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Protein

Tubulin-folding cofactor B

Gene

Tbcb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:17184771). May function as a negative regulator of axonal growth (PubMed:17217416).By similarity2 Publications

GO - Biological processi

Keywordsi

Molecular functionChaperone, Developmental protein
Biological processDifferentiation, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1913661 Tbcb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000835351 – 244Tubulin-folding cofactor BAdd BLAST244

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei65Phosphoserine; by PAK1By similarity1
Modified residuei98PhosphotyrosineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei128Phosphoserine; by PAK1By similarity1
Modified residuei219N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation by PAK1 is required for normal function.By similarity
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
PhosphoSitePlusiQ9D1E6

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

BgeeiENSMUSG00000006095 Expressed in 284 organ(s), highest expression level in facial nucleus
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 (PubMed:17184771). Interacts with GAN. Interacts with DCTN1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

IntActiQ9D1E6, 2 interactors
MINTiQ9D1E6
STRINGi10090.ENSMUSP00000006254

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9D1E6
SMRiQ9D1E6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D1E6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini183 – 225CAP-GlyPROSITE-ProRule annotationAdd BLAST43

Sequence similaritiesi

Belongs to the TBCB family.Curated

Phylogenomic databases

eggNOGiKOG3206 Eukaryota
ENOG410YKGB LUCA
GeneTreeiENSGT00760000119173
HOGENOMiHOG000209180
HOVERGENiHBG003239
InParanoidiQ9D1E6
KOiK17262
OMAiYNEEEMQ
OrthoDBiEOG091G0M22
PhylomeDBiQ9D1E6
TreeFamiTF313444

Family and domain databases

Gene3Di2.30.30.190, 1 hit
InterProiView protein in InterPro
IPR036859 CAP-Gly_dom_sf
IPR000938 CAP-Gly_domain
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF01302 CAP_GLY, 1 hit
PF14560 Ubiquitin_2, 1 hit
SMARTiView protein in SMART
SM01052 CAP_GLY, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF74924 SSF74924, 1 hit
PROSITEiView protein in PROSITE
PS00845 CAP_GLY_1, 1 hit
PS50245 CAP_GLY_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti84R → S in BAB26939 (PubMed:16141072).Curated1

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

Similar proteinsi

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V6ENMR-A11-92[»]
1WHGNMR-A134-233[»]
ProteinModelPortaliQ9D1E6
SMRiQ9D1E6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1E6, 2 interactors
MINTiQ9D1E6
STRINGi10090.ENSMUSP00000006254

PTM databases

iPTMnetiQ9D1E6
PhosphoSitePlusiQ9D1E6

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
OrthoDBiEOG091G0M22
PhylomeDBiQ9D1E6
TreeFamiTF313444

Miscellaneous databases

EvolutionaryTraceiQ9D1E6
PROiPR:Q9D1E6
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006095 Expressed in 284 organ(s), highest expression level in facial nucleus
CleanExiMM_TBCB
GenevisibleiQ9D1E6 MM

Family and domain databases

Gene3Di2.30.30.190, 1 hit
InterProiView protein in InterPro
IPR036859 CAP-Gly_dom_sf
IPR000938 CAP-Gly_domain
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF01302 CAP_GLY, 1 hit
PF14560 Ubiquitin_2, 1 hit
SMARTiView protein in SMART
SM01052 CAP_GLY, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF74924 SSF74924, 1 hit
PROSITEiView protein in PROSITE
PS00845 CAP_GLY_1, 1 hit
PS50245 CAP_GLY_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTBCB_MOUSE
AccessioniPrimary (citable) accession number: Q9D1E6
Secondary accession number(s): Q9CWR6, Q9DCZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2003
Last modified: September 12, 2018
This is version 129 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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