Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit theta

Gene

CCT8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.1 Publication

GO - Molecular functioni

  • ATPase activity, coupled Source: ProtInc
  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

GO - Biological processi

  • binding of sperm to zona pellucida Source: Ensembl
  • pore complex assembly Source: Ensembl
  • positive regulation of establishment of protein localization to telomere Source: BHF-UCL
  • positive regulation of protein localization to Cajal body Source: BHF-UCL
  • positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein folding Source: Reactome
  • protein stabilization Source: BHF-UCL
  • toxin transport Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000156261-MONOMER.
ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5620922. BBSome-mediated cargo-targeting to cilium.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit theta
Short name:
TCP-1-theta
Alternative name(s):
CCT-theta
Renal carcinoma antigen NY-REN-15
Gene namesi
Name:CCT8
Synonyms:C21orf112, CCTQ, KIAA0002
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:1623. CCT8.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • centrosome Source: MGI
  • chaperonin-containing T-complex Source: UniProtKB
  • cilium Source: UniProtKB-KW
  • cytoplasm Source: BHF-UCL
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • intermediate filament cytoskeleton Source: HPA
  • microtubule Source: UniProtKB
  • nucleoplasm Source: HPA
  • zona pellucida receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi10694.
OpenTargetsiENSG00000156261.
PharmGKBiPA26186.

Polymorphism and mutation databases

BioMutaiCCT8.
DMDMi9988062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001283732 – 548T-complex protein 1 subunit thetaAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei23PhosphoserineCombined sources1
Modified residuei30PhosphotyrosineCombined sources1
Modified residuei162PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei269PhosphoserineCombined sources1
Modified residuei317PhosphoserineCombined sources1
Modified residuei318N6-acetyllysineCombined sources1
Modified residuei400N6-acetyllysineCombined sources1
Cross-linki459Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei466N6-acetyllysineCombined sources1
Modified residuei505PhosphotyrosineCombined sources1
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei537PhosphoserineCombined sources1
Cross-linki539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP50990.
MaxQBiP50990.
PaxDbiP50990.
PeptideAtlasiP50990.
PRIDEiP50990.
TopDownProteomicsiP50990-1. [P50990-1]

2D gel databases

OGPiP50990.
REPRODUCTION-2DPAGEIPI00784090.
P50990.

PTM databases

iPTMnetiP50990.
PhosphoSitePlusiP50990.
SwissPalmiP50990.

Expressioni

Gene expression databases

BgeeiENSG00000156261.
CleanExiHS_CCT8.
ExpressionAtlasiP50990. baseline and differential.
GenevisibleiP50990. HS.

Organism-specific databases

HPAiHPA018520.
HPA021051.
HPA029426.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Interacts with DYX1C1 (By similarity).By similarity

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi115933. 179 interactors.
DIPiDIP-38124N.
IntActiP50990. 112 interactors.
MINTiMINT-1152593.
STRINGi9606.ENSP00000286788.

Structurei

3D structure databases

ProteinModelPortaliP50990.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiP50990.
KOiK09500.
OMAiKYGLMAV.
OrthoDBiEOG091G05WZ.
PhylomeDBiP50990.
TreeFamiTF105699.

Family and domain databases

CDDicd03341. TCP1_theta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P50990-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN
60 70 80 90 100
GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG
110 120 130 140 150
TNFVLVFAGA LLELAEELLR IGLSVSEVIE GYEIACRKAH EILPNLVCCS
160 170 180 190 200
AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA KLIAQACVSI FPDSGHFNVD
210 220 230 240 250
NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI
260 270 280 290 300
TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM
310 320 330 340 350
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV
360 370 380 390 400
YLSEVGDTQV VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK
410 420 430 440 450
VLTRDKRLVP GGGATEIELA KQITSYGETC PGLEQYAIKK FAEAFEAIPR
460 470 480 490 500
ALAENSGVKA NEVISKLYAV HQEGNKNVGL DIEAEVPAVK DMLEAGILDT
510 520 530 540
YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDDDQND
Length:548
Mass (Da):59,621
Last modified:January 23, 2007 - v4
Checksum:i566A6622BC2D15E9
GO
Isoform 2 (identifier: P50990-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALHVPKAPGFAQMLKEGAK → M

Note: No experimental confirmation available.
Show »
Length:529
Mass (Da):57,645
Checksum:i7468208B8A3B84E2
GO
Isoform 3 (identifier: P50990-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: MALHVPKAPG...AATILRELEV → MDQMV

Note: No experimental confirmation available.
Show »
Length:475
Mass (Da):51,586
Checksum:i2D97E8F445125063
GO

