| UniProt ID | TCPQ_YEAST | |
|---|---|---|
| UniProt AC | P47079 | |
| Protein Name | T-complex protein 1 subunit theta | |
| Gene Name | CCT8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 568 | |
| 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 (By similarity).. | |
| Protein Sequence | MSLRLPQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDKNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPVAQQAGEIPYFNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGAVKTDHLYKGVDIDGESDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKKAGGPRAPQGPRPGNWDQED | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSLRLPQNP ------CCCCCCCCC | 23.38 | 28152593 | |
| 15 | Ubiquitination | NPNAGLFKQGYNSYS CCCCCCCCCCCCCCC | 48.10 | 23749301 | |
| 30 | Acetylation | NADGQIIKSIAAIRE CCCHHHHHHHHHHHH | 37.12 | 24489116 | |
| 30 | Ubiquitination | NADGQIIKSIAAIRE CCCHHHHHHHHHHHH | 37.12 | 15699485 | |
| 44 | Phosphorylation | ELHQMCLTSMGPCGR HHHHHHHHCCCCCCC | 16.25 | 26447709 | |
| 45 | Phosphorylation | LHQMCLTSMGPCGRN HHHHHHHCCCCCCCC | 14.59 | 26447709 | |
| 65 | Phosphorylation | HLGKIIITNDAATML CCCEEEEECCHHHHH | 19.35 | 22369663 | |
| 70 | Phosphorylation | IITNDAATMLRELDI EEECCHHHHHHHHCC | 20.61 | 22369663 | |
| 119 | Phosphorylation | NVSEKLISMGLSAVE CHHHHHHHCCCCHHH | 19.75 | 24909858 | |
| 153 | Acetylation | VVGEITDKNDKNELL HHHEECCCCCHHHHH | 59.40 | 24489116 | |
| 156 | Acetylation | EITDKNDKNELLKMI EECCCCCHHHHHHHH | 62.81 | 24489116 | |
| 171 | Ubiquitination | KPVISSKKYGSEDIL HHHHHCCCCCCHHHH | 57.71 | 15699485 | |
| 216 | Phosphorylation | VVKIMGGSLSNSTVI EEEEECCCCCCCEEE | 23.93 | 22369663 | |
| 218 | Phosphorylation | KIMGGSLSNSTVIKG EEECCCCCCCEEEEE | 30.36 | 22369663 | |
| 220 | Phosphorylation | MGGSLSNSTVIKGMV ECCCCCCCEEEEEEE | 22.22 | 22369663 | |
| 221 | Phosphorylation | GGSLSNSTVIKGMVF CCCCCCCEEEEEEEE | 30.42 | 22369663 | |
| 224 | Ubiquitination | LSNSTVIKGMVFNRE CCCCEEEEEEEECCC | 36.30 | 17644757 | |
| 237 | Ubiquitination | REPEGHVKSLSEDKK CCCCCCCCCCCCCCC | 39.75 | 17644757 | |
| 246 | Ubiquitination | LSEDKKHKVAVFTCP CCCCCCCCEEEEECC | 40.54 | 17644757 | |
| 262 | Ubiquitination | DIANTETKGTVLLHN CCCCCCCCCEEEEEC | 46.48 | 17644757 | |
| 278 | Acetylation | QEMLDFSKGEEKQID HHHHCCCCCCHHHHH | 71.04 | 24489116 | |
| 278 | Ubiquitination | QEMLDFSKGEEKQID HHHHCCCCCCHHHHH | 71.04 | 17644757 | |
| 282 | Acetylation | DFSKGEEKQIDAMMK CCCCCCHHHHHHHHH | 48.53 | 24489116 | |
| 282 | Ubiquitination | DFSKGEEKQIDAMMK CCCCCCHHHHHHHHH | 48.53 | 17644757 | |
| 322 | Acetylation | RYGILVLKVPSKFEL HCCEEEEECCCHHHH | 44.62 | 22865919 | |
| 326 | Acetylation | LVLKVPSKFELRRLC EEEECCCHHHHHHHH | 36.47 | 24489116 | |
| 339 | Phosphorylation | LCRVCGATPLPRLGA HHHHHCCCCCCCCCC | 15.61 | 27214570 | |
| 359 | Acetylation | LGLVETVKTMEIGGD HCCEEEEEEEEECCE | 49.96 | 24489116 | |
| 359 | Ubiquitination | LGLVETVKTMEIGGD HCCEEEEEEEEECCE | 49.96 | 17644757 | |
| 372 | Acetylation | GDRVTVFKQEQGEIS CEEEEEEEECCCCCC | 48.89 | 24489116 | |
| 372 | Ubiquitination | GDRVTVFKQEQGEIS CEEEEEEEECCCCCC | 48.89 | 23749301 | |
| 381 | Phosphorylation | EQGEISRTSTIILRG CCCCCCEEEEEEEEC | 24.35 | 21126336 | |
| 383 | Phosphorylation | GEISRTSTIILRGAT CCCCEEEEEEEECCC | 16.07 | 28889911 | |
| 390 | Phosphorylation | TIILRGATQNNLDDI EEEEECCCCCCHHHH | 34.35 | 28132839 | |
| 413 | Acetylation | AAVKGLMKPSGGKLL HHHHHCCCCCCCCCC | 40.86 | 24489116 | |
| 418 | Ubiquitination | LMKPSGGKLLPGAGA CCCCCCCCCCCCCCC | 50.83 | 24961812 | |
| 450 | Ubiquitination | GLLQLAIKQFAVAFE HHHHHHHHHHHHHHC | 33.48 | 17644757 | |
| 491 | Ubiquitination | VTEPGAVKTDHLYKG CCCCCCCCCCEEECC | 47.93 | 17644757 | |
| 497 | Acetylation | VKTDHLYKGVDIDGE CCCCEEECCCCCCCC | 59.84 | 24489116 | |
| 497 | Ubiquitination | VKTDHLYKGVDIDGE CCCCEEECCCCCCCC | 59.84 | 17644757 | |
| 505 | Phosphorylation | GVDIDGESDEGVKDI CCCCCCCCCCCCCHH | 46.63 | 27214570 | |
| 518 | Phosphorylation | DIREENIYDMLATKK HHHHHCHHHHHHHCC | 13.59 | 22369663 | |
| 523 | Phosphorylation | NIYDMLATKKFAINV CHHHHHHHCCEEHHH | 30.70 | 22369663 |
| 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_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCPQ_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 TCPQ_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, AND MASSSPECTROMETRY. | |
