UniProt ID | TCPZ_YEAST | |
---|---|---|
UniProt AC | P39079 | |
Protein Name | T-complex protein 1 subunit zeta | |
Gene Name | CCT6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 546 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.. | |
Protein Sequence | MSLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAGNIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGELLRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLLQVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQHLSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGFFYSSADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPDKGFVIINQKGIDPMSLDVFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFSGLVYQETIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRAVANVLKDKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEALLVIPKTLVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDPTIEGIWDSYRVLRNAITGATGIASNLLLCDELLRAGRSTLKETPQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSLQLLNPK ------CCCCCCCCC | 25.48 | 30377154 | |
2 | Acetylation | ------MSLQLLNPK ------CCCCCCCCC | 25.48 | 22814378 | |
9 | Ubiquitination | SLQLLNPKAESLRRD CCCCCCCCHHHHHHH | 64.81 | 24961812 | |
9 | Acetylation | SLQLLNPKAESLRRD CCCCCCCCHHHHHHH | 64.81 | 24489116 | |
40 | Ubiquitination | LETNLGPKGTLKMLV HHCCCCCCCEEEEEE | 63.83 | 23749301 | |
64 | Phosphorylation | KDGKVLLTEMQIQSP CCCCEEEEEEEECCC | 25.83 | 28889911 | |
70 | Phosphorylation | LTEMQIQSPTAVLIA EEEEEECCCHHHHHH | 26.33 | 28152593 | |
72 | Phosphorylation | EMQIQSPTAVLIARA EEEECCCHHHHHHHH | 34.35 | 29688323 | |
131 | Acetylation | IARKESMKFLDEFKI HHHHHHHHHHHCCCC | 52.64 | 24489116 | |
137 | Acetylation | MKFLDEFKISKTNLS HHHHHCCCCCCCCCC | 43.98 | 24489116 | |
211 | Acetylation | PKDTTFIKGLVLDHG CCCCCEEEEEECCCC | 41.84 | 24489116 | |
245 | Phosphorylation | VSLEYEKTEVNSGFF EEEEEECEEECCCCC | 32.97 | 22369663 | |
249 | Phosphorylation | YEKTEVNSGFFYSSA EECEEECCCCCCCCH | 42.00 | 22369663 | |
253 | Phosphorylation | EVNSGFFYSSADQRD EECCCCCCCCHHHHH | 10.23 | 22369663 | |
254 | Phosphorylation | VNSGFFYSSADQRDK ECCCCCCCCHHHHHH | 17.56 | 22369663 | |
255 | Phosphorylation | NSGFFYSSADQRDKL CCCCCCCCHHHHHHH | 25.20 | 22369663 | |
291 | Acetylation | VCGMDPDKGFVIINQ CCCCCCCCCEEEEEC | 60.69 | 24489116 | |
311 | Acetylation | MSLDVFAKHNILALR HHHHHHHHHHHHHHH | 26.22 | 24489116 | |
392 | Acetylation | HYALAQTKDAVRDGL CCEEHHCHHHHHHHH | 31.45 | 24489116 | |
542 | Ubiquitination | RAGRSTLKETPQ--- HHCHHHHHCCCC--- | 60.68 | 23749301 | |
544 | Phosphorylation | GRSTLKETPQ----- CHHHHHCCCC----- | 25.96 | 23749301 |
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 TCPZ_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCPZ_YEAST !! |
* 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 TCPZ_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-249, AND MASSSPECTROMETRY. |