Full text data of CCT7
CCT7
(CCTH, NIP7-1)
[Confidence: high (present in two of the MS resources)]
T-complex protein 1 subunit eta; TCP-1-eta (CCT-eta; HIV-1 Nef-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit eta; TCP-1-eta (CCT-eta; HIV-1 Nef-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00018465
IPI00018465 T-complex protein 1, eta subunit delta and gamma in membrane 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
IPI00018465 T-complex protein 1, eta subunit delta and gamma in membrane 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
Q99832
ID TCPH_HUMAN Reviewed; 543 AA.
AC Q99832; A8K7E6; A8MWI8; B7WNW9; B7Z4T9; B7Z4Z7; O14871; Q6FI26;
read moreDT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
DE AltName: Full=HIV-1 Nef-interacting protein;
GN Name=CCT7; Synonyms=CCTH, NIP7-1;
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).
RX PubMed=9819444;
RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.;
RT "Maturation of human cyclin E requires the function of eukaryotic
RT chaperonin CCT.";
RL Mol. Cell. Biol. 18:7584-7589(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Cerebellum, and Heart;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 1-10; 56-67; 85-123; 127-144; 178-193; 200-217;
RP 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND
RP 500-535, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, Hepatoma, and Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K.,
RA von Kriegsheim A.F., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1).
RA Fukushi M., Kimura T., Yamamoto N.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 107-123, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-320, AND MASS
RP 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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 (By similarity).
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 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q99832-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99832-2; Sequence=VSP_043573, VSP_043574;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q99832-3; Sequence=VSP_043572;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q99832-4; Sequence=VSP_043573;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
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DR EMBL; AF026292; AAC96011.1; -; mRNA.
DR EMBL; CR536511; CAG38749.1; -; mRNA.
DR EMBL; AK291961; BAF84650.1; -; mRNA.
DR EMBL; AK293597; BAH11543.1; -; mRNA.
DR EMBL; AK297846; BAH12675.1; -; mRNA.
DR EMBL; AK298153; BAH12733.1; -; mRNA.
DR EMBL; AC010913; AAX88902.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99739.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99740.1; -; Genomic_DNA.
DR EMBL; BC019296; AAH19296.1; -; mRNA.
DR EMBL; BC088351; AAH88351.1; -; mRNA.
DR EMBL; U83843; AAB41437.1; -; mRNA.
DR RefSeq; NP_001009570.1; NM_001009570.2.
DR RefSeq; NP_001159756.1; NM_001166284.1.
DR RefSeq; NP_001159757.1; NM_001166285.1.
DR RefSeq; NP_006420.1; NM_006429.3.
DR UniGene; Hs.368149; -.
DR ProteinModelPortal; Q99832; -.
DR SMR; Q99832; 6-523.
DR DIP; DIP-51608N; -.
DR IntAct; Q99832; 49.
DR MINT; MINT-1131353; -.
DR STRING; 9606.ENSP00000258091; -.
DR PhosphoSite; Q99832; -.
DR DMDM; 3041738; -.
DR REPRODUCTION-2DPAGE; IPI00018465; -.
DR PaxDb; Q99832; -.
DR PRIDE; Q99832; -.
DR DNASU; 10574; -.
DR Ensembl; ENST00000258091; ENSP00000258091; ENSG00000135624.
DR Ensembl; ENST00000398422; ENSP00000381456; ENSG00000135624.
DR Ensembl; ENST00000539919; ENSP00000437824; ENSG00000135624.
DR Ensembl; ENST00000540468; ENSP00000442058; ENSG00000135624.
DR GeneID; 10574; -.
DR KEGG; hsa:10574; -.
DR UCSC; uc002siz.3; human.
DR CTD; 10574; -.
DR GeneCards; GC02P073460; -.
DR HGNC; HGNC:1622; CCT7.
DR HPA; HPA008425; -.
DR MIM; 605140; gene.
DR neXtProt; NX_Q99832; -.
DR PharmGKB; PA26185; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226730; -.
DR HOVERGEN; HBG001052; -.
DR InParanoid; Q99832; -.
DR KO; K09499; -.
DR OMA; CVWEPSI; -.
DR OrthoDB; EOG7V49Z2; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT7; human.
