Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit epsilon

Gene

Cct5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit epsilon
Short name:
TCP-1-epsilon
Alternative name(s):
CCT-epsilon
Gene namesi
Name:Cct5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi735161. Cct5.

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 – 541540T-complex protein 1 subunit epsilonPRO_0000271396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei539 – 5391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ68FQ0.
PRIDEiQ68FQ0.

2D gel databases

World-2DPAGE0004:Q68FQ0.

PTM databases

iPTMnetiQ68FQ0.

Expressioni

Gene expression databases

GenevisibleiQ68FQ0. RN.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (By similarity). Interacts with DYX1C1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi254817. 1 interaction.
IntActiQ68FQ0. 3 interactions.
MINTiMINT-4575257.
STRINGi10116.ENSRNOP00000015886.

Structurei

3D structure databases

ProteinModelPortaliQ68FQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
HOVERGENiHBG106507.
InParanoidiQ68FQ0.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiQ68FQ0.
TreeFamiTF105638.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q68FQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT
60 70 80 90 100
SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD
110 120 130 140 150
EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARIAIQHLDK
160 170 180 190 200
ISDNVLVDIN NPEPLIQTAK TTLGSKVVNS CHRQMAEIAV NAVLTVADME
210 220 230 240 250
RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KEVLNAKIAI
260 270 280 290 300
LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIA QIKETGANLA
310 320 330 340 350
ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS
360 370 380 390 400
EKLGFAGVVR EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR
410 420 430 440 450
SLHDALCVIR NLIRDNRVVY GGGAAEISCA LAVSQEADKC PTLEQYAMRA
460 470 480 490 500
FADALEVIPM ALSENSGMNP IQTMTEVRAR QVKESNPALG IDCLHKGSND
510 520 530 540
MQYQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E
Length:541
Mass (Da):59,537
Last modified:October 11, 2004 - v1
Checksum:iB19EFC616DB63C7E
GO

Sequence cautioni

The sequence AAH59165.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC059165 mRNA. Translation: AAH59165.1. Sequence problems.
BC079441 mRNA. Translation: AAH79441.1.
RefSeqiNP_001004078.1. NM_001004078.1.
UniGeneiRn.92645.

Genome annotation databases

EnsembliENSRNOT00000015886; ENSRNOP00000015886; ENSRNOG00000011632.
GeneIDi294864.
KEGGirno:294864.
UCSCiRGD:735161. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC059165 mRNA. Translation: AAH59165.1. Sequence problems.
BC079441 mRNA. Translation: AAH79441.1.
RefSeqiNP_001004078.1. NM_001004078.1.
UniGeneiRn.92645.

3D structure databases

ProteinModelPortaliQ68FQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi254817. 1 interaction.
IntActiQ68FQ0. 3 interactions.
MINTiMINT-4575257.
STRINGi10116.ENSRNOP00000015886.

PTM databases

iPTMnetiQ68FQ0.

2D gel databases

World-2DPAGE0004:Q68FQ0.

Proteomic databases

PaxDbiQ68FQ0.
PRIDEiQ68FQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015886; ENSRNOP00000015886; ENSRNOG00000011632.
GeneIDi294864.
KEGGirno:294864.
UCSCiRGD:735161. rat.

Organism-specific databases

CTDi22948.
RGDi735161. Cct5.

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOGENOMiHOG000226735.
HOVERGENiHBG106507.
InParanoidiQ68FQ0.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiQ68FQ0.
TreeFamiTF105638.

Enzyme and pathway databases

ReactomeiR-RNO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

PROiQ68FQ0.

Gene expression databases

GenevisibleiQ68FQ0. RN.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012718. Chap_CCT_epsi.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02343. chap_CCT_epsi. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Pituitary and Testis.
  2. Lubec G., Afjehi-Sadat L., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 248-261 AND 324-340, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiTCPE_RAT
AccessioniPrimary (citable) accession number: Q68FQ0
Secondary accession number(s): Q6PCT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 100 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, Direct protein sequencing, 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.