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Protein

Tubulin-specific chaperone E

Gene

Tbce

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

Functioni

Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation.2 Publications

GO - Molecular functioni

  • unfolded protein binding Source: MGI

GO - Biological processi

  • adult locomotory behavior Source: MGI
  • axonogenesis Source: MGI
  • developmental growth Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • muscle atrophy Source: MGI
  • peripheral nervous system neuron axonogenesis Source: MGI
  • post-chaperonin tubulin folding pathway Source: UniProtKB
  • post-embryonic development Source: MGI
  • protein folding Source: MGI
  • tubulin complex assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-specific chaperone E
Alternative name(s):
Tubulin-folding cofactor E
Gene namesi
Name:Tbce
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1917680. Tbce.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 524523Tubulin-specific chaperone EPRO_0000083539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei460 – 4601N6-acetyllysineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CIV8.
MaxQBiQ8CIV8.
PaxDbiQ8CIV8.
PRIDEiQ8CIV8.

PTM databases

PhosphoSiteiQ8CIV8.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8CIV8.
CleanExiMM_TBCE.
ExpressionAtlasiQ8CIV8. baseline and differential.
GenevisibleiQ8CIV8. 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. Cofactors B and E can form a heterodimer which binds to alpha-tubulin and enhances their ability to dissociate tubulin heterodimers.1 Publication

GO - Molecular functioni

  • unfolded protein binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047880.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi442 – 45110Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi458 – 4636Combined sources
Helixi468 – 4769Combined sources
Turni477 – 4804Combined sources
Turni483 – 4853Combined sources
Beta strandi487 – 4915Combined sources
Beta strandi499 – 5013Combined sources
Beta strandi505 – 5095Combined sources
Helixi510 – 5123Combined sources
Beta strandi519 – 5235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJNNMR-A441-524[»]
ProteinModelPortaliQ8CIV8.
SMRiQ8CIV8. Positions 10-75, 116-367, 441-524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CIV8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 7145CAP-GlyPROSITE-ProRule annotationAdd
BLAST
Repeati154 – 17522LRR 1Add
BLAST
Repeati180 – 20122LRR 2Add
BLAST
Repeati206 – 22722LRR 3Add
BLAST
Repeati231 – 25323LRR 4Add
BLAST
Repeati254 – 27522LRR 5Add
BLAST
Repeati279 – 30022LRR 6Add
BLAST
Repeati309 – 33022LRR 7Add
BLAST
Domaini343 – 38139LRRCTAdd
BLAST

Sequence similaritiesi

Belongs to the TBCE family.Curated
Contains 1 CAP-Gly domain.PROSITE-ProRule annotation
Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ8CIV8.
OMAiVSLRNCA.
PhylomeDBiQ8CIV8.
TreeFamiTF313455.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
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]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF54236. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CIV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDILPLDVI GRRVEVNGEY ATVRFCGAVP PVAGLWLGVE WDNPERGKHD
60 70 80 90 100
GSHEGTMYFK CRHPTGGSFV RPSKVNFGDD FLTALKKRYV LEDGPDDDEN
110 120 130 140 150
SCSLKVGSKQ VQTIGFEHIT KKQSQLRALQ DISLWNCAVS HAGEQGRIAE
160 170 180 190 200
ACPNIRVVNL SKNLLSTWDE VVLIAEQLKD LEALDLSENK LQFPSDSPTL
210 220 230 240 250
TRTFSTLKTL VLNKTGITWT EVLHCAPSWP VLEELYLKSN NISISERPVN
260 270 280 290 300
VLQKMRLLDL SSNPSIDESQ LSLIADLPRL EHLVLSDIGL SSIHFPDAEI
310 320 330 340 350
GCKTSMFPAL KYLIVNDNQI SEWSFINELD KLQSLQALSC TRNPLSKADK
360 370 380 390 400
AEEIIIAKIA QLRTLNRCQI LPEERRGAEL DYRKAFGNEW RKAGGHPDPD
410 420 430 440 450
KNRPNAAFLS AHPRYQLLCC KYGAPEDEEL KTQQPFMLKK QLLTLKIKCS
460 470 480 490 500
NQPERQILEK QLPDSMTVQK VKGLLSRLLK VPVSELLLSY ESSKMPGREI
510 520
ELENDLQPLQ FYSVENGDCL LVRW
Length:524
Mass (Da):59,086
Last modified:March 1, 2003 - v1
Checksum:iE95280086D80FEF8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti348 – 3481A → V.1 Publication
Natural varianti524 – 5241W → G.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082332 mRNA. Translation: AAL92570.1.
AK167383 mRNA. Translation: BAE39475.1.
BC050206 mRNA. Translation: AAH50206.1.
CCDSiCCDS26247.1.
RefSeqiNP_848027.1. NM_178337.3.
UniGeneiMm.260209.

Genome annotation databases

EnsembliENSMUST00000039894; ENSMUSP00000047880; ENSMUSG00000039233.
GeneIDi70430.
KEGGimmu:70430.
UCSCiuc007pmq.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082332 mRNA. Translation: AAL92570.1.
AK167383 mRNA. Translation: BAE39475.1.
BC050206 mRNA. Translation: AAH50206.1.
CCDSiCCDS26247.1.
RefSeqiNP_848027.1. NM_178337.3.
UniGeneiMm.260209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJNNMR-A441-524[»]
ProteinModelPortaliQ8CIV8.
SMRiQ8CIV8. Positions 10-75, 116-367, 441-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047880.

PTM databases

PhosphoSiteiQ8CIV8.

Proteomic databases

EPDiQ8CIV8.
MaxQBiQ8CIV8.
PaxDbiQ8CIV8.
PRIDEiQ8CIV8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039894; ENSMUSP00000047880; ENSMUSG00000039233.
GeneIDi70430.
KEGGimmu:70430.
UCSCiuc007pmq.2. mouse.

Organism-specific databases

CTDi6905.
MGIiMGI:1917680. Tbce.

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ8CIV8.
OMAiVSLRNCA.
PhylomeDBiQ8CIV8.
TreeFamiTF313455.

Miscellaneous databases

EvolutionaryTraceiQ8CIV8.
PROiQ8CIV8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CIV8.
CleanExiMM_TBCE.
ExpressionAtlasiQ8CIV8. baseline and differential.
GenevisibleiQ8CIV8. MM.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
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]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF54236. 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. "A missense mutation in Tbce causes progressive motor neuronopathy in mice."
    Martin N., Jaubert J., Gounon P., Salido E., Haase G., Szatanik M., Guenet J.-L.
    Nat. Genet. 32:443-447(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS VAL-348 AND GLY-524.
    Strain: 129S2/SvPas.
  2. "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: Liver.
  3. "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: 129/Sv X 129/SvCp.
    Tissue: Embryonic stem cell.
  4. "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 TBCB.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Lung, Spleen and Testis.
  6. "Solution structure of the C-terminal ubiquitin-like domain."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: STRUCTURE BY NMR OF 441-524.

Entry informationi

Entry nameiTBCE_MOUSE
AccessioniPrimary (citable) accession number: Q8CIV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 118 of the entry and version 1 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.