Full text data of TCP1
TCP1
(CCT1, CCTA)
[Confidence: high (present in two of the MS resources)]
T-complex protein 1 subunit alpha; TCP-1-alpha (CCT-alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
T-complex protein 1 subunit alpha; TCP-1-alpha (CCT-alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00290566
IPI00290566 T-complex protein 1, alpha subunit interesting not membrane but others are, 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
IPI00290566 T-complex protein 1, alpha subunit interesting not membrane but others are, 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
P17987
ID TCPA_HUMAN Reviewed; 556 AA.
AC P17987; E1P5B2; Q15556; Q5TCM3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
GN Name=TCP1; Synonyms=CCT1, CCTA;
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].
RC TISSUE=Testis;
RX PubMed=2377466; DOI=10.1093/nar/18.14.4247;
RA Kirchhoff C., Willison K.R.;
RT "Nucleotide and amino-acid sequence of human testis-derived TCP1.";
RL Nucleic Acids Res. 18:4247-4247(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 1-11, AND ACETYLATION AT MET-1.
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 [7]
RP PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-365 AND 462-516.
RX PubMed=3653076;
RA Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V.,
RA Gorman P., Sheer D., Trowsdale J.;
RT "The human homologue of the mouse T-complex gene, TCP1, is located on
RT chromosome 6 but is not near the HLA region.";
RL EMBO J. 6:1967-1974(1987).
RN [9]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=1630492; DOI=10.1038/358249a0;
RA Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.;
RT "T-complex polypeptide-1 is a subunit of a heteromeric particle in the
RT eukaryotic cytosol.";
RL Nature 358:249-252(1992).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181; THR-182 AND
RP SER-544, AND MASS 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-400, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-7.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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.
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DR EMBL; X52882; CAA37064.1; -; mRNA.
DR EMBL; BT006969; AAP35615.1; -; mRNA.
DR EMBL; AL135914; CAI21851.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47616.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47618.1; -; Genomic_DNA.
DR EMBL; BC000665; AAH00665.1; -; mRNA.
DR EMBL; M26885; AAA61059.1; -; Genomic_DNA.
DR EMBL; M27272; AAA61060.1; -; Genomic_DNA.
DR EMBL; M26889; AAA61060.1; JOINED; Genomic_DNA.
DR PIR; S10486; S10486.
DR RefSeq; NP_110379.2; NM_030752.2.
DR RefSeq; XP_005267172.1; XM_005267115.1.
DR UniGene; Hs.363137; -.
DR ProteinModelPortal; P17987; -.
DR SMR; P17987; 2-534.
DR DIP; DIP-33676N; -.
DR IntAct; P17987; 54.
DR MINT; MINT-4999235; -.
DR STRING; 9606.ENSP00000317334; -.
DR PhosphoSite; P17987; -.
DR DMDM; 135538; -.
DR OGP; P17987; -.
DR REPRODUCTION-2DPAGE; IPI00290566; -.
DR REPRODUCTION-2DPAGE; P17987; -.
DR UCD-2DPAGE; P17987; -.
DR PaxDb; P17987; -.
DR PeptideAtlas; P17987; -.
DR PRIDE; P17987; -.
DR DNASU; 6950; -.
DR Ensembl; ENST00000321394; ENSP00000317334; ENSG00000120438.
DR GeneID; 6950; -.
DR KEGG; hsa:6950; -.
DR UCSC; uc003qsr.3; human.
DR CTD; 6950; -.
DR GeneCards; GC06M160199; -.
DR HGNC; HGNC:11655; TCP1.
DR HPA; CAB017460; -.
DR HPA; HPA027337; -.
DR HPA; HPA031082; -.
DR MIM; 186980; gene.
DR neXtProt; NX_P17987; -.
DR PharmGKB; PA36406; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226729; -.
DR HOVERGEN; HBG001052; -.
DR InParanoid; P17987; -.
DR KO; K09493; -.
DR OMA; IMRIDTL; -.
DR OrthoDB; EOG7K3TKJ; -.
DR PhylomeDB; P17987; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; TCP1; human.
