Search Results
Overview
| Uniprot ID | A0A4X1W928 |
|---|---|
| Protein Name | T-complex protein 1 subunit eta |
| Gene Name | CCT7 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 140 | ATQLAVNKIKEIAVT |
| 142 | QLAVNKIKEIAVTVK |
| 149 | KEIAVTVKKEDKVEQ |
| 162 | EQRKLLEKCAMTALS |
| 177 | SKLISQQKAFFAKMV |
| 223 | VAGVAFKKTFSYAGF |
| 255 | ELELKAEKDNAEIRV |
| 292 | RIYHSGAKVVLSKLP |
| 325 | RVPEEDLKRTMMACG |
| 371 | NFFTGCPKAKTCTII |
| 373 | FTGCPKAKTCTIILR |
| 435 | YSRTIPGKQQLLIGA |
| 52 | LGPRGMDKLIVDGRG |
| 60 | LIVDGRGKATISNDG |
| 82 | DVVHPAAKTLVDIAK |
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
Protein Sequence
10
MLLREKGPTP
20
VILLKEGTDS
30
SQGIPQLVSN
40
ISACQVIAEA
50
VRTTLGPRGM
60
DKLIVDGRGK
70
ATISNDGATI
80
LKLLDVVHPA
90
AKTLVDIAKS
100
QDAEVGDGTT
110
SVTLLAAEFL
120
KQVKPYVEEG
130
LHPQIIIRAF
140
RTATQLAVNK
150
IKEIAVTVKK
160
EDKVEQRKLL
170
EKCAMTALSS
180
KLISQQKAFF
190
AKMVVDAVMM
200
LDDLLQLKMI
210
GIKKVQGGAL
220
EESQLVAGVA
230
FKKTFSYAGF
240
EMQPKKYHNP
250
MIALLNVELE
260
LKAEKDNAEI
270
RVHTVEDYQA
280
IVDAEWNILY
290
DKLERIYHSG
300
AKVVLSKLPI
310
GDVATQYFAD
320
RDMFCAGRVP
330
EEDLKRTMMA
340
CGGSIQTSVN
350
ALSSDVLGRC
360
QVFEETQIGG
370
ERYNFFTGCP
380
KAKTCTIILR
390
GGAEQFMEET
400
ERSLHDAIMI
410
VRRAIKNDSV
420
VAGGGAIEME
430
LSKYLRDYSR
440
TIPGKQQLLI
450
GAYAKALEII
460
PRQLCDNAGF
470
DATNILNKLR
480
ARHAQGGTWY
490
GVDINNEDIA
500
DNFEAFVWEP
510
AMVRINALTA
520
ASEAACLIVS
530
VDETIKNPRS
540
TVDAPPAAGR
GRGRGRPH
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0044297 | cell body |
| Cellular Component | GO:0005832 | chaperonin-containing T-complex |
| Cellular Component | GO:0005874 | microtubule |
| 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:0042802 | identical protein binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0050821 | protein stabilization |
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.