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Protein

T-complex protein 1 subunit theta

Gene

Cct8

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-MMU-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
Gene namesi
Name:Cct8
Synonyms:Cctq
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:107183. Cct8.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 548547T-complex protein 1 subunit thetaPRO_0000128374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei30 – 301PhosphotyrosineBy similarity
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki235 – 235Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei400 – 4001N6-acetyllysineCombined sources
Modified residuei466 – 4661N6-acetyllysineBy similarity
Modified residuei505 – 5051PhosphotyrosineBy similarity
Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki539 – 539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP42932.
PaxDbiP42932.
PRIDEiP42932.

2D gel databases

REPRODUCTION-2DPAGEP42932.

PTM databases

iPTMnetiP42932.
PhosphoSiteiP42932.
SwissPalmiP42932.

Expressioni

Gene expression databases

BgeeiP42932.
CleanExiMM_CCT8.
ExpressionAtlasiP42932. baseline and differential.
GenevisibleiP42932. MM.

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 (By similarity). Interacts with DYX1C1.By similarity1 Publication

Protein-protein interaction databases

BioGridi198572. 39 interactions.
IntActiP42932. 39 interactions.
MINTiMINT-1865136.
STRINGi10090.ENSMUSP00000026704.

Structurei

3D structure databases

ProteinModelPortaliP42932.
SMRiP42932. Positions 13-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
HOVERGENiHBG103107.
InParanoidiP42932.
KOiK09500.
OMAiWGLKYAV.
OrthoDBiEOG7JQBN8.
PhylomeDBiP42932.
TreeFamiTF105699.

Family and domain databases

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]

Sequencei

Sequence statusi: Complete.

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

P42932-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALHVPKAPG FAQMLKDGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN
60 70 80 90 100
GMNKMVINRL EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG
110 120 130 140 150
TNFVLVFAGA LLELAEELLR IGLSVSEVIS GYEIACKKAH EILPELVCCS
160 170 180 190 200
AKNLRDVDEV SSLLRTSIMS KQYGSETFLA KLIAQACVSI FPDSGNFNVD
210 220 230 240 250
NIRVCKILGS GIYSSSVLHG MVFKKETEGD VTSVKDAKIA VYSCPFDGMI
260 270 280 290 300
TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIAGTGANV IVTGGKVADI
310 320 330 340 350
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPKLTPPV QEEMGHCDSV
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 NEVISKLYSV HQEGNKNVGL DIEAEVPAVK DMLEASILDT
510 520 530 540
YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK DWDDDQND
Length:548
Mass (Da):59,555
Last modified:January 23, 2007 - v3
Checksum:i4B5265250CFF1FE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37164 mRNA. Translation: CAA85521.1.
BC009007 mRNA. Translation: AAH09007.1.
CCDSiCCDS37384.1.
PIRiJC4073.
RefSeqiNP_033970.3. NM_009840.3.
UniGeneiMm.328673.

Genome annotation databases

EnsembliENSMUST00000026704; ENSMUSP00000026704; ENSMUSG00000025613.
GeneIDi12469.
KEGGimmu:12469.
UCSCiuc007zul.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z37164 mRNA. Translation: CAA85521.1.
BC009007 mRNA. Translation: AAH09007.1.
CCDSiCCDS37384.1.
PIRiJC4073.
RefSeqiNP_033970.3. NM_009840.3.
UniGeneiMm.328673.

3D structure databases

ProteinModelPortaliP42932.
SMRiP42932. Positions 13-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198572. 39 interactions.
IntActiP42932. 39 interactions.
MINTiMINT-1865136.
STRINGi10090.ENSMUSP00000026704.

PTM databases

iPTMnetiP42932.
PhosphoSiteiP42932.
SwissPalmiP42932.

2D gel databases

REPRODUCTION-2DPAGEP42932.

Proteomic databases

EPDiP42932.
PaxDbiP42932.
PRIDEiP42932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026704; ENSMUSP00000026704; ENSMUSG00000025613.
GeneIDi12469.
KEGGimmu:12469.
UCSCiuc007zul.1. mouse.

Organism-specific databases

CTDi10694.
MGIiMGI:107183. Cct8.

Phylogenomic databases

eggNOGiKOG0362. Eukaryota.
ENOG410XPXR. LUCA.
HOVERGENiHBG103107.
InParanoidiP42932.
KOiK09500.
OMAiWGLKYAV.
OrthoDBiEOG7JQBN8.
PhylomeDBiP42932.
TreeFamiTF105699.

Enzyme and pathway databases

ReactomeiR-MMU-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-MMU-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

ChiTaRSiCct8. mouse.
PROiP42932.
SOURCEiSearch...

Gene expression databases

BgeeiP42932.
CleanExiMM_CCT8.
ExpressionAtlasiP42932. baseline and differential.
GenevisibleiP42932. MM.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic chaperonin containing TCP-1."
    Kubota H., Hynes G., Willison K.
    Gene 154:231-236(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 8-16; 63-74; 156-165; 172-181; 207-224; 261-296; 308-314; 368-400; 408-421; 441-450; 477-504 AND 510-520, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J and OF1.
    Tissue: Brain and Hippocampus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: INTERACTION WITH DYX1C1.
  7. Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTCPQ_MOUSE
AccessioniPrimary (citable) accession number: P42932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.