SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q92837

- FRAT1_HUMAN

UniProt

Q92837 - FRAT1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proto-oncogene FRAT1

Gene
FRAT1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. embryonic axis specification Source: Ensembl
  2. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_11065. Beta-catenin phosphorylation cascade.
REACT_200610. 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: Chromosome 10

Organism-specific databases

HGNCiHGNC:3944. FRAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28361.

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.
GenevestigatoriQ92837.

Organism-specific databases

HPAiCAB037271.
CAB046472.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi115340. 14 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 – 2099
Helixi212 – 2198

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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

Phylogenomic databases

eggNOGiNOG43447.
HOGENOMiHOG000112642.
HOVERGENiHBG051660.
InParanoidiQ92837.
KOiK03069.
OMAiGKQGIPQ.
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

MPCRREEEEE AGEEAEGEEE EEDSFLLLQQ SVALGSSGEV DRLVAQIGET    50
LQLDAAQHSP ASPCGPPGAP LRAPGPLAAA VPADKARSPA VPLLLPPALA 100
ETVGPAPPGV LRCALGDRGR VRGRAAPYCV AELATGPSAL SPLPPQADLD 150
GPPGAGKQGI PQPLSGPCRR GWLRGAAASR RLQQRRGSQP ETRTGDDDPH 200
RLLQQLVLSG NLIKEAVRRL HSRRLQLRAK LPQRPLLGPL SAPVHEPPSP 250
RSPRAACSDP GASGRAQLRT GDGVLVPGS 279
Length:279
Mass (Da):29,093
Last modified:August 16, 2004 - v3
Checksum:i629AFD6CEA1DC0BD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581H → D in AAB97096. 1 Publication
Sequence conflicti179 – 1791S → P in AAH34476. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi51338813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58975 mRNA. Translation: AAB97096.2 .
AB074890 mRNA. Translation: BAB86352.1 .
AL355490 Genomic DNA. Translation: CAI40773.1 .
BC034476 mRNA. Translation: AAH34476.1 .
CCDSi CCDS7455.1.
RefSeqi NP_005470.2. NM_005479.3.
UniGenei Hs.126057.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GNG X-ray 2.60 X/Y 188-226 [» ]
3ZRK X-ray 2.37 X/Y 197-226 [» ]
3ZRL X-ray 2.48 X/Y 197-226 [» ]
3ZRM X-ray 2.49 X/Y 197-226 [» ]
4AFJ X-ray 1.98 X/Y 197-226 [» ]
ProteinModelPortali Q92837.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115340. 14 interactions.
IntActi Q92837. 13 interactions.
MINTi MINT-100904.
STRINGi 9606.ENSP00000360060.

PTM databases

PhosphoSitei Q92837.

Polymorphism databases

DMDMi 51338813.

Proteomic databases

PaxDbi Q92837.
PRIDEi Q92837.

Protocols and materials databases

DNASUi 10023.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371021 ; ENSP00000360060 ; ENSG00000165879 .
GeneIDi 10023.
KEGGi hsa:10023.
UCSCi uc001knc.1. human.

Organism-specific databases

CTDi 10023.
GeneCardsi GC10P099069.
HGNCi HGNC:3944. FRAT1.
HPAi CAB037271.
CAB046472.
MIMi 602503. gene.
neXtProti NX_Q92837.
PharmGKBi PA28361.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43447.
HOGENOMi HOG000112642.
HOVERGENi HBG051660.
InParanoidi Q92837.
KOi K03069.
OMAi GKQGIPQ.
OrthoDBi EOG72ZCH6.
PhylomeDBi Q92837.
TreeFami TF330804.

Enzyme and pathway databases

Reactomei REACT_11065. Beta-catenin phosphorylation cascade.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinki Q92837.

Miscellaneous databases

EvolutionaryTracei Q92837.
GeneWikii FRAT1.
GenomeRNAii 10023.
NextBioi 37873.
PROi Q92837.
SOURCEi Search...

Gene expression databases

Bgeei Q92837.
CleanExi HS_FRAT1.
Genevestigatori Q92837.

Family and domain databases

InterProi IPR008014. GSK3-bd.
[Graphical view ]
Pfami PF05350. GSK-3_bind. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 115 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