| UniProt ID | TCPA_YEAST | |
|---|---|---|
| UniProt AC | P12612 | |
| Protein Name | T-complex protein 1 subunit alpha | |
| Gene Name | TCP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 559 | |
| 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 | MSQLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKMLVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVVIIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTLGKETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDVKRRSYRNYGLDLIRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPEPPKEDPHDH | |
| 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 | ------MSQLFNNSR ------CCCCCCCCC | 35.27 | 28152593 | |
| 2 | Acetylation | ------MSQLFNNSR ------CCCCCCCCC | 35.27 | 22814378 | |
| 8 | Phosphorylation | MSQLFNNSRSDTLFL CCCCCCCCCCCEEEE | 33.98 | 30377154 | |
| 10 | Phosphorylation | QLFNNSRSDTLFLGG CCCCCCCCCEEEECC | 34.47 | 30377154 | |
| 12 | Phosphorylation | FNNSRSDTLFLGGEK CCCCCCCEEEECCEE | 22.21 | 28889911 | |
| 19 | Acetylation | TLFLGGEKISGDDIR EEEECCEECCCHHCC | 45.51 | 24489116 | |
| 19 | Ubiquitination | TLFLGGEKISGDDIR EEEECCEECCCHHCC | 45.51 | 23749301 | |
| 21 | Phosphorylation | FLGGEKISGDDIRNQ EECCEECCCHHCCCC | 47.43 | 28889911 | |
| 42 | Phosphorylation | AVANVVKSSLGPVGL HHHHHHHHCCCCCCC | 21.13 | 22369663 | |
| 43 | Phosphorylation | VANVVKSSLGPVGLD HHHHHHHCCCCCCCC | 31.46 | 22369663 | |
| 163 | Phosphorylation | LINIAKTSMSSKIIG HHHHHHHCCCCCCCC | 18.89 | 27017623 | |
| 189 | Phosphorylation | DALLAVKTQNSKGEI HHHHHHHCCCCCCCC | 26.78 | 27017623 | |
| 197 | Acetylation | QNSKGEIKYPVKAVN CCCCCCCCCCHHHHC | 38.92 | 24489116 | |
| 201 | Acetylation | GEIKYPVKAVNVLKA CCCCCCHHHHCHHHH | 41.95 | 24489116 | |
| 298 | Phosphorylation | AGAQVVLTTKGIDDL CCCCEEEECCCHHHH | 18.17 | 19823750 | |
| 299 | Phosphorylation | GAQVVLTTKGIDDLC CCCEEEECCCHHHHH | 24.10 | 19823750 | |
| 308 | Acetylation | GIDDLCLKEFVEAKI CHHHHHHHHHHHHHH | 48.38 | 24489116 | |
| 314 | Acetylation | LKEFVEAKIMGVRRC HHHHHHHHHHCCHHC | 21.51 | 24489116 | |
| 381 | Phosphorylation | IKGTSKHSSSSIILR EECCCCCCCCEEEEC | 35.33 | 21440633 | |
| 382 | Phosphorylation | KGTSKHSSSSIILRG ECCCCCCCCEEEECC | 28.02 | 27017623 | |
| 393 | Phosphorylation | ILRGANDYSLDEMER EECCCCCCCHHHHHH | 15.79 | 27017623 | |
| 394 | Phosphorylation | LRGANDYSLDEMERS ECCCCCCCHHHHHHH | 32.01 | 27017623 | |
| 410 | Acetylation | HDSLSVVKRTLESGN HHHHHHHHHHHHCCC | 37.19 | 22865919 | |
| 468 | Ubiquitination | TLAVNAAKDSSELVA HHHHHHCCCCHHHHH | 56.59 | 23749301 | |
| 468 | Acetylation | TLAVNAAKDSSELVA HHHHHHCCCCHHHHH | 56.59 | 24489116 | |
| 468 | Succinylation | TLAVNAAKDSSELVA HHHHHHCCCCHHHHH | 56.59 | 23954790 | |
| 476 | Acetylation | DSSELVAKLRSYHAA CCHHHHHHHHHHHHH | 36.63 | 24489116 | |
| 488 | Acetylation | HAASQMAKPEDVKRR HHHHHCCCHHHHHCH | 43.53 | 22865919 | |
| 500 | Phosphorylation | KRRSYRNYGLDLIRG HCHHHHHHCHHHHCC | 15.29 | 21440633 | |
| 508 | Acetylation | GLDLIRGKIVDEIHA CHHHHCCCHHHHHHC | 29.70 | 24489116 | |
| 553 | Acetylation | TVDPEPPKEDPHDH- ECCCCCCCCCCCCC- | 82.53 | 24489116 |
| 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_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCPA_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 TCPA_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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 THR-12, AND MASSSPECTROMETRY. | |
