UniProtKB - Q06787 (FMR1_HUMAN)
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- BLAST>sp|Q06787|FMR1_HUMAN Synaptic functional regulator FMR1 OS=Homo sapiens OX=9606 GN=FMR1 PE=1 SV=1 MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDIN ESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKP ATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKR AHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGAN IQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKN GKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKE NSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYH LNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRG HGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRG QGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSS EGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
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Synaptic functional regulator FMR1
FMR1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
30 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 FXS. - Ref.13"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: ASSOCIATION IN MRNP, RNA-BINDING. - Ref.14"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. - Ref.23"Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function."
Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T., Darnell R.B.
Cell 107:489-499(2001) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN. - Ref.24"The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif."
Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., Moine H.
EMBO J. 20:4803-4813(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.25"Evidence that fragile X mental retardation protein is a negative regulator of translation."
Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U.
Hum. Mol. Genet. 10:329-338(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FXR1 AND FXR2, SUBUNIT, RNA-BINDING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.28"The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding."
Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B., Mandel J.L., Pastore A.
Biochemistry 42:10437-10444(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, RNA-BINDING, DOMAIN. - Ref.31"The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo."
Sung Y.J., Dolzhanskaya N., Nolin S.L., Brown T., Currie J.R., Denman R.B.
J. Biol. Chem. 278:15669-15678(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME. - Ref.33"The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences."
Chen L., Yun S.W., Seto J., Liu W., Toth M.
Neuroscience 120:1005-1017(2003) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING. - Ref.34"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: INTERACTION WITH IGF2BP1, RNA-BINDING. - Ref.35"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: RNA-BINDING, INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, DOMAIN. - Ref.36"Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway."
Jin P., Zarnescu D.C., Ceman S., Nakamoto M., Mowrey J., Jongens T.A., Nelson D.L., Moses K., Warren S.T.
Nat. Neurosci. 7:113-117(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ASSOCIATION WITH MICRORNA, INTERACTION WITH AGO2. - Ref.43"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 FXS ASN-304, RNA-BINDING, DOMAIN. - Ref.46"Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs."
Plante I., Davidovic L., Ouellet D.L., Gobeil L.A., Tremblay S., Khandjian E.W., Provost P.
J. Biomed. Biotechnol. 2006:64347-64347(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.48"Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses."
Antar L.N., Li C., Zhang H., Carroll R.C., Bassell G.J.
Mol. Cell. Neurosci. 32:37-48(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.49"A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability."
Zalfa F., Eleuteri B., Dickson K.S., Mercaldo V., De Rubeis S., di Penta A., Tabolacci E., Chiurazzi P., Neri G., Grant S.G., Bagni C.
Nat. Neurosci. 10:578-587(2007) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING. - Ref.53"The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer."
Didiot M.C., Tian Z., Schaeffer C., Subramanian M., Mandel J.L., Moine H.
Nucleic Acids Res. 36:4902-4912(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING. - Ref.54"Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA."
Menon L., Mader S.A., Mihailescu M.R.
RNA 14:1644-1655(2008) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN. - Ref.55"Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein."
Faehling M., Mrowka R., Steege A., Kirschner K.M., Benko E., Foerstera B., Persson P.B., Thiele B.J., Meier J.C., Scholz H.
J. Biol. Chem. 284:4255-4266(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME AND MRNP. - Ref.56"Fragile X mental retardation protein FMRP binds mRNAs in the nucleus."
Kim M., Bellini M., Ceman S.
Mol. Cell. Biol. 29:214-228(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NXF1, RNA-BINDING, SUBCELLULAR LOCATION. - Ref.57"A novel function for fragile X mental retardation protein in translational activation."
Bechara E.G., Didiot M.C., Melko M., Davidovic L., Bensaid M., Martin P., Castets M., Pognonec P., Khandjian E.W., Moine H., Bardoni B.
PLoS Biol. 7:E16-E16(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.58"Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack."
Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G., Sigworth F.J., Navaratnam D., Kaczmarek L.K.
Nat. Neurosci. 13:819-821(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KCNT1. - Ref.59"FMRP targets distinct mRNA sequence elements to regulate protein expression."
Ascano M. Jr., Mukherjee N., Bandaru P., Miller J.B., Nusbaum J.D., Corcoran D.L., Langlois C., Munschauer M., Dewell S., Hafner M., Williams Z., Ohler U., Tuschl T.
Nature 492:382-386(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.60"FMRP and myelin protein expression in oligodendrocytes."
Giampetruzzi A., Carson J.H., Barbarese E.
Mol. Cell. Neurosci. 56:333-341(2013) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF FUNCTION, TISSUE SPECIFICITY. - Ref.62"A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response."
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y.
Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN, CHARACTERIZATION OF VARIANT FXS GLN-138, MUTAGENESIS OF THR-102 AND TYR-103. - Ref.63"MOV10 and FMRP regulate AGO2 association with microRNA recognition elements."
Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J., Arcila M.L., Kosik K.S., Ceman S.
Cell Rep. 9:1729-1741(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MOV10, RNA-BINDING. - Ref.66"FMRP interacts with G-quadruplex structures in the 3'-UTR of its dendritic target Shank1 mRNA."
Zhang Y., Gaetano C.M., Williams K.R., Bassell G.J., Mihailescu M.R.
RNA Biol. 11:1364-1374(2014) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN, MUTAGENESIS OF SER-500. - Ref.71"Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome."
Siomi H., Choi M., Siomi M.C., Nussbaum R.L., Dreyfuss G.
Cell 77:33-39(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, RNA-BINDING. - Ref.77"Fragile X syndrome due to a missense mutation."
Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X., Warren S.T.
Eur. J. Hum. Genet. 22:1185-1189(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLU-266, CHARACTERIZATION OF VARIANT FXS GLU-266, RNA-BINGING, ASSOCIATION WITH POLYRIBOSOME. - Ref.78"Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLN-138, CHARACTERIZATION OF VARIANT FXS GLN-138, FUNCTION, INTERACTION WITH KCNMB4, DOMAIN.
<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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
<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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
<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.64"Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus."
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.
Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP (MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FXS ASN-304 (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION).
Miscellaneous
<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><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- chromatin binding Source: UniProtKB
- dynein complex binding Source: UniProtKB
- G-quadruplex 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
- identical protein 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
- ion channel binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- methylated histone 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
- microtubule binding Source: UniProtKB
- miRNA 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
- mRNA 3'-UTR 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
- mRNA 5'-UTR 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
- mRNA 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
- poly(G) 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
- poly(U) 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
- protein heterodimerization activity 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
- protein homodimerization activity 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
- ribosome binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- 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
- RNA stem-loop 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
- RNA strand annealing activity 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
- sequence-specific mRNA 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
- siRNA 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
- translation initiation factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- translation repressor activity 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
<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><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular response to DNA damage stimulus 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
- cellular response to hydroxyurea Source: UniProtKB
- cellular response to UV Source: UniProtKB
- cellular response to virus 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
- gene silencing by RNA Source: UniProtKB-KW
- glutamate receptor signaling pathway Source: UniProtKB
- modulation by host of viral RNA genome replication Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- mRNA processing Source: UniProtKB-KW
- mRNA transport Source: UniProtKB
- negative regulation of cytoplasmic translation Source: UniProtKB
- negative regulation of long term synaptic depression Source: UniProtKB
- negative regulation of mRNA catabolic process Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of synaptic vesicle exocytosis Source: UniProtKB
- negative regulation of translational initiation Source: UniProtKB
- negative regulation of voltage-gated calcium channel activity Source: UniProtKB
- positive regulation of dendritic spine development Source: UniProtKB
- positive regulation of filopodium assembly Source: UniProtKB
- positive regulation of gene silencing by miRNA 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
- positive regulation of histone phosphorylation 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
- positive regulation of intracellular transport of viral material Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of mRNA 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
- positive regulation of proteasomal protein catabolic process Source: UniProtKB
- positive regulation of receptor internalization 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
- positive regulation of response to DNA damage stimulus 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
- positive regulation of translation 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
- regulation of alternative mRNA splicing, via spliceosome 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
- regulation of dendritic spine development 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
- regulation of filopodium assembly 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
- regulation of gene silencing by miRNA Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of mRNA stability Source: UniProtKB
- regulation of neuronal action potential 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
- regulation of neurotransmitter secretion Source: UniProtKB
- RNA splicing Source: UniProtKB-KW
- viral process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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>Keywordsi
| Molecular function | Activator, Repressor, Ribonucleoprotein, RNA-binding |
| Biological process | DNA damage, Host-virus interaction, mRNA processing, mRNA splicing, mRNA transport, Neurogenesis, RNA-mediated gene silencing, Translation regulation, Transport |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q06787 |
<p>This section 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><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Synaptic functional regulator FMR1CuratedAlternative name(s): Fragile X mental retardation protein 1Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Short name: FMRP1 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
Short name: Protein FMR-11 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
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102081.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3775 FMR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 309550 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q06787 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- postsynaptic cell membrane By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- presynaptic cell membrane By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Cell membrane By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- postsynaptic cell membrane By similarity
Nucleus
- Nucleus 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.20"Different targets for the fragile X-related proteins revealed by their distinct nuclear localizations."
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B., Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 8:863-869(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.45"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, ASSOCIATION WITH POLYRIBOSOME, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-500. - Ref.56"Fragile X mental retardation protein FMRP binds mRNAs in the nucleus."
Kim M., Bellini M., Ceman S.
Mol. Cell. Biol. 29:214-228(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NXF1, RNA-BINDING, SUBCELLULAR LOCATION.
- nucleolus 4 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.29"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. - Ref.45"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, ASSOCIATION WITH POLYRIBOSOME, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-500. - Ref.65"Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin."
Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L., Piekorz R.P., Ahmadian M.R.
PLoS ONE 9:E91465-E91465(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CYFIP2; EIF5; NCL AND RPLP0 (ISOFORM 6), SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 527-ARG--ARG-534 AND 613-GLN--LYS-617. - Ref.68"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.
- Nucleus 3 Publications
Other locations
- centromere By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Chromosome By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Cytoplasm 7 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.11"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, TISSUE SPECIFICITY. - 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 FXS. - Ref.14"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. - Ref.20"Different targets for the fragile X-related proteins revealed by their distinct nuclear localizations."
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B., Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 8:863-869(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.29"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. - Ref.51"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: SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.56"Fragile X mental retardation protein FMRP binds mRNAs in the nucleus."
Kim M., Bellini M., Ceman S.
Mol. Cell. Biol. 29:214-228(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NXF1, RNA-BINDING, SUBCELLULAR LOCATION.
- perinuclear region 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.65"Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin."
Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L., Piekorz R.P., Ahmadian M.R.
PLoS ONE 9:E91465-E91465(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CYFIP2; EIF5; NCL AND RPLP0 (ISOFORM 6), SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 527-ARG--ARG-534 AND 613-GLN--LYS-617.
- Cytoplasmic ribonucleoprotein granule 6 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.18"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: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.26"Transport of fragile X mental retardation protein via granules in neurites of PC12 cells."
De Diego Otero Y., Severijnen L.A., van Cappellen G., Schrier M., Oostra B., Willemsen R.
Mol. Cell. Biol. 22:8332-8341(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.30"Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs."
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.
Hum. Mol. Genet. 12:3087-3096(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, MUTAGENESIS OF SER-500. - Ref.47"Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP."
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.
J. Cell Sci. 119:1933-1946(2006) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION.
- Perikaryon 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.26"Transport of fragile X mental retardation protein via granules in neurites of PC12 cells."
De Diego Otero Y., Severijnen L.A., van Cappellen G., Schrier M., Oostra B., Willemsen R.
Mol. Cell. Biol. 22:8332-8341(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION.
- Cell projection 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.26"Transport of fragile X mental retardation protein via granules in neurites of PC12 cells."
De Diego Otero Y., Severijnen L.A., van Cappellen G., Schrier M., Oostra B., Willemsen R.
Mol. Cell. Biol. 22:8332-8341(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION.
- axon By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- dendrite By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- dendritic spine By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- synaptosome By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- growth cone 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.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION.
- filopodium tip By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- synapse By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Stress granule 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.47"Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP."
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.
J. Cell Sci. 119:1933-1946(2006) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.50"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, SUBCELLULAR LOCATION. - Ref.51"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: SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304.
Note: Colocalizes with H2AFX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (By similarity). Localizes on meiotic pachytene-stage chromosomes (By similarity). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (By similarity). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:10196376). Localizes to cytoplasmic ribonucleoprotein granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:9659908, PubMed:14532325). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:12417734, PubMed:15380484). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (By similarity). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (By similarity). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (By similarity). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (PubMed:12417734, PubMed:18093976, PubMed:16636078). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (By similarity). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (PubMed:18632687, PubMed:18664458, PubMed:16636078).By similarity- centromere By similarity
- Ref.18"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: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.20"Different targets for the fragile X-related proteins revealed by their distinct nuclear localizations."
