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HUMAN:TCPH

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) CCT7 (synonyms: CCTH, NIP7-1)
Protein Name(s) T-complex protein 1 subunit eta

TCP-1-eta CCT-eta HIV-1 Nef-interacting protein

External Links
UniProt Q99832
EMBL AF026292
CR536511
AK291961
AK293597
AK297846
AK298153
AC010913
CH471053
CH471053
BC019296
BC088351
U83843
CCDS CCDS42696.1
CCDS46336.1
CCDS54366.1
CCDS54367.1
RefSeq NP_001009570.1
NP_001159756.1
NP_001159757.1
NP_006420.1
UniGene Hs.368149
ProteinModelPortal Q99832
SMR Q99832
BioGrid 115825
DIP DIP-51608N
IntAct Q99832
MINT MINT-1131353
STRING 9606.ENSP00000258091
PhosphoSite Q99832
DMDM 3041738
REPRODUCTION-2DPAGE IPI00018465
MaxQB Q99832
PaxDb Q99832
PRIDE Q99832
DNASU 10574
Ensembl ENST00000258091
ENST00000398422
ENST00000539919
ENST00000540468
GeneID 10574
KEGG hsa:10574
UCSC uc002siz.3
uc002sja.3
uc010yri.2
CTD 10574
GeneCards GC02P073460
HGNC HGNC:1622
HPA HPA008425
MIM 605140
neXtProt NX_Q99832
PharmGKB PA26185
eggNOG COG0459
GeneTree ENSGT00550000074832
HOGENOM HOG000226730
HOVERGEN HBG001052
InParanoid Q99832
KO K09499
OMA NINACQV
OrthoDB EOG7V49Z2
PhylomeDB Q99832
TreeFam TF105641
Reactome REACT_16907
REACT_16936
REACT_16956
REACT_17050
ChiTaRS CCT7
GeneWiki CCT7
GenomeRNAi 10574
NextBio 40131
PRO PR:Q99832
Proteomes UP000005640
Bgee Q99832
CleanEx HS_CCT7
ExpressionAtlas Q99832
Genevestigator Q99832
GO GO:0044297
GO:0005832
GO:0005737
GO:0005829
GO:0070062
GO:0005874
GO:0005739
GO:0002199
GO:0005524
GO:0051082
GO:0051084
GO:0007339
GO:0044267
GO:0006457
Gene3D 1.10.560.10
3.30.260.10
3.50.7.10
InterPro IPR012720
IPR017998
IPR002194
IPR002423
IPR027409
IPR027413
IPR027410
PANTHER PTHR11353
PTHR11353:SF22
Pfam PF00118
PRINTS PR00304
SUPFAM SSF48592
SSF52029
TIGRFAMs TIGR02345
PROSITE PS00750
PS00751
PS00995

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:1904874

positive regulation of telomerase RNA localization to Cajal body

PMID:25467444[1]

ECO:0007001

high throughput mutant phenotypic evidence used in manual assertion

P

  • part_of:(GO:0032212)
  • transports_or_maintains_localization_of:(RNAcentral:URS00004A7003_9606)
  • transports_or_maintains_localization_of:(RNAcentral:URS00004416C5_9606)

Seeded From UniProt

complete

involved_in

GO:1904871

positive regulation of protein localization to Cajal body

PMID:25467444[1]

ECO:0007001

high throughput mutant phenotypic evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032212

positive regulation of telomere maintenance via telomerase

PMID:25467444[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:Q9BUR4)

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:25467444[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

stabilizes:(UniProtKB:Q9BUR4)

Seeded From UniProt

complete

part_of

GO:0005832

chaperonin-containing T-complex

PMID:23011926[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:20458337[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000639)

Seeded From UniProt

complete

involved_in

GO:1904851

positive regulation of establishment of protein localization to telomere

PMID:25467444[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

transports_or_maintains_localization_of:(UniProtKB:Q9BUR4)

Seeded From UniProt

complete

part_of

GO:0005874

microtubule

PMID:21525035[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005832

chaperonin-containing T-complex

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:107184
PANTHER:PTN000143937
PomBase:SPBC25H2.12c
SGD:S000003647
UniProtKB:O77323
UniProtKB:Q2NKZ1
UniProtKB:Q99832

C

Seeded From UniProt

complete

involved_in

GO:1901998

toxin transport

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P80313
ensembl:ENSMUSP00000032078

P

Seeded From UniProt

complete

part_of

GO:0044297

cell body

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P80313
ensembl:ENSMUSP00000032078

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P80313
ensembl:ENSMUSP00000032078

F

Seeded From UniProt

complete

involved_in

GO:0007339

binding of sperm to zona pellucida

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P80313
ensembl:ENSMUSP00000032078

P

Seeded From UniProt

complete

part_of

GO:0005832

chaperonin-containing T-complex

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P80313
ensembl:ENSMUSP00000032078

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002194
InterPro:IPR002423
InterPro:IPR012720

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002194
InterPro:IPR012720

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002194
InterPro:IPR012720

F

Seeded From UniProt

complete

part_of

GO:0005832

chaperonin-containing T-complex

PMID:25467444[1]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9819444[6]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:9819444[6]
Reactome:R-HSA-390466

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:9819444[6]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-8850539
Reactome:R-HSA-8850534
Reactome:R-HSA-8850529
Reactome:R-HSA-8850527
Reactome:R-HSA-6814124
Reactome:R-HSA-6814121
Reactome:R-HSA-6814120
Reactome:R-HSA-6814119
Reactome:R-HSA-391266

ECO:0000304

author statement supported by traceable reference used in manual assertion









C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Freund, A et al. (2014) Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1. Cell 159 1389-403 PubMed GONUTS page
  2. ↑ Knee, KM et al. (2013) Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress Chaperones 18 137-44 PubMed GONUTS page
  3. ↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
  4. ↑ Bharti, P et al. (2011) PEX14 is required for microtubule-based peroxisome motility in human cells. J. Cell. Sci. 124 1759-68 PubMed GONUTS page
  5. ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Won, KA et al. (1998) Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. Mol. Cell. Biol. 18 7584-9 PubMed GONUTS page
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