDCLINAAKT
HHHHCHHHHHHHHHH		3.8624333276
147S-palmitoylationTDELGRDCLINAAKT
HHHHCHHHHHHHHHH		3.8628526873
157PhosphorylationNAAKTSMSSKIIGIN
HHHHHCCCCCCCCCC		28.3922802335
158PhosphorylationAAKTSMSSKIIGING
HHHHCCCCCCCCCCH		21.1622802335
181PhosphorylationDAVLAVKYTDARGQP
HHHEEEEEECCCCCC		11.8529514104
199AcetylationVNSVNILKAHGRSQI
CCHHHHHHHCCCHHH		34.24-
204PhosphorylationILKAHGRSQIESMLI
HHHHCCCHHHHHHHC		39.8522871156
208PhosphorylationHGRSQIESMLINGYA
CCCHHHHHHHCCCEE		22.1022871156
214PhosphorylationESMLINGYALNCVVG
HHHHCCCEEHHHEEC		11.9229895711
218GlutathionylationINGYALNCVVGSQGM
CCCEEHHHEECCCCC		2.4624333276
236S-nitrosocysteineIVNAKIACLDFSLQK
HHCEEEEEEEHHCCC		4.22-
236S-palmitoylationIVNAKIACLDFSLQK
HHCEEEEEEEHHCCC		4.2228526873
240PhosphorylationKIACLDFSLQKTKMK
EEEEEEHHCCCCCCC		29.5630352176
243PhosphoglycerylationCLDFSLQKTKMKLGV
EEEHHCCCCCCCCCE		56.24-
272AcetylationQRESDITKERIQKIL
HHCCHHCHHHHHHHH		45.3823954790
281PhosphorylationRIQKILATGANVILT
HHHHHHHCCCCEEEE		33.1222802335
288PhosphorylationTGANVILTTGGIDDM
CCCCEEEECCCCCHH		16.5722802335
289PhosphorylationGANVILTTGGIDDMY
CCCEEEECCCCCHHH		29.9322802335
296PhosphorylationTGGIDDMYLKYFVEA
CCCCCHHHHHHHHHH		13.6722802335
317MalonylationRVLKRDLKHVAKASG
HHHHHHHHHHHHHHC		40.0826320211
317AcetylationRVLKRDLKHVAKASG
HHHHHHHHHHHHHHC		40.0823201123
357S-palmitoylationEVVQERICDDELILI
HHHHHHCCCCEEEEE		7.2628526873
357S-nitrosocysteineEVVQERICDDELILI
HHHHHHCCCCEEEEE		7.26-
357GlutathionylationEVVQERICDDELILI
HHHHHHCCCCEEEEE		7.2624333276
365UbiquitinationDDELILIKNTKARTS
CCEEEEEECCCCCCC		55.9322790023
365AcetylationDDELILIKNTKARTS
CCEEEEEECCCCCCC		55.9323236377
368UbiquitinationLILIKNTKARTSASI
EEEEECCCCCCCCHH		45.31-
371PhosphorylationIKNTKARTSASIILR
EECCCCCCCCHHHHC		33.2429899451
374PhosphorylationTKARTSASIILRGAN
CCCCCCCHHHHCCCC		15.2129176673
385GlutathionylationRGANDFMCDEMERSL
CCCCCHHCHHHHHHH		3.9624333276
385S-nitrosocysteineRGANDFMCDEMERSL
CCCCCHHCHHHHHHH		3.96-
397GlutathionylationRSLHDALCVVKRVLE
HHHHHHHHHHHHHHH		3.3824333276
397S-nitrosocysteineRSLHDALCVVKRVLE
HHHHHHHHHHHHHHH		3.38-
400MalonylationHDALCVVKRVLELKS
HHHHHHHHHHHHHCC		19.1826320211
400AcetylationHDALCVVKRVLELKS
HHHHHHHHHHHHHCC		19.1823806337
400SuccinylationHDALCVVKRVLELKS
HHHHHHHHHHHHHCC		19.1823806337
466AcetylationDSTDLVAKLRAFHNE
CCHHHHHHHHHHHHH		30.9023954790
466UbiquitinationDSTDLVAKLRAFHNE
CCHHHHHHHHHHHHH		30.90-
484AcetylationNPERKNLKWIGLDLV
CCCCCCCEEEEEEEE		46.2722826441
489UbiquitinationNLKWIGLDLVHGKPR
CCEEEEEEEECCCCC		41.2427667366
492UbiquitinationWIGLDLVHGKPRDNK
EEEEEEECCCCCCCC		45.9527667366
494AcetylationGLDLVHGKPRDNKQA
EEEEECCCCCCCCCC		23.2323806337
494MalonylationGLDLVHGKPRDNKQA
EEEEECCCCCCCCCC		23.2326320211
494UbiquitinationGLDLVHGKPRDNKQA
EEEEECCCCCCCCCC		23.23-
499MalonylationHGKPRDNKQAGVFEP
CCCCCCCCCCCCCCC		45.9026320211
515UbiquitinationIVKVKSLKFATEAAI
EEEEECCCCHHHHHH		39.79-
532AcetylationLRIDDLIKLHPESKD
EEHHHHHHHCCCCCC		48.3023236377
532UbiquitinationLRIDDLIKLHPESKD
EEHHHHHHHCCCCCC		48.3022790023
538UbiquitinationIKLHPESKDDKHGSY
HHHCCCCCCCCCCCC		69.1822790023
541UbiquitinationHPESKDDKHGSYENA
CCCCCCCCCCCCCCC		61.0627667366
541MalonylationHPESKDDKHGSYENA
CCCCCCCCCCCCCCC		61.0626320211
544PhosphorylationSKDDKHGSYENAVHS
CCCCCCCCCCCCCCC		29.0625521595
545PhosphorylationKDDKHGSYENAVHSG
CCCCCCCCCCCCCCC		20.1427742792
551PhosphorylationSYENAVHSGALDD--
CCCCCCCCCCCCC--		21.1127087446
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 TCPA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPA_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 TCPA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_MOUSESkp1aphysical
21343341
FBXL2_MOUSEFbxl2physical
21343341
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCPA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, ANDMASS SPECTROMETRY.

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