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Q92837 (FRAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene FRAT1
Alternative name(s):
Frequently rearranged in advanced T-cell lymphomas 1
Short name=FRAT-1
Gene names
Name:FRAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

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

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Belongs to the GSK-3-binding protein family.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCytoplasm
   DiseaseProto-oncogene
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

embryonic axis specification

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Proto-oncogene FRAT1
PRO_0000087332

Regions

Region198 – 22023Involved in GSK-3 binding
Compositional bias6 – 2217Glu-rich (highly acidic)
Compositional bias6 – 105Poly-Glu
Compositional bias13 – 2210Poly-Glu

Amino acid modifications

Modified residue881Phosphoserine Ref.7

Experimental info

Sequence conflict581H → D in AAB97096. Ref.1
Sequence conflict1791S → P in AAH34476. Ref.5

Secondary structure

..... 279
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92837 [UniParc].

Last modified August 16, 2004. Version 3.
Checksum: 629AFD6CEA1DC0BD

FASTA27929,093
        10         20         30         40         50         60 
MPCRREEEEE AGEEAEGEEE EEDSFLLLQQ SVALGSSGEV DRLVAQIGET LQLDAAQHSP 

        70         80         90        100        110        120 
ASPCGPPGAP LRAPGPLAAA VPADKARSPA VPLLLPPALA ETVGPAPPGV LRCALGDRGR 

       130        140        150        160        170        180 
VRGRAAPYCV AELATGPSAL SPLPPQADLD GPPGAGKQGI PQPLSGPCRR GWLRGAAASR 

       190        200        210        220        230        240 
RLQQRRGSQP ETRTGDDDPH RLLQQLVLSG NLIKEAVRRL HSRRLQLRAK LPQRPLLGPL 

       250        260        270 
SAPVHEPPSP RSPRAACSDP GASGRAQLRT GDGVLVPGS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58975 mRNA. Translation: AAB97096.2.
AB074890 mRNA. Translation: BAB86352.1.
AL355490 Genomic DNA. Translation: CAI40773.1.
BC034476 mRNA. Translation: AAH34476.1.
CCDSCCDS7455.1.
RefSeqNP_005470.2. NM_005479.3.
UniGeneHs.126057.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ92837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115340. 14 interactions.
IntActQ92837. 13 interactions.
MINTMINT-100904.
STRING9606.ENSP00000360060.

PTM databases

PhosphoSiteQ92837.

Polymorphism databases

DMDM51338813.

Proteomic databases

PaxDbQ92837.
PRIDEQ92837.

Protocols and materials databases

DNASU10023.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371021; ENSP00000360060; ENSG00000165879.
GeneID10023.
KEGGhsa:10023.
UCSCuc001knc.1. human.

Organism-specific databases

CTD10023.
GeneCardsGC10P099069.
HGNCHGNC:3944. FRAT1.
HPACAB037271.
CAB046472.
MIM602503. gene.
neXtProtNX_Q92837.
PharmGKBPA28361.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43447.
HOGENOMHOG000112642.
HOVERGENHBG051660.
InParanoidQ92837.
KOK03069.
OMAGKQGIPQ.
OrthoDBEOG72ZCH6.
PhylomeDBQ92837.
TreeFamTF330804.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ92837.

Gene expression databases

BgeeQ92837.
CleanExHS_FRAT1.
GenevestigatorQ92837.

Family and domain databases

InterProIPR008014. GSK3-bd.
[Graphical view]
PfamPF05350. GSK-3_bind. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92837.
GeneWikiFRAT1.
GenomeRNAi10023.
NextBio37873.
PROQ92837.
SOURCESearch...

Entry information

Entry nameFRAT1_HUMAN
AccessionPrimary (citable) accession number: Q92837
Secondary accession number(s): Q5JTI1, Q8NE74, Q8TDW9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM