P50990 (TCPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CCT8
Synonyms:	C21orf112, CCTQ, KIAA0002

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.15
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.9 Ref.15
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › microtubule organizing center › centrosome Ref.15.
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 component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete 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.7. 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_component	aggresome Inferred from direct assay. Source: HPA cell body Inferred from electronic annotation. Source: Ensembl centrosome Inferred from direct assay Ref.15. 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 20458337. 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 548	547	T-complex protein 1 subunit theta		PRO_0000128373
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
	Modified residue	23	1	Phosphoserine Ref.12 Ref.13
	Modified residue	30	1	Phosphotyrosine Ref.13
	Modified residue	318	1	N6-acetyllysine Ref.14
	Modified residue	400	1	N6-acetyllysine Ref.14
	Modified residue	466	1	N6-acetyllysine Ref.14
	Modified residue	505	1	Phosphotyrosine Ref.10
	Cross-link	225		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
	Cross-link	235		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Natural variations
	Natural variant	4	1	H → Q. Corresponds to variant rs16983693 [ dbSNP | Ensembl ].		VAR_052270
	Natural variant	409	1	V → I. Corresponds to variant rs8129954 [ dbSNP | Ensembl ].		VAR_052271
Experimental info
	Sequence conflict	50	1	N → K Ref.1
	Sequence conflict	50	1	N → K Ref.2
	Sequence conflict	391	1	A → V in BAA02792. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P50990 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 566A6622BC2D15E9	FASTA	548	59,621
	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

References

	« Hide 'large scale' referencesShow '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]. 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]	"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. , 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].
[5]	"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]. Tissue: Chondrosarcoma and Liver.
[6]	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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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].
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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].
[15]	"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.
[16]	"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. AL163249 Genomic DNA. Translation: CAB90433.1. BC072001 mRNA. Translation: AAH72001.1. BC095470 mRNA. Translation: AAH95470.1. Z37163 mRNA. Translation: CAA85520.1.
PIR	PC4021.
RefSeq	NP_001269836.1. NM_001282907.1. NP_001269838.1. NM_001282909.1. NP_006576.2. NM_006585.3.
UniGene	Hs.125113.
3D structure databases
ProteinModelPortal	P50990.
SMR	P50990. Positions 13-528.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	115933. 92 interactions.
DIP	DIP-38124N.
IntAct	P50990. 40 interactions.
MINT	MINT-1152593.
STRING	9606.ENSP00000286788.
PTM databases
PhosphoSite	P50990.
Polymorphism databases
DMDM	9988062.
2D gel databases
OGP	P50990.
REPRODUCTION-2DPAGE	IPI00784090. P50990.
Proteomic databases
PaxDb	P50990.
PRIDE	P50990.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286788; ENSP00000286788; ENSG00000156261.
GeneID	10694.
KEGG	hsa:10694.
UCSC	uc002yna.3. human.
Organism-specific databases
CTD	10694.
GeneCards	GC21M030428.
HGNC	HGNC:1623. CCT8.
HPA	HPA018520. HPA021051. HPA029426.
neXtProt	NX_P50990.
PharmGKB	PA26186.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0459.
HOGENOM	HOG000226734.
HOVERGEN	HBG103107.
InParanoid	P50990.
KO	K09500.
OMA	KDWDDDQ.
OrthoDB	EOG7JQBN8.
PhylomeDB	P50990.
TreeFam	TF105699.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P50990.
Bgee	P50990.
CleanEx	HS_CCT8.
Genevestigator	P50990.
Family and domain databases
Gene3D	1.10.560.10. 2 hits. 3.30.260.10. 2 hits. 3.50.7.10. 1 hit.
InterPro	IPR012721. 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]
PANTHER	PTHR11353. PTHR11353. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. [Graphical view]
PRINTS	PR00304. TCOMPLEXTCP1.
SUPFAM	SSF48592. SSF48592. 2 hits. SSF52029. SSF52029. 1 hit.
TIGRFAMs	TIGR02346. chap_CCT_theta. 1 hit.
PROSITE	PS00750. TCP1_1. 1 hit. PS00751. TCP1_2. 1 hit. PS00995. TCP1_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CCT8. human.
GeneWiki	CCT8.
GenomeRNAi	10694.
NextBio	40649.
PRO	P50990.

Entry information

Entry name

TCPQ_HUMAN

Accession

Primary (citable) accession number: P50990
Secondary accession number(s): A6NN54, Q4VBP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	April 16, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.