Search Results
Overview
| Uniprot ID | A0A8D1QR27 |
|---|---|
| Protein Name | T-complex protein 1 subunit epsilon |
| Gene Name | CCT5 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 176 | AKTTLGSKVVNSCHR |
| 20 | GRPFLIIKDQDRKSR |
| 214 | ELIKVEGKVGGRLED |
| 223 | GGRLEDTKLIKGVIV |
| 226 | LEDTKLIKGVIVDKD |
| 290 | PKPKTKHKLDVTSVE |
| 300 | VTSVEDYKALQKYEK |
| 304 | EDYKALQKYEKEKFE |
| 309 | LQKYEKEKFEEMIRQ |
| 393 | EISFGTTKDKMLVIE |
| 395 | SFGTTKDKMLVIEQC |
| 417 | IFIRGGNKMIIEEAK |
| 424 | KMIIEEAKRSLHDAL |
| 508 | EVRARQVKEMNPALG |
| 538 | VIETLIGKKQQISLA |
| 539 | IETLIGKKQQISLAT |
| 554 | 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
SLGPNGLDKM
70
MVDKDGDVTV
80
TNDGATILSM
90
MDVDHQIAKL
100
MVELSKSQDD
110
EIGDGTTGVV
120
VLAGALLEEA
130
EQLLDRGIHP
140
IRIADGYEQA
150
ARIAIEHLDK
160
ISDSVLVDMK
170
DTEPLIQTAK
180
TTLGSKVVNS
190
CHRQMAEIAV
200
NAVLTVADMQ
210
RRDVDFELIK
220
VEGKVGGRLE
230
DTKLIKGVIV
240
DKDFSHPQMP
250
KVSPGPPQLR
260
ALPPLPASSR
270
VCLSPQQVED
280
AKIAILTCPF
290
EPPKPKTKHK
300
LDVTSVEDYK
310
ALQKYEKEKF
320
EEMIRQIKET
330
GANLAICQWG
340
FDDEANHLLL
350
QNNLPAVRWV
360
GGPEIELIAI
370
ATGGRIVPRF
380
SELTPEKLGF
390
AGLVKEISFG
400
TTKDKMLVIE
410
QCKNSRAVTI
420
FIRGGNKMII
430
EEAKRSLHDA
440
LCVIRNLIRD
450
NRVVYGGGAA
460
EIACALAVSQ
470
EADKCPTLEQ
480
YAMRAFADAL
490
EVIPMALAEN
500
SGMNPIQTMT
510
EVRARQVKEM
520
NPALGIDCLH
530
KGTNDMKQQH
540
VIETLIGKKQ
550
QISLATQMVR
560
MILKIDDIRK
PGESEE
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0044297 | cell body |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
| Molecular Function | GO:0048487 | beta-tubulin binding |
| Molecular Function | GO:0031681 | G-protein beta-subunit binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0009615 | response to virus |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005832 | chaperonin-containing T-complex |
| Cellular Component | GO:0005874 | microtubule |
| Molecular Function | GO:0005524 | ATP 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.