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P50990 (TCPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-complex protein 1 subunit theta

Short name=TCP-1-theta
Alternative name(s):
CCT-theta
Renal carcinoma antigen NY-REN-15
Gene names
Name:CCT8
Synonyms:C21orf112, CCTQ, KIAA0002
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16

Subunit structure

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. Ref.10 Ref.16

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.16.

Sequence similarities

Belongs to the TCP-1 chaperonin family.

Sequence caution

The sequence BAA02792.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

ATP catabolic process

Traceable author statement Ref.8. Source: GOC

binding of sperm to zona pellucida

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

   Cellular_componentaggresome

Inferred from direct assay. Source: HPA

cell body

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay Ref.16. Source: MGI

chaperonin-containing T-complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay PubMed 16780588. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

zona pellucida receptor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Traceable author statement Ref.8. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50990-1)

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.
Isoform 2 (identifier: P50990-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALHVPKAPGFAQMLKEGAK → M
Note: No experimental confirmation available.
Isoform 3 (identifier: P50990-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: MALHVPKAPG...AATILRELEV → MDQMV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 548547T-complex protein 1 subunit theta
PRO_0000128373

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue231Phosphoserine Ref.13 Ref.14
Modified residue301Phosphotyrosine Ref.14
Modified residue3181N6-acetyllysine Ref.15
Modified residue4001N6-acetyllysine Ref.15
Modified residue4661N6-acetyllysine Ref.15
Modified residue5051Phosphotyrosine Ref.11
Cross-link225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12
Cross-link235Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

Natural variations

Alternative sequence1 – 7878MALHV…RELEV → MDQMV in isoform 3.
VSP_054691
Alternative sequence1 – 2020MALHV…KEGAK → M in isoform 2.
VSP_054692
Natural variant41H → Q.
Corresponds to variant rs16983693 [ dbSNP | Ensembl ].
VAR_052270
Natural variant4091V → I.
Corresponds to variant rs8129954 [ dbSNP | Ensembl ].
VAR_052271

Experimental info

Sequence conflict501N → K Ref.1
Sequence conflict501N → K Ref.2
Sequence conflict3911A → V in BAA02792. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 566A6622BC2D15E9

FASTA54859,621
        10         20         30         40         50         60 
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL 

        70         80         90        100        110        120 
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR 

       130        140        150        160        170        180 
IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA 

       190        200        210        220        230        240 
KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA 

       250        260        270        280        290        300 
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM 

       310        320        330        340        350        360 
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV 

       370        380        390        400        410        420 
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA 

       430        440        450        460        470        480 
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL 

       490        500        510        520        530        540 
DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK 


DWDDDQND 

« Hide

Isoform 2 [UniParc].

Checksum: 7468208B8A3B84E2
Show »

FASTA52957,645
Isoform 3 [UniParc].

Checksum: 2D97E8F445125063
Show »

FASTA47551,586

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[2]"Nucleotide sequence surrounding the locus marker D21S246 on human chromosome 21."
Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.
DNA Res. 2:187-189(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J., Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Cerebellum.
[5]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Chondrosarcoma and Liver.
[7]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421; 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"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] OF 33-65 (ISOFORM 1/2).
[9]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[10]"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACRG.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-235.
Tissue: Mammary cancer.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33528.1.
PIRPC4021.
RefSeqNP_001269836.1. NM_001282907.1. [P50990-2]
NP_001269838.1. NM_001282909.1. [P50990-3]
NP_006576.2. NM_006585.3. [P50990-1]
UniGeneHs.125113.

3D structure databases

ProteinModelPortalP50990.
SMRP50990. Positions 13-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115933. 93 interactions.
DIPDIP-38124N.
IntActP50990. 40 interactions.
MINTMINT-1152593.
STRING9606.ENSP00000286788.

PTM databases

PhosphoSiteP50990.

Polymorphism databases

DMDM9988062.

2D gel databases

OGPP50990.
REPRODUCTION-2DPAGEIPI00784090.
P50990.

Proteomic databases

MaxQBP50990.
PaxDbP50990.
PRIDEP50990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286788; ENSP00000286788; ENSG00000156261.
ENST00000540844; ENSP00000442730; ENSG00000156261.
ENST00000542732; ENSP00000444984; ENSG00000156261.
GeneID10694.
KEGGhsa:10694.
UCSCuc002yna.3. human. [P50990-1]

Organism-specific databases

CTD10694.
GeneCardsGC21M030428.
HGNCHGNC:1623. CCT8.
HPAHPA018520.
HPA021051.
HPA029426.
neXtProtNX_P50990.
PharmGKBPA26186.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000226734.
HOVERGENHBG103107.
InParanoidP50990.
KOK09500.
OMAKDWDDDQ.
OrthoDBEOG7JQBN8.
PhylomeDBP50990.
TreeFamTF105699.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP50990.
BgeeP50990.
CleanExHS_CCT8.
GenevestigatorP50990.

Family and domain databases

Gene3D1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProIPR012721. 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]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00304. TCOMPLEXTCP1.
SUPFAMSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsTIGR02346. chap_CCT_theta. 1 hit.
PROSITEPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCT8. human.
GeneWikiCCT8.
GenomeRNAi10694.
NextBio35471264.
PROP50990.

Entry information

Entry nameTCPQ_HUMAN
AccessionPrimary (citable) accession number: P50990
Secondary accession number(s): A6NN54 expand/collapse secondary AC list , B4DEM7, B4DQH4, Q4VBP8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM