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Protein

Tubulin-folding cofactor B

Gene

Tbcb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.By similarity2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-folding cofactor B
Alternative name(s):
Cytoskeleton-associated protein 1
Cytoskeleton-associated protein CKAPI
Tubulin-specific chaperone B
Gene namesi
Name:Tbcb
Synonyms:Ckap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1913661. Tbcb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Disruption phenotypei

Mice display significantly longer axons than wild-type mice. Overexpression of Tbcb causes microtubule depolymerization, growth cone retraction and axonal damage followed by neuronal degeneration.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Tubulin-folding cofactor BPRO_0000083535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei65 – 651Phosphoserine; by PAK1By similarity
Modified residuei98 – 981PhosphotyrosineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei128 – 1281Phosphoserine; by PAK1By similarity
Modified residuei219 – 2191N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylation by PAK1 is required for normal function.
Ubiquitinated in the presence of GAN which targets it for degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D1E6.
MaxQBiQ9D1E6.
PaxDbiQ9D1E6.
PeptideAtlasiQ9D1E6.
PRIDEiQ9D1E6.

PTM databases

iPTMnetiQ9D1E6.
PhosphoSiteiQ9D1E6.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain. Broadly distributed throughout the neonate brain but restricted mainly to ependymary cells in the adult brain where it is concentrated in the cilia.1 Publication

Developmental stagei

In the embryo, expression increases at E12.5-E14.5. Levels are highest in pre- and postnatal stages which coincide with peaks of cerebral and cerebellar neurogenesis (at protein level).1 Publication

Gene expression databases

BgeeiQ9D1E6.
CleanExiMM_TBCB.
GenevisibleiQ9D1E6. MM.

Interactioni

Subunit structurei

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). Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers. Binds to GAN.By similarity1 Publication

Protein-protein interaction databases

IntActiQ9D1E6. 2 interactions.
MINTiMINT-4137117.
STRINGi10090.ENSMUSP00000006254.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 177Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 285Combined sources
Helixi34 – 4411Combined sources
Turni49 – 513Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 664Combined sources
Beta strandi70 – 734Combined sources
Beta strandi76 – 783Combined sources
Beta strandi84 – 885Combined sources
Helixi137 – 14711Combined sources
Helixi150 – 1567Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi175 – 18410Combined sources
Beta strandi186 – 20015Combined sources
Beta strandi206 – 2083Combined sources
Turni218 – 2203Combined sources
Beta strandi221 – 2244Combined sources
Helixi226 – 2283Combined sources
Beta strandi229 – 2335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V6ENMR-A11-92[»]
1WHGNMR-A134-233[»]
ProteinModelPortaliQ9D1E6.
SMRiQ9D1E6. Positions 11-92, 134-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D1E6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 22543CAP-GlyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TBCB family.Curated
Contains 1 CAP-Gly domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3206. Eukaryota.
ENOG410YKGB. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000209180.
HOVERGENiHBG003239.
InParanoidiQ9D1E6.
KOiK17262.
OMAiYNEEEMQ.
OrthoDBiEOG7C2R2R.
PhylomeDBiQ9D1E6.
TreeFamiTF313444.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
PF14560. Ubiquitin_2. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D1E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVTGISAPT VMVFISSSLN SFRSEKRYSR SLTIAEFKCK LELVVGSPAS
60 70 80 90 100
CMELELYGAD DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGVRLGEYED
110 120 130 140 150
VSKVEKYEIS PEAYERRQNT VRSFMKRSKL GPYNEELRAQ QEAEAAQRLS
160 170 180 190 200
EEKAQASAIS VGSRCEVRAP DHSLRRGTVM YVGLTDFKPG YWVGVRYDEP
210 220 230 240
LGKNDGSVNG KRYFECQAKY GAFVKPSAVT VGDFPEEDYG LDEM
Length:244
Mass (Da):27,386
Last modified:March 1, 2003 - v2
Checksum:i03BC7F0134F9289C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841R → S in BAB26939 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002316 mRNA. Translation: BAB22009.1.
AK003655 mRNA. Translation: BAB22918.2.
AK010438 mRNA. Translation: BAB26939.1.
BC010684 mRNA. Translation: AAH10684.1.
CCDSiCCDS21083.1.
RefSeqiNP_079824.2. NM_025548.3.
UniGeneiMm.27947.

Genome annotation databases

EnsembliENSMUST00000006254; ENSMUSP00000006254; ENSMUSG00000006095.
GeneIDi66411.
KEGGimmu:66411.
UCSCiuc009gds.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002316 mRNA. Translation: BAB22009.1.
AK003655 mRNA. Translation: BAB22918.2.
AK010438 mRNA. Translation: BAB26939.1.
BC010684 mRNA. Translation: AAH10684.1.
CCDSiCCDS21083.1.
RefSeqiNP_079824.2. NM_025548.3.
UniGeneiMm.27947.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V6ENMR-A11-92[»]
1WHGNMR-A134-233[»]
ProteinModelPortaliQ9D1E6.
SMRiQ9D1E6. Positions 11-92, 134-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1E6. 2 interactions.
MINTiMINT-4137117.
STRINGi10090.ENSMUSP00000006254.

PTM databases

iPTMnetiQ9D1E6.
PhosphoSiteiQ9D1E6.

Proteomic databases

EPDiQ9D1E6.
MaxQBiQ9D1E6.
PaxDbiQ9D1E6.
PeptideAtlasiQ9D1E6.
PRIDEiQ9D1E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006254; ENSMUSP00000006254; ENSMUSG00000006095.
GeneIDi66411.
KEGGimmu:66411.
UCSCiuc009gds.2. mouse.

Organism-specific databases

CTDi1155.
MGIiMGI:1913661. Tbcb.

Phylogenomic databases

eggNOGiKOG3206. Eukaryota.
ENOG410YKGB. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000209180.
HOVERGENiHBG003239.
InParanoidiQ9D1E6.
KOiK17262.
OMAiYNEEEMQ.
OrthoDBiEOG7C2R2R.
PhylomeDBiQ9D1E6.
TreeFamiTF313444.

Miscellaneous databases

EvolutionaryTraceiQ9D1E6.
PROiQ9D1E6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1E6.
CleanExiMM_TBCB.
GenevisibleiQ9D1E6. MM.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 1 hit.
PF14560. Ubiquitin_2. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation."
    Kortazar D., Fanarraga M.L., Carranza G., Bellido J., Villegas J.C., Avila J., Zabala J.C.
    Exp. Cell Res. 313:425-436(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBCE.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Solution structure of a N-terminal ubiquitin-like domain in mouse tubulin-specific chaperone B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 11-92.
  8. "Solution structure of the CAP-Gly domain in mouse tubulin-specific chaperone B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2003) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 134-233.

Entry informationi

Entry nameiTBCB_MOUSE
AccessioniPrimary (citable) accession number: Q9D1E6
Secondary accession number(s): Q9CWR6, Q9DCZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.