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Protein

Proto-oncogene FRAT1

Gene

FRAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_11065. Beta-catenin phosphorylation cascade.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinkiQ92837.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene FRAT1
Alternative name(s):
Frequently rearranged in advanced T-cell lymphomas 1
Short name:
FRAT-1
Gene namesi
Name:FRAT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3944. FRAT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28361.

Polymorphism and mutation databases

BioMutaiFRAT1.
DMDMi51338813.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Proto-oncogene FRAT1PRO_0000087332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ92837.
PRIDEiQ92837.

PTM databases

PhosphoSiteiQ92837.

Expressioni

Gene expression databases

BgeeiQ92837.
CleanExiHS_FRAT1.
GenevisibleiQ92837. HS.

Organism-specific databases

HPAiCAB046472.

Interactioni

Subunit structurei

Binds DVL1. Binds GSK-3 and prevent GSK-3-dependent phosphorylation.1 Publication

Protein-protein interaction databases

BioGridi115340. 15 interactions.
IntActiQ92837. 13 interactions.
MINTiMINT-100904.
STRINGi9606.ENSP00000360060.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi201 – 2099Combined sources
Helixi212 – 2198Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GNGX-ray2.60X/Y188-226[»]
3ZRKX-ray2.37X/Y197-226[»]
3ZRLX-ray2.48X/Y197-226[»]
3ZRMX-ray2.49X/Y197-226[»]
4AFJX-ray1.98X/Y197-226[»]
ProteinModelPortaliQ92837.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92837.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 22023Involved in GSK-3 bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 2217Glu-rich (highly acidic)Add
BLAST
Compositional biasi6 – 105Poly-Glu
Compositional biasi13 – 2210Poly-Glu

Sequence similaritiesi

Belongs to the GSK-3-binding protein family.Curated

Phylogenomic databases

eggNOGiNOG43447.
GeneTreeiENSGT00390000007081.
HOGENOMiHOG000112642.
HOVERGENiHBG051660.
InParanoidiQ92837.
KOiK03069.
OMAiQHPERRS.
OrthoDBiEOG72ZCH6.
PhylomeDBiQ92837.
TreeFamiTF330804.

Family and domain databases

InterProiIPR008014. GSK3-bd.
[Graphical view]
PfamiPF05350. GSK-3_bind. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPCRREEEEE AGEEAEGEEE EEDSFLLLQQ SVALGSSGEV DRLVAQIGET
60 70 80 90 100
LQLDAAQHSP ASPCGPPGAP LRAPGPLAAA VPADKARSPA VPLLLPPALA
110 120 130 140 150
ETVGPAPPGV LRCALGDRGR VRGRAAPYCV AELATGPSAL SPLPPQADLD
160 170 180 190 200
GPPGAGKQGI PQPLSGPCRR GWLRGAAASR RLQQRRGSQP ETRTGDDDPH
210 220 230 240 250
RLLQQLVLSG NLIKEAVRRL HSRRLQLRAK LPQRPLLGPL SAPVHEPPSP
260 270
RSPRAACSDP GASGRAQLRT GDGVLVPGS
Length:279
Mass (Da):29,093
Last modified:August 16, 2004 - v3
Checksum:i629AFD6CEA1DC0BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581H → D in AAB97096 (PubMed:9034327).Curated
Sequence conflicti179 – 1791S → P in AAH34476 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58975 mRNA. Translation: AAB97096.2.
AB074890 mRNA. Translation: BAB86352.1.
AL355490 Genomic DNA. Translation: CAI40773.1.
BC034476 mRNA. Translation: AAH34476.1.
CCDSiCCDS7455.1.
RefSeqiNP_005470.2. NM_005479.3.
UniGeneiHs.126057.

Genome annotation databases

EnsembliENST00000371021; ENSP00000360060; ENSG00000165879.
GeneIDi10023.
KEGGihsa:10023.
UCSCiuc001knc.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58975 mRNA. Translation: AAB97096.2.
AB074890 mRNA. Translation: BAB86352.1.
AL355490 Genomic DNA. Translation: CAI40773.1.
BC034476 mRNA. Translation: AAH34476.1.
CCDSiCCDS7455.1.
RefSeqiNP_005470.2. NM_005479.3.
UniGeneiHs.126057.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GNGX-ray2.60X/Y188-226[»]
3ZRKX-ray2.37X/Y197-226[»]
3ZRLX-ray2.48X/Y197-226[»]
3ZRMX-ray2.49X/Y197-226[»]
4AFJX-ray1.98X/Y197-226[»]
ProteinModelPortaliQ92837.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115340. 15 interactions.
IntActiQ92837. 13 interactions.
MINTiMINT-100904.
STRINGi9606.ENSP00000360060.

PTM databases

PhosphoSiteiQ92837.

Polymorphism and mutation databases

BioMutaiFRAT1.
DMDMi51338813.

Proteomic databases

PaxDbiQ92837.
PRIDEiQ92837.

Protocols and materials databases

DNASUi10023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371021; ENSP00000360060; ENSG00000165879.
GeneIDi10023.
KEGGihsa:10023.
UCSCiuc001knc.1. human.

Organism-specific databases

CTDi10023.
GeneCardsiGC10P099069.
HGNCiHGNC:3944. FRAT1.
HPAiCAB046472.
MIMi602503. gene.
neXtProtiNX_Q92837.
PharmGKBiPA28361.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43447.
GeneTreeiENSGT00390000007081.
HOGENOMiHOG000112642.
HOVERGENiHBG051660.
InParanoidiQ92837.
KOiK03069.
OMAiQHPERRS.
OrthoDBiEOG72ZCH6.
PhylomeDBiQ92837.
TreeFamiTF330804.

Enzyme and pathway databases

ReactomeiREACT_11065. Beta-catenin phosphorylation cascade.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinkiQ92837.

Miscellaneous databases

ChiTaRSiFRAT1. human.
EvolutionaryTraceiQ92837.
GeneWikiiFRAT1.
GenomeRNAii10023.
NextBioi37873.
PROiQ92837.
SOURCEiSearch...

Gene expression databases

BgeeiQ92837.
CleanExiHS_FRAT1.
GenevisibleiQ92837. HS.

Family and domain databases

InterProiIPR008014. GSK3-bd.
[Graphical view]
PfamiPF05350. GSK-3_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas."
    Jonkers J., Korswagen H.C., Acton D., Breuer M., Berns A.
    EMBO J. 16:441-450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Jonkers J., Korswagen H.C., Acton D., Breuer M., Berns A.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 170.
  3. "Molecular cloning and expression of proto-oncogene FRAT1 in human cancer."
    Saitoh T., Mine T., Katoh M.
    Int. J. Oncol. 20:785-789(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Tissue: Testis.
  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].
    Tissue: Testis.
  6. "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin."
    Hino S., Michiue T., Asashima M., Kikuchi A.
    J. Biol. Chem. 278:14066-14073(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DVL1, ROLE IN WNT SIGNALING.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation."
    Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R., Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G., Reith A.D.
    Structure 9:1143-1152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 198-223 IN COMPLEX WITH GSK-3.

Entry informationi

Entry nameiFRAT1_HUMAN
AccessioniPrimary (citable) accession number: Q92837
Secondary accession number(s): Q5JTI1, Q8NE74, Q8TDW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 16, 2004
Last modified: July 22, 2015
This is version 124 of the entry and version 3 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.