CCT7 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0007339Biological processbinding of sperm to zona pellucida
GO_1904871Biological processpositive regulation of protein localization to Cajal body
GO_0061077Biological processchaperone-mediated protein folding
GO_1904874Biological processpositive regulation of telomerase RNA localization to Cajal body
GO_1904851Biological processpositive regulation of establishment of protein localization to telomere
GO_0006457Biological processprotein folding
GO_0050821Biological processprotein stabilization
GO_0032212Biological processpositive regulation of telomere maintenance via telomerase
GO_0005874Cellular componentmicrotubule
GO_0005832Cellular componentchaperonin-containing T-complex
GO_0070062Cellular componentextracellular exosome
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_0044297Cellular componentcell body
GO_0044183Molecular functionprotein folding chaperone
GO_0051082Molecular functionunfolded protein binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0005524Molecular functionATP binding
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameCCT7
Protein nameT-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (HIV-1 Nef-interacting protein) [Cleaved into: T-complex protein 1 subunit eta, N-terminally processed]
Chaperonin containing TCP1 subunit 7
T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta)
SynonymshCG_1997313
CCTH
NIP7-1
DescriptionFUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis . The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance . The TRiC complex plays a role in the folding of actin and tubulin (Probable). .

FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. .

FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. .

FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. .

AccessionsF8WAM2
ENST00000399032.2
ENST00000540468.5 [Q99832-4]
F8WBP8
ENST00000409924.7
B7Z1C9
ENST00000398422.2 [Q99832-2]
ENST00000258091.10 [Q99832-1]
ENST00000539919.5 [Q99832-3]
Q6IBT3
Q99832