Search Results
Overview
| Uniprot ID | A0A5G2QMG1 |
|---|---|
| Protein Name | T-complex protein 1 subunit beta |
| Gene Name | CCT2 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | EAESLIAKKIHPQTI |
| 102 | AESLIAKKIHPQTII |
| 136 | DHGSDEVKFRQDLMN |
| 163 | HHKDHFTKLAVEAVL |
| 173 | VEAVLRLKGSGNLEA |
| 185 | LEAIHVIKKLGGSLA |
| 205 | EGFLLDKKIGVNQPK |
| 212 | KIGVNQPKRIENAKI |
| 230 | NTGMDTDKIKIFGSR |
| 232 | GMDTDKIKIFGSRVR |
| 245 | VRVDSTAKVAEIEHA |
| 254 | AEIEHAEKEKMKEKV |
| 266 | EKVERILKHGINCFI |
| 32 | LGPKGMDKILLSSGR |
| 505 | LRVDNIIKAAPRYCN |
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
ERAETARLSS
20
FIGAIAIGDL
30
VKSTLGPKGM
40
DKILLSSGRD
50
ASLMVTNDGA
60
TILKNIGVDN
70
PAAKVLVDMS
80
RVQDDEVGDG
90
TTSVTVLAAE
100
LLREAESLIA
110
KKIHPQTIIA
120
GWREATKAAR
130
QALLNSAVDH
140
GSDEVKFRQD
150
LMNIAGTTLS
160
SKLLTHHKDH
170
FTKLAVEAVL
180
RLKGSGNLEA
190
IHVIKKLGGS
200
LADSYLDEGF
210
LLDKKIGVNQ
220
PKRIENAKIL
230
IANTGMDTDK
240
IKIFGSRVRV
250
DSTAKVAEIE
260
HAEKEKMKEK
270
VERILKHGIN
280
CFINRSLIYN
290
YPEQLFGAAG
300
VMAIEHADFA
310
GVERLALVTG
320
GEIASTFDHP
330
ELVKLGSCKL
340
IEEVMIGEDK
350
LIHFSGVALV
360
SEACTIVLRG
370
ATQQILDEAE
380
RSLHDALCVL
390
AQTVKDSRTV
400
YGGGCSEMLM
410
AHAVTQLANR
420
TPGKEAVAME
430
SYAKALRMLP
440
TIIADNAGYD
450
SADLVAQLRA
460
AHSEGNTTAG
470
LDMKEGTIGD
480
MAVLGITESF
490
QVKRQVLLSA
500
AEAAEVILRV
510
DNIIKAAPRY
CNTLKNIS
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| 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.