Human Gene CCT7 (uc002siz.3) Description and Page Index
  Description: Homo sapiens chaperonin containing TCP1, subunit 7 (eta) (CCT7), transcript variant 1, mRNA.
RefSeq Summary (NM_006429): This gene encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6. [provided by RefSeq, Oct 2009].
Transcript (Including UTRs)
   Position: hg19 chr2:73,461,364-73,480,150 Size: 18,787 Total Exon Count: 12 Strand: +
Coding Region
   Position: hg19 chr2:73,461,507-73,479,989 Size: 18,483 Coding Exon Count: 12 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
Genomic Sequence (chr2:73,461,364-73,480,150)mRNA (may differ from genome)Protein (543 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards
neXtProtOMIMPubMedReactomeStanford SOURCEUniProtKB

-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=T-complex protein 1 subunit eta; Short=TCP-1-eta; AltName: Full=CCT-eta; AltName: Full=HIV-1 Nef-interacting protein;
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 (By similarity).
SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the TCP-1 chaperonin family.

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): CCT7
CDC HuGE Published Literature: CCT7
Positive Disease Associations: Breath Tests
Related Studies:
  1. Breath Tests
    , , . [PubMed 0]
  2. Breath Tests
    , , . [PubMed 0]

-  MalaCards Disease Associations
  MalaCards Gene Search: CCT7
Diseases sorted by gene-association score: myocardial infarction, susceptibility to, 1* (400), myocardial infarction* (100), babesiosis (10), giant axonal neuropathy (5), dupuytren contracture (5)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 125.05 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 3055.24 RPKM

View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -61.60143-0.431 Picture PostScript Text
3' UTR -39.10161-0.243 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR012720 - Chap_CCT_eta
IPR017998 - Chaperone_TCP-1
IPR002194 - Chaperonin_TCP-1_CS
IPR002423 - Cpn60/TCP-1

Pfam Domains:
PF00118 - TCP-1/cpn60 chaperonin family

SCOP Domains:
48592 - GroEL equatorial domain-like
52029 - GroEL apical domain-like
54849 - GroEL-intermediate domain like

ModBase Predicted Comparative 3D Structure on Q99832
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologGenome BrowserGenome BrowserGenome BrowserGenome Browser
Gene Details  Gene DetailsGene DetailsGene Details
Gene Sorter  Gene SorterGene SorterGene Sorter
  Protein SequenceProtein SequenceProtein SequenceProtein Sequence

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0042802 identical protein binding
GO:0044183 protein binding involved in protein folding
GO:0051082 unfolded protein binding

Biological Process:
GO:0006457 protein folding
GO:0006458 'de novo' protein folding
GO:0007339 binding of sperm to zona pellucida
GO:0032212 positive regulation of telomere maintenance via telomerase
GO:0050821 protein stabilization
GO:0061077 chaperone-mediated protein folding
GO:1901998 toxin transport
GO:1904851 positive regulation of establishment of protein localization to telomere
GO:1904871 positive regulation of protein localization to Cajal body
GO:1904874 positive regulation of telomerase RNA localization to Cajal body

Cellular Component:
GO:0002199 zona pellucida receptor complex
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005874 microtubule
GO:0044297 cell body
GO:0070062 extracellular exosome

-  Descriptions from all associated GenBank mRNAs
  BC088351 - Homo sapiens chaperonin containing TCP1, subunit 7 (eta), mRNA (cDNA clone MGC:110985 IMAGE:6202511), complete cds.
AK291961 - Homo sapiens cDNA FLJ77695 complete cds, highly similar to Homo sapiens chaperonin containing TCP1, subunit 7 (eta) (CCT7),mRNA.
AK293597 - Homo sapiens cDNA FLJ54832 complete cds, highly similar to T-complex protein 1 subunit eta.
AK297846 - Homo sapiens cDNA FLJ54074 complete cds, highly similar to T-complex protein 1 subunit eta.
AK298153 - Homo sapiens cDNA FLJ59364 complete cds, highly similar to T-complex protein 1 subunit eta.
AK302078 - Homo sapiens cDNA FLJ54568 complete cds, highly similar to T-complex protein 1 subunit eta.
AK098549 - Homo sapiens cDNA FLJ25683 fis, clone TST04180, highly similar to T-COMPLEX PROTEIN 1, ETA SUBUNIT.
AK293175 - Homo sapiens cDNA FLJ59454 complete cds, highly similar to T-complex protein 1 subunit eta.
AF026292 - Homo sapiens chaperonin containing t-complex polypeptide 1, eta subunit (Ccth) mRNA, complete cds.
BC019296 - Homo sapiens chaperonin containing TCP1, subunit 7 (eta), mRNA (cDNA clone MGC:4110 IMAGE:2905446), complete cds.
JD192140 - Sequence 173164 from Patent EP1572962.
AK222478 - Homo sapiens mRNA for chaperonin containing TCP1, subunit 7 (eta) variant, clone: adKA03022.
JD066587 - Sequence 47611 from Patent EP1572962.
CU676420 - Synthetic construct Homo sapiens gateway clone IMAGE:100023479 5' read CCT7 mRNA.
CR456719 - Homo sapiens full open reading frame cDNA clone RZPDo834H033D for gene CCT7, chaperonin containing TCP1, subunit 7 (eta); complete cds, incl. stopcodon.
AB385063 - Synthetic construct DNA, clone: pF1KB5205, Homo sapiens CCT7 gene for T-complex protein 1 subunit eta, complete cds, without stop codon, in Flexi system.
DQ893464 - Synthetic construct clone IMAGE:100006094; FLH193374.01X; RZPDo839F0778D chaperonin containing TCP1, subunit 7 (eta) (CCT7) gene, encodes complete protein.
DQ896334 - Synthetic construct Homo sapiens clone IMAGE:100010794; FLH193370.01L; RZPDo839F0768D chaperonin containing TCP1, subunit 7 (eta) (CCT7) gene, encodes complete protein.
CR536511 - Homo sapiens full open reading frame cDNA clone RZPDo834H1221D for gene CCT7, chaperonin containing TCP1, subunit 7 (eta); complete cds, incl. stopcodon.
KJ898247 - Synthetic construct Homo sapiens clone ccsbBroadEn_07641 CCT7 gene, encodes complete protein.
U83843 - Human HIV-1 Nef interacting protein (Nip7-1) mRNA, partial cds.
DQ586779 - Homo sapiens piRNA piR-53891, complete sequence.
AK098825 - Homo sapiens cDNA FLJ25959 fis, clone TST06756, highly similar to T-COMPLEX PROTEIN 1, ETA SUBUNIT.
JD363830 - Sequence 344854 from Patent EP1572962.
JD543815 - Sequence 524839 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q99832 (Reactome details) participates in the following event(s):

R-HSA-389954 Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC
R-HSA-389961 ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex
R-HSA-389970 Actin/tubulin:prefoldin complex associates with CCT/TriC
R-HSA-390470 Association of CCT/TriC with other substrates during biosynthesis (unknown chaperone)
R-HSA-391266 Association of CCT/TriC with sphingosine kinase 1
R-HSA-6814119 TRiC/CCT binds unfolded G-protein beta subunit
R-HSA-390453 Hydrolysis of ATP and release of folded actin from CCT/TriC
R-HSA-8850527 PDCL releases folded G-beta from TRiC/CCT
R-HSA-8850539 Release of GNB5:RGS dimers from CCT/TRiC
R-HSA-390459 Exchange of ADP for ATP in CCT/TriC:actin complex
R-HSA-6814124 ATP binds G-protein beta associated TRiC/CCT
R-HSA-8850529 RGS proteins bind GNB5 and CCT/TRiC
R-HSA-8850534 PDCL promotes G-protein beta 5 folding
R-HSA-6814121 PDCL binds G-protein beta and TRiC/CCT
R-HSA-6814120 ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-390450 Folding of actin by CCT/TriC
R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding
R-HSA-390466 Chaperonin-mediated protein folding
R-HSA-391251 Protein folding
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: A8K7E6, A8MWI8, B7WNW9, B7Z4T9, B7Z4Z7, CCTH, NIP7-1, NM_006429, NP_001159757, O14871, Q6FI26, Q99832, TCPH_HUMAN
UCSC ID: uc002siz.3
RefSeq Accession: NM_006429
Protein: Q99832 (aka TCPH_HUMAN)
CCDS: CCDS46336.1

-  Gene Model Information
category: coding nonsense-mediated-decay: no RNA accession: NM_006429.3
exon count: 12CDS single in 3' UTR: no RNA size: 1948
ORF size: 1632CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 3464.00frame shift in genome: no % Coverage: 99.38
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.