Search Results
Overview
| Uniprot ID | I3LR32 |
|---|---|
| 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 |
| 265 | PKPKTKHKLDVTSVE |
| 275 | VTSVEDYKALQKYEK |
| 279 | EDYKALQKYEKEKFE |
| 284 | LQKYEKEKFEEMIRQ |
| 368 | EISFGTTKDKMLVIE |
| 370 | SFGTTKDKMLVIEQC |
| 392 | IFIRGGNKMIIEEAK |
| 399 | KMIIEEAKRSLHDAL |
| 483 | EVRARQVKEMNPALG |
| 513 | VIETLIGKKQQISLA |
| 514 | IETLIGKKQQISLAT |
| 529 | 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
KQVEDAKIAI
260
LTCPFEPPKP
270
KTKHKLDVTS
280
VEDYKALQKY
290
EKEKFEEMIR
300
QIKETGANLA
310
ICQWGFDDEA
320
NHLLLQNNLP
330
AVRWVGGPEI
340
ELIAIATGGR
350
IVPRFSELTP
360
EKLGFAGLVK
370
EISFGTTKDK
380
MLVIEQCKNS
390
RAVTIFIRGG
400
NKMIIEEAKR
410
SLHDALCVIR
420
NLIRDNRVVY
430
GGGAAEIACA
440
LAVSQEADKC
450
PTLEQYAMRA
460
FADALEVIPM
470
ALAENSGMNP
480
IQTMTEVRAR
490
QVKEMNPALG
500
IDCLHKGTND
510
MKQQHVIETL
520
IGKKQQISLA
530
TQMVRMILKI
540
DDIRKPGESE
E
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005832 | chaperonin-containing T-complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| 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.