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B., Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 8:863-869(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.26"Transport of fragile X mental retardation protein via granules in neurites of PC12 cells."
De Diego Otero Y., Severijnen L.A., van Cappellen G., Schrier M., Oostra B., Willemsen R.
Mol. Cell. Biol. 22:8332-8341(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.30"Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs."
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.
Hum. Mol. Genet. 12:3087-3096(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, MUTAGENESIS OF SER-500. - Ref.47"Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP."
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.
J. Cell Sci. 119:1933-1946(2006) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.50"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, SUBCELLULAR LOCATION. - Ref.51"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: SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
9 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
Other locations
- Cytoplasm 2 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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN. - Ref.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
- perinuclear region 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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
- Cytoplasm 2 Publications
Other locations
- Cytoplasm 2 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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN. - Ref.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
- Cytoplasm 2 Publications
Nucleus
- Nucleus 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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN.
- Cajal body 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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
Note: Colocalizes with Colin and SMN in Cajal bodies (PubMed:24204304).- Nucleus 1 Publication
Nucleus
- Nucleus 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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN.
- Cajal body 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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
- Nucleus 1 Publication
Cytosol
- cytosol Source: HPA
Nucleus
- Cajal body 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
- nucleolus 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
- nucleoplasm 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
- nucleus 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
Plasma Membrane
- extrinsic component of plasma membrane Source: UniProtKB
- postsynaptic membrane Source: UniProtKB-SubCell
- presynaptic membrane Source: UniProtKB-SubCell
Other locations
- axon Source: UniProtKB
- axon terminus Source: UniProtKB
- cell junction Source: UniProtKB-KW
- cell projection 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
- chromocenter Source: UniProtKB
- chromosome Source: UniProtKB
- chromosome, centromeric region Source: UniProtKB-SubCell
- cytoplasm 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
- cytoplasmic ribonucleoprotein granule 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
- cytoplasmic stress granule Source: UniProtKB-SubCell
- dendrite Source: UniProtKB
- dendritic filopodium Source: UniProtKB
- dendritic spine Source: UniProtKB
- filopodium tip Source: UniProtKB
- glial cell projection Source: UniProtKB
- growth cone 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
- growth cone filopodium Source: UniProtKB
- membrane Source: UniProtKBInferred from high throughput direct assayi
- messenger ribonucleoprotein complex Source: CAFA <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
- mRNA cap binding complex Source: UniProtKB
- neuron projection 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
- neuronal ribonucleoprotein granule Source: UniProtKB
- perikaryon 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
- perinuclear region of cytoplasm 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
- polysome 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
- postsynapse Source: UniProtKB
- postsynaptic density Source: UniProtKB
- presynapse Source: UniProtKB
- ribonucleoprotein complex 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
- synapse Source: UniProtKB
- viral replication complex 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
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
Cell junction, Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Membrane, Nucleus, Postsynaptic cell membrane, Synapse, Synaptosome<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section 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">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Fragile X syndrome (FXS)19 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 FXS. - 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 FXS. - Ref.18"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: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.20"Different targets for the fragile X-related proteins revealed by their distinct nuclear localizations."
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B., Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 8:863-869(1999) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.25"Evidence that fragile X mental retardation protein is a negative regulator of translation."
Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U.
Hum. Mol. Genet. 10:329-338(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FXR1 AND FXR2, SUBUNIT, RNA-BINDING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.43"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 FXS ASN-304, RNA-BINDING, DOMAIN. - Ref.51"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: SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.59"FMRP targets distinct mRNA sequence elements to regulate protein expression."
Ascano M. Jr., Mukherjee N., Bandaru P., Miller J.B., Nusbaum J.D., Corcoran D.L., Langlois C., Munschauer M., Dewell S., Hafner M., Williams Z., Ohler U., Tuschl T.
Nature 492:382-386(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10). - Ref.62"A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response."
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y.
Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN, CHARACTERIZATION OF VARIANT FXS GLN-138, MUTAGENESIS OF THR-102 AND TYR-103. - Ref.64"Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus."
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.
Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP (MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FXS ASN-304 (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION). - Ref.69"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 FXS ASN-304. - Ref.70"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 FXS ASN-304. - Ref.71"Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome."
Siomi H., Choi M., Siomi M.C., Nussbaum R.L., Dreyfuss G.
Cell 77:33-39(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, RNA-BINDING. - Ref.72"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 VARIANT FXS ASN-304. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION. - Ref.77"Fragile X syndrome due to a missense mutation."
Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X., Warren S.T.
Eur. J. Hum. Genet. 22:1185-1189(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLU-266, CHARACTERIZATION OF VARIANT FXS GLU-266, RNA-BINGING, ASSOCIATION WITH POLYRIBOSOME. - Ref.78"Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLN-138, CHARACTERIZATION OF VARIANT FXS GLN-138, FUNCTION, INTERACTION WITH KCNMB4, DOMAIN.
Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.
Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]
Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.
Nat. Genet. 4:335-340(1993) [PubMed] [Europe PMC] [Abstract]
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]
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B., Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 8:863-869(1999) [PubMed] [Europe PMC] [Abstract]
Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U.
Hum. Mol. Genet. 10:329-338(2001) [PubMed] [Europe PMC] [Abstract]
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]
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]
Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.
J. Biol. Chem. 283:5598-5610(2008) [PubMed] [Europe PMC] [Abstract]
Ascano M. Jr., Mukherjee N., Bandaru P., Miller J.B., Nusbaum J.D., Corcoran D.L., Langlois C., Munschauer M., Dewell S., Hafner M., Williams Z., Ohler U., Tuschl T.
Nature 492:382-386(2012) [PubMed] [Europe PMC] [Abstract]
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y.
Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.
Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]
Valverde R., Pozdnyakova I., Kajander T., Venkatraman J., Regan L.
Structure 15:1090-1098(2007) [PubMed] [Europe PMC] [Abstract]
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]
Siomi H., Choi M., Siomi M.C., Nussbaum R.L., Dreyfuss G.
Cell 77:33-39(1994) [PubMed] [Europe PMC] [Abstract]
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]
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]
Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X., Warren S.T.
Eur. J. Hum. Genet. 22:1185-1189(2014) [PubMed] [Europe PMC] [Abstract]
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_064507 | 138 | R → Q in FXS; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075977 | 266 | G → E in FXS; reduces association with polyribosome; reduces RNA-binding. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_005234 | 304 | I → N in FXS; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2. 14 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
| 1 |
Fragile X tremor/ataxia syndrome (FXTAS)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.74"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.
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]
Premature ovarian failure 1 (POF1)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.19"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.
Murray A., Webb J., Grimley S., Conway G., Jacobs P.
J. Med. Genet. 35:637-640(1998) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 102 | T → A: Reduces binding to nucleosome. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 103 | Y → L: Reduces binding to nucleosome. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 125 – 126 | 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
| 2 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 500 | S → A: Loss of phosphorylation. Does not affect interaction with MCRS1. Does not affect localization to cytoplasmic granules. Does not affect association with polyribosome. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 500 | S → D: Does not affect RNA-binding to G-quadruplex structure. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 527 – 534 | RRGDGRRR → EEGDGEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 613-E--E-617. 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
| 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 544 | 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 546 | 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 613 – 617 | QKKEK → EEEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 527-E--E-534. 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
| 5 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
Disease mutation, Mental retardation, Premature ovarian failureOrganism-specific databases
DisGeNET More...DisGeNETi | 2332 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | FMR1 |
MalaCards human disease database More...MalaCardsi | FMR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 300623 phenotype 300624 phenotype 311360 phenotype 616034 phenotype |
Open Targets More...OpenTargetsi | ENSG00000102081 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 908 Fragile X syndrome 93256 Fragile X-associated tremor/ataxia syndrome 619 Primary ovarian failure 261483 Xq27.3q28 duplication syndrome |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28191 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FMR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 544328 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000050102 | 1 – 632 | Synaptic functional regulator FMR1Add BLAST | 632 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1 | N-acetylmethionineCombined 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
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 337 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 370 | PhosphoserineCombined 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
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 463 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 471 | Omega-N-methylarginineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 500 | PhosphoserineCombined 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
<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
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 544 | 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
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 620 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
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.30"Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs."
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.
Hum. Mol. Genet. 12:3087-3096(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, MUTAGENESIS OF SER-500.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<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.44"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. - Ref.47"Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP."
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.
J. Cell Sci. 119:1933-1946(2006) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, SUBUNIT, SUBCELLULAR LOCATION.
<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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
Acetylation, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q06787 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q06787 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q06787 |
PeptideAtlas More...PeptideAtlasi | Q06787 |
PRoteomics IDEntifications database More...PRIDEi | Q06787 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58477 58478 [Q06787-2] 58479 [Q06787-3] 58480 [Q06787-4] 58481 [Q06787-5] 58482 [Q06787-6] 58483 [Q06787-7] 58484 [Q06787-8] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q06787 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q06787 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section 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 protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<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.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. - 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 FXS. - Ref.60"FMRP and myelin protein expression in oligodendrocytes."
Giampetruzzi A., Carson J.H., Barbarese E.
Mol. Cell. Neurosci. 56:333-341(2013) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF FUNCTION, TISSUE SPECIFICITY. - Ref.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.64"Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus."
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.
Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP (MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FXS ASN-304 (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION).
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102081 |
CleanEx database of gene expression profiles More...CleanExi | HS_FMR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q06787 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q06787 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB012444 HPA050118 HPA056084 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section 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 <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
31 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.13"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: ASSOCIATION IN MRNP, RNA-BINDING. - Ref.15"The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2."
Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A., Nussbaum R.L., Dreyfuss G.
EMBO J. 14:5358-5366(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT. - Ref.17"Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them."
Siomi M.C., Zhang Y., Siomi H., Dreyfuss G.
Mol. Cell. Biol. 16:3825-3832(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1 AND FXR2, ASSOCIATION WITH RIBOSOMES. - Ref.18"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: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.21"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. - Ref.22"Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome."
Brown V., Jin P., Ceman S., Darnell J.C., O'Donnell W.T., Tenenbaum S.A., Jin X., Feng Y., Wilkinson K.D., Keene J.D., Darnell R.B., Warren S.T.
Cell 107:477-487(2001) [PubMed] [Europe PMC] [Abstract]Cited for: ASSOCIATION WITH POLYRIBOSOME. - Ref.25"Evidence that fragile X mental retardation protein is a negative regulator of translation."
Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U.
Hum. Mol. Genet. 10:329-338(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH FXR1 AND FXR2, SUBUNIT, RNA-BINDING, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.28"The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding."
Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B., Mandel J.L., Pastore A.
Biochemistry 42:10437-10444(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, RNA-BINDING, DOMAIN. - Ref.29"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. - Ref.30"Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs."
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.
Hum. Mol. Genet. 12:3087-3096(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, MUTAGENESIS OF SER-500. - Ref.31"The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo."
Sung Y.J., Dolzhanskaya N., Nolin S.L., Brown T., Currie J.R., Denman R.B.
J. Biol. Chem. 278:15669-15678(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME. - Ref.32"RNA cargoes associating with FMRP reveal deficits in cellular functioning in Fmr1 null mice."
Miyashiro K.Y., Beckel-Mitchener A., Purk T.P., Becker K.G., Barret T., Liu L., Carbonetto S., Weiler I.J., Greenough W.T., Eberwine J.
Neuron 37:417-431(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ASSOCIATION WITH MRNP. - Ref.34"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: INTERACTION WITH IGF2BP1, RNA-BINDING. - Ref.35"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: RNA-BINDING, INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, DOMAIN. - Ref.36"Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway."
Jin P., Zarnescu D.C., Ceman S., Nakamoto M., Mowrey J., Jongens T.A., Nelson D.L., Moses K., Warren S.T.
Nat. Neurosci. 7:113-117(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ASSOCIATION WITH MICRORNA, INTERACTION WITH AGO2. - Ref.39"Evidence for the association of the human regulatory protein Ki-1/57 with the translational machinery."
Goncalves K.A., Bressan G.C., Saito A., Morello L.G., Zanchin N.I., Kobarg J.
FEBS Lett. 585:2556-2560(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HABP4. - Ref.45"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, ASSOCIATION WITH POLYRIBOSOME, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-500. - Ref.47"Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP."
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.
J. Cell Sci. 119:1933-1946(2006) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, SUBUNIT, SUBCELLULAR LOCATION. - Ref.50"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, SUBCELLULAR LOCATION. - Ref.51"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: SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.52"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, ASSOCIATION WITH THE SMN CORE COMPLEX, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FXS ASN-304. - Ref.55"Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein."
Faehling M., Mrowka R., Steege A., Kirschner K.M., Benko E., Foerstera B., Persson P.B., Thiele B.J., Meier J.C., Scholz H.
J. Biol. Chem. 284:4255-4266(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME AND MRNP. - Ref.56"Fragile X mental retardation protein FMRP binds mRNAs in the nucleus."
Kim M., Bellini M., Ceman S.
Mol. Cell. Biol. 29:214-228(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NXF1, RNA-BINDING, SUBCELLULAR LOCATION. - Ref.58"Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack."
Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G., Sigworth F.J., Navaratnam D., Kaczmarek L.K.
Nat. Neurosci. 13:819-821(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH KCNT1. - Ref.62"A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response."
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y.
Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN, CHARACTERIZATION OF VARIANT FXS GLN-138, MUTAGENESIS OF THR-102 AND TYR-103. - Ref.63"MOV10 and FMRP regulate AGO2 association with microRNA recognition elements."
Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J., Arcila M.L., Kosik K.S., Ceman S.
Cell Rep. 9:1729-1741(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MOV10, RNA-BINDING. - Ref.65"Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin."
Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L., Piekorz R.P., Ahmadian M.R.
PLoS ONE 9:E91465-E91465(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CYFIP2; EIF5; NCL AND RPLP0 (ISOFORM 6), SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 527-ARG--ARG-534 AND 613-GLN--LYS-617. - Ref.68"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. - Ref.75"Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells."
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S., van Cappellen G., Oostra B.A., Willemsen R.
Exp. Neurol. 189:343-353(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT FXS ASN-304, INTERACTION WITH FXR1 AND RPLP0, SUBCELLULAR LOCATION. - Ref.77"Fragile X syndrome due to a missense mutation."
Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X., Warren S.T.
Eur. J. Hum. Genet. 22:1185-1189(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLU-266, CHARACTERIZATION OF VARIANT FXS GLU-266, RNA-BINGING, ASSOCIATION WITH POLYRIBOSOME. - Ref.78"Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLN-138, CHARACTERIZATION OF VARIANT FXS GLN-138, FUNCTION, INTERACTION WITH KCNMB4, DOMAIN.
<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.64"Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus."
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C., Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.
Nat. Commun. 5:3259-3259(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP (MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FXS ASN-304 (MICROBIAL INFECTION), INDUCTION (MICROBIAL INFECTION).
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section 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><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-366305,EBI-366305 | ||
| CYFIP1 | Q7L576 | 4 | EBI-366305,EBI-1048143 | |
| CYFIP2 | Q96F07 | 2 | EBI-366305,EBI-2433893 | |
| FSD2 | A1L4K1 | 3 | EBI-10224470,EBI-5661036 | |
| FXR2 | P51116 | 3 | EBI-10224470,EBI-740459 |
<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><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein 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
- ion channel binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- methylated histone 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
- microtubule binding Source: UniProtKB
- protein heterodimerization activity 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
- protein homodimerization activity 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
- translation initiation factor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108619, 65 interactors |
Database of interacting proteins More...DIPi | DIP-29509N |
Protein interaction database and analysis system More...IntActi | Q06787, 47 interactors |
Molecular INTeraction database More...MINTi | Q06787 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000359506 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 15 – 23 | 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 | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 25 – 32 | 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 | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 33 – 35 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 40 – 43 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 44 – 46 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 64 – 69 | 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 | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 71 – 75 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 78 – 88 | 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 | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 97 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 100 – 103 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 104 – 108 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 109 – 111 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 112 – 114 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 123 – 125 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 127 – 132 | 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 | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 135 – 138 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 139 – 141 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 144 – 147 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 148 – 154 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 157 – 162 | 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 | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 163 – 166 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 167 – 173 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 177 – 198 | 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 | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 220 – 224 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 227 – 229 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 230 – 234 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 236 – 238 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 239 – 245 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 250 – 256 | 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 | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 257 – 260 | 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 | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 261 – 268 | 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 | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 269 – 279 | 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 | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 281 – 289 | 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 | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 290 – 292 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 293 – 297 | 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 | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 299 – 301 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 302 – 311 | 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 | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 314 – 321 | 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 | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 398 – 406 | 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 | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 407 – 422 | 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 | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 432 – 434 | 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 | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 535 – 538 | 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 | 4 |
3D structure databases
Database of protein disorder More...DisProti | DP00134 |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q06787 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q06787 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q06787 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section 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><a href='/help/domain' target='_top'>More...</a></p>Domaini | 4 – 50 | Agenet-like 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 Add BLAST | 47 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section 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><a href='/help/domain' target='_top'>More...</a></p>Domaini | 63 – 115 | Agenet-like 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 Add BLAST | 53 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section 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><a href='/help/domain' target='_top'>More...</a></p>Domaini | 222 – 251 | 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 Add BLAST | 30 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section 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><a href='/help/domain' target='_top'>More...</a></p>Domaini | 285 – 314 | 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 Add BLAST | 30 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 184 | Required for nuclear localizationBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi Add BLAST | 184 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 172 – 211 | Necessary for interaction with CYFIP1, CYFIP2, FXR1 and FXR2By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi 2 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
| 40 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 397 – 491 | Required for nuclear export2 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
| 95 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 419 – 632 | Interaction with RANBP91 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
| 214 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 534 – 548 | RNA-binding RGG-boxAdd BLAST | 15 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 424 – 443 | Nuclear export signalBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi Add BLAST | 20 | |
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 527 – 534 | Nucleolar localization signal 11 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
| 8 | |
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 613 – 617 | Nucleolar localization signal 21 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
| 5 |
<p>This subsection of the ‘Family and domains’ section 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><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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.23"Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function."
Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T., Darnell R.B.
Cell 107:489-499(2001) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN. - Ref.24"The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif."
Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., Moine H.
EMBO J. 20:4803-4813(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.28"The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding."
Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B., Mandel J.L., Pastore A.
Biochemistry 42:10437-10444(2003) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, RNA-BINDING, DOMAIN. - Ref.30"Fragile X Mental Retardation protein determinants required for its association with polyribosomal mRNPs."
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.
Hum. Mol. Genet. 12:3087-3096(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN, MUTAGENESIS OF SER-500. - Ref.43"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 FXS ASN-304, RNA-BINDING, DOMAIN. - Ref.46"Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs."
Plante I., Davidovic L., Ouellet D.L., Gobeil L.A., Tremblay S., Khandjian E.W., Provost P.
J. Biomed. Biotechnol. 2006:64347-64347(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.54"Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA."
Menon L., Mader S.A., Mihailescu M.R.
RNA 14:1644-1655(2008) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN. - Ref.57"A novel function for fragile X mental retardation protein in translational activation."
Bechara E.G., Didiot M.C., Melko M., Davidovic L., Bensaid M., Martin P., Castets M., Pognonec P., Khandjian E.W., Moine H., Bardoni B.
PLoS Biol. 7:E16-E16(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, DOMAIN. - Ref.62"A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response."
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S., Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J., Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E., Fischle W., Warren S.T., Page D.C., Shi Y.
Cell 157:869-881(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN, CHARACTERIZATION OF VARIANT FXS GLN-138, MUTAGENESIS OF THR-102 AND TYR-103. - Ref.66"FMRP interacts with G-quadruplex structures in the 3'-UTR of its dendritic target Shank1 mRNA."
Zhang Y., Gaetano C.M., Williams K.R., Bassell G.J., Mihailescu M.R.
RNA Biol. 11:1364-1374(2014) [PubMed] [Europe PMC] [Abstract]Cited for: RNA-BINDING, DOMAIN, MUTAGENESIS OF SER-500. - Ref.78"Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT FXS GLN-138, CHARACTERIZATION OF VARIANT FXS GLN-138, FUNCTION, INTERACTION WITH KCNMB4, DOMAIN.
<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.61"Nuclear fragile X mental retardation protein is localized to Cajal bodies."
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J., De Koninck P., Khandjian E.W.
PLoS Genet. 9:E1003890-E1003890(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6 AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT FXS ASN-304 (ISOFORM 10).
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IF9J Eukaryota ENOG410ZDJG LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000017033 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG005739 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q06787 |
KEGG Orthology (KO) More...KOi | K15516 |
Identification of Orthologs from Complete Genome Data More...OMAi | NERETCG |
Database of Orthologous Groups More...OrthoDBi | EOG091G08EZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q06787 |
TreeFam database of animal gene trees More...TreeFami | TF105427 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1370.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR008395 Agenet-like_dom IPR032196 FXMR_C2 IPR022034 FXMRP1_C_core IPR004087 KH_dom IPR004088 KH_dom_type_1 IPR036612 KH_dom_type_1_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF05641 Agenet, 1 hit PF16098 FXMR_C2, 1 hit PF12235 FXMRP1_C_core, 1 hit PF00013 KH_1, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00322 KH, 2 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54791 SSF54791, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51641 AGENET_LIKE, 2 hits PS50084 KH_TYPE_1, 2 hits |
<p>This section 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 <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (11)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 11 <p>This subsection of the ‘Sequence’ section 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><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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
The sequence of this isoform differs from the canonical sequence as follows:
376-396: Missing.
580-596: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
491-502: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
491-502: Missing.
580-596: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
491-515: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
491-515: Missing.
580-596: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
580-596: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
376-396: Missing.
491-515: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
376-396: Missing.
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>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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN.
The sequence of this isoform differs from the canonical sequence as follows:
426-632: EVDQLRLERL...GQQPLVNGVP → LQQRKRGRAS...QTAWMVSNHS
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 LNYLKLQQRK RGRASCAEET DGGVEGEEED
460 470 480 490 500
KEEEDVEEAS KETTITPEQI IVHVIQERLK EEQQMDPFRS ELTAIMKGVS
510 520 530
TLKHYRIPPV KVVGCARVKI VTRRKRSQTA WMVSNHS
<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.16"Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms."
Sittler A., Devys D., Weber C., Mandel J.L.
Hum. Mol. Genet. 5:95-102(1996) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10 AND 11), DOMAIN.
The sequence of this isoform differs from the canonical sequence as follows:
376-396: Missing.
426-632: EVDQLRLERL...GQQPLVNGVP → LQQRKRGRAS...QTAWMVSNHS
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
NYLKLQQRKR GRASCAEETD GGVEGEEEDK EEEDVEEASK ETTITPEQII
460 470 480 490 500
VHVIQERLKE EQQMDPFRSE LTAIMKGVST LKHYRIPPVK VVGCARVKIV
510
TRRKRSQTAW MVSNHS
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 294 – 295 | Missing in AAA52458 (PubMed:1710175).Curated | 2 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_064507 | 138 | R → Q in FXS; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029278 | 145 | A → S. Corresponds to variant dbSNP:rs29281EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075977 | 266 | G → E in FXS; reduces association with polyribosome; reduces RNA-binding. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_005234 | 304 | I → N in FXS; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2. 14 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_005235 | 546 | R → H1 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
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002823 | 376 – 396 | Missing in isoform 1, isoform 8, isoform 9 and isoform 11. 3 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
| 21 | |
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058423 | 426 – 632 | EVDQL…VNGVP → LQQRKRGRASCAEETDGGVE GEEEDKEEEDVEEASKETTI TPEQIIVHVIQERLKEEQQM DPFRSELTAIMKGVSTLKHY RIPPVKVVGCARVKIVTRRK RSQTAWMVSNHS in isoform 10 and isoform 11. 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
| 207 | |
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002825 | 491 – 515 | 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
| 25 | |
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002824 | 491 – 502 | Missing in isoform 2 and isoform 3. CuratedAdd BLAST | 12 | |