DR GeneWiki; T-complex_1; -.
DR GenomeRNAi; 6950; -.
DR NextBio; 27215; -.
DR PRO; PR:P17987; -.
DR ArrayExpress; P17987; -.
DR Bgee; P17987; -.
DR CleanEx; HS_TCP1; -.
DR Genevestigator; P17987; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; 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; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005720; C:nuclear heterochromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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 GO; GO:0007021; P:tubulin complex assembly; NAS:UniProtKB.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
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:SF20; PTHR11353:SF20; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 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; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 556 T-complex protein 1 subunit alpha.
FT /FTId=PRO_0000128302.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 181 181 Phosphotyrosine.
FT MOD_RES 182 182 Phosphothreonine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 400 400 N6-acetyllysine.
FT MOD_RES 544 544 Phosphoserine.
FT MOD_RES 551 551 Phosphoserine.
FT VARIANT 7 7 V -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036258.
FT CONFLICT 480 480 R -> S (in Ref. 8; AAA61060).
FT CONFLICT 537 540 SKDD -> ILRI (in Ref. 1; CAA37064).
SQ SEQUENCE 556 AA; 60344 MW; 486ECA836EA258A1 CRC64;
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK
YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
KHGSYEDAVH SGALND
//
ID TCPA_HUMAN Reviewed; 556 AA.
AC P17987; E1P5B2; Q15556; Q5TCM3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=T-complex protein 1 subunit alpha;
DE Short=TCP-1-alpha;
DE AltName: Full=CCT-alpha;
GN Name=TCP1; Synonyms=CCT1, CCTA;
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].
RC TISSUE=Testis;
RX PubMed=2377466; DOI=10.1093/nar/18.14.4247;
RA Kirchhoff C., Willison K.R.;
RT "Nucleotide and amino-acid sequence of human testis-derived TCP1.";
RL Nucleic Acids Res. 18:4247-4247(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 1-11, AND ACETYLATION AT MET-1.
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 [7]
RP PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526,
RP AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-365 AND 462-516.
RX PubMed=3653076;
RA Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V.,
RA Gorman P., Sheer D., Trowsdale J.;
RT "The human homologue of the mouse T-complex gene, TCP1, is located on
RT chromosome 6 but is not near the HLA region.";
RL EMBO J. 6:1967-1974(1987).
RN [9]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=1630492; DOI=10.1038/358249a0;
RA Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.;
RT "T-complex polypeptide-1 is a subunit of a heteromeric particle in the
RT eukaryotic cytosol.";
RL Nature 358:249-252(1992).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181; THR-182 AND
RP SER-544, AND MASS 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-400, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-7.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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.
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DR EMBL; X52882; CAA37064.1; -; mRNA.
DR EMBL; BT006969; AAP35615.1; -; mRNA.
DR EMBL; AL135914; CAI21851.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47616.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47618.1; -; Genomic_DNA.
DR EMBL; BC000665; AAH00665.1; -; mRNA.
DR EMBL; M26885; AAA61059.1; -; Genomic_DNA.
DR EMBL; M27272; AAA61060.1; -; Genomic_DNA.
DR EMBL; M26889; AAA61060.1; JOINED; Genomic_DNA.
DR PIR; S10486; S10486.
DR RefSeq; NP_110379.2; NM_030752.2.
DR RefSeq; XP_005267172.1; XM_005267115.1.
DR UniGene; Hs.363137; -.
DR ProteinModelPortal; P17987; -.
DR SMR; P17987; 2-534.
DR DIP; DIP-33676N; -.
DR IntAct; P17987; 54.
DR MINT; MINT-4999235; -.
DR STRING; 9606.ENSP00000317334; -.
DR PhosphoSite; P17987; -.
DR DMDM; 135538; -.
DR OGP; P17987; -.
DR REPRODUCTION-2DPAGE; IPI00290566; -.
DR REPRODUCTION-2DPAGE; P17987; -.
DR UCD-2DPAGE; P17987; -.
DR PaxDb; P17987; -.
DR PeptideAtlas; P17987; -.
DR PRIDE; P17987; -.
DR DNASU; 6950; -.
DR Ensembl; ENST00000321394; ENSP00000317334; ENSG00000120438.
DR GeneID; 6950; -.
DR KEGG; hsa:6950; -.
DR UCSC; uc003qsr.3; human.
DR CTD; 6950; -.
DR GeneCards; GC06M160199; -.
DR HGNC; HGNC:11655; TCP1.
DR HPA; CAB017460; -.
DR HPA; HPA027337; -.
DR HPA; HPA031082; -.
DR MIM; 186980; gene.
DR neXtProt; NX_P17987; -.
DR PharmGKB; PA36406; -.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000226729; -.
DR HOVERGEN; HBG001052; -.
DR InParanoid; P17987; -.
DR KO; K09493; -.
DR OMA; IMRIDTL; -.
DR OrthoDB; EOG7K3TKJ; -.
DR PhylomeDB; P17987; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; TCP1; human.
DR GeneWiki; T-complex_1; -.
DR GenomeRNAi; 6950; -.
DR NextBio; 27215; -.
DR PRO; PR:P17987; -.
DR ArrayExpress; P17987; -.
DR Bgee; P17987; -.
DR CleanEx; HS_TCP1; -.
DR Genevestigator; P17987; -.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; 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; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005720; C:nuclear heterochromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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 GO; GO:0007021; P:tubulin complex assembly; NAS:UniProtKB.
DR Gene3D; 1.10.560.10; -; 2.
DR Gene3D; 3.30.260.10; -; 2.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012715; Chap_CCT_alpha.
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:SF20; PTHR11353:SF20; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 2.
DR SUPFAM; SSF52029; SSF52029; 1.
DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 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; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 556 T-complex protein 1 subunit alpha.
FT /FTId=PRO_0000128302.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 181 181 Phosphotyrosine.
FT MOD_RES 182 182 Phosphothreonine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 400 400 N6-acetyllysine.
FT MOD_RES 544 544 Phosphoserine.
FT MOD_RES 551 551 Phosphoserine.
FT VARIANT 7 7 V -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036258.
FT CONFLICT 480 480 R -> S (in Ref. 8; AAA61060).
FT CONFLICT 537 540 SKDD -> ILRI (in Ref. 1; CAA37064).
SQ SEQUENCE 556 AA; 60344 MW; 486ECA836EA258A1 CRC64;
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT
ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK
YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS
LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF
VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE
LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS
IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
KHGSYEDAVH SGALND
//
MIM
186980
*RECORD*
*FIELD* NO
186980
*FIELD* TI
*186980 T-COMPLEX 1; TCP1
;;T-COMPLEX HOMOLOG TCP1
*FIELD* TX
A role in the folding of newly translated proteins in the cytosol has
read morebeen proposed for t-complex polypeptide-1 (TCP1). Tubulin (e.g., 191110)
is a major cytosolic protein whose assembly into microtubules is
critical to many cellular processes. Yaffe et al. (1992) examined the
biogenesis of alpha- and beta-tubulin in rabbit reticulocyte lysate.
They found that newly translated tubulin subunits entered a 900-kD
complex which contained as its major constituent a 58-kD protein that
crossreacted with a monoclonal antiserum against mouse TCP1. This led
them to conclude that TCP1 functions as a cytosolic chaperone in the
biosynthesis of tubulin.
By use of a cDNA probe for the mouse tcp1 locus, part of the t-complex,
Willison et al. (1985) assigned the homologous locus to chromosome 6.
The finding was confirmed by means of a cDNA probe for the human TCP1
gene. Suspicion that some human malformations are the result of mutation
in the t-complex loci is discussed elsewhere (182940). TCP1 codes for a
protein which is abundantly expressed in testes as well as in other
tissues. Using the cloned gene and a panel of somatic cell hybrids, as
well as in situ hybridization, Willison et al. (1987) assigned the gene
to 6q23-qter; thus, it is not closely linked to the HLA complex. For
this reason and others, TCP1 is not likely to be a human equivalent of
the mouse t-complex. Blanche et al. (1987) found that TCP1 is not linked
to HLA and GLO1 and is probably excluded from 6p. This result was
consistent with the reported localization to 6q23-qter. By in situ
hybridization, Fonatsch et al. (1987) concluded that the TCP1 locus is
probably in the 6q25-q27 region. Blanche et al. (1992) demonstrated that
the TCP1 and plasminogen (173350) genes show no recombination and are
located about 50 cM proximal to TCP10 (187020), which is located in band
6q27.
