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Protein

Tubulin-specific chaperone E

Gene

TBCE

Organism
Bos taurus (Bovine)
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

Enzyme and pathway databases

ReactomeiR-BTA-389977. Post-chaperonin tubulin folding pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-specific chaperone E
Alternative name(s):
Tubulin-folding cofactor E
Gene namesi
Name:TBCE
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 28

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 – 528527Tubulin-specific chaperone EPRO_0000083537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei464 – 4641N6-acetyllysineBy similarity
Modified residuei496 – 4961PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ32KS0.
PRIDEiQ32KS0.

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

STRINGi9913.ENSBTAP00000018249.

Structurei

3D structure databases

ProteinModelPortaliQ32KS0.
SMRiQ32KS0. Positions 445-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 7145CAP-GlyPROSITE-ProRule annotationAdd
BLAST
Repeati152 – 17625LRR 1Add
BLAST
Repeati178 – 20629LRR 2Add
BLAST
Repeati207 – 22923LRR 3Add
BLAST
Repeati231 – 25323LRR 4Add
BLAST
Repeati254 – 27421LRR 5Add
BLAST
Repeati279 – 30022LRR 6Add
BLAST
Repeati309 – 33022LRR 7Add
BLAST
Domaini343 – 38543LRRCTAdd
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.
InParanoidiQ32KS0.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
TreeFamiTF313455.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
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.
PS51450. LRR. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q32KS0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSTSTSDVI GRRVEVNGEH ATVRFSGLVP PVAGLWLGVE WDNPERGKHD
60 70 80 90 100
GSHEGTVYFK CRHPTAGSFI RPHKVNFGVD FLTAIKNRYV LEDEPKEEET
110 120 130 140 150
EQIVIIGNKP VETIGFDSVI KQQSQLSKLQ DVSLRNCAVN GAGDKGEIAK
160 170 180 190 200
ACPNIRSIDL SKNLLSSWEE VIDIADQLKH LEVLNLSENK LTSPSSSPSP
210 220 230 240 250
TGTFPTLKVL VLNRTGVTWA EVLRCASGWP VLEKLYLESN NIIISERPTD
260 270 280 290 300
VLQTVKLLDL SSNQLIDENQ LFLIAYLPRL EQLILSDIGI SSIHFPDAGI
310 320 330 340 350
GCKTSMFPSL QYLVLNDNQI AQWSFMNELD KLQSLHALSC TRNPLTEGSK
360 370 380 390 400
DAQTTRQFII ARIGQLRTLN KCAIEPEERR GAELDYRKAF GNEWKKAGGH
410 420 430 440 450
QDPEKNRPNE EFLAAHPRYQ ALCLKYGAPE DGELKTQQPF LLKNQLLTLK
460 470 480 490 500
IKYPNQHDQK VIEKQLPDSM TVQKVKGLLS RLLKVPVSEL LLSYESPKMP
510 520
GKEVELENDL QPLRFYSVEN GDCLLVRW
Length:528
Mass (Da):59,327
Last modified:December 6, 2005 - v1
Checksum:i494FCF1A4F3A1C86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431I → V in ABG66995 (PubMed:16305752).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT026156 mRNA. Translation: ABG66995.1.
BC109955 mRNA. Translation: AAI09956.1.
RefSeqiNP_001033121.1. NM_001038032.2.
XP_005226263.1. XM_005226206.3.
XP_015316413.1. XM_015460927.1.
UniGeneiBt.3254.

Genome annotation databases

EnsembliENSBTAT00000018249; ENSBTAP00000018249; ENSBTAG00000013735.
GeneIDi505066.
KEGGibta:505066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT026156 mRNA. Translation: ABG66995.1.
BC109955 mRNA. Translation: AAI09956.1.
RefSeqiNP_001033121.1. NM_001038032.2.
XP_005226263.1. XM_005226206.3.
XP_015316413.1. XM_015460927.1.
UniGeneiBt.3254.

3D structure databases

ProteinModelPortaliQ32KS0.
SMRiQ32KS0. Positions 445-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018249.

Proteomic databases

PaxDbiQ32KS0.
PRIDEiQ32KS0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018249; ENSBTAP00000018249; ENSBTAG00000013735.
GeneIDi505066.
KEGGibta:505066.

Organism-specific databases

CTDi6905.

Phylogenomic databases

eggNOGiKOG3207. Eukaryota.
ENOG410YS3M. LUCA.
GeneTreeiENSGT00530000063405.
HOGENOMiHOG000154513.
HOVERGENiHBG084170.
InParanoidiQ32KS0.
OMAiVSLRNCA.
OrthoDBiEOG7T1RB1.
TreeFamiTF313455.

Enzyme and pathway databases

ReactomeiR-BTA-389977. Post-chaperonin tubulin folding pathway.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
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.
PS51450. LRR. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.

Entry informationi

Entry nameiTBCE_BOVIN
AccessioniPrimary (citable) accession number: Q32KS0
Secondary accession number(s): Q0V8R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 86 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.