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Protein

Tubulin-folding cofactor B

Gene

TBCB

Organism
Homo sapiens (Human)
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. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.
SIGNORiQ99426.

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:CG22, CKAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1989. TBCB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: ProtInc
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651S → A: Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-128. 1 Publication
Mutagenesisi128 – 1281S → A: Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-65. 1 Publication

Organism-specific databases

PharmGKBiPA162405357.

Polymorphism and mutation databases

BioMutaiTBCB.
DMDMi3023518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Tubulin-folding cofactor BPRO_0000083534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei65 – 651Phosphoserine; by PAK11 Publication
Modified residuei98 – 981PhosphotyrosineCombined sources
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei128 – 1281Phosphoserine; by PAK11 Publication
Modified residuei219 – 2191N6-acetyllysineCombined sources

Post-translational modificationi

Phosphorylation by PAK1 is required for normal function.1 Publication
Ubiquitinated in the presence of GAN which targets it for degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99426.
MaxQBiQ99426.
PaxDbiQ99426.
PeptideAtlasiQ99426.
PRIDEiQ99426.

2D gel databases

OGPiQ99426.

PTM databases

iPTMnetiQ99426.
PhosphoSiteiQ99426.

Expressioni

Tissue specificityi

Found in most tissues.

Gene expression databases

BgeeiQ99426.
CleanExiHS_TBCB.
ExpressionAtlasiQ99426. baseline and differential.
GenevisibleiQ99426. HS.

Organism-specific databases

HPAiHPA041428.
HPA041722.

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. Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers. Binds to GAN.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GANQ9H2C03EBI-764356,EBI-764342
USP7Q930092EBI-764356,EBI-302474

Protein-protein interaction databases

BioGridi107575. 43 interactions.
DIPiDIP-34409N.
IntActiQ99426. 5 interactions.
MINTiMINT-2855745.
STRINGi9606.ENSP00000221855.

Structurei

3D structure databases

ProteinModelPortaliQ99426.
SMRiQ99426. Positions 11-93, 134-233.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ99426.
KOiK17262.
OMAiYNEEEMQ.
OrthoDBiEOG7C2R2R.
PhylomeDBiQ99426.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99426-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEVTGVSAPT VTVFISSSLN TFRSEKRYSR SLTIAEFKCK LELLVGSPAS
60 70 80 90 100
CMELELYGVD DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGARLGEYED
110 120 130 140 150
VSRVEKYTIS QEAYDQRQDT VRSFLKRSKL GRYNEEERAQ QEAEAAQRLA
160 170 180 190 200
EEKAQASSIP VGSRCEVRAA GQSPRRGTVM YVGLTDFKPG YWIGVRYDEP
210 220 230 240
LGKNDGSVNG KRYFECQAKY GAFVKPAVVT VGDFPEEDYG LDEI
Length:244
Mass (Da):27,326
Last modified:July 15, 1998 - v2
Checksum:iE984C7C74A105384
GO
Isoform 2 (identifier: Q99426-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Note: No experimental confirmation available.
Show »
Length:193
Mass (Da):21,801
Checksum:iF4C073C91A3AE400
GO

Sequence cautioni

The sequence AAB51182.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281S → R in AAB67716 (PubMed:9265649).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 2. 1 PublicationVSP_055521Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013488 mRNA. Translation: AAB67716.1.
BT007424 mRNA. Translation: AAP36092.1.
CR541971 mRNA. Translation: CAG46769.1.
AD001527 Genomic DNA. Translation: AAB51182.1. Sequence problems.
BC005969 mRNA. Translation: AAH05969.1.
BC052812 mRNA. Translation: AAH52812.1.
D49738 mRNA. Translation: BAA08572.1.
CCDSiCCDS12488.1. [Q99426-1]
CCDS74344.1. [Q99426-2]
RefSeqiNP_001272.2. NM_001281.2. [Q99426-1]
NP_001287900.1. NM_001300971.1. [Q99426-2]
UniGeneiHs.31053.

