Full text data of CCT6A
CCT6A
(CCT6, CCTZ)
[Confidence: high (present in two of the MS resources)]
T-complex protein 1 subunit zeta; TCP-1-zeta (Acute morphine dependence-related protein 2; CCT-zeta-1; HTR3; Tcp20)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit zeta; TCP-1-zeta (Acute morphine dependence-related protein 2; CCT-zeta-1; HTR3; Tcp20)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00027626
IPI00027626 Chaperonin Containing TCP1, subunit 6A isoform a T-complex protein 1, zeta subunit 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
IPI00027626 Chaperonin Containing TCP1, subunit 6A isoform a T-complex protein 1, zeta subunit 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
P40227
ID TCPZ_HUMAN Reviewed; 531 AA.
AC P40227; A6NCD2; Q3KP28; Q75LP4; Q96S46;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=Acute morphine dependence-related protein 2;
DE AltName: Full=CCT-zeta-1;
DE AltName: Full=HTR3;
DE AltName: Full=Tcp20;
GN Name=CCT6A; Synonyms=CCT6, CCTZ;
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 [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP 324-339.
RX PubMed=8034610;
RA Li W.-Z., Lin P., Frydman J., Boal T.R., Cardillo T.S., Richard L.M.,
RA Toth D., Lichtman M.A., Hartl F.-U., Sherman F., Segel G.B.;
RT "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and
RT yeast.";
RL J. Biol. Chem. 269:18616-18622(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lee Y.-K., Yoo Y.-D.;
RT "Homo sapiens chaperonin mRNA sequence.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang H., Gao X., Li L., Wang B., Huang Y., Han J.;
RT "Homo sapiens chaperonin (MoDP) mRNA expressed in SH-SY5Y
RT neuroblastoma cells.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-233 (ISOFORM 2).
RC TISSUE=Lung carcinoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 98-531 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=1352881; DOI=10.1073/pnas.89.13.6060;
RA Segel G.B., Boal T.R., Cardillo T.S., Murant F.G., Lichtman M.A.,
RA Sherman F.;
RT "Isolation of a gene encoding a chaperonin-like protein by
RT complementation of yeast amino acid transport mutants with human
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6060-6064(1992).
RN [7]
RP PROTEIN SEQUENCE OF 2-15.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 105-117 AND 160-180, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-365; LYS-377 AND
RP LYS-388, 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 [11]
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. Known to play a role, in vitro, in the
CC 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40227-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40227-2; Sequence=VSP_044918;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58676.1; Type=Erroneous initiation;
CC Sequence=BU540578; Type=Miscellaneous discrepancy; Note=Several sequencing errors;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; L27706; AAA61061.1; -; mRNA.
DR EMBL; AF385084; AAK61354.1; -; mRNA.
DR EMBL; AB063318; BAB61032.1; -; mRNA.
DR EMBL; AC092101; AAS07451.1; -; Genomic_DNA.
DR EMBL; AC092579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106942; AAI06943.1; -; mRNA.
DR EMBL; BU540578; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M94083; AAA58676.1; ALT_INIT; mRNA.
DR PIR; S48087; S48087.
DR RefSeq; NP_001009186.1; NM_001009186.1.
DR RefSeq; NP_001753.1; NM_001762.3.
DR UniGene; Hs.82916; -.
DR ProteinModelPortal; P40227; -.
DR SMR; P40227; 4-525.
DR DIP; DIP-33558N; -.
DR IntAct; P40227; 46.
DR MINT; MINT-1156875; -.
DR STRING; 9606.ENSP00000275603; -.
DR PhosphoSite; P40227; -.
DR DMDM; 730922; -.
DR DOSAC-COBS-2DPAGE; P40227; -.
DR REPRODUCTION-2DPAGE; IPI00027626; -.
DR REPRODUCTION-2DPAGE; P40227; -.
DR SWISS-2DPAGE; P40227; -.
DR UCD-2DPAGE; P40227; -.
DR PaxDb; P40227; -.
DR PeptideAtlas; P40227; -.
DR PRIDE; P40227; -.
