Search Results
Overview
| Uniprot ID | A0A4X1TK46 |
|---|---|
| Protein Name | T-complex protein 1 subunit epsilon |
| Gene Name | CCT5 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 121 | AKTTLGSKVVNSCHR |
| 159 | ELIKVEGKVGGRLED |
| 168 | GGRLEDTKLIKGVIV |
| 171 | LEDTKLIKGVIVDKD |
| 20 | GRPFLIIKDQDRKSR |
| 210 | PKPKTKHKLDVTSVE |
| 220 | VTSVEDYKALQKYEK |
| 224 | EDYKALQKYEKEKFE |
| 229 | LQKYEKEKFEEMIRQ |
| 313 | EISFGTTKDKMLVIE |
| 315 | SFGTTKDKMLVIEQC |
| 337 | IFIRGGNKMIIEEAK |
| 344 | KMIIEEAKRSLHDAL |
| 428 | EVRARQVKEMNPALG |
| 458 | VIETLIGKKQQISLA |
| 459 | IETLIGKKQQISLAT |
| 474 | QMVRMILKIDDIRKP |
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia
Protein Sequence
10
MASVGTLAFD
20
EYGRPFLIIK
30
DQDRKSRLMG
40
LEALKSHIMA
50
AKAVANTMKT
60
SLGPNVLAGA
70
LLEEAEQLLD
80
RGIHPIRIAD
90
GYEQAARIAI
100
EHLDKISDSV
110
LVDMKDTEPL
120
IQTAKTTLGS
130
KVVNSCHRQM
140
AEIAVNAVLT
150
VADMQRRDVD
160
FELIKVEGKV
170
GGRLEDTKLI
180
KGVIVDKDFS
190
HPQMPKQVED
200
AKIAILTCPF
210
EPPKPKTKHK
220
LDVTSVEDYK
230
ALQKYEKEKF
240
EEMIRQIKET
250
GANLAICQWG
260
FDDEANHLLL
270
QNNLPAVRWV
280
GGPEIELIAI
290
ATGGRIVPRF
300
SELTPEKLGF
310
AGLVKEISFG
320
TTKDKMLVIE
330
QCKNSRAVTI
340
FIRGGNKMII
350
EEAKRSLHDA
360
LCVIRNLIRD
370
NRVVYGGGAA
380
EIACALAVSQ
390
EADKCPTLEQ
400
YAMRAFADAL
410
EVIPMALAEN
420
SGMNPIQTMT
430
EVRARQVKEM
440
NPALGIDCLH
450
KGTNDMKQQH
460
VIETLIGKKQ
470
QISLATQMVR
480
MILKIDDIRK
PGESEE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005832 | chaperonin-containing T-complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
| Molecular Function | GO:0051082 | unfolded protein binding |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.