| <p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002826 | 580 – 596 | Missing in isoform 1, isoform 3, isoform 5 and isoform 7. CuratedAdd BLAST | 17 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L29074 Genomic DNA Translation: AAB18828.1 L29074 Genomic DNA Translation: AAB18829.1 L29074 Genomic DNA Translation: AAB18830.1 L29074 Genomic DNA Translation: AAB18831.1 L29074 Genomic DNA Translation: AAB18832.1 L29074 Genomic DNA Translation: AAB18833.1 KJ534836 mRNA Translation: AHW56476.1 CH471171 Genomic DNA Translation: EAW61294.1 CH471171 Genomic DNA Translation: EAW61296.1 CH471171 Genomic DNA Translation: EAW61298.1 CH471171 Genomic DNA Translation: EAW61301.1 CH471171 Genomic DNA Translation: EAW61302.1 CH471171 Genomic DNA Translation: EAW61303.1 BC086957 mRNA Translation: AAH86957.1 M67468 mRNA Translation: AAA52458.1 Different initiation. X69962 mRNA Translation: CAA49586.1 S65791 mRNA Translation: AAB28395.2 L19476 Genomic DNA Translation: AAA62452.2 L19477 Genomic DNA Translation: AAA62453.1 L19478 Genomic DNA Translation: AAA62454.1 L19479 Genomic DNA Translation: AAA62455.1 L19480 Genomic DNA Translation: AAA62456.1 L19481 Genomic DNA Translation: AAA62457.1 L19482 Genomic DNA Translation: AAA62458.1 L19483 Genomic DNA Translation: AAA62459.1 L19484 Genomic DNA Translation: AAA62460.1 L19485 Genomic DNA Translation: AAA62461.1 L19486 Genomic DNA Translation: AAA62462.1 L19487 Genomic DNA Translation: AAA62463.1 L19488 Genomic DNA Translation: AAA62464.1 L19489 Genomic DNA Translation: AAA62465.1 L19490 Genomic DNA Translation: AAA62466.1 Sequence problems. L19491 Genomic DNA Translation: AAA62467.1 Sequence problems. L19492 Genomic DNA Translation: AAA62468.1 L19493 Genomic DNA Translation: AAA62469.1 S76590 Genomic DNA Translation: AAD14228.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14682.1 [Q06787-1] CCDS55518.1 [Q06787-10] CCDS55519.1 [Q06787-9] CCDS76039.1 [Q06787-8] |
Protein sequence database of the Protein Information Resource More...PIRi | I68614 S45243 A40724 |
NCBI Reference Sequences More...RefSeqi | NP_001172004.1, NM_001185075.1 [Q06787-10] NP_001172005.1, NM_001185076.1 [Q06787-9] NP_001172010.1, NM_001185081.1 [Q06787-11] NP_001172011.1, NM_001185082.1 [Q06787-8] NP_002015.1, NM_002024.5 [Q06787-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.103183 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000218200; ENSP00000218200; ENSG00000102081 [Q06787-9] ENST00000370470; ENSP00000359501; ENSG00000102081 [Q06787-6] ENST00000370471; ENSP00000359502; ENSG00000102081 [Q06787-10] ENST00000370475; ENSP00000359506; ENSG00000102081 [Q06787-1] ENST00000440235; ENSP00000413764; ENSG00000102081 [Q06787-8] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2332 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2332 |
UCSC genome browser More...UCSCi | uc004fck.5 human [Q06787-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length |
|---|
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q06787 | UPI00019643F1 | 134 | |||
| UPI00064D0D58 | 747 | ||||
| UPI0004ED4D21 | 646 | ||||
| UPI0005FB5139 | 644 | ||||
| UPI0003C15C66 | 547 | ||||
| +229 | |||||
| Q06787-2 | UPI0004F0844F | 650 | |||
| UPI00080A61CF | 650 | ||||
| UPI000B5124C2 | 650 | ||||
| UPI00020AD6E6 | 642 | ||||
| UPI0005FB0DF1 | 623 | ||||
| +210 | |||||
| Q06787-5 | UPI000B4FE0D5 | 646 | |||
| UPI0005FC0057 | 619 | ||||
| UPI0003C12837 | 522 | ||||
| UPI00095333F0 | 619 | ||||
| UPI0003C425B7 | 608 | ||||
| +105 | |||||
| Q06787-6 | UPI000B4FE0D5 | 646 | |||
| UPI0005FC0057 | 619 | ||||
| UPI0003C12837 | 522 | ||||
| UPI00095333F0 | 619 | ||||
| UPI0003C425B7 | 608 | ||||
| +105 | |||||
| Q06787-8 | UPI0004F0B6BC | 625 | |||
| UPI000809CD76 | 625 | ||||
| UPI000B507B29 | 625 | ||||
| UPI00020AD6E7 | 617 | ||||
| Putative fragile x mental retardation protein 1 (Fragment) | 605 | ||||
| +124 | |||||
| Q06787-9 | UPI0004F0844F | 650 | |||
| UPI00080A61CF | 650 | ||||
| UPI000B5124C2 | 650 | ||||
| UPI00020AD6E6 | 642 | ||||
| UPI0005FB0DF1 | 623 | ||||
| +210 | |||||
| Q06787-10 | UPI0003C00ECE | 556 | |||
| UPI0003BBEC62 | 538 | ||||
| Fragile X mental retardation 1 | 537 | ||||
| FMR1 isoform 5 | 537 | ||||
| Fragile X mental retardation 1 | 537 | ||||
| +50 | |||||
| Q06787-11 | UPI00020AD6E9 | 547 | |||
| UPI0003C008AC | 535 | ||||
| UPI0003BB6F57 | 517 | ||||
| UPI0002258153 | 516 | ||||
| UPI000642EF04 | 516 | ||||
| +21 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q06787 | UPI00019643F1 | 134 | |||
| UPI00064D0D58 | 747 | ||||
| UPI0004ED4D21 | 646 | ||||
| UPI0009515608 | 644 | ||||
| UPI0005FB5139 | 644 | ||||
| +281 | |||||
| Q06787-2 | UPI000B5124C2 | 650 | |||
| UPI00080A61CF | 650 | ||||
| UPI0004F0844F | 650 | ||||
| UPI00020AD6E6 | 642 | ||||
| UPI0009517E52 | 623 | ||||
| +533 | |||||
| Q06787-5 | UPI000B4FE0D5 | 646 | |||
| UPI00095333F0 | 619 | ||||
| UPI0005FC0057 | 619 | ||||
| UPI0003C12837 | 522 | ||||
| UPI0003C425B7 | 608 | ||||
| +255 | |||||
| Q06787-6 | UPI000B4FE0D5 | 646 | |||
| UPI00095333F0 | 619 | ||||
| UPI0005FC0057 | 619 | ||||
| UPI0003C12837 | 522 | ||||
| UPI0003C425B7 | 608 | ||||
| +255 | |||||
| Q06787-8 | UPI000B5124C2 | 650 | |||
| UPI00080A61CF | 650 | ||||
| UPI0004F0844F | 650 | ||||
| UPI00020AD6E6 | 642 | ||||
| UPI0009517E52 | 623 | ||||
| +533 | |||||
| Q06787-9 | UPI000B5124C2 | 650 | |||
| UPI00080A61CF | 650 | ||||
| UPI0004F0844F | 650 | ||||
| UPI00020AD6E6 | 642 | ||||
| UPI0009517E52 | 623 | ||||
| +533 | |||||
| Q06787-10 | UPI000B4FE0D5 | 646 | |||
| UPI00095333F0 | 619 | ||||
| UPI0005FC0057 | 619 | ||||
| UPI0003C12837 | 522 | ||||
| UPI0003C425B7 | 608 | ||||
| +255 | |||||
| Q06787-11 | UPI00020AD6E9 | 547 | |||
| UPI0003C008AC | 535 | ||||
| UPI0003BB6F57 | 517 | ||||
| UPI000BB736B2 | 516 | ||||
| UPI00059B1B9C | 516 | ||||
