Tubulin-specific chaperone B - Caenorhabditis elegans

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Reviewed, UniProtKB/Swiss-Prot Q20728 (TBCB_CAEEL)

Last modified January 19, 2010. Version 63. History...

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

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Names and origin

Protein names

Recommended name:
    Tubulin-specific chaperone B
Alternative name(s):
    Tubulin-folding cofactor B
      Short name=CoB

Gene names

ORF Names:

F53F4.3

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the TBCB family. Contains 1 CAP-Gly domain.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Molecular function	Chaperone
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 229

229

Tubulin-specific chaperone B

PRO_0000083546

Regions

Domain

170 – 212

CAP-Gly

Secondary structure

229

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q20728-1 [UniParc].

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

229

25,441

        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

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References

	« Hide 'large scale' referencesShow '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.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z77663 Genomic DNA. Translation: CAB01212.1.

PIR

T22581.

RefSeq

NP_506367.1.

UniGene

Cel.3444

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LPL	X-ray	1.77	A	135-229	[»]
1T0Y	NMR	-	A	1-120	[»]
1TOV	X-ray	1.77	A	132-229	[»]

ModBase

Search...

Genome annotation databases

Ensembl

F53F4.3; F53F4.3; F53F4.3; Caenorhabditis elegans. [Genome view]

GeneID

186176.

KEGG

cel:F53F4.3.

NMPDR

fig|6239.3.peg.20325.

UCSC

F53F4.3. c. elegans.

Organism-specific databases

CTD

186176.

WormBase

WBGene00009987. F53F4.3.

WormPep

F53F4.3. CE10958. [WorfDB]

Phylogenomic databases

eggNOG

meNOG12410.

HOGENOM

HBG385175.

InParanoid

Q20728.

OMA

WVGVRYD.

PhylomeDB

Q20728.

Gene expression databases

ArrayExpress

Q20728.

Family and domain databases

InterPro

IPR000938. Cytoskel-assoc-prot_CAP-Gly.
[Graphical view]

Pfam

PF01302. CAP_GLY. 1 hit.
[Graphical view]

PROSITE

PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

930902.

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Entry information

Entry name

TBCB_CAEEL

Accession

Primary (citable) accession number: Q20728

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project

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