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CCT2 chaperonin containing TCP1 subunit 2 [ Homo sapiens (human) ]

Gene ID: 10576, updated on 4-Nov-2018

Summary

Official Symbol
CCT2provided by HGNC
Official Full Name
chaperonin containing TCP1 subunit 2provided by HGNC
Primary source
HGNC:HGNC:1615
See related
Ensembl:ENSG00000166226 MIM:605139; Vega:OTTHUMG00000169383
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
CCTB; 99D8.1; PRO1633; CCT-beta; HEL-S-100n; TCP-1-beta
Summary
The protein encoded by this gene is 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. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
Expression
Broad expression in testis (RPKM 107.5), bone marrow (RPKM 41.1) and 24 other tissues See more
Orthologs

Genomic context

See CCT2 in Genome Data Viewer
Location:
12q15
Exon count:
17
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 12 NC_000012.12 (69585428..69601577)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (69979206..70010595)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes Neighboring gene fibroblast growth factor receptor substrate 2 Neighboring gene small nucleolar RNA, H/ACA box 113 Neighboring gene microRNA 3913-1 Neighboring gene microRNA 3913-2 Neighboring gene uncharacterized LOC105369823 Neighboring gene leucine rich repeat containing 10 Neighboring gene bestrophin 3

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Jun 15 11:32:44 2016

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
Knockdown of chaperonin containing TCP1, subunit 2 (CCT2) by siRNA inhibits HIV-1 replication in HeLa P4/R5 cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Gag-Pol gag-pol Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Nef nef Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Pr55(Gag) gag Tandem affinity purification and mass spectrometry analysis identify chaperonin containing TCP1 subunit 2 (CCT2), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Tat tat Expression of HIV-1 Tat upregulates the abundance of chaperonin containing TCP1, subunit 2 (CCT2) in the nucleoli of Jurkat T-cells PubMed
Vif vif HIV-1 Vif interacts with CCT2 PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • Association of TriC/CCT with target proteins during biosynthesis, organism-specific biosystem (from REACTOME)
    Association of TriC/CCT with target proteins during biosynthesis, organism-specific biosystemTRiC has broad recognition specificities, but in the cell it interacts with only a defined set of substrates (Yam et al. 2008). Many of its substrates that are targeted during biosynthesis are conse...
  • BBSome-mediated cargo-targeting to cilium, organism-specific biosystem (from REACTOME)
    BBSome-mediated cargo-targeting to cilium, organism-specific biosystemThe BBSome is a stable complex consisting of 7 Bardet-Biedl proteins (BBS1, 2, 4, 5, 7, 8 and 9) and BBIP10 that has roles in promoting IFT and trafficking proteins to the cilum (Blacque et al, 2004;...
  • Cargo trafficking to the periciliary membrane, organism-specific biosystem (from REACTOME)
    Cargo trafficking to the periciliary membrane, organism-specific biosystemProteomic studies suggest that the cilium is home to approximately a thousand proteins, and has a unique protein and lipid make up relative to the bulk cytoplasm and plasma membrane (Pazour et al, 20...
  • Chaperonin-mediated protein folding, organism-specific biosystem (from REACTOME)
    Chaperonin-mediated protein folding, organism-specific biosystemThe eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and...
  • Cilium Assembly, organism-specific biosystem (from REACTOME)
    Cilium Assembly, organism-specific biosystemCilia are membrane covered organelles that extend from the surface of eukaryotic cells. Cilia may be motile, such as respiratory cilia) or non-motile (such as the primary cilium) and are distinguishe...
  • Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding, organism-specific biosystem (from REACTOME)
    Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding, organism-specific biosystemThe chaperonin complex TRiC/CCT is needed for the proper folding of all five G-protein beta subunits (Wells et al. 2006). TRiC/CCT cooperates with the phosducin-like protein PDCL (commonly known as P...
  • Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystem (from REACTOME)
    Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystemIn the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
  • Folding of actin by CCT/TriC, organism-specific biosystem (from REACTOME)
    Folding of actin by CCT/TriC, organism-specific biosystemNucleotide-independent transfer of beta-actin from prefoldin to CCT occurs when prefoldin binds to CCT (Vainberg et al., 1998). Following ATP- dependent folding within CCT (Gao et al., 1992), beta-a...
  • Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystem (from REACTOME)
    Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystemTriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Fiv...
  • Immune System, organism-specific biosystem (from REACTOME)
    Immune System, organism-specific biosystemHumans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first crit...
  • Innate Immune System, organism-specific biosystem (from REACTOME)
    Innate Immune System, organism-specific biosystemInnate immunity encompases the nonspecific part of immunity tha are part of an individual's natural biologic makeup
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • Neutrophil degranulation, organism-specific biosystem (from REACTOME)
    Neutrophil degranulation, organism-specific biosystemNeutrophils are the most abundant leukocytes (white blood cells), indispensable in defending the body against invading microorganisms. In response to infection, neutrophils leave the circulation and ...
  • Organelle biogenesis and maintenance, organism-specific biosystem (from REACTOME)
    Organelle biogenesis and maintenance, organism-specific biosystemThis module describes the biogenesis of organelles. Organelles are subcellular structures of distinctive morphology and function. The organelles of human cells include: mitochondria, endoplasmic reti...
  • Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystem (from REACTOME)
    Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystemUnfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
  • Protein folding, organism-specific biosystem (from REACTOME)
    Protein folding, organism-specific biosystemDue to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • MGC142074, MGC142076

Gene Ontology Provided by GOA

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding involved in protein folding IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin protein ligase binding IPI
Inferred from Physical Interaction
more info
PubMed 
unfolded protein binding NAS
Non-traceable Author Statement
more info
PubMed 
Component Evidence Code Pubs
azurophil granule lumen TAS
Traceable Author Statement
more info
 
cell body IEA
Inferred from Electronic Annotation
more info
 
chaperonin-containing T-complex IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
chaperonin-containing T-complex IDA
Inferred from Direct Assay
more info
PubMed 
cytosol IDA
Inferred from Direct Assay
more info
 
cytosol NAS
Non-traceable Author Statement
more info
PubMed 
cytosol TAS
Traceable Author Statement
more info
 
extracellular exosome HDA PubMed 
extracellular region TAS
Traceable Author Statement
more info
 
microtubule IDA
Inferred from Direct Assay
more info
PubMed 
myelin sheath IEA
Inferred from Electronic Annotation
more info
 
zona pellucida receptor complex IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
T-complex protein 1 subunit beta
Names
T-complex protein 1, beta subunit
chaperonin containing TCP1, subunit 2 (beta)
chaperonin containing t-complex polypeptide 1, beta subunit
chaperonin containing t-complex polypeptide 1, subunit 2
epididymis secretory sperm binding protein Li 100n

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001198842.1NP_001185771.1  T-complex protein 1 subunit beta isoform 2

    See identical proteins and their annotated locations for NP_001185771.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (2) is shorter at the N-terminus compared to isoform 1.
    Source sequence(s)
    AA401491, AK316408
    Consensus CDS
    CCDS55843.1
    UniProtKB/Swiss-Prot
    P78371
    Related
    ENSP00000445471.2, OTTHUMP00000240978, ENST00000543146.2, OTTHUMT00000403828
    Conserved Domains (1) summary
    cd03336
    Location:1480
    TCP1_beta; TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL) ...
  2. NM_006431.2NP_006422.1  T-complex protein 1 subunit beta isoform 1

    See identical proteins and their annotated locations for NP_006422.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longer isoform (1).
    Source sequence(s)
    AA401491, AF026166, CB138063
    Consensus CDS
    CCDS8991.1
    UniProtKB/Swiss-Prot
    P78371
    UniProtKB/TrEMBL
    V9HW96
    Related
    ENSP00000299300.6, OTTHUMP00000240975, ENST00000299300.10, OTTHUMT00000403818
    Conserved Domains (1) summary
    cd03336
    Location:11527
    TCP1_beta; TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL) ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000012.12 Reference GRCh38.p12 Primary Assembly

    Range
    69585428..69601577
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
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