Search Results
Overview
| Uniprot ID | D0G0C8 |
|---|---|
| Protein Name | T-complex protein 1 subunit beta |
| Gene Name | CCT2 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 119 | EAESLIAKKIHPQTI |
| 120 | AESLIAKKIHPQTII |
| 154 | DHGSDEVKFRQDLMN |
| 181 | HHKDHFTKLAVEAVL |
| 191 | VEAVLRLKGSGNLEA |
| 203 | LEAIHVIKKLGGSLA |
| 223 | EGFLLDKKIGVNQPK |
| 230 | KIGVNQPKRIENAKI |
| 248 | NTGMDTDKIKIFGSR |
| 250 | GMDTDKIKIFGSRVR |
| 263 | VRVDSTAKVAEIEHA |
| 272 | AEIEHAEKEKMKEKV |
| 284 | EKVERILKHGINCFI |
| 50 | LGPKGMDKILLSSGR |
| 522 | LRVDNIIKAAPRKRV |
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
MASLSLAPVN
20
IFKAGADEER
30
AETARLSSFI
40
GAIAIGDLVK
50
STLGPKGMDK
60
ILLSSGRDAS
70
LMVTNDGATI
80
LKNIGVDNPA
90
AKVLVDMSRV
100
QDDEVGDGTT
110
SVTVLAAELL
120
REAESLIAKK
130
IHPQTIIAGW
140
REATKAARQA
150
LLNSAVDHGS
160
DEVKFRQDLM
170
NIAGTTLSSK
180
LLTHHKDHFT
190
KLAVEAVLRL
200
KGSGNLEAIH
210
VIKKLGGSLA
220
DSYLDEGFLL
230
DKKIGVNQPK
240
RIENAKILIA
250
NTGMDTDKIK
260
IFGSRVRVDS
270
TAKVAEIEHA
280
EKEKMKEKVE
290
RILKHGINCF
300
INRQLIYNYP
310
EQLFGAAGVM
320
AIEHADFAGV
330
ERLALVTGGE
340
IASTFDHPEL
350
VKLGSCKLIE
360
EVMIGEDKLI
370
HFSGVALGEA
380
CTIVLRGATQ
390
QILDEAERSL
400
HDALCVLAQT
410
VKDSRTVYGG
420
GCSEMLMAHA
430
VTQLANRTPG
440
KEAVAMESYA
450
KALRMLPTII
460
ADNAGYDSAD
470
LVAQLRAAHS
480
EGNTTAGLDM
490
KEGTIGDMAV
500
LGITESFQVK
510
RQVLLSAAEA
520
AEVILRVDNI
530
IKAAPRKRVP
DHHPC
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 |
| Cellular Component | GO:0002199 | zona pellucida receptor 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:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:1904874 | positive regulation of telomerase RNA localization to Cajal body |
| 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.