Q92837 (FRAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proto-oncogene FRAT1

Alternative name(s):
Frequently rearranged in advanced T-cell lymphomas 1
Short name=FRAT-1

Gene names

Name:

FRAT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Wnt signaling pathway
Cellular component	Cytoplasm
Disease	Proto-oncogene
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 279

279

Proto-oncogene FRAT1

PRO_0000087332

Regions

Region

198 – 220

23

Involved in GSK-3 binding

Compositional bias

6 – 22

17

Glu-rich (highly acidic)

Compositional bias

6 – 10

5

Poly-Glu

Compositional bias

13 – 22

10

Poly-Glu

Amino acid modifications

Modified residue

88

1

Phosphoserine Ref.7

Experimental info

Sequence conflict

58

1

H → D in AAB97096. Ref.1

Sequence conflict

179

1

S → P in AAH34476. Ref.5

Secondary structure

1

.

.

.

.

.

279

Helix Strand Turn

Details...

Helix

201 – 209

9

Helix

212 – 219

8

Sequences

	Sequence		Length	Mass (Da)
	Q92837 [UniParc]. Last modified August 16, 2004. Version 3. Checksum: 629AFD6CEA1DC0BD	FASTA	279	29,093
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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.

IPI

IPI00023762.

RefSeq

NP_005470.2. NM_005479.3.

UniGene

Hs.126057.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q92837.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92837. 12 interactions.

STRING

9606.ENSP00000360060.

PTM databases

PhosphoSite

Q92837.

Polymorphism databases

DMDM

51338813.

Proteomic databases

PaxDb

Q92837.

PRIDE

Q92837.

Protocols and materials databases

DNASU

10023.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371021; ENSP00000360060; ENSG00000165879.

GeneID

10023.

KEGG

hsa:10023.

UCSC

uc001knc.1. human.

Organism-specific databases

CTD

10023.

GeneCards

GC10P099069.

HGNC

HGNC:3944. FRAT1.

HPA

CAB037271.
CAB046472.

MIM

602503. gene.

neXtProt

NX_Q92837.

PharmGKB

PA28361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43447.

HOGENOM

HOG000112642.

HOVERGEN

HBG051660.

InParanoid

Q92837.

KO

K03069.

OMA

APVHEPP.

OrthoDB

EOG4SF97G.

PhylomeDB

Q92837.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.

Gene expression databases

Bgee

Q92837.

CleanEx

HS_FRAT1.

Genevestigator

Q92837.

GermOnline

ENSG00000165879. Homo sapiens.

Family and domain databases

InterPro

IPR008014. GSK3-bd.
[Graphical view]

Pfam

PF05350. GSK-3_bind. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q92837.

GenomeRNAi

10023.

NextBio

37873.

SOURCE

Search...

Entry information

Entry name

FRAT1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.