Genome annotation databases

EnsembliENST00000221855; ENSP00000221855; ENSG00000105254. [Q99426-1]
ENST00000585746; ENSP00000467487; ENSG00000105254. [Q99426-2]
GeneIDi1155.
KEGGihsa:1155.
UCSCiuc002odg.2. human. [Q99426-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013488 mRNA. Translation: AAB67716.1.
BT007424 mRNA. Translation: AAP36092.1.
CR541971 mRNA. Translation: CAG46769.1.
AD001527 Genomic DNA. Translation: AAB51182.1. Sequence problems.
BC005969 mRNA. Translation: AAH05969.1.
BC052812 mRNA. Translation: AAH52812.1.
D49738 mRNA. Translation: BAA08572.1.
CCDSiCCDS12488.1. [Q99426-1]
CCDS74344.1. [Q99426-2]
RefSeqiNP_001272.2. NM_001281.2. [Q99426-1]
NP_001287900.1. NM_001300971.1. [Q99426-2]
UniGeneiHs.31053.

3D structure databases

ProteinModelPortaliQ99426.
SMRiQ99426. Positions 11-93, 134-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107575. 43 interactions.
DIPiDIP-34409N.
IntActiQ99426. 5 interactions.
MINTiMINT-2855745.
STRINGi9606.ENSP00000221855.

PTM databases

iPTMnetiQ99426.
PhosphoSiteiQ99426.

Polymorphism and mutation databases

BioMutaiTBCB.
DMDMi3023518.

2D gel databases

OGPiQ99426.

Proteomic databases

EPDiQ99426.
MaxQBiQ99426.
PaxDbiQ99426.
PeptideAtlasiQ99426.
PRIDEiQ99426.

Protocols and materials databases

DNASUi1155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221855; ENSP00000221855; ENSG00000105254. [Q99426-1]
ENST00000585746; ENSP00000467487; ENSG00000105254. [Q99426-2]
GeneIDi1155.
KEGGihsa:1155.
UCSCiuc002odg.2. human. [Q99426-1]

Organism-specific databases

CTDi1155.
GeneCardsiTBCB.
HGNCiHGNC:1989. TBCB.
HPAiHPA041428.
HPA041722.
MIMi601303. gene.
neXtProtiNX_Q99426.
PharmGKBiPA162405357.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3206. Eukaryota.
ENOG410YKGB. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000209180.
HOVERGENiHBG003239.
InParanoidiQ99426.
KOiK17262.
OMAiYNEEEMQ.
OrthoDBiEOG7C2R2R.
PhylomeDBiQ99426.
TreeFamiTF313444.

Enzyme and pathway databases

ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.
SIGNORiQ99426.

Miscellaneous databases

ChiTaRSiTBCB. human.
GeneWikiiTBCB.
GenomeRNAii1155.
PROiQ99426.
SOURCEiSearch...

Gene expression databases

BgeeiQ99426.
CleanExiHS_TBCB.
ExpressionAtlasiQ99426. baseline and differential.
GenevisibleiQ99426. HS.

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. "Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors."
    Tian G., Lewis S.A., Feierbach B., Stearns T., Rommelaere H., Ampe C., Cowan N.J.
    J. Cell Biol. 138:821-832(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Bone marrow and Uterus.
  6. "Cloning, expression, and mapping of CKAPI, which encodes a putative cytoskeleton-associated protein containing a CAP-Gly domain."
    Watanabe T.K., Shimizu F., Nagata M., Kawai A., Fujiwara T., Nakamura Y., Takahashi E., Hirai Y.
    Cytogenet. Cell Genet. 72:208-211(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-244 (ISOFORM 1).
    Tissue: Fetal brain.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway."
    Wang W., Ding J., Allen E., Zhu P., Zhang L., Vogel H., Yang Y.
    Curr. Biol. 15:2050-2055(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  9. "p21-activated kinase 1 regulates microtubule dynamics by phosphorylating tubulin cofactor B."
    Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S., Marcus S., Goodson H.V., Sahin A.A., Kumar R.
    Mol. Cell. Biol. 25:3726-3736(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65 AND SER-128, MUTAGENESIS OF SER-65 AND SER-128.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBCB_HUMAN
AccessioniPrimary (citable) accession number: Q99426
Secondary accession number(s): O00111
, O00674, O14728, Q6FGY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: June 8, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  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.