Full text data of TBCA
TBCA
[Confidence: low (only semi-automatic identification from reviews)]
Tubulin-specific chaperone A (TCP1-chaperonin cofactor A; Tubulin-folding cofactor A; CFA)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tubulin-specific chaperone A (TCP1-chaperonin cofactor A; Tubulin-folding cofactor A; CFA)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75347
ID TBCA_HUMAN Reviewed; 108 AA.
AC O75347;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 119.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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 [5]
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
CC the 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the TBCA family.
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CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF038952; AAC39866.1; -; mRNA.
DR EMBL; BT007354; AAP36018.1; -; mRNA.
DR EMBL; BC018210; AAH18210.1; -; mRNA.
DR RefSeq; NP_004598.1; NM_004607.2.
DR UniGene; Hs.291212; -.
DR PDB; 1H7C; X-ray; 1.80 A; A=1-108.
DR PDBsum; 1H7C; -.
DR ProteinModelPortal; O75347; -.
DR SMR; O75347; 4-106.
DR IntAct; O75347; 3.
DR STRING; 9606.ENSP00000369736; -.
DR PhosphoSite; O75347; -.
DR OGP; O75347; -.
DR SWISS-2DPAGE; O75347; -.
DR PaxDb; O75347; -.
DR PeptideAtlas; O75347; -.
DR PRIDE; O75347; -.
DR DNASU; 6902; -.
DR Ensembl; ENST00000380377; ENSP00000369736; ENSG00000171530.
DR GeneID; 6902; -.
DR KEGG; hsa:6902; -.
DR UCSC; uc003kfh.1; human.
DR CTD; 6902; -.
DR GeneCards; GC05M077022; -.
DR HGNC; HGNC:11579; TBCA.
DR HPA; HPA036487; -.
DR MIM; 610058; gene.
DR neXtProt; NX_O75347; -.
DR PharmGKB; PA36343; -.
DR eggNOG; NOG235957; -.
DR HOGENOM; HOG000213817; -.
DR HOVERGEN; HBG004499; -.
DR InParanoid; O75347; -.
DR KO; K17292; -.
DR OMA; LVKEKMM; -.
DR OrthoDB; EOG7P8PB5; -.
DR PhylomeDB; O75347; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR EvolutionaryTrace; O75347; -.
DR GeneWiki; TBCA; -.
DR GenomeRNAi; 6902; -.
DR NextBio; 26989; -.
DR PRO; PR:O75347; -.
DR ArrayExpress; O75347; -.
DR Bgee; O75347; -.
DR CleanEx; HS_TBCA; -.
DR Genevestigator; O75347; -.
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:0051087; F:chaperone binding; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; TAS:ProtInc.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR InterPro; IPR004226; CofA_tubulin-bd.
DR PANTHER; PTHR21500; PTHR21500; 1.
DR Pfam; PF02970; TBCA; 1.
DR ProDom; PD010430; CofA_tubulin_bd; 1.
DR SUPFAM; SSF46988; SSF46988; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 108 Tubulin-specific chaperone A.
FT /FTId=PRO_0000080039.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT HELIX 5 44
FT HELIX 49 61
FT HELIX 64 84
FT HELIX 86 88
FT HELIX 92 105
SQ SEQUENCE 108 AA; 12855 MW; 222D8D945A5CD162 CRC64;
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES
RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA
//
ID TBCA_HUMAN Reviewed; 108 AA.
AC O75347;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 119.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
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 [5]
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
CC the 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the TBCA family.
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; AF038952; AAC39866.1; -; mRNA.
DR EMBL; BT007354; AAP36018.1; -; mRNA.
DR EMBL; BC018210; AAH18210.1; -; mRNA.
DR RefSeq; NP_004598.1; NM_004607.2.
DR UniGene; Hs.291212; -.
DR PDB; 1H7C; X-ray; 1.80 A; A=1-108.
DR PDBsum; 1H7C; -.
DR ProteinModelPortal; O75347; -.
DR SMR; O75347; 4-106.
DR IntAct; O75347; 3.
DR STRING; 9606.ENSP00000369736; -.
DR PhosphoSite; O75347; -.
DR OGP; O75347; -.
DR SWISS-2DPAGE; O75347; -.
DR PaxDb; O75347; -.
DR PeptideAtlas; O75347; -.
DR PRIDE; O75347; -.
DR DNASU; 6902; -.
DR Ensembl; ENST00000380377; ENSP00000369736; ENSG00000171530.
DR GeneID; 6902; -.
DR KEGG; hsa:6902; -.
DR UCSC; uc003kfh.1; human.
DR CTD; 6902; -.
DR GeneCards; GC05M077022; -.
DR HGNC; HGNC:11579; TBCA.
DR HPA; HPA036487; -.
DR MIM; 610058; gene.
DR neXtProt; NX_O75347; -.
DR PharmGKB; PA36343; -.
DR eggNOG; NOG235957; -.
DR HOGENOM; HOG000213817; -.
DR HOVERGEN; HBG004499; -.
DR InParanoid; O75347; -.
DR KO; K17292; -.
DR OMA; LVKEKMM; -.
DR OrthoDB; EOG7P8PB5; -.
DR PhylomeDB; O75347; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR EvolutionaryTrace; O75347; -.
DR GeneWiki; TBCA; -.
DR GenomeRNAi; 6902; -.
DR NextBio; 26989; -.
DR PRO; PR:O75347; -.
DR ArrayExpress; O75347; -.
DR Bgee; O75347; -.
DR CleanEx; HS_TBCA; -.
DR Genevestigator; O75347; -.
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:0051087; F:chaperone binding; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; TAS:ProtInc.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR InterPro; IPR004226; CofA_tubulin-bd.
DR PANTHER; PTHR21500; PTHR21500; 1.
DR Pfam; PF02970; TBCA; 1.
DR ProDom; PD010430; CofA_tubulin_bd; 1.
DR SUPFAM; SSF46988; SSF46988; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Microtubule; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 108 Tubulin-specific chaperone A.
FT /FTId=PRO_0000080039.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT HELIX 5 44
FT HELIX 49 61
FT HELIX 64 84
FT HELIX 86 88
FT HELIX 92 105
SQ SEQUENCE 108 AA; 12855 MW; 222D8D945A5CD162 CRC64;
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES
RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA
//
MIM
610058
*RECORD*
*FIELD* NO
610058
*FIELD* TI
*610058 TUBULIN-SPECIFIC CHAPERONE A; TBCA
;;CHAPERONIN COFACTOR A
*FIELD* TX
DESCRIPTION
read more
Microtubules are polymers of alpha-tubulin (see TUBA1; 191110) and
beta-tubulin (see TUBB; 191130) that participate in essential cell
functions. A multistep process involving molecular chaperones and
cofactors, including TBCA, produces tubulin heterodimers competent to
polymerize. TBCA specifically interacts with a folding intermediate of
beta-tubulin and acts as a molecular chaperone (Nolasco et al., 2005).
CLONING
By sequencing cDNAs obtained from umbilical cord blood CD34
(142230)-positive hematopoietic stem/progenitor cells, Mao et al. (1998)
identified TBCA.
GENE FUNCTION
Tian et al. (1996) found that purified bovine cofactor A formed a stable
complex with beta-tubulin intermediates generated by ATP-dependent
action of the cytosolic chaperonin complex. Through this interaction,
cofactor A appeared to increase the rate of tubulin cycling and,
secondarily, to stimulate the ATPase activity of the complex.
Using small interfering RNA to silence TBCA expression in HeLa and MCF7
mammary carcinoma cell lines, Nolasco et al. (2005) found that TBCA was
essential for cell viability. TBCA knockdown produced a decrease in the
amount of soluble tubulin, modifications in microtubules, and G1 cell
cycle arrest. In MCF7 cells, cell death was preceded by a change in cell
shape resembling differentiation.
MAPPING
The International Radiation Hybrid mapping Consortium mapped the TBCA
gene to chromosome 5 (TMAP SHGC-34767).
*FIELD* RF
1. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
2. Nolasco, S.; Bellido, J.; Goncalves, J.; Zabala, J. C.; Soares,
H.: Tubulin cofactor A gene silencing in mammalian cells induces
changes in microtubule cytoskeleton, cell cycle arrest and cell death. FEBS
Lett. 579: 3515-3524, 2005.
3. Tian, G.; Huang, Y.; Rommelaere, H.; Vandekerckhove, J.; Ampe,
C.; Cowan, N. J.: Pathway leading to correctly folded beta-tubulin. Cell 86:
287-296, 1996.
*FIELD* CD
Patricia A. Hartz: 4/18/2006
*FIELD* ED
mgross: 04/18/2006
*RECORD*
*FIELD* NO
610058
*FIELD* TI
*610058 TUBULIN-SPECIFIC CHAPERONE A; TBCA
;;CHAPERONIN COFACTOR A
*FIELD* TX
DESCRIPTION
read more
Microtubules are polymers of alpha-tubulin (see TUBA1; 191110) and
beta-tubulin (see TUBB; 191130) that participate in essential cell
functions. A multistep process involving molecular chaperones and
cofactors, including TBCA, produces tubulin heterodimers competent to
polymerize. TBCA specifically interacts with a folding intermediate of
beta-tubulin and acts as a molecular chaperone (Nolasco et al., 2005).
CLONING
By sequencing cDNAs obtained from umbilical cord blood CD34
(142230)-positive hematopoietic stem/progenitor cells, Mao et al. (1998)
identified TBCA.
GENE FUNCTION
Tian et al. (1996) found that purified bovine cofactor A formed a stable
complex with beta-tubulin intermediates generated by ATP-dependent
action of the cytosolic chaperonin complex. Through this interaction,
cofactor A appeared to increase the rate of tubulin cycling and,
secondarily, to stimulate the ATPase activity of the complex.
Using small interfering RNA to silence TBCA expression in HeLa and MCF7
mammary carcinoma cell lines, Nolasco et al. (2005) found that TBCA was
essential for cell viability. TBCA knockdown produced a decrease in the
amount of soluble tubulin, modifications in microtubules, and G1 cell
cycle arrest. In MCF7 cells, cell death was preceded by a change in cell
shape resembling differentiation.
MAPPING
The International Radiation Hybrid mapping Consortium mapped the TBCA
gene to chromosome 5 (TMAP SHGC-34767).
*FIELD* RF
1. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
2. Nolasco, S.; Bellido, J.; Goncalves, J.; Zabala, J. C.; Soares,
H.: Tubulin cofactor A gene silencing in mammalian cells induces
changes in microtubule cytoskeleton, cell cycle arrest and cell death. FEBS
Lett. 579: 3515-3524, 2005.
3. Tian, G.; Huang, Y.; Rommelaere, H.; Vandekerckhove, J.; Ampe,
C.; Cowan, N. J.: Pathway leading to correctly folded beta-tubulin. Cell 86:
287-296, 1996.
*FIELD* CD
Patricia A. Hartz: 4/18/2006
*FIELD* ED
mgross: 04/18/2006