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P35637

- FUS_HUMAN

UniProt

P35637 - FUS_HUMAN

Protein

RNA-binding protein FUS

Gene

FUS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

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

    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

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 FUSPRO_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.

    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

    1
    526
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini285 – 37187RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the RRM TET family.Curated
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri422 – 45332RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti338 – 3381T → N AA sequence (PubMed:10567410)Curated

    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. 1 PublicationVSP_005798

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 165 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