HUMAN:TCPG

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CCT3 (synonyms: CCTG, TRIC5)
Protein Name(s)	T-complex protein 1 subunit gamma TCP-1-gamma CCT-gamma hTRiC5
External Links
UniProt	P49368
EMBL	AK293477 AL833197 AL589685 BC006501 BC008019 X74801 U17104
CCDS	CCDS1140.2 CCDS30888.1
PIR	S61529
RefSeq	NP_001008800.1 NP_005989.3
UniGene	Hs.491494
ProteinModelPortal	P49368
SMR	P49368
BioGrid	113054
DIP	DIP-32970N
IntAct	P49368
MINT	MINT-260598
STRING	9606.ENSP00000357244
PhosphoSite	P49368
DMDM	66774185
DOSAC-COBS-2DPAGE	P49368
OGP	P49368
SWISS-2DPAGE	P49368
MaxQB	P49368
PaxDb	P49368
PRIDE	P49368
DNASU	7203
Ensembl	ENST00000295688 ENST00000368259
GeneID	7203
KEGG	hsa:7203
UCSC	uc001fol.2 uc001fon.2
CTD	7203
GeneCards	GC01M156278
HGNC	HGNC:1616
HPA	HPA006543
MIM	600114
neXtProt	NX_P49368
PharmGKB	PA26180
eggNOG	COG0459
GeneTree	ENSGT00570000079224
HOGENOM	HOG000226732
HOVERGEN	HBG104982
InParanoid	P49368
KO	K09495
OMA	TQCGLFE
OrthoDB	EOG7DJSKS
PhylomeDB	P49368
TreeFam	TF105649
Reactome	REACT_16907 REACT_16936 REACT_16956 REACT_17050
ChiTaRS	CCT3
GeneWiki	CCT3
GenomeRNAi	7203
NextBio	28226
PRO	PR:P49368
Proteomes	UP000005640
Bgee	P49368
CleanEx	HS_CCT3
ExpressionAtlas	P49368
Genevestigator	P49368
GO	GO:0044297 GO:0005832 GO:0005737 GO:0005856 GO:0005829 GO:0070062 GO:0005874 GO:0005886 GO:0002199 GO:0005524 GO:0044822 GO:0051082 GO:0051084 GO:0007339 GO:0044267 GO:0006457
Gene3D	1.10.560.10 3.30.260.10 3.50.7.10
InterPro	IPR012719 IPR017998 IPR002194 IPR002423 IPR027409 IPR027413 IPR027410
PANTHER	PTHR11353 PTHR11353:SF63
Pfam	PF00118
PRINTS	PR00304
SUPFAM	SSF48592 SSF52029
TIGRFAMs	TIGR02344
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:1904871	positive regulation of protein localization to Cajal body	PMID:25467444^[1]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P	transports_or_maintains_localization_of:(UniProtKB:Q9BUR4) part_of:(GO:0032212) part_of:(GO:0051973)	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:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[5]	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
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
enables	GO:0003723	RNA binding	PMID:22681889^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005874	microtubule	PMID:21525035^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005832	chaperonin-containing T-complex	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104708 PANTHER:PTN000143681 PomBase:SPBC1A4.08c SGD:S000003551 UniProtKB:P49368 UniProtKB:Q3T0K2 UniProtKB:Q8I5C4	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901998	toxin transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P80318 ensembl:ENSMUSP00000001452	P		Seeded From UniProt	complete
involved_in	GO:0046931	pore complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P80318 ensembl:ENSMUSP00000001452	P		Seeded From UniProt	complete
part_of	GO:0044297	cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P80318 ensembl:ENSMUSP00000001452	C		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:P80318 ensembl:ENSMUSP00000001452	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:P80318 ensembl:ENSMUSP00000001452	C		Seeded From UniProt	complete
part_of	GO:0002199	zona pellucida receptor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P80318 ensembl:ENSMUSP00000001452	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:IPR012719	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:IPR012719	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:IPR012719	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:8573069^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:8001976^[10] Reactome:R-HSA-390466	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:8001976^[10]	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
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
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
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Notes

References

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

↑ ^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
↑ 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
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ 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
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ 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
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Walkley, NA et al. (1996) Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma. Biochem. J. 313 ( Pt 2) 381-9 PubMed GONUTS page
↑ ^10.0 ^10.1 Sévigny, G et al. (1994) Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization. Genomics 22 634-6 PubMed GONUTS page

[PMID:25467444-1] 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

[PMID:23011926-2] 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

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-4] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-5] 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

[PMID:22681889-6] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:21525035-7] 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

[PMID:21873635-8] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8573069-9] Walkley, NA et al. (1996) Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma. Biochem. J. 313 ( Pt 2) 381-9 PubMed GONUTS page

[PMID:8001976-10] 10.0 ^10.1 Sévigny, G et al. (1994) Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization. Genomics 22 634-6 PubMed GONUTS page

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HUMAN:TCPG

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