Full text data of CCT8
CCT8
(C21orf112, CCTQ, KIAA0002)
[Confidence: high (present in two of the MS resources)]
T-complex protein 1 subunit theta; TCP-1-theta (CCT-theta; Renal carcinoma antigen NY-REN-15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit theta; TCP-1-theta (CCT-theta; Renal carcinoma antigen NY-REN-15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00302925
IPI00302925 T-complex protein 1, theta subunit Molecular chaperone; assist the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00302925 T-complex protein 1, theta subunit Molecular chaperone; assist the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P50990
ID TCPQ_HUMAN Reviewed; 548 AA.
AC P50990; A6NN54; Q4VBP8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
DE AltName: Full=Renal carcinoma antigen NY-REN-15;
GN Name=CCT8; Synonyms=C21orf112, CCTQ, KIAA0002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I.
RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT analysis of randomly sampled cDNA clones from human immature myeloid
RT cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8590283; DOI=10.1093/dnares/2.4.187;
RA Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.;
RT "Nucleotide sequence surrounding the locus marker D21S246 on human
RT chromosome 21.";
RL DNA Res. 2:187-189(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J.,
RA Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421;
RP 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-65.
RX PubMed=7890169; DOI=10.1016/0378-1119(94)00880-2;
RA Kubota H., Hynes G., Willison K.;
RT "The eighth Cct gene, Cctq, encoding the theta subunit of the
RT cytosolic chaperonin containing TCP-1.";
RL Gene 154:231-236(1995).
RN [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.M309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-235, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN BBS/CCT COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02792.2; Type=Erroneous initiation;
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DR EMBL; D13627; BAA02792.2; ALT_INIT; mRNA.
DR EMBL; D42052; BAA07652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163249; CAB90433.1; -; Genomic_DNA.
DR EMBL; BC072001; AAH72001.1; -; mRNA.
DR EMBL; BC095470; AAH95470.1; -; mRNA.
DR EMBL; Z37163; CAA85520.1; -; mRNA.
DR PIR; PC4021; PC4021.
DR RefSeq; NP_001269836.1; NM_001282907.1.
DR RefSeq; NP_001269838.1; NM_001282909.1.
DR RefSeq; NP_006576.2; NM_006585.3.
DR UniGene; Hs.125113; -.
DR ProteinModelPortal; P50990; -.
DR SMR; P50990; 13-528.
DR DIP; DIP-38124N; -.
DR IntAct; P50990; 38.
DR MINT; MINT-1152593; -.
DR STRING; 9606.ENSP00000286788; -.
DR PhosphoSite; P50990; -.
DR DMDM; 9988062; -.
DR OGP; P50990; -.
DR REPRODUCTION-2DPAGE; IPI00784090; -.
DR REPRODUCTION-2DPAGE; P50990; -.
DR PaxDb; P50990; -.
DR PRIDE; P50990; -.
DR Ensembl; ENST00000286788; ENSP00000286788; ENSG00000156261.
DR GeneID; 10694; -.
DR KEGG; hsa:10694; -.
DR UCSC; uc002yna.3; human.
DR CTD; 10694; -.
DR GeneCards; GC21M030428; -.
DR HGNC; HGNC:1623; CCT8.
DR HPA; HPA018520; -.
DR HPA; HPA021051; -.
DR HPA; HPA029426; -.
DR neXtProt; NX_P50990; -.
DR PharmGKB; PA26186; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226734; -.
DR HOVERGEN; HBG103107; -.
DR InParanoid; P50990; -.
DR KO; K09500; -.
DR OMA; KDWDDDQ; -.
DR OrthoDB; EOG7JQBN8; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT8; human.
DR GeneWiki; CCT8; -.
DR GenomeRNAi; 10694; -.
DR NextBio; 40649; -.
DR PRO; PR:P50990; -.
DR ArrayExpress; P50990; -.
DR Bgee; P50990; -.
DR CleanEx; HS_CCT8; -.
DR Genevestigator; P50990; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042623; F:ATPase activity, coupled; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02346; chap_CCT_theta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 548 T-complex protein 1 subunit theta.
FT /FTId=PRO_0000128373.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 23 23 Phosphoserine.
FT MOD_RES 30 30 Phosphotyrosine.
FT MOD_RES 318 318 N6-acetyllysine.
FT MOD_RES 400 400 N6-acetyllysine.
FT MOD_RES 466 466 N6-acetyllysine.
FT MOD_RES 505 505 Phosphotyrosine.
FT CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 4 4 H -> Q (in dbSNP:rs16983693).
FT /FTId=VAR_052270.
FT VARIANT 409 409 V -> I (in dbSNP:rs8129954).
FT /FTId=VAR_052271.
FT CONFLICT 50 50 N -> K (in Ref. 1 and 2).
FT CONFLICT 391 391 A -> V (in Ref. 1; BAA02792).
