<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. mRNA binding Source: ProtInc

   <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

   • 7692601

2. poly(A) RNA binding Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 22658674
   • 22681889

3. RNA binding Source: ProtInc

   <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

   • 8156595

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. central nervous system development Source: Ensembl
2. mRNA transport Source: UniProtKB-KW
3. negative regulation of translational initiation Source: UniProtKB

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Ligandⁱ

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. cell body Source: Ensembl
2. cytoplasm Source: HGNC

   <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

   • 16407062

3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 15121898

4. cytoplasmic stress granule Source: Ensembl
5. dendritic shaft Source: Ensembl
6. dendritic spine Source: Ensembl
7. membrane Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 19946888

8. microtubule Source: Ensembl
9. mRNA cap binding complex Source: UniProtKB
10. neuronal ribonucleoprotein granule Source: Ensembl
11. nucleolus Source: HGNC

    <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

    • 16407062

12. nucleoplasm Source: ProtInc

    <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ

    • 10888599

13. polysome Source: Ensembl
14. synapse Source: Ensembl

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>Provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim"><span class="caps">OMIM</span></a> database are represented with a <a href="/diseases">controlled vocabulary</a> in the following way:</p><p><a href='../manual/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Fragile X syndrome (FRAX)

[MIM:300624]: Common genetic disease (has a prevalence of one in every 2000 children) which is characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most fragile X syndrome patients results from an amplification of a CGG repeat region which is directly in front of the coding region.3 Publications

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment inⁱ

• Ref.10

  "The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein."
  Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.
  Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]

  Cited for: RNA-BINDING, INVOLVEMENT IN FRAX.
• Ref.12

  "The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation."
  Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.
  Nat. Genet. 4:335-340(1993) [PubMed] [Europe PMC] [Abstract]

  Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN FRAX.
• Ref.31

  "A point mutation in the FMR-1 gene associated with fragile X mental retardation."
  de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J.
  Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract]

  Cited for: VARIANT FRAX ASN-304.

Note: The disease is caused by mutations affecting the gene represented in this entry.

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	304 – 304	1	I → N in FRAX; alters protein folding and stability; the protein is able to bind RNA, but has reduced affinity for RNA at high salt concentrations. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.31 "A point mutation in the FMR-1 gene associated with fragile X mental retardation." de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J. Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FRAX ASN-304.		VAR_005234

Fragile X tremor/ataxia syndrome (FXTAS)

[MIM:300623]: In FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems.1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment inⁱ

• Ref.35

  "Intention tremor, parkinsonism, and generalized brain atrophy in male carriers of fragile X."
  Hagerman R.J., Leehey M., Heinrichs W., Tassone F., Wilson R., Hills J., Grigsby J., Gage B., Hagerman P.J.
  Neurology 57:127-130(2001) [PubMed] [Europe PMC] [Abstract]

  Cited for: INVOLVEMENT IN FXTAS.

Note: The disease is caused by mutations affecting the gene represented in this entry.

Premature ovarian failure 1 (POF1)

[MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment inⁱ

• Ref.15

  "Studies of FRAXA and FRAXE in women with premature ovarian failure."
  Murray A., Webb J., Grimley S., Conway G., Jacobs P.
  J. Med. Genet. 35:637-640(1998) [PubMed] [Europe PMC] [Abstract]

  Cited for: INVOLVEMENT IN POF1.

Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	125 – 126	2	TF → AA: Alters the structural integrity of the N-terminus and leads to aggregation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.29 "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction." Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G., Frenkiel T.A., Bardoni B., Pastore A. Structure 14:21-31(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-134, MUTAGENESIS OF 125-THR-PHE-126, SUBCELLULAR LOCATION, INTERACTION WITH NUFIP2.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	500 – 500	1	S → A: Loss of phosphorylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.17 "Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties." Siomi M.C., Higashijima K., Ishizuka A., Siomi H. Mol. Cell. Biol. 22:8438-8447(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-500, MUTAGENESIS OF SER-500.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	544 – 544	1	R → K: Reduces arginine methylation by 80%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.21 "Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein." Dolzhanskaya N., Merz G., Denman R.B. Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	546 – 546	1	R → K: Slightly reduced methylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.21 "Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein." Dolzhanskaya N., Merz G., Denman R.B. Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Diseaseⁱ

