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Protein

Tubulin-specific chaperone C

Gene

TBCC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin-folding protein; involved in the final step of the tubulin folding pathway.1 Publication

GO - Molecular functioni

  • chaperone binding Source: ProtInc
  • GTPase activity Source: UniProtKB

GO - Biological processi

  • cell morphogenesis Source: InterPro
  • post-chaperonin tubulin folding pathway Source: UniProtKB
  • protein folding Source: UniProtKB
  • tubulin complex assembly Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124659-MONOMER.
ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-specific chaperone C
Alternative name(s):
Tubulin-folding cofactor C
Short name:
CFC
Gene namesi
Name:TBCC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11580. TBCC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: ProtInc
  • microtubule Source: ProtInc
  • photoreceptor connecting cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi262R → A: Inhibits stimulation of tubulin GTPase activity. 1 Publication1

Organism-specific databases

DisGeNETi6903.
OpenTargetsiENSG00000124659.
PharmGKBiPA36344.

Polymorphism and mutation databases

BioMutaiTBCC.
DMDMi313104020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000800461 – 346Tubulin-specific chaperone CAdd BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei80PhosphoserineCombined sources1
Modified residuei168PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15814.
MaxQBiQ15814.
PaxDbiQ15814.
PeptideAtlasiQ15814.
PRIDEiQ15814.

PTM databases

iPTMnetiQ15814.
PhosphoSitePlusiQ15814.

Expressioni

Tissue specificityi

Expressed in the retina. Expressed in the rod and cone photoreceptors, extending from the inner segments (IS), through the outer nuclear layer (ONL) and into the synapses in the outer plexiform layer (OPL). Strongly expressed to the photoreceptor connecting cilium at the tips of the IS (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000124659.
CleanExiHS_TBCC.
GenevisibleiQ15814. HS.

Organism-specific databases

HPAiHPA035073.
HPA035074.

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.

GO - Molecular functioni

  • chaperone binding Source: ProtInc

Protein-protein interaction databases

BioGridi112766. 2 interactors.
DIPiDIP-46388N.
STRINGi9606.ENSP00000244625.

Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 37Combined sources6
Helixi40 – 43Combined sources4
Helixi49 – 55Combined sources7
Helixi56 – 77Combined sources22
Helixi81 – 100Combined sources20
Turni102 – 104Combined sources3
Helixi107 – 131Combined sources25
Beta strandi183 – 185Combined sources3
Beta strandi193 – 196Combined sources4
Helixi198 – 201Combined sources4
Beta strandi205 – 208Combined sources4
Beta strandi215 – 218Combined sources4
Beta strandi225 – 229Combined sources5
Beta strandi234 – 236Combined sources3
Beta strandi244 – 248Combined sources5
Beta strandi253 – 255Combined sources3
Beta strandi259 – 265Combined sources7
Beta strandi270 – 272Combined sources3
Beta strandi276 – 283Combined sources8
Beta strandi285 – 290Combined sources6
Helixi300 – 306Combined sources7
Beta strandi338 – 340Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L3LNMR-A26-135[»]
2YUHNMR-A181-346[»]
ProteinModelPortaliQ15814.
SMRiQ15814.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 323C-CAP/cofactor C-likePROSITE-ProRule annotationAdd BLAST153

Sequence similaritiesi

Belongs to the TBCC family.Curated
Contains 1 C-CAP/cofactor C-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2512. Eukaryota.
ENOG410Y28B. LUCA.
GeneTreeiENSGT00530000063741.
HOGENOMiHOG000030935.
HOVERGENiHBG017893.
InParanoidiQ15814.
OMAiEKSDFFA.
OrthoDBiEOG091G0K00.
PhylomeDBiQ15814.
TreeFamiTF105832.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR006599. CARP_motif.
IPR027684. TBCC.
IPR031925. TBCC_N.
IPR012945. Tubulin-bd_cofactor_C_dom.
[Graphical view]
PANTHERiPTHR15139. PTHR15139. 1 hit.
PfamiPF07986. TBCC. 1 hit.
PF16752. TBCC_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESVSCSAAA VRTGDMESQR DLSLVPERLQ RREQERQLEV ERRKQKRQNQ
60 70 80 90 100
EVEKENSHFF VATFVRERAA VEELLERAES VERLEEAASR LQGLQKLIND
110 120 130 140 150
SVFFLAAYDL RQGQEALARL QAALAERRRG LQPKKRFAFK TRGKDAASST
160 170 180 190 200
KVDAAPGIPP AVESIQDSPL PKKAEGDLGP SWVCGFSNLE SQVLEKRASE
210 220 230 240 250
LHQRDVLLTE LSNCTVRLYG NPNTLRLTKA HSCKLLCGPV STSVFLEDCS
260 270 280 290 300
DCVLAVACQQ LRIHSTKDTR IFLQVTSRAI VEDCSGIQFA PYTWSYPEID
310 320 330 340
KDFESSGLDR SKNNWNDVDD FNWLARDMAS PNWSILPEEE RNIQWD
Length:346
Mass (Da):39,248
Last modified:November 30, 2010 - v2
Checksum:i32732BB3411FCD20
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02682265V → A.4 PublicationsCorresponds to variant rs2234026dbSNPEnsembl.1
Natural variantiVAR_06742386E → D.1 PublicationCorresponds to variant rs144361927dbSNPEnsembl.1
Natural variantiVAR_026823157G → D.Corresponds to variant rs7742995dbSNPEnsembl.1
Natural variantiVAR_020448169P → S.Corresponds to variant rs2234027dbSNPEnsembl.1
Natural variantiVAR_024653180P → S.Corresponds to variant rs2234028dbSNPEnsembl.1
Natural variantiVAR_026824279A → T.Corresponds to variant rs12175072dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61234 mRNA. Translation: AAB17539.1.
BT007002 mRNA. Translation: AAP35648.1.
AK312681 mRNA. Translation: BAG35561.1.
AL353716 Genomic DNA. Translation: CAI14818.1.
BC017479 mRNA. Translation: AAH17479.1.
BC020170 mRNA. Translation: AAH20170.1.
CCDSiCCDS4872.1.
RefSeqiNP_003183.1. NM_003192.2.
UniGeneiHs.75064.