DR GeneWiki; CCT7; -.
DR GenomeRNAi; 10574; -.
DR NextBio; 40131; -.
DR PRO; PR:Q99832; -.
DR ArrayExpress; Q99832; -.
DR Bgee; Q99832; -.
DR CleanEx; HS_CCT7; -.
DR Genevestigator; Q99832; -.
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:0005739; C:mitochondrion; IEA:Ensembl.
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; IPR012720; Chap_CCT_eta.
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:SF22; PTHR11353:SF22; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02345; chap_CCT_eta; 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 CHAIN 1 543 T-complex protein 1 subunit eta.
FT /FTId=PRO_0000128365.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 67 67 N6-acetyllysine.
FT MOD_RES 320 320 N6-acetyllysine.
FT VAR_SEQ 1 44 Missing (in isoform 3).
FT /FTId=VSP_043572.
FT VAR_SEQ 3 89 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_043573.
FT VAR_SEQ 90 206 Missing (in isoform 2).
FT /FTId=VSP_043574.
FT VARIANT 259 259 T -> A (in dbSNP:rs2231427).
FT /FTId=VAR_052269.
FT CONFLICT 282 283 HH -> RQ (in Ref. 8; AAB41437).
FT CONFLICT 293 293 L -> P (in Ref. 8; AAB41437).
FT CONFLICT 336 336 A -> P (in Ref. 8; AAB41437).
FT CONFLICT 364 364 C -> L (in Ref. 8; AAB41437).
FT CONFLICT 374 376 LRG -> SPC (in Ref. 8; AAB41437).
FT CONFLICT 407 407 A -> P (in Ref. 8; AAB41437).
FT CONFLICT 411 411 A -> P (in Ref. 8; AAB41437).
SQ SEQUENCE 543 AA; 59367 MW; 9F1E33FA80E6238E CRC64;
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV
DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE TQIGGERYNF
FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGTWYGVDIN
NEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG
RPH
//
ID TCPH_HUMAN Reviewed; 543 AA.
AC Q99832; A8K7E6; A8MWI8; B7WNW9; B7Z4T9; B7Z4Z7; O14871; Q6FI26;
read moreDT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=T-complex protein 1 subunit eta;
DE Short=TCP-1-eta;
DE AltName: Full=CCT-eta;
DE AltName: Full=HIV-1 Nef-interacting protein;
GN Name=CCT7; Synonyms=CCTH, NIP7-1;
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).
RX PubMed=9819444;
RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.;
RT "Maturation of human cyclin E requires the function of eukaryotic
RT chaperonin CCT.";
RL Mol. Cell. Biol. 18:7584-7589(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Cerebellum, and Heart;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=PNS, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 1-10; 56-67; 85-123; 127-144; 178-193; 200-217;
RP 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND
RP 500-535, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, Hepatoma, and Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K.,
RA von Kriegsheim A.F., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1).
RA Fukushi M., Kimura T., Yamamoto N.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 107-123, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-320, AND MASS
RP 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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 (By similarity).
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 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q99832-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99832-2; Sequence=VSP_043573, VSP_043574;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q99832-3; Sequence=VSP_043572;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q99832-4; Sequence=VSP_043573;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
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DR EMBL; AF026292; AAC96011.1; -; mRNA.
DR EMBL; CR536511; CAG38749.1; -; mRNA.
DR EMBL; AK291961; BAF84650.1; -; mRNA.
DR EMBL; AK293597; BAH11543.1; -; mRNA.
DR EMBL; AK297846; BAH12675.1; -; mRNA.
DR EMBL; AK298153; BAH12733.1; -; mRNA.
DR EMBL; AC010913; AAX88902.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99739.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99740.1; -; Genomic_DNA.
DR EMBL; BC019296; AAH19296.1; -; mRNA.
DR EMBL; BC088351; AAH88351.1; -; mRNA.
DR EMBL; U83843; AAB41437.1; -; mRNA.
DR RefSeq; NP_001009570.1; NM_001009570.2.
DR RefSeq; NP_001159756.1; NM_001166284.1.
DR RefSeq; NP_001159757.1; NM_001166285.1.
DR RefSeq; NP_006420.1; NM_006429.3.
DR UniGene; Hs.368149; -.
DR ProteinModelPortal; Q99832; -.
DR SMR; Q99832; 6-523.
DR DIP; DIP-51608N; -.
DR IntAct; Q99832; 49.
DR MINT; MINT-1131353; -.
DR STRING; 9606.ENSP00000258091; -.
DR PhosphoSite; Q99832; -.
DR DMDM; 3041738; -.
DR REPRODUCTION-2DPAGE; IPI00018465; -.
DR PaxDb; Q99832; -.
DR PRIDE; Q99832; -.
DR DNASU; 10574; -.
DR Ensembl; ENST00000258091; ENSP00000258091; ENSG00000135624.
DR Ensembl; ENST00000398422; ENSP00000381456; ENSG00000135624.
DR Ensembl; ENST00000539919; ENSP00000437824; ENSG00000135624.
DR Ensembl; ENST00000540468; ENSP00000442058; ENSG00000135624.
DR GeneID; 10574; -.
DR KEGG; hsa:10574; -.
DR UCSC; uc002siz.3; human.
DR CTD; 10574; -.
DR GeneCards; GC02P073460; -.
DR HGNC; HGNC:1622; CCT7.
DR HPA; HPA008425; -.
DR MIM; 605140; gene.
DR neXtProt; NX_Q99832; -.
DR PharmGKB; PA26185; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226730; -.
DR HOVERGEN; HBG001052; -.
DR InParanoid; Q99832; -.
DR KO; K09499; -.
DR OMA; CVWEPSI; -.
DR OrthoDB; EOG7V49Z2; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; CCT7; human.
DR GeneWiki; CCT7; -.
DR GenomeRNAi; 10574; -.
DR NextBio; 40131; -.
DR PRO; PR:Q99832; -.
DR ArrayExpress; Q99832; -.
DR Bgee; Q99832; -.
DR CleanEx; HS_CCT7; -.
DR Genevestigator; Q99832; -.
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:0005739; C:mitochondrion; IEA:Ensembl.
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; IPR012720; Chap_CCT_eta.
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:SF22; PTHR11353:SF22; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02345; chap_CCT_eta; 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 CHAIN 1 543 T-complex protein 1 subunit eta.
FT /FTId=PRO_0000128365.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 67 67 N6-acetyllysine.
FT MOD_RES 320 320 N6-acetyllysine.
FT VAR_SEQ 1 44 Missing (in isoform 3).
FT /FTId=VSP_043572.
FT VAR_SEQ 3 89 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_043573.
FT VAR_SEQ 90 206 Missing (in isoform 2).
FT /FTId=VSP_043574.
FT VARIANT 259 259 T -> A (in dbSNP:rs2231427).
FT /FTId=VAR_052269.
FT CONFLICT 282 283 HH -> RQ (in Ref. 8; AAB41437).
FT CONFLICT 293 293 L -> P (in Ref. 8; AAB41437).
FT CONFLICT 336 336 A -> P (in Ref. 8; AAB41437).
FT CONFLICT 364 364 C -> L (in Ref. 8; AAB41437).
FT CONFLICT 374 376 LRG -> SPC (in Ref. 8; AAB41437).
FT CONFLICT 407 407 A -> P (in Ref. 8; AAB41437).
FT CONFLICT 411 411 A -> P (in Ref. 8; AAB41437).
SQ SEQUENCE 543 AA; 59367 MW; 9F1E33FA80E6238E CRC64;
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN
DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI
IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV
DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL
NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT
QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE TQIGGERYNF
FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL
RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGTWYGVDIN
NEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG
RPH
//
MIM
605140
*RECORD*
*FIELD* NO
605140
*FIELD* TI
*605140 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 7; CCT7
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 7;;
read moreCCT-ETA; CCTH
*FIELD* TX
DESCRIPTION
The chaperonin containing TCP1 (186980) complex (CCT), also called the
TCP1 ring complex, consists of 2 back-to-back rings, each containing 8
unique but homologous subunits, such as CCT7. CCT assists the folding of
newly translated polypeptide substrates through multiple rounds of
ATP-driven release and rebinding of partially folded intermediate forms.
Substrates of CCT include the cytoskeletal proteins actin (see 102560)
and tubulin (see 191130), as well as alpha-transducin (139330) (Won et
al., 1998).
CLONING
Cyclin E (CCNE1; 123837), a partner of the cyclin-dependent kinase CDK2
(116953), is implicated in the positive control of the G1/S phase
transition. CCNE1 degradation is regulated by ubiquitination and
proteasomal action, which occur upon autophosphorylation and activation
of the CCNE1-CDK2 complex. Using a yeast-based screen to identify
proteins that interact with CCNE1, Won et al. (1998) obtained a cDNA
encoding CCT7, which they called CCT-eta.
GENE FUNCTION
By mutation analysis, Won et al. (1998) found that CCT is essential for
CCNE1 maturation and accumulation.
MAPPING
By FISH, Edwards et al. (1997) mapped the CCT7 gene to chromosome 2p13.
*FIELD* RF
1. Edwards, M. C.; Liegeois, N.; Horecka, J.; DePinho, R. A.; Sprague,
G. F., Jr.; Tyers, M.; Elledge, S. J.: Human CPR (cell cycle progression
restoration) genes impart a Far- phenotype on yeast cells. Genetics 147:
1063-1076, 1997.
2. Won, K.-A.; Schumacher, R. J.; Farr, G. W.; Horwich, A. L.; Reed,
S. I.: Maturation of human cyclin E requires the function of eukaryotic
chaperonin CCT. Molec. Cell. Biol. 18: 7584-7589, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 7/9/2007
*FIELD* CD
Paul J. Converse: 7/12/2000
*FIELD* ED
carol: 10/31/2007
carol: 8/15/2007
terry: 7/9/2007
mgross: 11/20/2006
mgross: 7/14/2000
mgross: 7/13/2000
mgross: 7/12/2000
*RECORD*
*FIELD* NO
605140
*FIELD* TI
*605140 CHAPERONIN CONTAINING T-COMPLEX POLYPEPTIDE 1, SUBUNIT 7; CCT7
;;CHAPERONIN CONTAINING TCP1, SUBUNIT 7;;
read moreCCT-ETA; CCTH
*FIELD* TX
DESCRIPTION
The chaperonin containing TCP1 (186980) complex (CCT), also called the
TCP1 ring complex, consists of 2 back-to-back rings, each containing 8
unique but homologous subunits, such as CCT7. CCT assists the folding of
newly translated polypeptide substrates through multiple rounds of
ATP-driven release and rebinding of partially folded intermediate forms.
Substrates of CCT include the cytoskeletal proteins actin (see 102560)
and tubulin (see 191130), as well as alpha-transducin (139330) (Won et
al., 1998).
CLONING
Cyclin E (CCNE1; 123837), a partner of the cyclin-dependent kinase CDK2
(116953), is implicated in the positive control of the G1/S phase
transition. CCNE1 degradation is regulated by ubiquitination and
proteasomal action, which occur upon autophosphorylation and activation
of the CCNE1-CDK2 complex. Using a yeast-based screen to identify
proteins that interact with CCNE1, Won et al. (1998) obtained a cDNA
encoding CCT7, which they called CCT-eta.
GENE FUNCTION
By mutation analysis, Won et al. (1998) found that CCT is essential for
CCNE1 maturation and accumulation.
MAPPING
By FISH, Edwards et al. (1997) mapped the CCT7 gene to chromosome 2p13.
*FIELD* RF
1. Edwards, M. C.; Liegeois, N.; Horecka, J.; DePinho, R. A.; Sprague,
G. F., Jr.; Tyers, M.; Elledge, S. J.: Human CPR (cell cycle progression
restoration) genes impart a Far- phenotype on yeast cells. Genetics 147:
1063-1076, 1997.
2. Won, K.-A.; Schumacher, R. J.; Farr, G. W.; Horwich, A. L.; Reed,
S. I.: Maturation of human cyclin E requires the function of eukaryotic
chaperonin CCT. Molec. Cell. Biol. 18: 7584-7589, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 7/9/2007
*FIELD* CD
Paul J. Converse: 7/12/2000
*FIELD* ED
carol: 10/31/2007
carol: 8/15/2007
terry: 7/9/2007
mgross: 11/20/2006
mgross: 7/14/2000
mgross: 7/13/2000
mgross: 7/12/2000