DR Ensembl; ENST00000275603; ENSP00000275603; ENSG00000146731.
DR Ensembl; ENST00000335503; ENSP00000352019; ENSG00000146731.
DR GeneID; 908; -.
DR KEGG; hsa:908; -.
DR UCSC; uc003trm.1; human.
DR CTD; 908; -.
DR GeneCards; GC07P056086; -.
DR HGNC; HGNC:1620; CCT6A.
DR MIM; 104613; gene.
DR neXtProt; NX_P40227; -.
DR PharmGKB; PA26183; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226733; -.
DR HOVERGEN; HBG103725; -.
DR InParanoid; P40227; -.
DR KO; K09498; -.
DR OMA; HKPNVKG; -.
DR OrthoDB; EOG7SN8C9; -.
DR PhylomeDB; P40227; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; CCT6A; -.
DR GenomeRNAi; 908; -.
DR NextBio; 3744; -.
DR PRO; PR:P40227; -.
DR ArrayExpress; P40227; -.
DR Bgee; P40227; -.
DR CleanEx; HS_CCT6A; -.
DR Genevestigator; P40227; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0051082; F:unfolded protein binding; 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; IPR012722; Chap_CCT_zeta.
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 PANTHER; PTHR11353:SF21; PTHR11353:SF21; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 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 Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 531 T-complex protein 1 subunit zeta.
FT /FTId=PRO_0000128355.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 365 365 N6-acetyllysine.
FT MOD_RES 377 377 N6-acetyllysine.
FT MOD_RES 388 388 N6-acetyllysine.
FT VAR_SEQ 68 112 Missing (in isoform 2).
FT /FTId=VSP_044918.
FT VARIANT 229 229 Y -> C (in dbSNP:rs33922584).
FT /FTId=VAR_052268.
FT CONFLICT 301 303 SLD -> PLS (in Ref. 3; BAB61032).
SQ SEQUENCE 531 AA; 58024 MW; 43ABCF548CC82B81 CRC64;
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFEAAKEKA LQFLEEVKVS REMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
KQDEPIDLFM IEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKRK VCGDSDKGFV VINQKGIDPF
SLDALSKEGI VALRRAKRRN MERLTLACGG VALNSFDDLS PDCLGHAGLV YEYTLGEEKF
TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA VRDGLRAVKN AIDDGCVVPG AGAVEVAMAE
ALIKHKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKIQAEH SESGQLVGVD
LNTGEPMVAA EVGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
//
ID TCPZ_HUMAN Reviewed; 531 AA.
AC P40227; A6NCD2; Q3KP28; Q75LP4; Q96S46;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=T-complex protein 1 subunit zeta;
DE Short=TCP-1-zeta;
DE AltName: Full=Acute morphine dependence-related protein 2;
DE AltName: Full=CCT-zeta-1;
DE AltName: Full=HTR3;
DE AltName: Full=Tcp20;
GN Name=CCT6A; Synonyms=CCT6, CCTZ;
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 [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP 324-339.
RX PubMed=8034610;
RA Li W.-Z., Lin P., Frydman J., Boal T.R., Cardillo T.S., Richard L.M.,
RA Toth D., Lichtman M.A., Hartl F.-U., Sherman F., Segel G.B.;
RT "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and
RT yeast.";
RL J. Biol. Chem. 269:18616-18622(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lee Y.-K., Yoo Y.-D.;
RT "Homo sapiens chaperonin mRNA sequence.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang H., Gao X., Li L., Wang B., Huang Y., Han J.;
RT "Homo sapiens chaperonin (MoDP) mRNA expressed in SH-SY5Y
RT neuroblastoma cells.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-233 (ISOFORM 2).
RC TISSUE=Lung carcinoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 98-531 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=1352881; DOI=10.1073/pnas.89.13.6060;
RA Segel G.B., Boal T.R., Cardillo T.S., Murant F.G., Lichtman M.A.,
RA Sherman F.;
RT "Isolation of a gene encoding a chaperonin-like protein by
RT complementation of yeast amino acid transport mutants with human
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6060-6064(1992).
RN [7]
RP PROTEIN SEQUENCE OF 2-15.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 105-117 AND 160-180, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-365; LYS-377 AND
RP LYS-388, 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 [11]
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC upon ATP hydrolysis. Known to play a role, in vitro, in the
CC 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40227-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40227-2; Sequence=VSP_044918;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58676.1; Type=Erroneous initiation;
CC Sequence=BU540578; Type=Miscellaneous discrepancy; Note=Several sequencing errors;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L27706; AAA61061.1; -; mRNA.
DR EMBL; AF385084; AAK61354.1; -; mRNA.
DR EMBL; AB063318; BAB61032.1; -; mRNA.
DR EMBL; AC092101; AAS07451.1; -; Genomic_DNA.
DR EMBL; AC092579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106942; AAI06943.1; -; mRNA.
DR EMBL; BU540578; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M94083; AAA58676.1; ALT_INIT; mRNA.
DR PIR; S48087; S48087.
DR RefSeq; NP_001009186.1; NM_001009186.1.
DR RefSeq; NP_001753.1; NM_001762.3.
DR UniGene; Hs.82916; -.
DR ProteinModelPortal; P40227; -.
DR SMR; P40227; 4-525.
DR DIP; DIP-33558N; -.
DR IntAct; P40227; 46.
DR MINT; MINT-1156875; -.
DR STRING; 9606.ENSP00000275603; -.
DR PhosphoSite; P40227; -.
DR DMDM; 730922; -.
DR DOSAC-COBS-2DPAGE; P40227; -.
DR REPRODUCTION-2DPAGE; IPI00027626; -.
DR REPRODUCTION-2DPAGE; P40227; -.
DR SWISS-2DPAGE; P40227; -.
DR UCD-2DPAGE; P40227; -.
DR PaxDb; P40227; -.
DR PeptideAtlas; P40227; -.
DR PRIDE; P40227; -.
DR Ensembl; ENST00000275603; ENSP00000275603; ENSG00000146731.
DR Ensembl; ENST00000335503; ENSP00000352019; ENSG00000146731.
DR GeneID; 908; -.
DR KEGG; hsa:908; -.
DR UCSC; uc003trm.1; human.
DR CTD; 908; -.
DR GeneCards; GC07P056086; -.
DR HGNC; HGNC:1620; CCT6A.
DR MIM; 104613; gene.
DR neXtProt; NX_P40227; -.
DR PharmGKB; PA26183; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226733; -.
DR HOVERGEN; HBG103725; -.
DR InParanoid; P40227; -.
DR KO; K09498; -.
DR OMA; HKPNVKG; -.
DR OrthoDB; EOG7SN8C9; -.
DR PhylomeDB; P40227; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; CCT6A; -.
DR GenomeRNAi; 908; -.
DR NextBio; 3744; -.
DR PRO; PR:P40227; -.
DR ArrayExpress; P40227; -.
DR Bgee; P40227; -.
DR CleanEx; HS_CCT6A; -.
DR Genevestigator; P40227; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0051082; F:unfolded protein binding; 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; IPR012722; Chap_CCT_zeta.
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 PANTHER; PTHR11353:SF21; PTHR11353:SF21; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 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 Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 531 T-complex protein 1 subunit zeta.
FT /FTId=PRO_0000128355.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 365 365 N6-acetyllysine.
FT MOD_RES 377 377 N6-acetyllysine.
FT MOD_RES 388 388 N6-acetyllysine.
FT VAR_SEQ 68 112 Missing (in isoform 2).
FT /FTId=VSP_044918.
FT VARIANT 229 229 Y -> C (in dbSNP:rs33922584).
FT /FTId=VAR_052268.
FT CONFLICT 301 303 SLD -> PLS (in Ref. 3; BAB61032).
SQ SEQUENCE 531 AA; 58024 MW; 43ABCF548CC82B81 CRC64;
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG
NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG ELLKQADLYI SEGLHPRIIT
EGFEAAKEKA LQFLEEVKVS REMDRETLID VARTSLRTKV HAELADVLTE AVVDSILAIK
KQDEPIDLFM IEIMEMKHKS ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE
KTEVNSGFFY KSAEEREKLV KAERKFIEDR VKKIIELKRK VCGDSDKGFV VINQKGIDPF
SLDALSKEGI VALRRAKRRN MERLTLACGG VALNSFDDLS PDCLGHAGLV YEYTLGEEKF
TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA VRDGLRAVKN AIDDGCVVPG AGAVEVAMAE
ALIKHKPSVK GRAQLGVQAF ADALLIIPKV LAQNSGFDLQ ETLVKIQAEH SESGQLVGVD
LNTGEPMVAA EVGVWDNYCV KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
//
MIM
104613
*RECORD*
*FIELD* NO
104613
*FIELD* TI
*104613 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 6A; CCT6A
;;CCT6;;
T-COMPLEX HOMOLOG TCP20; TCP20;;
read moreHISTIDINE TRANSPORT REGULATOR 3; HTR3;;
AMINO ACID TRANSPORT DEFECT-COMPLEMENTING
*FIELD* TX
CLONING
Segel et al. (1992) used complementation of yeast to isolate a member of
a class of genes that carry out the probable function of protecting a
regulator protein from indigenous degradation. Although yeast cells
normally synthesize amino acids, mutants with biosynthetic defects
require uptake of exogenous amino acids for growth. Yeast can import a
wide range of amino acids by the general amino acid permease (GAP)
which, however, can be repressed with ammonium sulfate. Thus,
Saccharomyces cerevisiae with a defect in histidine biosynthesis and
histidine uptake does not grow on histidine-containing medium when GAP
is repressed by ammonium. Human cDNA clones can directly complement the
synthetic or transport defects or indirectly prevent the ammonium
repression. The deduced amino acid sequence encoded by one of these cDNA
clones in the experiments of Segel et al. (1992) suggested that a
chaperonin-like protein was responsible for complementation by
preventing ammonium repression. The amino acid sequence encoded by this
cDNA clone, designated HTR3 by them (presumably for 'histidine transport
regulator'), was related to that of the T-complex proteins (e.g., TCP1,
186980). However, further studies by Li et al. (1994) revealed that the
lack of ammonium repression of general amino acid permease also involved
secondary mutations which arose in the yeast transformant. Thus the
specific action of HTR3 on the yeast amino acid permease was uncertain.
Li et al. (1994) reported the nucleotide and amino acid sequences of the
human homolog of yeast Tcp20. They found that the TCP20 (CCT6A) protein
shows approximately 30% identity to TCP1, a known subunit of the
hetero-oligomeric TRiC (see, for example, 600114). Western blot analysis
of purified bovine TRiC with a TCP20-specific antibody indicated that
TCP20 is also a subunit of TRiC. Gene disruption studies showed that
Tcp20, like Tcp1, is an essential gene in yeast.
GENE FUNCTION
Segel et al. (1992) proposed that HTR3, TCP1, and others constitute a
class of chaperonins that are cytoplasmic proteins. Although a distinct
class, the cytoplasmic chaperonins have a weak but significant sequence
similarity to the chaperonin proteins (e.g., 118190).
*FIELD* RF
1. Li, W.-Z.; Lin, P.; Frydman, J.; Boal, T. R.; Cardillo, T. S.;
Richard, L. M.; Toth, D.; Lichtman, M. A.; Hartl, F.-U.; Sherman,
F.; Segel, G. B.: Tcp20, a subunit of the eukaryotic TRiC chaperonin
from humans and yeast. J. Biol. Chem. 269: 18616-18622, 1994.
2. Segel, G. B.; Boal, T. R.; Cardillo, T. S.; Murant, F. G.; Lichtman,
M. A.; Sherman, F.: Isolation of a gene encoding a chaperonin-like
protein by complementation of yeast amino acid transport mutants with
human cDNA. Proc. Nat. Acad. Sci. 89: 6060-6064, 1992.