Genome annotation databases

EnsembliENST00000372876; ENSP00000361967; ENSG00000124659.
GeneIDi6903.
KEGGihsa:6903.
UCSCiuc003osl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61234 mRNA. Translation: AAB17539.1.
BT007002 mRNA. Translation: AAP35648.1.
AK312681 mRNA. Translation: BAG35561.1.
AL353716 Genomic DNA. Translation: CAI14818.1.
BC017479 mRNA. Translation: AAH17479.1.
BC020170 mRNA. Translation: AAH20170.1.
CCDSiCCDS4872.1.
RefSeqiNP_003183.1. NM_003192.2.
UniGeneiHs.75064.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L3LNMR-A26-135[»]
2YUHNMR-A181-346[»]
ProteinModelPortaliQ15814.
SMRiQ15814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112766. 2 interactors.
DIPiDIP-46388N.
STRINGi9606.ENSP00000244625.

PTM databases

iPTMnetiQ15814.
PhosphoSitePlusiQ15814.

Polymorphism and mutation databases

BioMutaiTBCC.
DMDMi313104020.

Proteomic databases

EPDiQ15814.
MaxQBiQ15814.
PaxDbiQ15814.
PeptideAtlasiQ15814.
PRIDEiQ15814.

Protocols and materials databases

DNASUi6903.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372876; ENSP00000361967; ENSG00000124659.
GeneIDi6903.
KEGGihsa:6903.
UCSCiuc003osl.4. human.

Organism-specific databases

CTDi6903.
DisGeNETi6903.
GeneCardsiTBCC.
HGNCiHGNC:11580. TBCC.
HPAiHPA035073.
HPA035074.
MIMi602971. gene.
neXtProtiNX_Q15814.
OpenTargetsiENSG00000124659.
PharmGKBiPA36344.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2512. Eukaryota.
ENOG410Y28B. LUCA.
GeneTreeiENSGT00530000063741.
HOGENOMiHOG000030935.
HOVERGENiHBG017893.
InParanoidiQ15814.
OMAiEKSDFFA.
OrthoDBiEOG091G0K00.
PhylomeDBiQ15814.
TreeFamiTF105832.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124659-MONOMER.
ReactomeiR-HSA-389977. Post-chaperonin tubulin folding pathway.

Miscellaneous databases

ChiTaRSiTBCC. human.
EvolutionaryTraceiQ15814.
GenomeRNAii6903.
PROiQ15814.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124659.
CleanExiHS_TBCC.
GenevisibleiQ15814. HS.

Family and domain databases

Gene3Di2.160.20.70. 1 hit.
InterProiIPR017901. C-CAP_CF_C-like.
IPR016098. CAP/MinC_C.
IPR006599. CARP_motif.
IPR027684. TBCC.
IPR031925. TBCC_N.
IPR012945. Tubulin-bd_cofactor_C_dom.
[Graphical view]
PANTHERiPTHR15139. PTHR15139. 1 hit.
PfamiPF07986. TBCC. 1 hit.
PF16752. TBCC_N. 1 hit.
[Graphical view]
SMARTiSM00673. CARP. 2 hits.
[Graphical view]
PROSITEiPS51329. C_CAP_COFACTOR_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBCC_HUMAN
AccessioniPrimary (citable) accession number: Q15814
Secondary accession number(s): Q53Y43, Q5T787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 30, 2010
Last modified: November 2, 2016
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.