Sequence cautioni

The sequence BAA02792 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50N → K (PubMed:7584026).Curated1
Sequence conflicti50N → K (PubMed:8590283).Curated1
Sequence conflicti391A → V in BAA02792 (PubMed:7584026).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0522704H → Q.Corresponds to variant rs16983693dbSNPEnsembl.1
Natural variantiVAR_052271409V → I.Corresponds to variant rs8129954dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0546911 – 78MALHV…RELEV → MDQMV in isoform 3. 1 PublicationAdd BLAST78
Alternative sequenceiVSP_0546921 – 20MALHV…KEGAK → M in isoform 2. 1 PublicationAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13627 mRNA. Translation: BAA02792.2. Different initiation.
D42052 Genomic DNA. Translation: BAA07652.1. Sequence problems.
AF129075 Genomic DNA. No translation available.
AK293705 mRNA. Translation: BAG57138.1.
AK298801 mRNA. Translation: BAG60936.1.
AL163249 Genomic DNA. Translation: CAB90433.1.
BC072001 mRNA. Translation: AAH72001.1.
BC095470 mRNA. Translation: AAH95470.1.
Z37163 mRNA. Translation: CAA85520.1.
CCDSiCCDS33528.1. [P50990-1]
CCDS68180.1. [P50990-3]
CCDS68181.1. [P50990-2]
PIRiPC4021.
RefSeqiNP_001269836.1. NM_001282907.1. [P50990-2]
NP_001269838.1. NM_001282909.1. [P50990-3]
NP_006576.2. NM_006585.3. [P50990-1]
UniGeneiHs.125113.

Genome annotation databases

EnsembliENST00000286788; ENSP00000286788; ENSG00000156261. [P50990-1]
ENST00000540844; ENSP00000442730; ENSG00000156261. [P50990-3]
ENST00000626972; ENSP00000486921; ENSG00000156261. [P50990-2]
GeneIDi10694.
KEGGihsa:10694.
UCSCiuc002ynb.5. human. [P50990-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13627 mRNA. Translation: BAA02792.2. Different initiation.
D42052 Genomic DNA. Translation: BAA07652.1. Sequence problems.
AF129075 Genomic DNA. No translation available.
AK293705 mRNA. Translation: BAG57138.1.
AK298801 mRNA. Translation: BAG60936.1.
AL163249 Genomic DNA. Translation: CAB90433.1.
BC072001 mRNA. Translation: AAH72001.1.
BC095470 mRNA. Translation: AAH95470.1.
Z37163 mRNA. Translation: CAA85520.1.
CCDSiCCDS33528.1. [P50990-1]
CCDS68180.1. [P50990-3]
CCDS68181.1. [P50990-2]
PIRiPC4021.
RefSeqiNP_001269836.1. NM_001282907.1. [P50990-2]
NP_001269838.1. NM_001282909.1. [P50990-3]
NP_006576.2. NM_006585.3. [P50990-1]
UniGeneiHs.125113.

3D structure databases

ProteinModelPortaliP50990.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115933. 179 interactors.
DIPiDIP-38124N.
IntActiP50990. 112 interactors.
MINTiMINT-1152593.
STRINGi9606.ENSP00000286788.

PTM databases

iPTMnetiP50990.
PhosphoSitePlusiP50990.
SwissPalmiP50990.

Polymorphism and mutation databases

BioMutaiCCT8.
DMDMi9988062.

2D gel databases

OGPiP50990.
REPRODUCTION-2DPAGEIPI00784090.
P50990.

Proteomic databases

EPDiP50990.
MaxQBiP50990.
PaxDbiP50990.
PeptideAtlasiP50990.
PRIDEiP50990.
TopDownProteomicsiP50990-1. [P50990-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286788; ENSP00000286788; ENSG00000156261. [P50990-1]
ENST00000540844; ENSP00000442730; ENSG00000156261. [P50990-3]
ENST00000626972; ENSP00000486921; ENSG00000156261. [P50990-2]
GeneIDi10694.
KEGGihsa:10694.
UCSCiuc002ynb.5. human. [P50990-1]

Organism-specific databases

CTDi10694.
DisGeNETi10694.
GeneCardsiCCT8.
HGNCiHGNC:1623. CCT8.
HPAiHPA018520.
HPA021051.
HPA029426.
neXtProtiNX_P50990.
OpenTargetsiENSG00000156261.
PharmGKBiPA26186.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
GeneTreeiENSGT00550000074783.
HOGENOMiHOG000226734.
HOVERGENiHBG103107.
InParanoidiP50990.
KOiK09500.
OMAiKYGLMAV.
OrthoDBiEOG091G05WZ.
PhylomeDBiP50990.
TreeFamiTF105699.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000156261-MONOMER.
ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5620922. BBSome-mediated cargo-targeting to cilium.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

ChiTaRSiCCT8. human.
GeneWikiiCCT8.
GenomeRNAii10694.
PROiP50990.

Gene expression databases

BgeeiENSG00000156261.
CleanExiHS_CCT8.
ExpressionAtlasiP50990. baseline and differential.
GenevisibleiP50990. HS.

Family and domain databases

CDDicd03341. TCP1_theta. 1 hit.
Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012721. Chap_CCT_theta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02346. chap_CCT_theta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTCPQ_HUMAN
AccessioniPrimary (citable) accession number: P50990
Secondary accession number(s): A6NN54
, B4DEM7, B4DQH4, Q4VBP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 169 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.