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HUMAN:FUS

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) FUS (synonyms: TLS)
Protein Name(s) RNA-binding protein FUS

75 kDa DNA-pairing protein Oncogene FUS Oncogene TLS POMp75 Translocated in liposarcoma protein

External Links
UniProt P35637
EMBL S62140
S62138
X71427
X71428
AF071213
AF071213
AC009088
BC000402
BC002459
AJ295163
CCDS CCDS10707.1
CCDS58454.1
PIR S33798
S33799
RefSeq NP_001164105.1
NP_004951.1
UniGene Hs.46894
PDB 2LA6
2LCW
4FDD
4FQ3
PDBsum 2LA6
2LCW
4FDD
4FQ3
ProteinModelPortal P35637
SMR P35637
BioGrid 108797
DIP DIP-29857N
IntAct P35637
MINT MINT-5005976
STRING 9606.ENSP00000254108
PhosphoSite P35637
DMDM 544357
MaxQB P35637
PaxDb P35637
PRIDE P35637
DNASU 2521
Ensembl ENST00000254108
ENST00000380244
GeneID 2521
KEGG hsa:2521
UCSC uc002ebe.2
uc002ebh.3
CTD 2521
GeneCards GC16P031191
GeneReviews FUS
HGNC HGNC:4010
HPA CAB033036
CAB058691
HPA008784
MIM 137070
608030
612160
614782
neXtProt NX_P35637
Orphanet 803
275872
862
300605
79105
99967
PharmGKB PA28425
eggNOG NOG240581
GeneTree ENSGT00530000063105
HOGENOM HOG000038010
HOVERGEN HBG095056
InParanoid P35637
KO K13098
OrthoDB EOG7DZ8N7
PhylomeDB P35637
TreeFam TF322599
Reactome REACT_467
ChiTaRS FUS
GeneWiki FUS
GenomeRNAi 2521
NextBio 9927
PRO PR:P35637
Proteomes UP000005640
Bgee P35637
CleanEx HS_FUS
ExpressionAtlas P35637
Genevestigator P35637
GO GO:0005737
GO:0005654
GO:0005634
GO:0003677
GO:0042802
GO:0000166
GO:0044822
GO:0003723
GO:0008270
GO:0010467
GO:0000398
GO:0008380
Gene3D 3.30.70.330
4.10.1060.10
InterPro IPR012677
IPR000504
IPR001876
Pfam PF00076
PF00641
SMART SM00360
SM00547
PROSITE PS50102
PS01358
PS50199

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005634

nucleus

PMID:21909421[1]

ECO:0000314

C

Figure 2. Subcellular localization of FUS in prostate cancer cells

complete
CACAO 2130

GO:0003713

transcription coactivator activity

PMID:21909421[1]

ECO:0000314

F

Figure 1 establishes that FUS is complexed with AR. Figure 3 demonstrates that FUS possesses innate ability to regulate transcription. Figure 4 demonstrates that FUS modulates AR activity.

complete
CACAO 2132

enables

GO:0003682

chromatin binding

PMID:27731383[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:27731383[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0043484

regulation of RNA splicing

PMID:27731383[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043484

regulation of RNA splicing

PMID:25453086[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006357

regulation of transcription by RNA polymerase II

PMID:25453086[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051260

protein homooligomerization

PMID:25453086[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003682

chromatin binding

PMID:25453086[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008380

RNA splicing

PMID:26124092[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:26124092[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1905168

positive regulation of double-strand break repair via homologous recombination

PMID:10567410[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003713

transcription coactivator activity

PMID:21909421[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21909421[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22658674[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22681889[7]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0011571
MGI:MGI:1353633
MGI:MGI:99960
PANTHER:PTN000579998
UniProtKB:P35637
UniProtKB:Q01844
UniProtKB:Q92804

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:16365397[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23975937[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P35637

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18509338[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P35637

F

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1903508

positive regulation of nucleic acid-templated transcription

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0003713

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P56959
ensembl:ENSMUSP00000101858

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P56959
ensembl:ENSMUSP00000101858

C

Seeded From UniProt

complete

involved_in

GO:0071277

cellular response to calcium ion

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

enables

GO:0046966

thyroid hormone receptor binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

F

Seeded From UniProt

complete

enables

GO:0046965

retinoid X receptor binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

F

Seeded From UniProt

complete

part_of

GO:0044327

dendritic spine head

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

part_of

GO:0043204

perikaryon

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

part_of

GO:0043197

dendritic spine

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

part_of

GO:0043025

neuronal cell body

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

enables

GO:0035255

ionotropic glutamate receptor binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

F

Seeded From UniProt

complete

enables

GO:0031489

myosin V binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

F

Seeded From UniProt

complete

part_of

GO:0030425

dendrite

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

enables

GO:0030331

estrogen receptor binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

F

Seeded From UniProt

complete

part_of

GO:0005844

polysome

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5PQK2
ensembl:ENSRNOP00000033029

C

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000504
InterPro:IPR035979

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034459
InterPro:IPR034870

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034870

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:8510758[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:8510758[12]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-72160
Reactome:R-HSA-72143
Reactome:R-HSA-72139
Reactome:R-HSA-72130
Reactome:R-HSA-72127
Reactome:R-HSA-72124
Reactome:R-HSA-72107
Reactome:R-HSA-156661

ECO:0000304

author statement supported by traceable reference used in manual assertion








C

Seeded From UniProt

complete

involved_in

GO:0000398

mRNA splicing, via spliceosome

Reactome:R-HSA-72163

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Haile, S et al. (2011) FUS/TLS is a co-activator of androgen receptor in prostate cancer cells. PLoS ONE 6 e24197 PubMed GONUTS page
  2. 2.0 2.1 2.2 Yamaguchi, A & Takanashi, K (2016) FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription. Sci Rep 6 35195 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Yang, L et al. (2014) Self-assembled FUS binds active chromatin and regulates gene transcription. Proc. Natl. Acad. Sci. U.S.A. 111 17809-14 PubMed GONUTS page
  4. 4.0 4.1 Yu, Y & Reed, R (2015) FUS functions in coupling transcription to splicing by mediating an interaction between RNAP II and U1 snRNP. Proc. Natl. Acad. Sci. U.S.A. 112 8608-13 PubMed GONUTS page
  5. Baechtold, H et al. (1999) Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation. J. Biol. Chem. 274 34337-42 PubMed GONUTS page
  6. Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
  7. Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
  8. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  9. Radic, MZ et al. (2006) Heterogeneous nuclear ribonucleoprotein P2 is an autoantibody target in mice deficient for Mer, Axl, and Tyro3 receptor tyrosine kinases. J. Immunol. 176 68-74 PubMed GONUTS page
  10. Thomsen, C et al. (2013) A conserved N-terminal motif is required for complex formation between FUS, EWSR1, TAF15 and their oncogenic fusion proteins. FASEB J. 27 4965-74 PubMed GONUTS page
  11. Wang, X et al. (2008) Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription. Nature 454 126-30 PubMed GONUTS page
  12. 12.0 12.1 Crozat, A et al. (1993) Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature 363 640-4 PubMed GONUTS page