*FIELD* CN
Andre K. Cheng - updated: 4/17/1996
*FIELD* CD
Victor A. McKusick: 8/17/1992
*FIELD* ED
carol: 12/14/2012
mgross: 2/4/2009
mgross: 7/13/2000
mgross: 1/7/2000
alopez: 7/27/1999
alopez: 7/26/1999
dkim: 9/9/1998
mark: 4/17/1996
mark: 3/7/1996
carol: 4/6/1994
carol: 8/17/1992
*RECORD*
*FIELD* NO
104613
*FIELD* TI
*104613 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 6A; CCT6A
;;CCT6;;
T-COMPLEX HOMOLOG TCP20; TCP20;;
read moreHISTIDINE TRANSPORT REGULATOR 3; HTR3;;
AMINO ACID TRANSPORT DEFECT-COMPLEMENTING
*FIELD* TX
CLONING
Segel et al. (1992) used complementation of yeast to isolate a member of
a class of genes that carry out the probable function of protecting a
regulator protein from indigenous degradation. Although yeast cells
normally synthesize amino acids, mutants with biosynthetic defects
require uptake of exogenous amino acids for growth. Yeast can import a
wide range of amino acids by the general amino acid permease (GAP)
which, however, can be repressed with ammonium sulfate. Thus,
Saccharomyces cerevisiae with a defect in histidine biosynthesis and
histidine uptake does not grow on histidine-containing medium when GAP
is repressed by ammonium. Human cDNA clones can directly complement the
synthetic or transport defects or indirectly prevent the ammonium
repression. The deduced amino acid sequence encoded by one of these cDNA
clones in the experiments of Segel et al. (1992) suggested that a
chaperonin-like protein was responsible for complementation by
preventing ammonium repression. The amino acid sequence encoded by this
cDNA clone, designated HTR3 by them (presumably for 'histidine transport
regulator'), was related to that of the T-complex proteins (e.g., TCP1,
186980). However, further studies by Li et al. (1994) revealed that the
lack of ammonium repression of general amino acid permease also involved
secondary mutations which arose in the yeast transformant. Thus the
specific action of HTR3 on the yeast amino acid permease was uncertain.
Li et al. (1994) reported the nucleotide and amino acid sequences of the
human homolog of yeast Tcp20. They found that the TCP20 (CCT6A) protein
shows approximately 30% identity to TCP1, a known subunit of the
hetero-oligomeric TRiC (see, for example, 600114). Western blot analysis
of purified bovine TRiC with a TCP20-specific antibody indicated that
TCP20 is also a subunit of TRiC. Gene disruption studies showed that
Tcp20, like Tcp1, is an essential gene in yeast.
GENE FUNCTION
Segel et al. (1992) proposed that HTR3, TCP1, and others constitute a
class of chaperonins that are cytoplasmic proteins. Although a distinct
class, the cytoplasmic chaperonins have a weak but significant sequence
similarity to the chaperonin proteins (e.g., 118190).
*FIELD* RF
1. Li, W.-Z.; Lin, P.; Frydman, J.; Boal, T. R.; Cardillo, T. S.;
Richard, L. M.; Toth, D.; Lichtman, M. A.; Hartl, F.-U.; Sherman,
F.; Segel, G. B.: Tcp20, a subunit of the eukaryotic TRiC chaperonin
from humans and yeast. J. Biol. Chem. 269: 18616-18622, 1994.
2. Segel, G. B.; Boal, T. R.; Cardillo, T. S.; Murant, F. G.; Lichtman,
M. A.; Sherman, F.: Isolation of a gene encoding a chaperonin-like
protein by complementation of yeast amino acid transport mutants with
human cDNA. Proc. Nat. Acad. Sci. 89: 6060-6064, 1992.
*FIELD* CN
Andre K. Cheng - updated: 4/17/1996
*FIELD* CD
Victor A. McKusick: 8/17/1992
*FIELD* ED
carol: 12/14/2012
mgross: 2/4/2009
mgross: 7/13/2000
mgross: 1/7/2000
alopez: 7/27/1999
alopez: 7/26/1999
dkim: 9/9/1998
mark: 4/17/1996
mark: 3/7/1996
carol: 4/6/1994
carol: 8/17/1992