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 632	632	Fragile X mental retardation protein 1		PRO_0000050102	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1 – 1	1	N-acetylmethionine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.27 "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	337 – 337	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	370 – 370	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.25 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	500 – 500	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.17 "Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties." Siomi M.C., Higashijima K., Ishizuka A., Siomi H. Mol. Cell. Biol. 22:8438-8447(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-500, MUTAGENESIS OF SER-500.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	544 – 544	1	Omega-N-methylarginine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.21 "Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein." Dolzhanskaya N., Merz G., Denman R.B. Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.</p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	5 – 23	19	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	25 – 31	7	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	34 – 36	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	40 – 43	4	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	46 – 48	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	64 – 67	4	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	80 – 88	9	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	91 – 98	8	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	105 – 108	4	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	109 – 111	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	121 – 123	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	124 – 126	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2BKD
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	220 – 224	5	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	227 – 229	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	230 – 234	5	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	236 – 238	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	239 – 245	7	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	250 – 256	7	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	257 – 260	4	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	261 – 268	8	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	269 – 279	11	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	281 – 289	9	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	290 – 292	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	293 – 297	5	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	299 – 301	3	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	302 – 311	10	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	314 – 321	8	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	398 – 406	9	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	407 – 422	16	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2QND
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	535 – 538	4	Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei PDB:2LA5

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	4 – 50	47	Agenet-like 1			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	63 – 115	53	Agenet-like 2			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	222 – 251	30	KH 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00117			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	285 – 314	30	KH 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00117			Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	419 – 632	214	Interaction with RANBP9			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	534 – 548	15	RNA-binding RGG-box			Add BLAST

<p>Provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.</p><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (9)ⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry describes 9<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

Note: At least 12 different isoforms are produced.

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS GTNSEASNAS 
       510        520        530        540        550
ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG QGGRGRGGGF 
       560        570        580        590        600
KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS 
       610        620        630 
EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP            

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL 
       410        420        430        440        450
NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKSY VTDDGQGMGR 
       460        470        480        490        500
GSRPYRNRGH GRRGPGYTSG TNSEASNASE TESDHRDELS DWSLAPTEEE 
       510        520        530        540        550
RESFLRRGDG RRRGGGGRGQ GGRGRGGGFK GNDDHSRTDN RPRNPREAKG 
       560        570        580        590 
RTTDGSLQNT SSEGSRLRTG KDRNQKKEKP DSVDGQQPLV NGVP 

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS ESDHRDELSD 
       510        520        530        540        550
WSLAPTEEER ESFLRRGDGR RRGGGGRGQG GRGRGGGFKG NDDHSRTDNR 
       560        570        580        590        600
PRNPREAKGR TTDGSLQIRV DCNNERSVHT KTLQNTSSEG SRLRTGKDRN 
       610        620
QKKEKPDSVD GQQPLVNGVP                                  

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS ESDHRDELSD 
       510        520        530        540        550
WSLAPTEEER ESFLRRGDGR RRGGGGRGQG GRGRGGGFKG NDDHSRTDNR 
       560        570        580        590        600
PRNPREAKGR TTDGSLQNTS SEGSRLRTGK DRNQKKEKPD SVDGQQPLVN 

GVP                                             

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS APTEEERESF 
       510        520        530        540        550
LRRGDGRRRG GGGRGQGGRG RGGGFKGNDD HSRTDNRPRN PREAKGRTTD 
       560        570        580        590        600
GSLQIRVDCN NERSVHTKTL QNTSSEGSRL RTGKDRNQKK EKPDSVDGQQ 

PLVNGVP                                             

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS APTEEERESF 
       510        520        530        540        550
LRRGDGRRRG GGGRGQGGRG RGGGFKGNDD HSRTDNRPRN PREAKGRTTD 
       560        570        580        590
GSLQNTSSEG SRLRTGKDRN QKKEKPDSVD GQQPLVNGVP            

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP 
       410        420        430        440        450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP 
       460        470        480        490        500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS GTNSEASNAS 
       510        520        530        540        550
ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG QGGRGRGGGF 
       560        570        580        590        600
KGNDDHSRTD NRPRNPREAK GRTTDGSLQN TSSEGSRLRT GKDRNQKKEK 
       610 
PDSVDGQQPL VNGVP                                  

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL 
       410        420        430        440        450
NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKSY VTDDGQGMGR 
       460        470        480        490        500
GSRPYRNRGH GRRGPGYTSA PTEEERESFL RRGDGRRRGG GGRGQGGRGR 
       510        520        530        540        550
GGGFKGNDDH SRTDNRPRNP REAKGRTTDG SLQIRVDCNN ERSVHTKTLQ 
       560        570        580 
NTSSEGSRLR TGKDRNQKKE KPDSVDGQQP LVNGVP            

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP 
        60         70         80         90        100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 
       110        120        130        140        150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF 
       160        170        180        190        200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM 
       210        220        230        240        250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 
       260        270        280        290        300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 
       310        320        330        340        350
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP 
       360        370        380        390        400
EEKKHLDIKE NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL 
       410        420        430        440        450
NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKSY VTDDGQGMGR 
       460        470        480        490        500
GSRPYRNRGH GRRGPGYTSG TNSEASNASE TESDHRDELS DWSLAPTEEE 
       510        520        530        540        550
RESFLRRGDG RRRGGGGRGQ GGRGRGGGFK GNDDHSRTDN RPRNPREAKG 
       560        570        580        590        600
RTTDGSLQIR VDCNNERSVH TKTLQNTSSE GSRLRTGKDR NQKKEKPDSV 
       610 
DGQQPLVNGV P                                  

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	294 – 295	2	Missing in AAA52458. (PubMed:1710175)Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	138 – 138	1	R → Q Rare variant found in a developmentally delayed male; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.38 "Identification of novel FMR1 variants by massively parallel sequencing in developmentally delayed males." Collins S.C., Bray S.M., Suhl J.A., Cutler D.J., Coffee B., Zwick M.E., Warren S.T. Am. J. Med. Genet. A 152:2512-2520(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLN-138.		VAR_064507
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	145 – 145	1	A → S. Corresponds to variant rs29281 [ dbSNP | Ensembl ].		VAR_029278
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	304 – 304	1	I → N in FRAX; alters protein folding and stability; the protein is able to bind RNA, but has reduced affinity for RNA at high salt concentrations. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.31 "A point mutation in the FMR-1 gene associated with fragile X mental retardation." de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J. Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FRAX ASN-304.		VAR_005234
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	546 – 546	1	R → H.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.33 "Novel point mutation within intron 10 of FMR-1 gene causing fragile X syndrome." Wang Y.-C., Lin M.-L., Lin S.J., Li Y.-C., Li S.-Y. Hum. Mutat. 10:393-399(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-546.		VAR_005235

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	376 – 396	21	Missing in isoform 1, isoform 8 and isoform 9. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism." Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J. , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M. Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9). Ref.6 "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 8).		VSP_002823	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	491 – 515	25	Missing in isoform 4, isoform 5 and isoform 8. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.6 "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 8).		VSP_002825	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	491 – 502	12	Missing in isoform 2 and isoform 3. Curated		VSP_002824	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	580 – 596	17	Missing in isoform 1, isoform 3, isoform 5 and isoform 7. Curated		VSP_002826	Add BLAST

Sequence databases

Genome annotation databases

Polymorphism databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityⁱ

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome."
   Verkerk A.J.M.H., Pieretti M., Sutcliffe J.S., Fu Y.H., Kuhl D.P., Pizzuti A., Reiner O., Richards S., Victoria M.F., Zhang F., Eussen B.E., van Ommen G.-J.B., Blonden L.A.J., Riggins G.J., Chastain J.L., Kunst C.B., Galjaard H., Caskey C.T.

   , Nelson D.L., Oostra B.A., Warren S.T.
   Cell 65:905-914(1991) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
   Tissue: Fetal brain.
   
2. "Alternative splicing in the fragile X gene FMR1."
   Verkerk A.J.M.H., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A.
   Hum. Mol. Genet. 2:399-404(1993) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY.
   Tissue: Fetal brain and Liver.
   
3. Erratum
   Verkerk A.J.H.M., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A.
   Hum. Mol. Genet. 2:1348-1348(1993) [PubMed] [Europe PMC] [Abstract]
4. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
   Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.

   , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
   Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
   Tissue: Fetal brain.
   
5. "The DNA sequence of the human X chromosome."
   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.

   , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
   Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
6. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.

   , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
7. "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 8).
   Tissue: Placenta.
   
8. "Fine structure of the human FMR1 gene."
   Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
   Hum. Mol. Genet. 2:1147-1153(1993) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34; 36-139; 141-293; 295-490 AND 492-632.
9. Erratum
   Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
   Hum. Mol. Genet. 3:684-685(1994) [PubMed] [Europe PMC] [Abstract]
10. Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 18-34.
11. "Two new cases of FMR1 deletion associated with mental impairment."
    Hirst M., Grewal P., Flannery A., Slatter R., Maher E., Barton D., Fryns J.-P., Davies K.
    Am. J. Hum. Genet. 56:67-74(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
12. "The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein."
    Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.
    Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, INVOLVEMENT IN FRAX.
13. "Characterization and localization of the FMR-1 gene product associated with fragile X syndrome."
    Verheij C., Bakker C.E., de Graaff E., Keulemans J., Willemsen R., Verkerk A.J.M.H., Galjaard H., Reuser A.J.J., Hoogeveen A.T., Oostra B.A.
    Nature 363:722-724(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
14. "The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation."
    Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.
    Nat. Genet. 4:335-340(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN FRAX.
15. "FMR1 protein: conserved RNP family domains and selective RNA binding."
    Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T.
    Science 262:563-566(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
16. "FXR1, an autosomal homolog of the fragile X mental retardation gene."
    Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L., Dreyfuss G.
    EMBO J. 14:2401-2408(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, SUBCELLULAR LOCATION.
17. "Studies of FRAXA and FRAXE in women with premature ovarian failure."
    Murray A., Webb J., Grimley S., Conway G., Jacobs P.
    J. Med. Genet. 35:637-640(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN POF1.
18. "A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein."
    Bardoni B., Schenck A., Mandel J.-L.
    Hum. Mol. Genet. 8:2557-2566(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUFIP1.
19. "Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties."
    Siomi M.C., Higashijima K., Ishizuka A., Siomi H.
    Mol. Cell. Biol. 22:8438-8447(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-500, MUTAGENESIS OF SER-500.
20. "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization."
    Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.
    Hum. Mol. Genet. 12:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUFIP2, SUBCELLULAR LOCATION.
21. "Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs."
    Rackham O., Brown C.M.
    EMBO J. 23:3346-3355(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A RNP GRANULE COMPLEX WITH IGF2BP1, INTERACTION WITH IGF2BP1.
22. "The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
    Menon R.P., Gibson T.J., Pastore A.
    J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP9.
23. "Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein."
    Dolzhanskaya N., Merz G., Denman R.B.
    Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.
24. "The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons."
    Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A., Bardoni B., Khandjian E.W.
    Hum. Mol. Genet. 15:1525-1538(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCRS1, SUBCELLULAR LOCATION.
25. "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.
26. "In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein."
    Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.
    J. Biol. Chem. 283:5598-5610(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMN AND THE SMN CORE COMPLEX.
27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
    
28. "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].
29. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
30. "The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome."
    Musco G., Kharrat A., Stier G., Fraternali F., Gibson T.J., Nilges M., Pastore A.
    Nat. Struct. Biol. 4:712-716(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 216-280.
31. "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction."
    Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G., Frenkiel T.A., Bardoni B., Pastore A.
    Structure 14:21-31(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-134, MUTAGENESIS OF 125-THR-PHE-126, SUBCELLULAR LOCATION, INTERACTION WITH NUFIP2.
32. "Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein."
    Valverde R., Pozdnyakova I., Kajander T., Venkatraman J., Regan L.
    Structure 15:1090-1098(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 397-425, CHARACTERIZATION OF VARIANT FRAX ASN-304.
33. "A point mutation in the FMR-1 gene associated with fragile X mental retardation."
    de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J.
    Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FRAX ASN-304.
34. "Characterization of FMR1 proteins isolated from different tissues."
    Verheij C., de Graaff E., Bakker C.E., Willemsen R., Willems P.J., Meijer N., Galjaard H., Reuser A.J.J., Oostra B.A., Hoogeveen A.T.
    Hum. Mol. Genet. 4:895-901(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF FRAX ASN-304.
35. "Novel point mutation within intron 10 of FMR-1 gene causing fragile X syndrome."
    Wang Y.-C., Lin M.-L., Lin S.J., Li Y.-C., Li S.-Y.
    Hum. Mutat. 10:393-399(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-546.
36. "FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association."
    Feng Y., Absher D., Eberhart D.E., Brown V., Malter H.E., Warren S.T.
    Mol. Cell 1:109-118(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
37. "Intention tremor, parkinsonism, and generalized brain atrophy in male carriers of fragile X."
    Hagerman R.J., Leehey M., Heinrichs W., Tassone F., Wilson R., Hills J., Grigsby J., Gage B., Hagerman P.J.
    Neurology 57:127-130(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FXTAS.
38. "Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes."
    Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A., Eddy S.R., Darnell R.B.
    Genes Dev. 19:903-918(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
39. "Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP."
    Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., Meister G., Keidel E., Fischer U.
    Hum. Mol. Genet. 17:3236-3246(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304, SUBUNIT, INTERACTION WITH TDRD3.
40. "Identification of novel FMR1 variants by massively parallel sequencing in developmentally delayed males."
    Collins S.C., Bray S.M., Suhl J.A., Cutler D.J., Coffee B., Zwick M.E., Warren S.T.
    Am. J. Med. Genet. A 152:2512-2520(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLN-138.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Miscellaneous

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. Human chromosome X
   Human chromosome X: 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

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