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Reviewed, UniProtKB/Swiss-Prot Q20728 (TBCB_CAEEL)

Last modified July 22, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tubulin-specific chaperone B
Alternative name(s):
    Tubulin folding cofactor B
      Short name=CoB
Gene names
ORF Names: F53F4.3
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

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

CytoplasmBy similarity. CytoplasmcytoskeletonBy similarity.

Sequence similarities

Belongs to the TBCB family.

Contains 1 CAP-Gly domain.

Ontologies

Keywords

   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 229229Tubulin-specific chaperone B

Regions

Domain170 – 21243CAP-Gly

Secondary structure

.................................. 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q20728-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C465365DAE378A0F

FASTA22925,441
        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 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]"Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain."
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.
J. Biol. Chem. 277:48596-48601(2002) [PubMed: 12221106] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 135-229.
[3]"Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B."
Lytle B.L., Peterson F.C., Qiu S.H., Luo M., Zhao Q., Markley J.L., Volkman B.F.
J. Biol. Chem. 279:46787-46793(2004) [PubMed: 15364906] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-120.

Cross-references

Sequence databases

Z77663 Genomic DNA. Translation: CAB01212.1.
PIRT22581.
RefSeqNP_506367.1.
UniGeneCel.3444

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LPLX-ray1.77A135-229[»]
1T0YNMR-A1-120[»]
1TOVX-ray1.77A132-229[»]
ModBaseSearch...

Genome annotation databases

EnsemblF53F4.3. Caenorhabditis elegans. [Contig view]
GeneID186176.
KEGGcel:F53F4.3.
NMPDRfig|6239.3.peg.20325.

Organism-specific databases

WormBaseWBGene00009987. F53F4.3.
WormPepF53F4.3. CE10958. [WorfDB]

Gene expression databases

ArrayExpressQ20728.

Family and domain databases

InterProIPR000938. Cytoskel-assoc-prot_CAP-Gly.
[Graphical view]
PfamPF01302. CAP_GLY. 1 hit.
[Graphical view]
PROSITEPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProDomQ20728.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameTBCB_CAEEL
AccessionPrimary (citable) accession number: Q20728
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 22, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents