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Protein

T-complex protein 1 subunit epsilon

Gene

Cct5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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-MMU-390471. Association of TriC/CCT with target proteins during biosynthesis.

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
Synonyms:Ccte, Kiaa0098
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:107185. Cct5.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • centrosome Source: MGI
  • chaperonin-containing T-complex Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • microtubule Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleolus Source: MGI
  • zona pellucida receptor complex Source: MGI
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_0000128347Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP80316.
MaxQBiP80316.
PaxDbiP80316.
PRIDEiP80316.

2D gel databases

REPRODUCTION-2DPAGEIPI00116279.
P80316.
SWISS-2DPAGEP80316.

PTM databases

iPTMnetiP80316.
PhosphoSiteiP80316.
SwissPalmiP80316.

Expressioni

Gene expression databases

BgeeiP80316.
CleanExiMM_CCT5.
ExpressionAtlasiP80316. baseline and differential.
GenevisibleiP80316. MM.

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 similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ThegQ9JMB12EBI-772379,EBI-1390549

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198568. 8 interactions.
IntActiP80316. 11 interactions.
MINTiMINT-1870041.
STRINGi10090.ENSMUSP00000022842.

Structurei

3D structure databases

ProteinModelPortaliP80316.
SMRiP80316. Positions 18-226, 376-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOVERGENiHBG106507.
InParanoidiP80316.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiP80316.
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.

P80316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT
60 70 80 90 100
SLGPNGLDKM MVDKDGDVTI TNDGATILSM MDVDHQIAKL MVELSKSQDD
110 120 130 140 150
EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARIAIQHLDK
160 170 180 190 200
ISDKVLVDIN NPEPLIQTAK TTLGSKVINS CHRQMAEIAV NAVLTVADME
210 220 230 240 250
RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KKVVDAKIAI
260 270 280 290 300
LTCPFEPPKP KTKHKLDVMS VEDYKALQKY EKEKFEEMIK QIKETGANLA
310 320 330 340 350
ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS
360 370 380 390 400
EKLGFAGVVQ EISFGTTKDK MLVIEKCKNS 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):59,624
Last modified:June 1, 1994 - v1
Checksum:iE05316785ADB7612
GO

Sequence cautioni

The sequence BAC97866.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271R → H in BAE23007 (PubMed:16141072).Curated
Sequence conflicti48 – 481M → I in BAE27146 (PubMed:16141072).Curated
Sequence conflicti74 – 741G → D in BAE32250 (PubMed:16141072).Curated
Sequence conflicti125 – 1251D → E in BAE27146 (PubMed:16141072).Curated
Sequence conflicti191 – 1911N → D in BAE39906 (PubMed:16141072).Curated
Sequence conflicti493 – 4931C → Y in BAE29518 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31555 mRNA. Translation: CAA83430.1.
AB022158 Genomic DNA. Translation: BAA81876.1.
AK129056 mRNA. Translation: BAC97866.1. Different initiation.
AK088184 mRNA. Translation: BAC40194.1.
AK133857 mRNA. Translation: BAE21891.1.
AK136493 mRNA. Translation: BAE23007.1.
AK145445 mRNA. Translation: BAE26441.1.
AK146405 mRNA. Translation: BAE27146.1.
AK146425 mRNA. Translation: BAE27159.1.
AK150390 mRNA. Translation: BAE29518.1.
AK153911 mRNA. Translation: BAE32250.1.
AK167895 mRNA. Translation: BAE39906.1.
BC094427 mRNA. Translation: AAH94427.1.
CCDSiCCDS27411.1.
PIRiS43061.
RefSeqiNP_031663.1. NM_007637.2.
UniGeneiMm.282158.

Genome annotation databases

EnsembliENSMUST00000022842; ENSMUSP00000022842; ENSMUSG00000022234.
GeneIDi12465.
KEGGimmu:12465.
UCSCiuc007vkj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31555 mRNA. Translation: CAA83430.1.
AB022158 Genomic DNA. Translation: BAA81876.1.
AK129056 mRNA. Translation: BAC97866.1. Different initiation.
AK088184 mRNA. Translation: BAC40194.1.
AK133857 mRNA. Translation: BAE21891.1.
AK136493 mRNA. Translation: BAE23007.1.
AK145445 mRNA. Translation: BAE26441.1.
AK146405 mRNA. Translation: BAE27146.1.
AK146425 mRNA. Translation: BAE27159.1.
AK150390 mRNA. Translation: BAE29518.1.
AK153911 mRNA. Translation: BAE32250.1.
AK167895 mRNA. Translation: BAE39906.1.
BC094427 mRNA. Translation: AAH94427.1.
CCDSiCCDS27411.1.
PIRiS43061.
RefSeqiNP_031663.1. NM_007637.2.
UniGeneiMm.282158.

3D structure databases

ProteinModelPortaliP80316.
SMRiP80316. Positions 18-226, 376-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198568. 8 interactions.
IntActiP80316. 11 interactions.
MINTiMINT-1870041.
STRINGi10090.ENSMUSP00000022842.

PTM databases

iPTMnetiP80316.
PhosphoSiteiP80316.
SwissPalmiP80316.

2D gel databases

REPRODUCTION-2DPAGEIPI00116279.
P80316.
SWISS-2DPAGEP80316.

Proteomic databases

EPDiP80316.
MaxQBiP80316.
PaxDbiP80316.
PRIDEiP80316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022842; ENSMUSP00000022842; ENSMUSG00000022234.
GeneIDi12465.
KEGGimmu:12465.
UCSCiuc007vkj.1. mouse.

Organism-specific databases

CTDi22948.
MGIiMGI:107185. Cct5.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0357. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074988.
HOVERGENiHBG106507.
InParanoidiP80316.
KOiK09497.
OMAiVDHEIAK.
OrthoDBiEOG722J8B.
PhylomeDBiP80316.
TreeFamiTF105638.

Enzyme and pathway databases

ReactomeiR-MMU-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

ChiTaRSiCct5. mouse.
NextBioi281334.
PROiP80316.
SOURCEiSearch...

Gene expression databases

BgeeiP80316.
CleanExiMM_CCT5.
ExpressionAtlasiP80316. baseline and differential.
GenevisibleiP80316. MM.

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. "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin."
    Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.
    Curr. Biol. 4:89-99(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
  2. "Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits."
    Kubota H., Yokota S., Yanagi H., Yura T.
    Eur. J. Biochem. 262:492-500(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J, DBA/2J and NOD.
    Tissue: Bone marrow, Colon and Thymus.
  5. "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].
    Strain: C57BL/6J.
    Tissue: Eye.
  6. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 28-35; 50-59; 203-210; 248-261; 264-275; 324-340; 353-368; 382-388 AND 497-513, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. Cited for: INTERACTION WITH DYX1C1.

Entry informationi

Entry nameiTCPE_MOUSE
AccessioniPrimary (citable) accession number: P80316
Secondary accession number(s): Q3TIE0
, Q3U530, Q3UCU4, Q3UJK9, Q3UWA9, Q542K3, Q6ZQJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 13, 2016
This is version 140 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.