SQ SEQUENCE 548 AA; 59621 MW; 566A6622BC2D15E9 CRC64;
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR
IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA
KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL
DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
DWDDDQND
//
ID TCPQ_HUMAN Reviewed; 548 AA.
AC P50990; A6NN54; Q4VBP8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
DE AltName: Full=Renal carcinoma antigen NY-REN-15;
GN Name=CCT8; Synonyms=C21orf112, CCTQ, KIAA0002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I.
RT The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT analysis of randomly sampled cDNA clones from human immature myeloid
RT cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8590283; DOI=10.1093/dnares/2.4.187;
RA Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.;
RT "Nucleotide sequence surrounding the locus marker D21S246 on human
RT chromosome 21.";
RL DNA Res. 2:187-189(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J.,
RA Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421;
RP 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-65.
RX PubMed=7890169; DOI=10.1016/0378-1119(94)00880-2;
RA Kubota H., Hynes G., Willison K.;
RT "The eighth Cct gene, Cctq, encoding the theta subunit of the
RT cytosolic chaperonin containing TCP-1.";
RL Gene 154:231-236(1995).
RN [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.M309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-235, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN BBS/CCT COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family
RT chaperonins and mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC role in the assembly of BBSome, a complex involved in ciliogenesis
CC regulating transports vesicles to the cilia. Known to play a role,
CC in vitro, in the folding of actin and tubulin.
CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02792.2; Type=Erroneous initiation;
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DR EMBL; D13627; BAA02792.2; ALT_INIT; mRNA.
DR EMBL; D42052; BAA07652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163249; CAB90433.1; -; Genomic_DNA.
DR EMBL; BC072001; AAH72001.1; -; mRNA.
DR EMBL; BC095470; AAH95470.1; -; mRNA.
DR EMBL; Z37163; CAA85520.1; -; mRNA.
DR PIR; PC4021; PC4021.
DR RefSeq; NP_001269836.1; NM_001282907.1.
DR RefSeq; NP_001269838.1; NM_001282909.1.
DR RefSeq; NP_006576.2; NM_006585.3.
DR UniGene; Hs.125113; -.
DR ProteinModelPortal; P50990; -.
DR SMR; P50990; 13-528.
DR DIP; DIP-38124N; -.
DR IntAct; P50990; 38.
DR MINT; MINT-1152593; -.
DR STRING; 9606.ENSP00000286788; -.
DR PhosphoSite; P50990; -.
DR DMDM; 9988062; -.
DR OGP; P50990; -.
DR REPRODUCTION-2DPAGE; IPI00784090; -.
DR REPRODUCTION-2DPAGE; P50990; -.
DR PaxDb; P50990; -.
DR PRIDE; P50990; -.
DR Ensembl; ENST00000286788; ENSP00000286788; ENSG00000156261.
DR GeneID; 10694; -.
DR KEGG; hsa:10694; -.
DR UCSC; uc002yna.3; human.
DR CTD; 10694; -.
DR GeneCards; GC21M030428; -.
DR HGNC; HGNC:1623; CCT8.
DR HPA; HPA018520; -.
DR HPA; HPA021051; -.
DR HPA; HPA029426; -.
DR neXtProt; NX_P50990; -.
DR PharmGKB; PA26186; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226734; -.
DR HOVERGEN; HBG103107; -.
DR InParanoid; P50990; -.
DR KO; K09500; -.
DR OMA; KDWDDDQ; -.
DR OrthoDB; EOG7JQBN8; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT8; human.
DR GeneWiki; CCT8; -.
DR GenomeRNAi; 10694; -.
DR NextBio; 40649; -.
DR PRO; PR:P50990; -.
DR ArrayExpress; P50990; -.
DR Bgee; P50990; -.
DR CleanEx; HS_CCT8; -.
DR Genevestigator; P50990; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042623; F:ATPase activity, coupled; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom.
DR InterPro; IPR027413; GROEL-like_equatorial.
DR InterPro; IPR027410; TCP-1-like_intermed.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02346; chap_CCT_theta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 548 T-complex protein 1 subunit theta.
FT /FTId=PRO_0000128373.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 23 23 Phosphoserine.
FT MOD_RES 30 30 Phosphotyrosine.
FT MOD_RES 318 318 N6-acetyllysine.
FT MOD_RES 400 400 N6-acetyllysine.
FT MOD_RES 466 466 N6-acetyllysine.
FT MOD_RES 505 505 Phosphotyrosine.
FT CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 235 235 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 4 4 H -> Q (in dbSNP:rs16983693).
FT /FTId=VAR_052270.
FT VARIANT 409 409 V -> I (in dbSNP:rs8129954).
FT /FTId=VAR_052271.
FT CONFLICT 50 50 N -> K (in Ref. 1 and 2).
FT CONFLICT 391 391 A -> V (in Ref. 1; BAA02792).
SQ SEQUENCE 548 AA; 59621 MW; 566A6622BC2D15E9 CRC64;
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR
IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA
KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL
DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
DWDDDQND
//