TCPW_HUMAN
ID TCPW_HUMAN Reviewed; 530 AA.
AC Q92526; B4DX20; B4DYB0; Q8TC34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 5.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=T-complex protein 1 subunit zeta-2;
DE Short=TCP-1-zeta-2;
DE AltName: Full=CCT-zeta-2;
DE AltName: Full=CCT-zeta-like;
DE AltName: Full=TCP-1-zeta-like;
DE AltName: Full=Testis-specific Tcp20;
DE AltName: Full=Testis-specific protein TSA303 {ECO:0000303|PubMed:8812458};
GN Name=CCT6B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-247, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8812458; DOI=10.1006/geno.1996.0467;
RA Ozaki K., Kuroki T., Hayashi S., Nakamura Y.;
RT "Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a
RT differential mRNA display method.";
RL Genomics 36:316-319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-17 AND
RP ALA-48.
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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., Buerckstuemmer T.,
RA 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: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis. {ECO:0000305|PubMed:8812458}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter. {ECO:0000305|PubMed:8812458}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8812458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92526-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92526-2; Sequence=VSP_043040;
CC Name=3;
CC IsoId=Q92526-3; Sequence=VSP_047129;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:8812458}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; D78333; BAA11347.1; -; mRNA.
DR EMBL; AK301773; BAG63232.1; -; mRNA.
DR EMBL; AK302344; BAG63672.1; -; mRNA.
DR EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026125; AAH26125.1; -; mRNA.
DR EMBL; BC027591; AAH27591.1; -; mRNA.
DR CCDS; CCDS32617.1; -. [Q92526-1]
DR CCDS; CCDS54105.1; -. [Q92526-2]
DR CCDS; CCDS54106.1; -. [Q92526-3]
DR RefSeq; NP_001180458.1; NM_001193529.2. [Q92526-3]
DR RefSeq; NP_001180459.1; NM_001193530.1. [Q92526-2]
DR RefSeq; NP_006575.2; NM_006584.3. [Q92526-1]
DR AlphaFoldDB; Q92526; -.
DR SMR; Q92526; -.
DR BioGRID; 115932; 219.
DR DIP; DIP-53269N; -.
DR IntAct; Q92526; 70.
DR MINT; Q92526; -.
DR STRING; 9606.ENSP00000327191; -.
DR iPTMnet; Q92526; -.
DR PhosphoSitePlus; Q92526; -.
DR SwissPalm; Q92526; -.
DR BioMuta; CCT6B; -.
DR DMDM; 327478610; -.
DR REPRODUCTION-2DPAGE; IPI00220656; -.
DR EPD; Q92526; -.
DR jPOST; Q92526; -.
DR MassIVE; Q92526; -.
DR MaxQB; Q92526; -.
DR PaxDb; Q92526; -.
DR PeptideAtlas; Q92526; -.
DR PRIDE; Q92526; -.
DR ProteomicsDB; 5399; -.
DR ProteomicsDB; 75285; -. [Q92526-1]
DR ProteomicsDB; 75286; -. [Q92526-2]
DR Antibodypedia; 27366; 131 antibodies from 24 providers.
DR DNASU; 10693; -.
DR Ensembl; ENST00000314144.10; ENSP00000327191.5; ENSG00000132141.14. [Q92526-1]
DR Ensembl; ENST00000421975.7; ENSP00000398044.3; ENSG00000132141.14. [Q92526-3]
DR Ensembl; ENST00000436961.7; ENSP00000400917.3; ENSG00000132141.14. [Q92526-2]
DR GeneID; 10693; -.
DR KEGG; hsa:10693; -.
DR MANE-Select; ENST00000314144.10; ENSP00000327191.5; NM_006584.4; NP_006575.2.
DR UCSC; uc002hig.4; human. [Q92526-1]
DR CTD; 10693; -.
DR DisGeNET; 10693; -.
DR GeneCards; CCT6B; -.
DR HGNC; HGNC:1621; CCT6B.
DR HPA; ENSG00000132141; Tissue enriched (testis).
DR MIM; 610730; gene.
DR neXtProt; NX_Q92526; -.
DR OpenTargets; ENSG00000132141; -.
DR PharmGKB; PA26184; -.
DR VEuPathDB; HostDB:ENSG00000132141; -.
DR eggNOG; KOG0359; Eukaryota.
DR GeneTree; ENSGT00940000156339; -.
DR HOGENOM; CLU_008891_3_1_1; -.
DR InParanoid; Q92526; -.
DR OMA; LMEVANT; -.
DR OrthoDB; 482152at2759; -.
DR PhylomeDB; Q92526; -.
DR TreeFam; TF106333; -.
DR PathwayCommons; Q92526; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; Q92526; -.
DR BioGRID-ORCS; 10693; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; CCT6B; human.
DR GenomeRNAi; 10693; -.
DR Pharos; Q92526; Tdark.
DR PRO; PR:Q92526; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92526; protein.
DR Bgee; ENSG00000132141; Expressed in sperm and 127 other tissues.
DR ExpressionAtlas; Q92526; baseline and differential.
DR Genevisible; Q92526; HS.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03342; TCP1_zeta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012722; Chap_CCT_zeta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02347; chap_CCT_zeta; 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 Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..530
FT /note="T-complex protein 1 subunit zeta-2"
FT /id="PRO_0000128363"
FT VAR_SEQ 68..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043040"
FT VAR_SEQ 206..242
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047129"
FT VARIANT 17
FT /note="R -> Q (in dbSNP:rs9635769)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060297"
FT VARIANT 48
FT /note="V -> A (in dbSNP:rs2230552)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060298"
FT VARIANT 247
FT /note="G -> A (in dbSNP:rs2230553)"
FT /evidence="ECO:0000269|PubMed:8812458"
FT /id="VAR_057269"
FT CONFLICT 18..30
FT /note="AALAVNICAARGL -> QLWLSIYAPPRV (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> G (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="S -> T (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..178
FT /note="VLA -> LFP (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="G -> P (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..530
FT /note="LK -> QMMIEFKINPSRR (in Ref. 1; BAA11347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 57821 MW; AE28A28E3826C196 CRC64;
MAAIKAVNSK AEVARARAAL AVNICAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLDEMQIQ HPTASLIAKV ATAQDDVTGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIA
EGFEAAKIKA LEVLEEVKVT KEMKRKILLD VARTSLQTKV HAELADVLTE VVVDSVLAVR
RPGYPIDLFM VEIMEMKHKL GTDTKLIQGL VLDHGARHPD MKKRVEDAFI LICNVSLEYE
KTEVNSGFFY KTAEEKEKLV KAERKFIEDR VQKIIDLKDK VCAQSNKGFV VINQKGIDPF
SLDSLAKHGI VALRRAKRRN MERLSLACGG MAVNSFEDLT VDCLGHAGLV YEYTLGEEKF
TFIEECVNPC SVTLLVKGPN KHTLTQVKDA IRDGLRAIKN AIEDGCMVPG AGAIEVAMAE
ALVTYKNSIK GRARLGVQAF ADALLIIPKV LAQNAGYDPQ ETLVKVQAEH VESKQLVGVD
LNTGEPMVAA DAGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK
