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P35637 (FUS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein FUS
Alternative name(s):
75 kDa DNA-pairing protein
Oncogene FUS
Oncogene TLS
POMp75
Translocated in liposarcoma protein
Gene names
Name:FUS
Synonyms:TLS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP. Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Nucleus Ref.22 Ref.23.

Tissue specificity

Ubiquitous.

Post-translational modification

Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine. Ref.13

Involvement in disease

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. Ref.22 Ref.23 Ref.24 Ref.25

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. Ref.26

Sequence similarities

Belongs to the RRM TET family.

Contains 1 RanBP2-type zinc finger.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P35637-1)

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.
Isoform Short (identifier: P35637-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526RNA-binding protein FUS
PRO_0000081591

Regions

Domain285 – 37187RRM
Zinc finger422 – 45332RanBP2-type
Compositional bias1 – 165165Gln/Gly/Ser/Tyr-rich
Compositional bias166 – 267102Gly-rich
Compositional bias371 – 526156Arg/Gly-rich

Sites

Site1751Breakpoint for translocation to form chimeric FUS/ATF1 protein
Site266 – 2672Breakpoint for translocation to form FUS/TLS-CHOP oncogene

Amino acid modifications

Modified residue2211Phosphoserine Ref.18
Modified residue2421Asymmetric dimethylarginine Ref.13
Modified residue2441Asymmetric dimethylarginine Ref.13
Modified residue2481Asymmetric dimethylarginine Ref.13
Modified residue2511Asymmetric dimethylarginine Ref.13
Modified residue2591Asymmetric dimethylarginine Ref.13
Modified residue2771Phosphoserine Ref.16
Modified residue2861Phosphothreonine Ref.16
Modified residue3771Asymmetric dimethylarginine Ref.13
Modified residue3831Asymmetric dimethylarginine Ref.13
Modified residue3861Asymmetric dimethylarginine Ref.13
Modified residue3881Asymmetric dimethylarginine Ref.13
Modified residue3941Asymmetric dimethylarginine Ref.13
Modified residue4071Asymmetric dimethylarginine Ref.13
Modified residue4731Asymmetric dimethylarginine Ref.13
Modified residue4761Asymmetric dimethylarginine Ref.13
Modified residue4811Asymmetric dimethylarginine Ref.13
Modified residue4851Asymmetric dimethylarginine Ref.13
Modified residue4871Asymmetric dimethylarginine Ref.13
Modified residue4911Asymmetric dimethylarginine Ref.13
Modified residue4951Asymmetric dimethylarginine Ref.13
Modified residue4981Asymmetric dimethylarginine Ref.13
Modified residue5031Asymmetric dimethylarginine Ref.13

Natural variations

Alternative sequence64 – 652TG → S in isoform Short.
VSP_005798
Natural variant1911G → S in ALS6. Ref.24
VAR_068918
Natural variant2161R → C in ALS6 and ETM4. Ref.24 Ref.26
VAR_068919
Natural variant2251G → V in ALS6. Ref.24
VAR_068920
Natural variant2301G → C in ALS6. Ref.24
VAR_068921
Natural variant2341R → C in ALS6. Ref.24
VAR_068922
Natural variant2441R → C in ALS6. Ref.22
VAR_054837
Natural variant2541M → V Found in a patient with frontotemporal lobar degeneration. Ref.25
VAR_065229
Natural variant3121K → Q in a breast cancer sample; somatic mutation. Ref.21
VAR_035481
Natural variant4311P → L in ETM4. Ref.26
Corresponds to variant rs186547381 [ dbSNP | Ensembl ].
VAR_068923
Natural variant5071G → D in ALS6. Ref.24
VAR_068924
Natural variant5141R → G in ALS6. Ref.23
VAR_054838
Natural variant5141R → S in ALS6. Ref.22
VAR_054839
Natural variant5151G → C in ALS6. Ref.22
VAR_054840
Natural variant5171H → Q Does not affect protein nuclear localization. Ref.22
VAR_054841
Natural variant5181R → K in ALS6. Ref.22
VAR_054842
Natural variant5211R → C in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.22 Ref.23 Ref.24
VAR_054843
Natural variant5211R → G in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.22
VAR_054844
Natural variant5211R → H in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.22 Ref.23 Ref.25
VAR_054845
Natural variant5221R → G in ALS6. Ref.22
VAR_054846
Natural variant5241R → S in ALS6. Ref.22
VAR_054847
Natural variant5241R → T in ALS6. Ref.22
VAR_054848
Natural variant5251P → L in ALS6. Ref.22
VAR_054849

