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P35637

- FUS_HUMAN

UniProt

P35637 - FUS_HUMAN

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Protein
RNA-binding protein FUS
Gene
FUS, TLS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei175 – 1751Breakpoint for translocation to form chimeric FUS/ATF1 protein
Sitei266 – 2672Breakpoint for translocation to form FUS/TLS-CHOP oncogene

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri422 – 45332RanBP2-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: ProtInc
  3. identical protein binding Source: IntAct
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. RNA splicing Source: Reactome
  2. cell death Source: UniProtKB-KW
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome Source: Reactome
Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein FUS
Alternative name(s):
75 kDa DNA-pairing protein
Oncogene FUS
Oncogene TLS
POMp75
Translocated in liposarcoma protein
Gene namesi
Name:FUS
Synonyms:TLS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:4010. FUS.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3.
A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG.
Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis.
Note: The disease may be caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving FUS is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(12;16)(q13;p11.2) with ATF1 generates a chimeric FUS/ATF1 protein.
Amyotrophic lateral sclerosis 6 (ALS6) [MIM:608030]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911G → S in ALS6. 1 Publication
VAR_068918
Natural varianti216 – 2161R → C in ALS6 and ETM4. 2 Publications
VAR_068919
Natural varianti225 – 2251G → V in ALS6. 1 Publication
VAR_068920
Natural varianti230 – 2301G → C in ALS6. 1 Publication
VAR_068921
Natural varianti234 – 2341R → C in ALS6. 1 Publication
VAR_068922
Natural varianti244 – 2441R → C in ALS6. 1 Publication
VAR_054837
Natural varianti507 – 5071G → D in ALS6. 1 Publication
VAR_068924
Natural varianti514 – 5141R → G in ALS6. 1 Publication
VAR_054838
Natural varianti514 – 5141R → S in ALS6. 1 Publication
VAR_054839
Natural varianti515 – 5151G → C in ALS6. 1 Publication
VAR_054840
Natural varianti518 – 5181R → K in ALS6. 1 Publication
VAR_054842
Natural varianti521 – 5211R → C in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 3 Publications
VAR_054843
Natural varianti521 – 5211R → G in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 1 Publication
VAR_054844
Natural varianti521 – 5211R → H in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 3 Publications
VAR_054845
Natural varianti522 – 5221R → G in ALS6. 1 Publication
VAR_054846
Natural varianti524 – 5241R → S in ALS6. 1 Publication
VAR_054847
Natural varianti524 – 5241R → T in ALS6. 1 Publication
VAR_054848
Natural varianti525 – 5251P → L in ALS6. 1 Publication
VAR_054849
Tremor, hereditary essential 4 (ETM4) [MIM:614782]: A common movement disorder mainly characterized by postural tremor of the arms. Head, legs, trunk, voice, jaw, and facial muscles also may be involved. The condition can be aggravated by emotions, hunger, fatigue and temperature extremes, and may cause a functional disability or even incapacitation. Inheritance is autosomal dominant.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti216 – 2161R → C in ALS6 and ETM4. 2 Publications
VAR_068919
Natural varianti431 – 4311P → L in ETM4. 1 Publication
Corresponds to variant rs186547381 [ dbSNP | Ensembl ].
VAR_068923

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration, Proto-oncogene

Organism-specific databases

MIMi608030. phenotype.
612160. phenotype.
614782. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
275872. Frontotemporal dementia with motor neuron disease.
862. Hereditary essential tremor.
300605. Juvenile amyotrophic lateral sclerosis.
79105. Myxofibrosarcoma.
99967. Myxoid/round cell liposarcoma.
PharmGKBiPA28425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526RNA-binding protein FUS
PRO_0000081591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei242 – 2421Asymmetric dimethylarginine1 Publication
Modified residuei244 – 2441Asymmetric dimethylarginine1 Publication
Modified residuei248 – 2481Asymmetric dimethylarginine1 Publication
Modified residuei251 – 2511Asymmetric dimethylarginine1 Publication
Modified residuei259 – 2591Asymmetric dimethylarginine1 Publication
Modified residuei277 – 2771Phosphoserine1 Publication
Modified residuei286 – 2861Phosphothreonine1 Publication
Modified residuei377 – 3771Asymmetric dimethylarginine1 Publication
Modified residuei383 – 3831Asymmetric dimethylarginine1 Publication
Modified residuei386 – 3861Asymmetric dimethylarginine1 Publication
Modified residuei388 – 3881Asymmetric dimethylarginine1 Publication
Modified residuei394 – 3941Asymmetric dimethylarginine1 Publication
Modified residuei407 – 4071Asymmetric dimethylarginine1 Publication
Modified residuei473 – 4731Asymmetric dimethylarginine1 Publication
Modified residuei476 – 4761Asymmetric dimethylarginine1 Publication
Modified residuei481 – 4811Asymmetric dimethylarginine1 Publication
Modified residuei485 – 4851Asymmetric dimethylarginine1 Publication
Modified residuei487 – 4871Asymmetric dimethylarginine1 Publication
Modified residuei491 – 4911Asymmetric dimethylarginine1 Publication
Modified residuei495 – 4951Asymmetric dimethylarginine1 Publication
Modified residuei498 – 4981Asymmetric dimethylarginine1 Publication
Modified residuei503 – 5031Asymmetric dimethylarginine1 Publication

Post-translational modificationi

Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP35637.
PaxDbiP35637.
PRIDEiP35637.

PTM databases

PhosphoSiteiP35637.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP35637.
BgeeiP35637.
CleanExiHS_FUS.
GenevestigatoriP35637.

Organism-specific databases

HPAiCAB033036.
CAB058691.
HPA008784.

Interactioni

Subunit structurei

Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-400434,EBI-400434
DROSHAQ9NRR42EBI-400434,EBI-528367
EWSR1Q018445EBI-400434,EBI-739737
PLECQ151494EBI-400434,EBI-297903
TAF15Q928045EBI-400434,EBI-2255091
TP63Q9H3D42EBI-400434,EBI-2337775

Protein-protein interaction databases

BioGridi108797. 103 interactions.
DIPiDIP-29857N.
IntActiP35637. 46 interactions.
MINTiMINT-5005976.
STRINGi9606.ENSP00000254108.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi285 – 2906
Helixi298 – 3058
Turni306 – 3083
Turni315 – 3184
Beta strandi319 – 3268
Turni328 – 3303
Beta strandi332 – 34312
Helixi344 – 35411
Beta strandi358 – 3636
Beta strandi365 – 3684
Beta strandi379 – 3813
Helixi514 – 5218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LA6NMR-A282-370[»]
2LCWNMR-A278-385[»]
4FDDX-ray2.30B498-526[»]
4FQ3X-ray3.00B495-526[»]
ProteinModelPortaliP35637.
SMRiP35637. Positions 278-375.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini285 – 37187RRM
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 165165Gln/Gly/Ser/Tyr-rich
Add
BLAST
Compositional biasi166 – 267102Gly-rich
Add
BLAST
Compositional biasi371 – 526156Arg/Gly-rich
Add
BLAST

Sequence similaritiesi

Belongs to the RRM TET family.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG240581.
HOGENOMiHOG000038010.
HOVERGENiHBG095056.
InParanoidiP35637.
KOiK13098.
OrthoDBiEOG7DZ8N7.
PhylomeDBiP35637.
TreeFamiTF322599.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P35637-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MASNDYTQQA TQSYGAYPTQ PGQGYSQQSS QPYGQQSYSG YSQSTDTSGY    50
GQSSYSSYGQ SQNTGYGTQS TPQGYGSTGG YGSSQSSQSS YGQQSSYPGY 100
GQQPAPSSTS GSYGSSSQSS SYGQPQSGSY SQQPSYGGQQ QSYGQQQSYN 150
PPQGYGQQNQ YNSSSGGGGG GGGGGNYGQD QSSMSSGGGS GGGYGNQDQS 200
GGGGSGGYGQ QDRGGRGRGG SGGGGGGGGG GYNRSSGGYE PRGRGGGRGG 250
RGGMGGSDRG GFNKFGGPRD QGSRHDSEQD NSDNNTIFVQ GLGENVTIES 300
VADYFKQIGI IKTNKKTGQP MINLYTDRET GKLKGEATVS FDDPPSAKAA 350
IDWFDGKEFS GNPIKVSFAT RRADFNRGGG NGRGGRGRGG PMGRGGYGGG 400
GSGGGGRGGF PSGGGGGGGQ QRAGDWKCPN PTCENMNFSW RNECNQCKAP 450
KPDGPGGGPG GSHMGGNYGD DRRGGRGGYD RGGYRGRGGD RGGFRGGRGG 500
GDRGGFGPGK MDSRGEHRQD RRERPY 526
Length:526
Mass (Da):53,426
Last modified:June 1, 1994 - v1
Checksum:i88C8E263B7905549
GO
Isoform Short (identifier: P35637-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     64-65: TG → S

Show »
Length:525
Mass (Da):53,355
Checksum:i949558C718B4C19B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911G → S in ALS6. 1 Publication
VAR_068918
Natural varianti216 – 2161R → C in ALS6 and ETM4. 2 Publications
VAR_068919
Natural varianti225 – 2251G → V in ALS6. 1 Publication
VAR_068920
Natural varianti230 – 2301G → C in ALS6. 1 Publication
VAR_068921
Natural varianti234 – 2341R → C in ALS6. 1 Publication
VAR_068922
Natural varianti244 – 2441R → C in ALS6. 1 Publication
VAR_054837
Natural varianti254 – 2541M → V Found in a patient with frontotemporal lobar degeneration. 1 Publication
VAR_065229
Natural varianti312 – 3121K → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035481
Natural varianti431 – 4311P → L in ETM4. 1 Publication
Corresponds to variant rs186547381 [ dbSNP | Ensembl ].
VAR_068923
Natural varianti507 – 5071G → D in ALS6. 1 Publication
VAR_068924
Natural varianti514 – 5141R → G in ALS6. 1 Publication
VAR_054838
Natural varianti514 – 5141R → S in ALS6. 1 Publication
VAR_054839
Natural varianti515 – 5151G → C in ALS6. 1 Publication
VAR_054840
Natural varianti517 – 5171H → Q Does not affect protein nuclear localization. 1 Publication
VAR_054841
Natural varianti518 – 5181R → K in ALS6. 1 Publication
VAR_054842
Natural varianti521 – 5211R → C in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 3 Publications
VAR_054843
Natural varianti521 – 5211R → G in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 1 Publication
VAR_054844
Natural varianti521 – 5211R → H in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. 3 Publications
VAR_054845
Natural varianti522 – 5221R → G in ALS6. 1 Publication
VAR_054846
Natural varianti524 – 5241R → S in ALS6. 1 Publication
VAR_054847
Natural varianti524 – 5241R → T in ALS6. 1 Publication
VAR_054848
Natural varianti525 – 5251P → L in ALS6. 1 Publication
VAR_054849

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei64 – 652TG → S in isoform Short.
VSP_005798

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381T → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S62140 mRNA. Translation: AAB27102.1.
S62138 mRNA. Translation: AAB27103.1. Sequence problems.
X71427 mRNA. Translation: CAA50558.1. Sequence problems.
X71428 mRNA. Translation: CAA50559.1. Sequence problems.
AF071213 Genomic DNA. Translation: AAC35285.1.
AF071213 Genomic DNA. Translation: AAC35284.1.
AC009088 Genomic DNA. No translation available.
BC000402 mRNA. Translation: AAH00402.1.
BC002459 mRNA. Translation: AAH02459.1.
AJ295163 mRNA. Translation: CAC15058.1. Different termination.
CCDSiCCDS10707.1. [P35637-1]
CCDS58454.1. [P35637-2]
PIRiS33798.
S33799.
RefSeqiNP_001164105.1. NM_001170634.1. [P35637-2]
NP_004951.1. NM_004960.3. [P35637-1]
UniGeneiHs.46894.

Genome annotation databases

EnsembliENST00000254108; ENSP00000254108; ENSG00000089280. [P35637-1]
ENST00000380244; ENSP00000369594; ENSG00000089280. [P35637-2]
GeneIDi2521.
KEGGihsa:2521.
UCSCiuc002ebe.2. human. [P35637-1]
uc002ebh.3. human. [P35637-2]

Polymorphism databases

DMDMi544357.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S62140 mRNA. Translation: AAB27102.1 .
S62138 mRNA. Translation: AAB27103.1 . Sequence problems.
X71427 mRNA. Translation: CAA50558.1 . Sequence problems.
X71428 mRNA. Translation: CAA50559.1 . Sequence problems.
AF071213 Genomic DNA. Translation: AAC35285.1 .
AF071213 Genomic DNA. Translation: AAC35284.1 .
AC009088 Genomic DNA. No translation available.
BC000402 mRNA. Translation: AAH00402.1 .
BC002459 mRNA. Translation: AAH02459.1 .
AJ295163 mRNA. Translation: CAC15058.1 . Different termination.
CCDSi CCDS10707.1. [P35637-1 ]
CCDS58454.1. [P35637-2 ]
PIRi S33798.
S33799.
RefSeqi NP_001164105.1. NM_001170634.1. [P35637-2 ]
NP_004951.1. NM_004960.3. [P35637-1 ]
UniGenei Hs.46894.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LA6 NMR - A 282-370 [» ]
2LCW NMR - A 278-385 [» ]
4FDD X-ray 2.30 B 498-526 [» ]
4FQ3 X-ray 3.00 B 495-526 [» ]
ProteinModelPortali P35637.
SMRi P35637. Positions 278-375.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108797. 103 interactions.
DIPi DIP-29857N.
IntActi P35637. 46 interactions.
MINTi MINT-5005976.
STRINGi 9606.ENSP00000254108.

PTM databases

PhosphoSitei P35637.

Polymorphism databases

DMDMi 544357.

Proteomic databases

MaxQBi P35637.
PaxDbi P35637.
PRIDEi P35637.

Protocols and materials databases

DNASUi 2521.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254108 ; ENSP00000254108 ; ENSG00000089280 . [P35637-1 ]
ENST00000380244 ; ENSP00000369594 ; ENSG00000089280 . [P35637-2 ]
GeneIDi 2521.
KEGGi hsa:2521.
UCSCi uc002ebe.2. human. [P35637-1 ]
uc002ebh.3. human. [P35637-2 ]

Organism-specific databases

CTDi 2521.
GeneCardsi GC16P031191.
GeneReviewsi FUS.
HGNCi HGNC:4010. FUS.
HPAi CAB033036.
CAB058691.
HPA008784.
MIMi 137070. gene.
608030. phenotype.
612160. phenotype.
614782. phenotype.
neXtProti NX_P35637.
Orphaneti 803. Amyotrophic lateral sclerosis.
275872. Frontotemporal dementia with motor neuron disease.
862. Hereditary essential tremor.
300605. Juvenile amyotrophic lateral sclerosis.
79105. Myxofibrosarcoma.
99967. Myxoid/round cell liposarcoma.
PharmGKBi PA28425.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240581.
HOGENOMi HOG000038010.
HOVERGENi HBG095056.
InParanoidi P35637.
KOi K13098.
OrthoDBi EOG7DZ8N7.
PhylomeDBi P35637.
TreeFami TF322599.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi FUS. human.
GeneWikii FUS.
GenomeRNAii 2521.
NextBioi 9927.
PROi P35637.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35637.
Bgeei P35637.
CleanExi HS_FUS.
Genevestigatori P35637.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma."
    Crozat A., Aman P., Mandahl N., Ron D.
    Nature 363:640-644(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  2. "Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma."
    Rabbitts T.H., Forster A., Larson R., Nathan P.
    Nat. Genet. 4:175-180(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  3. "Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes."
    Morohoshi F., Ootsuka Y., Arai K., Ichikawa H., Mitani S., Munakata N., Ohki M.
    Gene 221:191-198(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM LONG).
    Tissue: Lung and Lymph.
  6. "Genetic characterization of angiomatoid fibrous histiocytoma identifies fusion of the FUS and ATF-1 genes induced by a chromosomal translocation involving bands 12q13 and 16p11."
    Waters B.L., Panagopoulos I., Allen E.F.
    Cancer Genet. Cytogenet. 121:109-116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-310, CHROMOSOMAL TRANSLOCATION WITH ATF1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
  7. "Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation."
    Baechtold H., Kuroda M., Sok J., Ron D., Lopez B.S., Akhmedov A.T.
    J. Biol. Chem. 274:34337-34342(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 235-244; 307-312; 335-345 AND 349-357, CHARACTERIZATION.
  8. "Human POMp75 is identified as the pro-oncoprotein TLF/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation."
    Bertrand P., Akhmedov A.T., Delacote F., Durrbach A., Lopez B.S.
    Oncogene 18:4515-4521(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 265-276; 317-331 AND 335-357, IDENTIFICATION.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 349-357, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation."
    Ichikawa H., Shimizu K., Hayashi Y., Ohki M.
    Cancer Res. 54:2865-2868(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION.
  11. "The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription."
    Zhang D., Paley A.J., Childs G.
    J. Biol. Chem. 273:18086-18091(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SF1.
  12. "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing."
    Yang L., Embree L.J., Tsai S., Hickstein D.D.
    J. Biol. Chem. 273:27761-27764(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFRS13A.
  13. "Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode."
    Rappsilber J., Friesen W.J., Paushkin S., Dreyfuss G., Mann M.
    Anal. Chem. 75:3107-3114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-242; ARG-244; ARG-248; ARG-251; ARG-259; ARG-377; ARG-383; ARG-386; ARG-388; ARG-394; ARG-407; ARG-473; ARG-476; ARG-481; ARG-485; ARG-487; ARG-491; ARG-495; ARG-498 AND ARG-503, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Intracellular characterization of DDX39, a novel growth-associated RNA helicase."
    Sugiura T., Sakurai K., Nagano Y.
    Exp. Cell Res. 313:782-790(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SARNP.
  15. "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
    Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
    Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD3.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND THR-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Northeast structural genomics consortium target HR6430A."
    Northeast structural genomics consortium (NESG)
    Submitted (MAY-2011) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 282-370.
  21. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-312.
  22. Cited for: VARIANTS ALS6 CYS-244; SER-514; CYS-515; LYS-518; CYS-521; GLY-521; HIS-521; GLY-522; SER-524; THR-524 AND LEU-525, VARIANT GLN-517, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT ALS6 GLY-521, CHARACTERIZATION OF VARIANT GLN-517.
  23. Cited for: VARIANTS ALS6 GLY-514; CYS-521 AND HIS-521, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ALS6 CYS-521 AND HIS-521.
  24. Cited for: VARIANTS ALS6 SER-191; CYS-216; VAL-225; CYS-230; CYS-234; ASP-507 AND CYS-521.
  25. Cited for: VARIANT ALS6 HIS-521, VARIANT VAL-254.
  26. Cited for: VARIANTS ETM4 CYS-216 AND LEU-431.

Entry informationi

Entry nameiFUS_HUMAN
AccessioniPrimary (citable) accession number: P35637
Secondary accession number(s): Q9H4A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 164 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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