The ACAT2 gene (100678) shows complementary overlapping with the 3-prime
region of the TCP1 gene in both mouse and human. These genes are encoded
on opposite strands of DNA, as well as in opposite transcriptional
orientation. Masuno et al. (1996) assigned the ACAT2 gene to 6q25.3-q26
by fluorescence in situ hybridization; thus the assignment of the TCP1
gene can be refined to 6q25.3-q26.
*FIELD* RF
1. Blanche, H.; Massart, C.; Dausset, J.; Cann, H.: TCP1 is not linked
to HLA, GLO1, PGK1P2 and other markers in a 45cM map of the short
arm of chromosome 6 (6p). (Abstract) Cytogenet. Cell Genet. 46:
581-582, 1987.
2. Blanche, H.; Wright, L. G.; Vergnaud, G.; de Gouyon, B.; Lauthier,
V.; Silver, L. M.; Dausset, J.; Cann, H. M.; Spielman, R. S.: Genetic
mapping of three human homologues of murine t-complex genes localizes
TCP10 to 6q27, 15 cM distal to TCP1 and PLG. Genomics 12: 826-828,
1992.
3. Fonatsch, C.; Gradl, G.; Ragoussis, J.; Ziegler, A.: Assignment
of the TCP1 locus to the long arm of human chromosome 6 by in situ
hybridization. Cytogenet. Cell Genet. 45: 109-112, 1987.
4. Masuno, M.; Fukao, T.; Song, X.-Q.; Yamaguchi, S.; Orii, T.; Kondo,
N.; Imaizumi, K.; Kuroki, Y.: Assignment of the human cytosolic acetoacetyl-coenzyme
A thiolase (ACAT2) gene to chromosome 6q25.3-q26. Genomics 36: 217-218,
1996.
5. Willison, K.; Dudley, K.; Spurr, N.; Goodfellow, P.: Chromosomal
assignment of TCP-1, the human homologue of a mouse t-complex locus.
(Abstract) Cytogenet. Cell Genet. 40: 779-780, 1985.
6. Willison, K.; Kelly, A.; Dudley, K.; Goodfellow, P.; Spurr, N.;
Groves, V.; Gorman, P.; Sheer, D.; Trowsdale, J.: The human homologue
of the mouse t-complex gene, TCP1, is located on chromosome 6 but
is not near the HLA region. EMBO J. 6: 1967-1974, 1987.
7. Yaffe, M. B.; Farr, G. W.; Miklos, D.; Horwich, A. L.; Sternlicht,
M. L.; Sternlicht, H.: TCP1 complex is a molecular chaperone in tubulin
biogenesis. Nature 358: 245-248, 1992.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 05/23/2003
psherman: 7/27/1999
dkim: 9/9/1998
mark: 9/12/1996
terry: 9/4/1996
terry: 5/5/1994
carol: 8/24/1992
carol: 6/2/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
186980
*FIELD* TI
*186980 T-COMPLEX 1; TCP1
;;T-COMPLEX HOMOLOG TCP1
*FIELD* TX
A role in the folding of newly translated proteins in the cytosol has
read morebeen proposed for t-complex polypeptide-1 (TCP1). Tubulin (e.g., 191110)
is a major cytosolic protein whose assembly into microtubules is
critical to many cellular processes. Yaffe et al. (1992) examined the
biogenesis of alpha- and beta-tubulin in rabbit reticulocyte lysate.
They found that newly translated tubulin subunits entered a 900-kD
complex which contained as its major constituent a 58-kD protein that
crossreacted with a monoclonal antiserum against mouse TCP1. This led
them to conclude that TCP1 functions as a cytosolic chaperone in the
biosynthesis of tubulin.
By use of a cDNA probe for the mouse tcp1 locus, part of the t-complex,
Willison et al. (1985) assigned the homologous locus to chromosome 6.
The finding was confirmed by means of a cDNA probe for the human TCP1
gene. Suspicion that some human malformations are the result of mutation
in the t-complex loci is discussed elsewhere (182940). TCP1 codes for a
protein which is abundantly expressed in testes as well as in other
tissues. Using the cloned gene and a panel of somatic cell hybrids, as
well as in situ hybridization, Willison et al. (1987) assigned the gene
to 6q23-qter; thus, it is not closely linked to the HLA complex. For
this reason and others, TCP1 is not likely to be a human equivalent of
the mouse t-complex. Blanche et al. (1987) found that TCP1 is not linked
to HLA and GLO1 and is probably excluded from 6p. This result was
consistent with the reported localization to 6q23-qter. By in situ
hybridization, Fonatsch et al. (1987) concluded that the TCP1 locus is
probably in the 6q25-q27 region. Blanche et al. (1992) demonstrated that
the TCP1 and plasminogen (173350) genes show no recombination and are
located about 50 cM proximal to TCP10 (187020), which is located in band
6q27.
The ACAT2 gene (100678) shows complementary overlapping with the 3-prime
region of the TCP1 gene in both mouse and human. These genes are encoded
on opposite strands of DNA, as well as in opposite transcriptional
orientation. Masuno et al. (1996) assigned the ACAT2 gene to 6q25.3-q26
by fluorescence in situ hybridization; thus the assignment of the TCP1
gene can be refined to 6q25.3-q26.
*FIELD* RF
1. Blanche, H.; Massart, C.; Dausset, J.; Cann, H.: TCP1 is not linked
to HLA, GLO1, PGK1P2 and other markers in a 45cM map of the short
arm of chromosome 6 (6p). (Abstract) Cytogenet. Cell Genet. 46:
581-582, 1987.
2. Blanche, H.; Wright, L. G.; Vergnaud, G.; de Gouyon, B.; Lauthier,
V.; Silver, L. M.; Dausset, J.; Cann, H. M.; Spielman, R. S.: Genetic
mapping of three human homologues of murine t-complex genes localizes
TCP10 to 6q27, 15 cM distal to TCP1 and PLG. Genomics 12: 826-828,
1992.
3. Fonatsch, C.; Gradl, G.; Ragoussis, J.; Ziegler, A.: Assignment
of the TCP1 locus to the long arm of human chromosome 6 by in situ
hybridization. Cytogenet. Cell Genet. 45: 109-112, 1987.
4. Masuno, M.; Fukao, T.; Song, X.-Q.; Yamaguchi, S.; Orii, T.; Kondo,
N.; Imaizumi, K.; Kuroki, Y.: Assignment of the human cytosolic acetoacetyl-coenzyme
A thiolase (ACAT2) gene to chromosome 6q25.3-q26. Genomics 36: 217-218,
1996.
5. Willison, K.; Dudley, K.; Spurr, N.; Goodfellow, P.: Chromosomal
assignment of TCP-1, the human homologue of a mouse t-complex locus.
(Abstract) Cytogenet. Cell Genet. 40: 779-780, 1985.
6. Willison, K.; Kelly, A.; Dudley, K.; Goodfellow, P.; Spurr, N.;
Groves, V.; Gorman, P.; Sheer, D.; Trowsdale, J.: The human homologue
of the mouse t-complex gene, TCP1, is located on chromosome 6 but
is not near the HLA region. EMBO J. 6: 1967-1974, 1987.
7. Yaffe, M. B.; Farr, G. W.; Miklos, D.; Horwich, A. L.; Sternlicht,
M. L.; Sternlicht, H.: TCP1 complex is a molecular chaperone in tubulin
biogenesis. Nature 358: 245-248, 1992.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 05/23/2003
psherman: 7/27/1999
dkim: 9/9/1998
mark: 9/12/1996
terry: 9/4/1996
terry: 5/5/1994
carol: 8/24/1992
carol: 6/2/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989