Experimental info

Sequence conflict3381T → N AA sequence Ref.7

Secondary structure

...................... 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 88C8E263B7905549

FASTA52653,426
        10         20         30         40         50         60 
MASNDYTQQA TQSYGAYPTQ PGQGYSQQSS QPYGQQSYSG YSQSTDTSGY GQSSYSSYGQ 

        70         80         90        100        110        120 
SQNTGYGTQS TPQGYGSTGG YGSSQSSQSS YGQQSSYPGY GQQPAPSSTS GSYGSSSQSS 

       130        140        150        160        170        180 
SYGQPQSGSY SQQPSYGGQQ QSYGQQQSYN PPQGYGQQNQ YNSSSGGGGG GGGGGNYGQD 

       190        200        210        220        230        240 
QSSMSSGGGS GGGYGNQDQS GGGGSGGYGQ QDRGGRGRGG SGGGGGGGGG GYNRSSGGYE 

       250        260        270        280        290        300 
PRGRGGGRGG RGGMGGSDRG GFNKFGGPRD QGSRHDSEQD NSDNNTIFVQ GLGENVTIES 

       310        320        330        340        350        360 
VADYFKQIGI IKTNKKTGQP MINLYTDRET GKLKGEATVS FDDPPSAKAA IDWFDGKEFS 

       370        380        390        400        410        420 
GNPIKVSFAT RRADFNRGGG NGRGGRGRGG PMGRGGYGGG GSGGGGRGGF PSGGGGGGGQ 

       430        440        450        460        470        480 
QRAGDWKCPN PTCENMNFSW RNECNQCKAP KPDGPGGGPG GSHMGGNYGD DRRGGRGGYD 

       490        500        510        520 
RGGYRGRGGD RGGFRGGRGG GDRGGFGPGK MDSRGEHRQD RRERPY 

« Hide

Isoform Short [UniParc].

Checksum: 949558C718B4C19B
Show »

