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UniProtKB/Swiss-Prot entry Q20728


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TBCB_CAEEL
Primary accession number Q20728
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    April 29, 2008 (Entry version 52)
Name and origin of the protein
Protein name Tubulin-specific chaperone B
Synonyms Tubulin folding cofactor B
CoB
Gene name
ORFNames: F53F4.3
From
Caenorhabditis elegans [TaxID: 6239] 
Taxonomy Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).
[2]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 135-229.
DOI=10.1074/jbc.M208512200; PubMed=12221106 [NCBI, ExPASy, EBI, Israel, Japan]
Li S., Finley J., Liu Z.J., Qiu S.H., Chen H., Luan C.H., Carson M., Tsao J., Johnson D., Lin G., Zhao J., Thomas W., Nagy L.A., Sha B., DeLucas L.J., Wang B.C., Luo M.;
"Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain.";
J. Biol. Chem. 277:48596-48601(2002).
[3]
STRUCTURE BY NMR OF 1-120.
DOI=10.1074/jbc.M409422200; PubMed=15364906 [NCBI, ExPASy, EBI, Israel, Japan]
Lytle B.L., Peterson F.C., Qiu S.H., Luo M., Zhao Q., Markley J.L., Volkman B.F.;
"Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B.";
J. Biol. Chem. 279:46787-46793(2004).
Comments
  • FUNCTION: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer (By similarity).
  • SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, cytoskeleton (By similarity).
  • SIMILARITY: Belongs to the TBCB family.
  • SIMILARITY: Contains 1 CAP-Gly domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z77663; CAB01212.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T22581; T22581.
RefSeq NP_506367.1; -.
UniGene Cel.3444
3D structure databases
PDB
1LPL; X-ray; 1.77 A; A=135-229.[ExPASy / RCSB / EBI]
1T0Y; NMR; -; A=1-120.[ExPASy / RCSB / EBI]
1TOV; X-ray; 1.77 A; A=132-229.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LPL; -.
1T0Y; -.
1TOV; -.
ModBase Q20728.
Organism-specific databases
WormBase WBGene00009987; F53F4.3.
WormPep F53F4.3; CE10958. [WormPep / WorfDB]
Gene expression databases
ArrayExpress Q20728; -.
Family and domain databases
InterPro IPR000938; Cytoskel-assoc-prot_CAP-Gly.
Graphical view of domain structure.
Pfam PF01302; CAP_GLY; 1.
Pfam graphical view of domain structure.
PROSITE PS00845; CAP_GLY_1; 1.
PS50245; CAP_GLY_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q20728.
Genome annotation databases
Ensembl F53F4.3; Caenorhabditis elegans. [Contig view]
GeneID 186176; -.
KEGG cel:F53F4.3; -.
NMPDR fig|6239.3.peg.20325; -.
Other
ProtoNet Q20728.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   229  229     Tubulin-specific chaperone B. PRO_0000083546
DOMAIN   170   212  43     CAP-Gly. 
STRAND   4    13  10      
STRAND   18    23  6      
HELIX   28    39  12      
TURN   43    45  3      
STRAND   46    51  6      
STRAND   53    60  8      
STRAND   65    67  3      
TURN   68    72  5      
STRAND   77    83  7      
HELIX   137   143  7      
STRAND   151   154  4      
STRAND   162   170  9      
STRAND   173   177  5      
STRAND   179   187  9      
STRAND   189   195  7      
STRAND   207   211  5      
HELIX   213   215  3      
STRAND   216   219  4      
Sequence information
Length: 229 AA [This is the length of the unprocessed precursor] Molecular weight: 25441 Da [This is the MW of the unprocessed precursor] CRC64: C465365DAE378A0F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTEVYDLEIT TNATDFPMEK KYPAGMSLND LKKKLELVVG TTVDSMRIQL FDGDDQLKGE 

        70         80         90        100        110        120 
LTDGAKSLKD LGVRDGYRIH AVDVTGGNED FKDESMVEKY EMSDDTYGKR TDSVRAWKKK 

       130        140        150        160        170        180 
MQEEQGSAAP MENESDKLNE EAAKNIMVGN RCEVTVGAQM ARRGEVAYVG ATKFKEGVWV 

       190        200        210        220 
GVKYDEPVGK NDGSVAGVRY FDCDPKYGGF VRPVDVKVGD FPELSIDEI 

Q20728 in FASTA format

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