ID TBCA_HUMAN Reviewed; 108 AA.
AC O75347; B4DT30;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=Tubulin-specific chaperone A;
DE AltName: Full=TCP1-chaperonin cofactor A;
DE AltName: Full=Tubulin-folding cofactor A;
DE Short=CFA;
GN Name=TBCA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12054808; DOI=10.1016/s0022-2836(02)00185-7;
RA Guasch A., Aloria K., Perez R., Avila J., Zabala J.C., Coll M.;
RT "Three-dimensional structure of human tubulin chaperone cofactor A.";
RL J. Mol. Biol. 318:1139-1149(2002).
CC -!- FUNCTION: Tubulin-folding protein; involved in the early step of the
CC tubulin folding pathway.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state.
CC -!- INTERACTION:
CC O75347; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2686341, EBI-750109;
CC O75347; PRO_0000449645 [P0DTC1]; Xeno; NbExp=2; IntAct=EBI-2686341, EBI-25475882;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75347-2; Sequence=VSP_056357;
CC -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR EMBL; AF038952; AAC39866.1; -; mRNA.
DR EMBL; BT007354; AAP36018.1; -; mRNA.
DR EMBL; AK300031; BAG61842.1; -; mRNA.
DR EMBL; AC026717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC035147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018210; AAH18210.1; -; mRNA.
DR CCDS; CCDS4040.1; -. [O75347-1]
DR CCDS; CCDS75263.1; -. [O75347-2]
DR RefSeq; NP_001284667.1; NM_001297738.1. [O75347-2]
DR RefSeq; NP_004598.1; NM_004607.2. [O75347-1]
DR PDB; 1H7C; X-ray; 1.80 A; A=2-108.
DR PDBsum; 1H7C; -.
DR AlphaFoldDB; O75347; -.
DR SMR; O75347; -.
DR BioGRID; 112765; 85.
DR IntAct; O75347; 19.
DR MINT; O75347; -.
DR STRING; 9606.ENSP00000306362; -.
DR GlyGen; O75347; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75347; -.
DR MetOSite; O75347; -.
DR PhosphoSitePlus; O75347; -.
DR BioMuta; TBCA; -.
DR OGP; O75347; -.
DR SWISS-2DPAGE; O75347; -.
DR EPD; O75347; -.
DR jPOST; O75347; -.
DR MassIVE; O75347; -.
DR MaxQB; O75347; -.
DR PaxDb; 9606-ENSP00000306362; -.
DR PeptideAtlas; O75347; -.
DR ProteomicsDB; 49916; -. [O75347-1]
DR ProteomicsDB; 5068; -.
DR Pumba; O75347; -.
DR TopDownProteomics; O75347-1; -. [O75347-1]
DR Antibodypedia; 24499; 292 antibodies from 27 providers.
DR DNASU; 6902; -.
DR Ensembl; ENST00000306388.10; ENSP00000306362.6; ENSG00000171530.15. [O75347-2]
DR Ensembl; ENST00000380377.9; ENSP00000369736.4; ENSG00000171530.15. [O75347-1]
DR GeneID; 6902; -.
DR KEGG; hsa:6902; -.
DR MANE-Select; ENST00000380377.9; ENSP00000369736.4; NM_004607.3; NP_004598.1.
DR UCSC; uc003kfi.2; human. [O75347-1]
DR AGR; HGNC:11579; -.
DR CTD; 6902; -.
DR DisGeNET; 6902; -.
DR GeneCards; TBCA; -.
DR HGNC; HGNC:11579; TBCA.
DR HPA; ENSG00000171530; Low tissue specificity.
DR MIM; 610058; gene.
DR neXtProt; NX_O75347; -.
DR OpenTargets; ENSG00000171530; -.
DR PharmGKB; PA36343; -.
DR VEuPathDB; HostDB:ENSG00000171530; -.
DR eggNOG; KOG3470; Eukaryota.
DR GeneTree; ENSGT00390000009710; -.
DR HOGENOM; CLU_130569_1_1_1; -.
DR InParanoid; O75347; -.
DR OMA; VIQECIM; -.
DR OrthoDB; 2727334at2759; -.
DR PhylomeDB; O75347; -.
DR TreeFam; TF313971; -.
DR PathwayCommons; O75347; -.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR SignaLink; O75347; -.
DR SIGNOR; O75347; -.
DR BioGRID-ORCS; 6902; 678 hits in 1161 CRISPR screens.
DR ChiTaRS; TBCA; human.
DR EvolutionaryTrace; O75347; -.
DR GeneWiki; TBCA; -.
DR GenomeRNAi; 6902; -.
DR Pharos; O75347; Tbio.
DR PRO; PR:O75347; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O75347; Protein.
DR Bgee; ENSG00000171530; Expressed in right adrenal gland cortex and 109 other cell types or tissues.
DR ExpressionAtlas; O75347; baseline and differential.
DR Genevisible; O75347; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; TAS:ProtInc.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 1.20.58.90; -; 1.
DR InterPro; IPR004226; TBCA.
DR InterPro; IPR036126; TBCA_sf.
DR PANTHER; PTHR21500; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR PANTHER; PTHR21500:SF3; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR Pfam; PF02970; TBCA; 1.
DR SUPFAM; SSF46988; Tubulin chaperone cofactor A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Cytoskeleton; Microtubule; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P80584"
FT CHAIN 2..108
FT /note="Tubulin-specific chaperone A"
FT /id="PRO_0000080039"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P80584"
FT VAR_SEQ 83..108
FT /note="ENEKDLEEAEEYKEARLVLDSVKLEA -> VSKDFCVMFKFFFSIQYMESQK
FT FKYLTLRTSWQYFLFTCPLYRYILK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056357"
FT HELIX 5..44
FT /evidence="ECO:0007829|PDB:1H7C"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:1H7C"
FT HELIX 64..84
FT /evidence="ECO:0007829|PDB:1H7C"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1H7C"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:1H7C"
SQ SEQUENCE 108 AA; 12855 MW; 222D8D945A5CD162 CRC64;
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES
RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA
//
