| UniProt ID | TCPB_YEAST | |
|---|---|---|
| UniProt AC | P39076 | |
| Protein Name | T-complex protein 1 subunit beta | |
| Gene Name | CCT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 527 | |
| 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 | MSVQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSNTCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAELLREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDLIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKLSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVDSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGINSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQPFLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVLGGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDSSELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSASEAAEVLLRVDNIIRARPRTANRQHM | |
| 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 | ------MSVQIFGDQ ------CCCEEECCH | 23.80 | 28132839 | |
| 2 | Acetylation | ------MSVQIFGDQ ------CCCEEECCH | 23.80 | 22814378 | |
| 44 | Ubiquitination | LGPKGMDKLLQSASS CCCCHHHHHHHHCCC | 42.05 | 23749301 | |
| 48 | Phosphorylation | GMDKLLQSASSNTCM HHHHHHHHCCCCEEE | 30.04 | 30377154 | |
| 50 | Phosphorylation | DKLLQSASSNTCMVT HHHHHHCCCCEEEEE | 29.39 | 30377154 | |
| 51 | Phosphorylation | KLLQSASSNTCMVTN HHHHHCCCCEEEEEC | 35.56 | 23749301 | |
| 53 | Phosphorylation | LQSASSNTCMVTNDG HHHCCCCEEEEECCC | 12.15 | 28889911 | |
| 65 | Ubiquitination | NDGATILKSIPLDNP CCCCEEEECCCCCCH | 42.35 | 23749301 | |
| 75 | Ubiquitination | PLDNPAAKVLVNISK CCCCHHHEEEEEEEC | 37.90 | 24961812 | |
| 75 | Acetylation | PLDNPAAKVLVNISK CCCCHHHEEEEEEEC | 37.90 | 24489116 | |
| 81 | Phosphorylation | AKVLVNISKVQDDEV HEEEEEEECCCCCCC | 22.90 | 30377154 | |
| 93 | Phosphorylation | DEVGDGTTSVTVLSA CCCCCCCEEEEHHCH | 27.08 | 19779198 | |
| 94 | Phosphorylation | EVGDGTTSVTVLSAE CCCCCCEEEEHHCHH | 18.67 | 19779198 | |
| 99 | Phosphorylation | TTSVTVLSAELLREA CEEEEHHCHHHHHHH | 18.50 | 19779198 | |
| 108 | Acetylation | ELLREAEKLIDQSKI HHHHHHHHHHHHCCC | 58.76 | 24489116 | |
| 114 | Acetylation | EKLIDQSKIHPQTII HHHHHHCCCCHHHHH | 39.13 | 24489116 | |
| 137 | Acetylation | AALDALTKAAVDNSH HHHHHHHHHHHHCCC | 34.89 | 24489116 | |
| 146 | Acetylation | AVDNSHDKTMFREDL HHHCCCCCCCCHHHH | 36.14 | 24489116 | |
| 164 | Ubiquitination | AKTTLSSKILSQDKD HHHHHHHHHHHCCHH | 44.27 | 17644757 | |
| 170 | Acetylation | SKILSQDKDHFAELA HHHHHCCHHHHHHHH | 45.53 | 24489116 | |
| 170 | Ubiquitination | SKILSQDKDHFAELA HHHHHCCHHHHHHHH | 45.53 | 17644757 | |
| 185 | Acetylation | TNAILRLKGSTNLEH HHHHHHHCCCCCHHH | 44.36 | 24489116 | |
| 216 | Acetylation | DEGFILAKKFGNNQP CCCCCEEHHHCCCCC | 45.23 | 24489116 | |
| 242 | Acetylation | NTTLDTDKVKIFGTK ECEECCCCEEEECEE | 47.74 | 24489116 | |
| 244 | 2-Hydroxyisobutyrylation | TLDTDKVKIFGTKFK EECCCCEEEECEEEE | 37.75 | - | |
| 244 | Acetylation | TLDTDKVKIFGTKFK EECCCCEEEECEEEE | 37.75 | 24489116 | |
| 249 | Acetylation | KVKIFGTKFKVDSTA CEEEECEEEEECCHH | 43.50 | 24489116 | |
| 251 | 2-Hydroxyisobutyrylation | KIFGTKFKVDSTAKL EEECEEEEECCHHHH | 46.84 | - | |
| 251 | Acetylation | KIFGTKFKVDSTAKL EEECEEEEECCHHHH | 46.84 | 25381059 | |
| 254 | Phosphorylation | GTKFKVDSTAKLAQL CEEEEECCHHHHHHH | 33.00 | 24909858 | |
| 255 | Phosphorylation | TKFKVDSTAKLAQLE EEEEECCHHHHHHHH | 24.29 | 19823750 | |
| 257 | Acetylation | FKVDSTAKLAQLEKA EEECCHHHHHHHHHH | 44.43 | 24489116 | |
| 263 | Acetylation | AKLAQLEKAEREKMK HHHHHHHHHHHHHHH | 65.23 | 24489116 | |
| 278 | Acetylation | NKIAKISKFGINTFI HHHHHHHHHCHHHHH | 51.59 | 24489116 | |
| 278 | Ubiquitination | NKIAKISKFGINTFI HHHHHHHHHCHHHHH | 51.59 | 17644757 | |
| 366 | Phosphorylation | CKAGEACTIVLRGAT CCCCCEEEEEEECCC | 22.59 | 22369663 | |
| 396 | Acetylation | SVLSQTTKETRTVLG HHHHHCCCHHCCEEC | 61.55 | 24489116 | |
| 396 | Ubiquitination | SVLSQTTKETRTVLG HHHHHCCCHHCCEEC | 61.55 | 23749301 | |
| 398 | Phosphorylation | LSQTTKETRTVLGGG HHHCCCHHCCEECCC | 32.94 | 19823750 | |
| 400 | Phosphorylation | QTTKETRTVLGGGCA HCCCHHCCEECCCHH | 27.74 | 19823750 | |
| 412 | Phosphorylation | GCAEMVMSKAVDTEA CHHHHHHHHHCCCCH | 13.17 | 19823750 | |
| 413 | Ubiquitination | CAEMVMSKAVDTEAQ HHHHHHHHHCCCCHH | 34.04 | 23749301 | |
| 417 | Phosphorylation | VMSKAVDTEAQNIDG HHHHHCCCCHHCCCC | 26.99 | 27017623 | |
| 425 | Ubiquitination | EAQNIDGKKSLAVEA CHHCCCCHHHHHHHH | 35.13 | 23749301 | |
| 426 | Ubiquitination | AQNIDGKKSLAVEAF HHCCCCHHHHHHHHH | 57.12 | 22817900 | |
| 427 | Phosphorylation | QNIDGKKSLAVEAFA HCCCCHHHHHHHHHH | 25.66 | 27214570 | |
| 490 | Phosphorylation | RQLGIVESYKLKRAV HHCCCEEEEHHHHHH | 19.37 | 28152593 | |
| 492 | Acetylation | LGIVESYKLKRAVVS CCCEEEEHHHHHHHC | 57.73 | 24489116 | |
| 499 | Phosphorylation | KLKRAVVSSASEAAE HHHHHHHCCHHHHHH | 17.37 | 30377154 |
| 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 TCPB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCPB_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 TCPB_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 SER-51 AND THR-53, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASSSPECTROMETRY. | |
