P35637 (FUS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15 Ref.16
Subcellular location	Nucleus Ref.21 Ref.22.
Tissue specificity	Ubiquitous.
Post-translational modification	Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine. Ref.13 Ref.14
Involvement in disease	Note=A chromosomal aberration involving FUS is found in a patient with malignant myxoid liposarcoma. Translocation t(12;16)(q13;p11) with DDIT3. Note=A chromosomal aberration involving FUS is a cause of acute myeloid leukemia (AML). Translocation t(16;21)(p11;q22) with ERG. Defects in FUS may be a cause of 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=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. Defects in FUS are the cause of amyotrophic lateral sclerosis type 6 (ALS6) [MIM:608030]. ALS6 is a familial form of amyotrophic lateral sclerosis. ALS is 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. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10%. Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the RRM TET family. Contains 1 RanBP2-type zinc finger. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Amyotrophic lateral sclerosis Disease mutation Neurodegeneration Proto-oncogene
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW nuclear mRNA splicing, via spliceosome Traceable author statement. Source: Reactome
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.12. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TP63	Q9H3D4	2	EBI-400434,EBI-2337775

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 526

526

RNA-binding protein FUS

PRO_0000081591

Regions

Domain

285 – 371

87

RRM

Zinc finger

422 – 453

32

RanBP2-type

Compositional bias

1 – 165

165

Gln/Gly/Ser/Tyr-rich

Compositional bias

166 – 267

102

Gly-rich

Compositional bias

371 – 526

156

Arg/Gly-rich

Sites

Site

175

1

Breakpoint for translocation to form chimeric FUS/ATF1 protein

Site

266 – 267

2

Breakpoint for translocation to form FUS/TLS-CHOP oncogene

Amino acid modifications

Modified residue

216

1

Omega-N-methylated arginine Ref.14

Modified residue

218

1

Omega-N-methylated arginine Ref.14

Modified residue

277

1

Phosphoserine Ref.17

Modified residue

286

1

Phosphothreonine Ref.17

Modified residue

346

1

Phosphoserine Ref.17

Natural variations

Alternative sequence

64 – 65

2

TG → S in isoform Short.

VSP_005798

Natural variant

244

1

R → C in ALS6. Ref.21

VAR_054837

Natural variant

254

1

M → V Found in a patient with frontotemporal lobar degeneration. Ref.23

VAR_065229

Natural variant

312

1

K → Q in a breast cancer sample; somatic mutation. Ref.20

VAR_035481

Natural variant

514

1

R → G in ALS6. Ref.22

VAR_054838

Natural variant

514

1

R → S in ALS6. Ref.21

VAR_054839

Natural variant

515

1

G → C in ALS6. Ref.21

VAR_054840

Natural variant

517

1

H → Q Does not affect protein nuclear localization. Ref.21

VAR_054841

Natural variant

518

1

R → K in ALS6. Ref.21

VAR_054842

Natural variant

521

1

R → C in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.21 Ref.22

VAR_054843

Natural variant

521

1

R → G in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.21

VAR_054844

Natural variant

521

1

R → H in ALS6; results in aberrant trafficking and cytoplasmic retention of the protein. Ref.21 Ref.22 Ref.23

VAR_054845

Natural variant

522

1

R → G in ALS6. Ref.21

VAR_054846

Natural variant

524

1

R → S in ALS6. Ref.21

VAR_054847

Natural variant

524

1

R → T in ALS6. Ref.21

VAR_054848

Natural variant

525

1

P → L in ALS6. Ref.21

VAR_054849

Experimental info

Sequence conflict

338

1

T → N AA sequence Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

526

Helix Strand Turn

Details...

Beta strand

285 – 290

6

Helix

298 – 305

8

Beta strand

320 – 326

7

Beta strand

336 – 343

8

Helix

344 – 354

11

Beta strand

365 – 368

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 88C8E263B7905549	FASTA	526	53,426
	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
	Isoform Short [UniParc]. Checksum: 949558C718B4C19B	FASTA	525	53,355
	10 20 30 40 50 60 MASNDYTQQA TQSYGAYPTQ PGQGYSQQSS QPYGQQSYSG YSQSTDTSGY GQSSYSSYGQ 70 80 90 100 110 120 SQNSYGTQST PQGYGSTGGY GSSQSSQSSY GQQSSYPGYG QQPAPSSTSG SYGSSSQSSS 130 140 150 160 170 180 YGQPQSGSYS QQPSYGGQQQ SYGQQQSYNP PQGYGQQNQY NSSSGGGGGG GGGGNYGQDQ 190 200 210 220 230 240 SSMSSGGGSG GGYGNQDQSG GGGSGGYGQQ DRGGRGRGGS GGGGGGGGGG YNRSSGGYEP 250 260 270 280 290 300 RGRGGGRGGR GGMGGSDRGG FNKFGGPRDQ GSRHDSEQDN SDNNTIFVQG LGENVTIESV 310 320 330 340 350 360 ADYFKQIGII KTNKKTGQPM INLYTDRETG KLKGEATVSF DDPPSAKAAI DWFDGKEFSG 370 380 390 400 410 420 NPIKVSFATR RADFNRGGGN GRGGRGRGGP MGRGGYGGGG SGGGGRGGFP SGGGGGGGQQ 430 440 450 460 470 480 RAGDWKCPNP TCENMNFSWR NECNQCKAPK PDGPGGGPGG SHMGGNYGDD RRGGRGGYDR 490 500 510 520 GGYRGRGGDR GGFRGGRGGG DRGGFGPGKM DSRGEHRQDR RERPY

References

	« Hide 'large scale' referencesShow '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: 8510758] [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: 7503811] [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: 9795213] [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: 15616553] [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: 15489334] [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: 11063792] [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: 10567410] [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 prolifieration." Bertrand P., Akhmedov A.T., Delacote F., Durrbach A., Lopez B.S. Oncogene 18:4515-4521(1999) [PubMed: 10442642] [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, 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: 8187069] [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: 9660765] [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: 9774382] [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: 12964758] [Abstract] Cited for: METHYLATION.
[14]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-216 AND ARG-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Intracellular characterization of DDX39, a novel growth-associated RNA helicase." Sugiura T., Sakurai K., Nagano Y. Exp. Cell Res. 313:782-790(2007) [PubMed: 17196963] [Abstract] Cited for: INTERACTION WITH SARNP.
[16]	"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: 18632687] [Abstract] Cited for: INTERACTION WITH TDRD3.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; THR-286 AND SER-346, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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.
[20]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-312.
[21]	"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. , 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: 19251627] [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.
[22]	"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. , de Belleroche J., Gallo J.M., Miller C.C., Shaw C.E. Science 323:1208-1211(2009) [PubMed: 19251628] [Abstract] Cited for: VARIANTS ALS6 GLY-514; CYS-521 AND HIS-521, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ALS6 CYS-521 AND HIS-521.
[23]	"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: 20124201] [Abstract] Cited for: VARIANT ALS6 HIS-521, VARIANT VAL-254.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00221354.
IPI00260715.

PIR

S33798.
S33799.

RefSeq

NP_001164105.1. NM_001170634.1.
NP_004951.1. NM_004960.3.

UniGene

Hs.46894.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LA6	NMR	-	A	282-370	[»]

ProteinModelPortal

P35637.

SMR

P35637. Positions 283-370, 417-455.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29857N.

IntAct

P35637. 28 interactions.

MINT

MINT-5005976.

STRING

P35637.

PTM databases

PhosphoSite

P35637.

Polymorphism databases

DMDM

544357.

Proteomic databases

PRIDE

P35637.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254108; ENSP00000254108; ENSG00000089280.

GeneID

2521.

KEGG

hsa:2521.

UCSC

uc002ebf.1. human.
uc002ebh.1. human.

Organism-specific databases

CTD

2521.

GeneCards

GC16P031191.

H-InvDB

HIX0012983.

HGNC

HGNC:4010. FUS.

HPA

HPA008784.

MIM

137070. gene.
608030. phenotype.
612160. phenotype.

neXtProt

NX_P35637.

Orphanet

803. Amyotrophic lateral sclerosis.
282. Frontotemporal dementia.
79105. Myxofibrosarcoma.
99967. Myxoid liposarcoma.

PharmGKB

PA28425.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17659.

HOVERGEN

HBG095056.

InParanoid

P35637.

OMA

QYNSSGG.

OrthoDB

EOG4DV5NH.

PhylomeDB

P35637.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P35637.

Bgee

P35637.

CleanEx

HS_FUS.

Genevestigator

P35637.

GermOnline

ENSG00000089280. Homo sapiens.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

KO

K13098.

Pfam

PF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

9927.

SOURCE

Search...

Entry information

Entry name

FUS_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.