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Protein

Translationally-controlled tumor protein homolog

Gene

p23fy

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in calcium binding and microtubule stabilization (By similarity). May be a guanine nucleotide-free chaperone (GFC).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Translationally-controlled tumor protein homolog
Short name:
TCTP
Alternative name(s):
p23fyp
Gene namesi
Name:p23fy
ORF Names:SPAC1F12.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1F12.02c.
PomBaseiSPAC1F12.02c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm 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 – 168168Translationally-controlled tumor protein homologPRO_0000211310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10344.

PTM databases

iPTMnetiQ10344.

Interactioni

Protein-protein interaction databases

BioGridi278935. 6 interactions.
MINTiMINT-4698972.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Turni7 – 104Combined sources
Turni16 – 183Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 318Combined sources
Beta strandi34 – 385Combined sources
Beta strandi62 – 665Combined sources
Helixi67 – 715Combined sources
Helixi81 – 10121Combined sources
Helixi106 – 12217Combined sources
Turni123 – 1286Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi154 – 1607Combined sources
Beta strandi164 – 1663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6QNMR-A1-168[»]
1H7YNMR-A1-168[»]
ProteinModelPortaliQ10344.
SMRiQ10344. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 168168TCTPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TCTP family.PROSITE-ProRule annotation
Contains 1 TCTP domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000203361.
InParanoidiQ10344.
OMAiCAMIEEG.
OrthoDBiEOG73V6XZ.
PhylomeDBiQ10344.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
IPR018103. Translation_control_tumour_CS.
IPR018105. Translational_control_tumour_p.
[Graphical view]
PANTHERiPTHR11991. PTHR11991. 1 hit.
PfamiPF00838. TCTP. 1 hit.
[Graphical view]
PRINTSiPR01653. TCTPROTEIN.
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS01002. TCTP_1. 1 hit.
PS01003. TCTP_2. 1 hit.
PS51797. TCTP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLYKDVISG DELVSDAYDL KEVDDIVYEA DCQMVTVKQG GDVDIGANPS
60 70 80 90 100
AEDAEENAEE GTETVNNLVY SFRLSPTSFD KKSYMSYIKG YMKAIKARLQ
110 120 130 140 150
ESNPERVPVF EKNAIGFVKK ILANFKDYDF YIGESMDPDA MVVLMNYRED
160
GITPYMIFFK DGLVSEKF
Length:168
Mass (Da):19,049
Last modified:October 1, 1996 - v1
Checksum:i52F749AF994C917F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93806.1.
PIRiT38060. S67445.
RefSeqiNP_594328.1. NM_001019749.2.

Genome annotation databases

EnsemblFungiiSPAC1F12.02c.1; SPAC1F12.02c.1:pep; SPAC1F12.02c.
GeneIDi2542475.
KEGGispo:SPAC1F12.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93806.1.
PIRiT38060. S67445.
RefSeqiNP_594328.1. NM_001019749.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6QNMR-A1-168[»]
1H7YNMR-A1-168[»]
ProteinModelPortaliQ10344.
SMRiQ10344. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278935. 6 interactions.
MINTiMINT-4698972.

PTM databases

iPTMnetiQ10344.

Proteomic databases

MaxQBiQ10344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1F12.02c.1; SPAC1F12.02c.1:pep; SPAC1F12.02c.
GeneIDi2542475.
KEGGispo:SPAC1F12.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1F12.02c.
PomBaseiSPAC1F12.02c.

Phylogenomic databases

HOGENOMiHOG000203361.
InParanoidiQ10344.
OMAiCAMIEEG.
OrthoDBiEOG73V6XZ.
PhylomeDBiQ10344.

Miscellaneous databases

EvolutionaryTraceiQ10344.
PROiQ10344.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
IPR018103. Translation_control_tumour_CS.
IPR018105. Translational_control_tumour_p.
[Graphical view]
PANTHERiPTHR11991. PTHR11991. 1 hit.
PfamiPF00838. TCTP. 1 hit.
[Graphical view]
PRINTSiPR01653. TCTPROTEIN.
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS01002. TCTP_1. 1 hit.
PS01003. TCTP_2. 1 hit.
PS51797. TCTP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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-78, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones."
    Thaw P., Baxter N.J., Hounslow A.M., Price C., Waltho J.P., Craven C.J.
    Nat. Struct. Biol. 8:701-704(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiTCTP_SCHPO
AccessioniPrimary (citable) accession number: Q10344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.