FASTA52553,355

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-312.
[22]"Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis."
Kwiatkowski T.J. Jr., Bosco D.A., Leclerc A.L., Tamrazian E., Vanderburg C.R., Russ C., Davis A., Gilchrist J., Kasarskis E.J., Munsat T., Valdmanis P., Rouleau G.A., Hosler B.A., Cortelli P., de Jong P.J., Yoshinaga Y., Haines J.L., Pericak-Vance M.A. expand/collapse author list , Yan J., Ticozzi N., Siddique T., McKenna-Yasek D., Sapp P.C., Horvitz H.R., Landers J.E., Brown R.H. Jr.
Science 323:1205-1208(2009) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6."
Vance C., Rogelj B., Hortobagyi T., De Vos K.J., Nishimura A.L., Sreedharan J., Hu X., Smith B., Ruddy D., Wright P., Ganesalingam J., Williams K.L., Tripathi V., Al-Saraj S., Al-Chalabi A., Leigh P.N., Blair I.P., Nicholson G. expand/collapse author list , de Belleroche J., Gallo J.M., Miller C.C., Shaw C.E.
Science 323:1208-1211(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS6 GLY-514; CYS-521 AND HIS-521, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ALS6 CYS-521 AND HIS-521.
[24]"Mutations of FUS gene in sporadic amyotrophic lateral sclerosis."
Corrado L., Del Bo R., Castellotti B., Ratti A., Cereda C., Penco S., Soraru G., Carlomagno Y., Ghezzi S., Pensato V., Colombrita C., Gagliardi S., Cozzi L., Orsetti V., Mancuso M., Siciliano G., Mazzini L., Comi G.P. expand/collapse author list , Gellera C., Ceroni M., D'Alfonso S., Silani V.
J. Med. Genet. 47:190-194(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS6 SER-191; CYS-216; VAL-225; CYS-230; CYS-234; ASP-507 AND CYS-521.
[25]"Genetic contribution of FUS to frontotemporal lobar degeneration."
Van Langenhove T., van der Zee J., Sleegers K., Engelborghs S., Vandenberghe R., Gijselinck I., Van den Broeck M., Mattheijssens M., Peeters K., De Deyn P.P., Cruts M., Van Broeckhoven C.
Neurology 74:366-371(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS6 HIS-521, VARIANT VAL-254.
[26]"Exome sequencing identifies fus mutations as a cause of essential tremor."
Merner N.D., Girard S.L., Catoire H., Bourassa C.V., Belzil V.V., Riviere J.B., Hince P., Levert A., Dionne-Laporte A., Spiegelman D., Noreau A., Diab S., Szuto A., Fournier H., Raelson J., Belouchi M., Panisset M., Cossette P. expand/collapse author list , Dupre N., Bernard G., Chouinard S., Dion P.A., Rouleau G.A.
Am. J. Hum. Genet. 91:313-319(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ETM4 CYS-216 AND LEU-431.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10707.1. [P35637-1]
CCDS58454.1. [P35637-2]
PIRS33798.
S33799.
RefSeqNP_001164105.1. NM_001170634.1. [P35637-2]
NP_004951.1. NM_004960.3. [P35637-1]
UniGeneHs.46894.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LA6NMR-A282-370[»]
2LCWNMR-A278-385[»]
4FDDX-ray2.30B498-526[»]
4FQ3X-ray3.00B495-526[»]
ProteinModelPortalP35637.
SMRP35637. Positions 278-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108797. 114 interactions.
DIPDIP-29857N.
IntActP35637. 46 interactions.
MINTMINT-5005976.
STRING9606.ENSP00000254108.

PTM databases

PhosphoSiteP35637.

Polymorphism databases

DMDM544357.

Proteomic databases

MaxQBP35637.
PaxDbP35637.
PRIDEP35637.

Protocols and materials databases

DNASU2521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254108; ENSP00000254108; ENSG00000089280. [P35637-1]
ENST00000380244; ENSP00000369594; ENSG00000089280. [P35637-2]
GeneID2521.
KEGGhsa:2521.
UCSCuc002ebe.2. human. [P35637-1]
uc002ebh.3. human. [P35637-2]

Organism-specific databases

CTD2521.
GeneCardsGC16P031191.
GeneReviewsFUS.
HGNCHGNC:4010. FUS.
HPACAB033036.
CAB058691.
HPA008784.
MIM137070. gene.
608030. phenotype.
612160. phenotype.
614782. phenotype.
neXtProtNX_P35637.
Orphanet803. 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.
PharmGKBPA28425.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240581.
HOGENOMHOG000038010.
HOVERGENHBG095056.
InParanoidP35637.
KOK13098.
OrthoDBEOG7DZ8N7.
PhylomeDBP35637.
TreeFamTF322599.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP35637.
BgeeP35637.
CleanExHS_FUS.
GenevestigatorP35637.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFUS. human.
GeneWikiFUS.
GenomeRNAi2521.
NextBio9927.
PROP35637.
SOURCESearch...

Entry information

Entry nameFUS_HUMAN
AccessionPrimary (citable) accession number: P35637
Secondary accession number(s): Q9H4A8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM