Human Gene TBCE (uc001hxa.1) Description and Page Index
  Description: Homo sapiens tubulin folding cofactor E (TBCE), transcript variant 1, mRNA.
RefSeq Summary (NM_001079515): Cofactor E is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].
Transcript (Including UTRs)
   Position: hg19 chr1:235,530,728-235,612,280 Size: 81,553 Total Exon Count: 17 Strand: +
Coding Region
   Position: hg19 chr1:235,543,365-235,612,077 Size: 68,713 Coding Exon Count: 16 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr1:235,530,728-235,612,280)mRNA (may differ from genome)Protein (527 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards
GeneNetworkH-INVHGNCHPRDLynxMGI
neXtProtOMIMPubMedReactomeStanford SOURCEUniProtKB
Wikipedia

-  Comments and Description Text from UniProtKB
  ID: TBCE_HUMAN
DESCRIPTION: RecName: Full=Tubulin-specific chaperone E; AltName: Full=Tubulin-folding cofactor E;
FUNCTION: 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.
SUBUNIT: 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.
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, cytoskeleton (By similarity).
DISEASE: Defects in TBCE are a cause of hypoparathyroidism- retardation-dysmorphism syndrome (HRD) [MIM:241410]; also known as hypoparathyroidism with short stature, mental retardation, and seizures or Sanjad-Sakati syndrome. HRD is an autosomal recessive disorder reported almost exclusively in Middle Eastern populations.
DISEASE: Defects in TBCE are the cause of Kenny-Caffey syndrome type 1 (KCS1) [MIM:244460]. KCS1 is similar to HRD with the additional features of osteosclerosis and recurrent bacterial infections.
SIMILARITY: Belongs to the TBCE family.
SIMILARITY: Contains 1 CAP-Gly domain.
SIMILARITY: Contains 7 LRR (leucine-rich) repeats.
SIMILARITY: Contains 1 LRRCT domain.

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): TBCE
CDC HuGE Published Literature: TBCE
Positive Disease Associations: adiposity
Related Studies:
  1. adiposity
    Lindgren ,et al. 2009, Genome-Wide Association Scan Meta-Analysis Identifies Three Loci Influencing Adiposity and Fat Distribution, PLoS genetics 2009 5- 6 : e1000508. [PubMed 19557161]
  2. Adiposity
    Cecilia M Lindgren et al. PLoS genetics 2009, Genome-wide association scan meta-analysis identifies three Loci influencing adiposity and fat distribution., PLoS genetics. [PubMed 19557161]

-  MalaCards Disease Associations
  MalaCards Gene Search: TBCE
Diseases sorted by gene-association score: hypoparathyroidism-retardation-dysmorphism syndrome* (1400), kenny-caffey syndrome, type 1* (1368), encephalopathy, progressive, with amyotrophy and optic atrophy* (1230), kenny-caffey syndrome (29), hypoparathyroidism (28), pseudopapilledema (16), sakati syndrome (13), branch retinal artery occlusion (9), band keratopathy (7), central retinal artery occlusion (5), spinal muscular atrophy (3), retinitis pigmentosa (1)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 14.93 RPKM in Thyroid
Total median expression: 445.87 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -65.10171-0.381 Picture PostScript Text
3' UTR -36.10203-0.178 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000938 - CAP-Gly_domain

Pfam Domains:
PF01302 - CAP-Gly domain
PF14560 - Ubiquitin-like domain

SCOP Domains:
74924 - Cap-Gly domain
52047 - RNI-like
52058 - L domain-like
52075 - Outer arm dynein light chain 1
54236 - Ubiquitin-like

ModBase Predicted Comparative 3D Structure on Q15813
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologGenome BrowserGenome BrowserGenome BrowserGenome BrowserGenome Browser
Gene DetailsGene Details Gene DetailsGene DetailsGene Details
Gene SorterGene Sorter Gene SorterGene SorterGene Sorter
 RGDEnsemblFlyBaseWormBaseSGD
 Protein SequenceProtein SequenceProtein SequenceProtein SequenceProtein Sequence
 AlignmentAlignmentAlignmentAlignmentAlignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0005515 protein binding
GO:0051087 chaperone binding

Biological Process:
GO:0000226 microtubule cytoskeleton organization
GO:0006457 protein folding
GO:0007023 post-chaperonin tubulin folding pathway
GO:0007052 mitotic spindle organization

Cellular Component:
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005874 microtubule


-  Descriptions from all associated GenBank mRNAs
  AK296185 - Homo sapiens cDNA FLJ59210 complete cds, highly similar to Tubulin-specific chaperone E.
AK298050 - Homo sapiens cDNA FLJ57032 complete cds, moderately similar to Tubulin-specific chaperone E.
AK292287 - Homo sapiens cDNA FLJ76932 complete cds, highly similar to Homo sapiens tubulin-specific chaperone e (TBCE), mRNA.
AK093397 - Homo sapiens cDNA FLJ36078 fis, clone TESTI2019859, highly similar to Human tubulin-folding cofactor E mRNA.
U61232 - Homo sapiens cofactor E mRNA, complete cds.
BC008654 - Homo sapiens tubulin folding cofactor E, mRNA (cDNA clone MGC:8912 IMAGE:3872809), complete cds.
JD026018 - Sequence 7042 from Patent EP1572962.
CU679015 - Synthetic construct Homo sapiens gateway clone IMAGE:100019779 5' read TBCE mRNA.
BT007086 - Homo sapiens tubulin-specific chaperone e mRNA, complete cds.
JF432206 - Synthetic construct Homo sapiens clone IMAGE:100073370 tubulin folding cofactor E (TBCE) gene, encodes complete protein.
KJ897640 - Synthetic construct Homo sapiens clone ccsbBroadEn_07034 TBCE gene, encodes complete protein.
JD033255 - Sequence 14279 from Patent EP1572962.
JD022480 - Sequence 3504 from Patent EP1572962.
JD028231 - Sequence 9255 from Patent EP1572962.
JD363598 - Sequence 344622 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q15813 (Reactome details) participates in the following event(s):

R-HSA-389963 alpha-tubulin:GTP:Cofactor B +Cofactor E -> alpha-tubulin:GTP: Cofactor E +Cofactor B
R-HSA-389978 alpha-tubulin:GTP + Cofactor E -> alpha-tubulin:GTP:Cofactor E
R-HSA-389974 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C-> Beta-tubulin:GDP :alpha-tubulin:GTP heterodimer +Cofactor E+ Cofactor D+ Cofactor C+ Pi
R-HSA-389976 Beta-tubulin:GTP:Cofactor D+alpha-tubulin:GTP:Cofactor E-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E
R-HSA-389964 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E+ Cofactor C-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-391251 Protein folding
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: NM_001079515, NP_003184, Q15813, TBCE_HUMAN
UCSC ID: uc001hxa.1
RefSeq Accession: NM_001079515
Protein: Q15813 (aka TBCE_HUMAN)
CCDS: CCDS1605.1

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_001079515.1
exon count: 17CDS single in 3' UTR: no RNA size: 1973
ORF size: 1584CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 3368.00frame shift in genome: no % Coverage: 99.24
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.