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Protein

Tubulin-specific chaperone E

Gene

Tbce

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Biological processi

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1305533. 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_0000083541Add
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

PaxDbiQ5FVQ9.
PRIDEiQ5FVQ9.

PTM databases

iPTMnetiQ5FVQ9.
PhosphoSiteiQ5FVQ9.

Expressioni

Gene expression databases

ExpressionAtlasiQ5FVQ9. baseline.
GenevisibleiQ5FVQ9. RN.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000042689.

Structurei

3D structure databases

ProteinModelPortaliQ5FVQ9.
SMRiQ5FVQ9. Positions 441-524.
ModBaseiSearch...
MobiDBiSearch...

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 – 27320LRR 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.
InParanoidiQ5FVQ9.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
PhylomeDBiQ5FVQ9.
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.

Q5FVQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDILPLDVI GRRVEVNGEY ATVRFCGAVP PVAGLWLGVE WDNPERGKHD
60 70 80 90 100
GSHEGTMYFK CRHPTGGSFV RPNIVNFGED FLTALKKRYV LTDGPDDDEK
110 120 130 140 150
SCSLKVGSKQ VQTIGFEHIT KKQSQLRSLQ DISLWKCAVS CAGERGRIAE
160 170 180 190 200
ACPNIRVVDL SKNLLSTWDE VILIAEQLKD LEALDLSENK LQFPSDSPTL
210 220 230 240 250
TRTFSTLKTL VLNKTGITWT EVLHCAPSWP VLQELYLKSN GISISERPVN
260 270 280 290 300
ALQNLRLLDL SSNPSIDESQ LCLIAYLPRL EHLLLSDIGL SSIHFPDAEI
310 320 330 340 350
GCKTSMFPAL TYLIVNDNQI SEWSFINELD KLQSLQALSC ARNPLTKGDK
360 370 380 390 400
AEEIIIAKIG QLKTLNRCQI LPEERRGAEL DYRKAFGKEW RKAGGHPDPD
410 420 430 440 450
RNRPSAEFLS AHPRYQLLCC KYGAPEDEEL KTQQPFMLKN QLLTLKIKCS
460 470 480 490 500
NQPEQQILEK QLPDSMTIQK VKGLLSRLLK VPVSELLLSY ESSKMPGREI
510 520
ELENDLQPLQ FYSVENGDCL LVRW
Length:524
Mass (Da):59,043
Last modified:March 1, 2005 - v1
Checksum:i865358549B0B9404
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089833 mRNA. Translation: AAH89833.1.
RefSeqiNP_001012161.1. NM_001012161.1.
UniGeneiRn.3547.

Genome annotation databases

EnsembliENSRNOT00000040743; ENSRNOP00000042689; ENSRNOG00000029667.
GeneIDi361255.
KEGGirno:361255.
UCSCiRGD:1305533. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089833 mRNA. Translation: AAH89833.1.
RefSeqiNP_001012161.1. NM_001012161.1.
UniGeneiRn.3547.

3D structure databases

ProteinModelPortaliQ5FVQ9.
SMRiQ5FVQ9. Positions 441-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000042689.

PTM databases

iPTMnetiQ5FVQ9.
PhosphoSiteiQ5FVQ9.

Proteomic databases

PaxDbiQ5FVQ9.
PRIDEiQ5FVQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000040743; ENSRNOP00000042689; ENSRNOG00000029667.
GeneIDi361255.
KEGGirno:361255.
UCSCiRGD:1305533. rat.

Organism-specific databases

CTDi6905.
RGDi1305533. Tbce.

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ5FVQ9.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
PhylomeDBiQ5FVQ9.
TreeFamiTF313455.

Miscellaneous databases

PROiQ5FVQ9.

Gene expression databases

ExpressionAtlasiQ5FVQ9. baseline.
GenevisibleiQ5FVQ9. RN.

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

  1. "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].
    Tissue: Liver.

Entry informationi

Entry nameiTBCE_RAT
AccessioniPrimary (citable) accession number: Q5FVQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2005
Last modified: June 8, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. 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.