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Protein

Probable T-complex protein 1 subunit eta

Gene

cct7

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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. 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-SPO-390471. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable T-complex protein 1 subunit eta
Short name:
TCP-1-eta
Alternative name(s):
CCT-eta
Gene namesi
Name:cct7
ORF Names:SPBC25H2.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC25H2.12c.
PomBaseiSPBC25H2.12c. cct7.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: PomBase
  • cytoplasm Source: PomBase
  • cytoskeleton Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Probable T-complex protein 1 subunit etaPRO_0000128371Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP87153.

PTM databases

iPTMnetiP87153.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi277099. 1 interaction.
IntActiP87153. 1 interaction.
MINTiMINT-4692653.

Structurei

3D structure databases

ProteinModelPortaliP87153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

HOGENOMiHOG000226730.
InParanoidiP87153.
KOiK09499.
OMAiIANNMER.
OrthoDBiEOG773XR5.
PhylomeDBiP87153.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
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]
PANTHERiPTHR11353:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P87153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLGGPQIPV IVLKEGTDDS QGRGQLLSNI NACVAVQDTI RTTLGPLGAD
60 70 80 90 100
KLMVDDRGEV VISNDGATIM KLLDIVHPAA KTLVDIARAQ DAEVGDGTTS
110 120 130 140 150
VVVFAGELLR EARTFVEDGV SSHLIIRGYR KAAQLAVNKI KEIAIHLDLS
160 170 180 190 200
DEGKLRDLLT KCASTAMNSK LIRSNSTFFT KMVVDAVLTL DQEDLNENMI
210 220 230 240 250
GIKKVPGGAM EDSLLVKGVA FKKTFSYAGF EQQPKFFKNP KILCLDVELE
260 270 280 290 300
LKAEKDNAEV RVDKVQEYQN IVDAEWRIIF SKLEAIVATG AKVVLSKLPI
310 320 330 340 350
GDLATQYFAD RDIFCAGRVA ADDLNRVVQA VGGSIQSTCS NIEEKHLGTC
360 370 380 390 400
DTFEERQIGG DRFNLFEGCP KAKTCTLILR GGADQFIAEV ERSLHDAIMI
410 420 430 440 450
VKHALKNNLV VAGGGACEME LSKYLRDYSL TISGKQQNFI AAFARSLEVI
460 470 480 490 500
PRQLCDNAGF DSTNILNKLR MQHAKGEMWA GVDMDSEGVA NNFEKFVWEP
510 520 530 540 550
STVKSNAILS ATEAATLILS VDETIKNEPS QQPQAPQGAL PPGAANRIMR

GRGRGMPR
Length:558
Mass (Da):60,687
Last modified:July 1, 1997 - v1
Checksum:iC4C1F843F44C5253
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB08778.1.
PIRiT40007.
RefSeqiNP_596355.1. NM_001022275.2.

Genome annotation databases

EnsemblFungiiSPBC25H2.12c.1; SPBC25H2.12c.1:pep; SPBC25H2.12c.
GeneIDi2540572.
KEGGispo:SPBC25H2.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB08778.1.
PIRiT40007.
RefSeqiNP_596355.1. NM_001022275.2.

3D structure databases

ProteinModelPortaliP87153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277099. 1 interaction.
IntActiP87153. 1 interaction.
MINTiMINT-4692653.

PTM databases

iPTMnetiP87153.

Proteomic databases

MaxQBiP87153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC25H2.12c.1; SPBC25H2.12c.1:pep; SPBC25H2.12c.
GeneIDi2540572.
KEGGispo:SPBC25H2.12c.

Organism-specific databases

EuPathDBiFungiDB:SPBC25H2.12c.
PomBaseiSPBC25H2.12c. cct7.

Phylogenomic databases

HOGENOMiHOG000226730.
InParanoidiP87153.
KOiK09499.
OMAiIANNMER.
OrthoDBiEOG773XR5.
PhylomeDBiP87153.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20801698.
PROiP87153.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012720. Chap_CCT_eta.
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]
PANTHERiPTHR11353:SF22. PTHR11353:SF22. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02345. chap_CCT_eta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTCPH_SCHPO
AccessioniPrimary (citable) accession number: P87153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: January 20, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.