| +70 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L29074 Genomic DNA Translation: AAB18828.1 L29074 Genomic DNA Translation: AAB18829.1 L29074 Genomic DNA Translation: AAB18830.1 L29074 Genomic DNA Translation: AAB18831.1 L29074 Genomic DNA Translation: AAB18832.1 L29074 Genomic DNA Translation: AAB18833.1 KJ534836 mRNA Translation: AHW56476.1 CH471171 Genomic DNA Translation: EAW61294.1 CH471171 Genomic DNA Translation: EAW61296.1 CH471171 Genomic DNA Translation: EAW61298.1 CH471171 Genomic DNA Translation: EAW61301.1 CH471171 Genomic DNA Translation: EAW61302.1 CH471171 Genomic DNA Translation: EAW61303.1 BC086957 mRNA Translation: AAH86957.1 M67468 mRNA Translation: AAA52458.1 Different initiation. X69962 mRNA Translation: CAA49586.1 S65791 mRNA Translation: AAB28395.2 L19476 Genomic DNA Translation: AAA62452.2 L19477 Genomic DNA Translation: AAA62453.1 L19478 Genomic DNA Translation: AAA62454.1 L19479 Genomic DNA Translation: AAA62455.1 L19480 Genomic DNA Translation: AAA62456.1 L19481 Genomic DNA Translation: AAA62457.1 L19482 Genomic DNA Translation: AAA62458.1 L19483 Genomic DNA Translation: AAA62459.1 L19484 Genomic DNA Translation: AAA62460.1 L19485 Genomic DNA Translation: AAA62461.1 L19486 Genomic DNA Translation: AAA62462.1 L19487 Genomic DNA Translation: AAA62463.1 L19488 Genomic DNA Translation: AAA62464.1 L19489 Genomic DNA Translation: AAA62465.1 L19490 Genomic DNA Translation: AAA62466.1 Sequence problems. L19491 Genomic DNA Translation: AAA62467.1 Sequence problems. L19492 Genomic DNA Translation: AAA62468.1 L19493 Genomic DNA Translation: AAA62469.1 S76590 Genomic DNA Translation: AAD14228.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14682.1 [Q06787-1] CCDS55518.1 [Q06787-10] CCDS55519.1 [Q06787-9] CCDS76039.1 [Q06787-8] |
Protein sequence database of the Protein Information Resource More...PIRi | I68614 S45243 A40724 |
NCBI Reference Sequences More...RefSeqi | NP_001172004.1, NM_001185075.1 [Q06787-10] NP_001172005.1, NM_001185076.1 [Q06787-9] NP_001172010.1, NM_001185081.1 [Q06787-11] NP_001172011.1, NM_001185082.1 [Q06787-8] NP_002015.1, NM_002024.5 [Q06787-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.103183 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2BKD | NMR | - | N | 1-134 | [»] | |
| 2FMR | NMR | - | A | 216-280 | [»] | |
| 2LA5 | NMR | - | B | 527-541 | [»] | |
| 2QND | X-ray | 1.90 | A/B | 216-425 | [»] | |
| 4OVA | X-ray | 3.00 | A/B/C/D | 1-209 | [»] | |
| 4QVZ | X-ray | 3.20 | A/B | 1-213 | [»] | |
| 4QW2 | X-ray | 2.99 | A/B | 1-213 | [»] | |
| 5DE5 | X-ray | 3.00 | B/D | 528-544 | [»] | |
| 5DE8 | X-ray | 3.10 | B/D | 528-544 | [»] | |
| 5DEA | X-ray | 2.80 | B/D | 528-544 | [»] | |
| 5UWJ | X-ray | 2.22 | D | 423-437 | [»] | |
| 5UWO | X-ray | 2.35 | D | 422-438 | [»] | |
Database of protein disorder More...DisProti | DP00134 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q06787 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q06787 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108619, 65 interactors |
Database of interacting proteins More...DIPi | DIP-29509N |
Protein interaction database and analysis system More...IntActi | Q06787, 47 interactors |
Molecular INTeraction database More...MINTi | Q06787 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000359506 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q06787 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q06787 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FMR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 544328 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q06787 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q06787 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q06787 |
PeptideAtlas More...PeptideAtlasi | Q06787 |
PRoteomics IDEntifications database More...PRIDEi | Q06787 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 58477 58478 [Q06787-2] 58479 [Q06787-3] 58480 [Q06787-4] 58481 [Q06787-5] 58482 [Q06787-6] 58483 [Q06787-7] 58484 [Q06787-8] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000218200; ENSP00000218200; ENSG00000102081 [Q06787-9] ENST00000370470; ENSP00000359501; ENSG00000102081 [Q06787-6] ENST00000370471; ENSP00000359502; ENSG00000102081 [Q06787-10] ENST00000370475; ENSP00000359506; ENSG00000102081 [Q06787-1] ENST00000440235; ENSP00000413764; ENSG00000102081 [Q06787-8] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2332 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2332 |
UCSC genome browser More...UCSCi | uc004fck.5 human [Q06787-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 2332 |
DisGeNET More...DisGeNETi | 2332 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102081.13 |
GeneCards: human genes, protein and diseases More...GeneCardsi | FMR1 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | FMR1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3775 FMR1 |
Human Protein Atlas More...HPAi | CAB012444 HPA050118 HPA056084 |
MalaCards human disease database More...MalaCardsi | FMR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 300623 phenotype 300624 phenotype 309550 gene 311360 phenotype 616034 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q06787 |
Open Targets More...OpenTargetsi | ENSG00000102081 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 908 Fragile X syndrome 93256 Fragile X-associated tremor/ataxia syndrome 619 Primary ovarian failure 261483 Xq27.3q28 duplication syndrome |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28191 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IF9J Eukaryota ENOG410ZDJG LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000017033 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG005739 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q06787 |
KEGG Orthology (KO) More...KOi | K15516 |
Identification of Orthologs from Complete Genome Data More...OMAi | NERETCG |
Database of Orthologous Groups More...OrthoDBi | EOG091G08EZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q06787 |
TreeFam database of animal gene trees More...TreeFami | TF105427 |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q06787 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | FMR1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q06787 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | FMR1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 2332 |
Protein Ontology More...PROi | PR:Q06787 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102081 |
CleanEx database of gene expression profiles More...CleanExi | HS_FMR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q06787 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q06787 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1370.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR008395 Agenet-like_dom IPR032196 FXMR_C2 IPR022034 FXMRP1_C_core IPR004087 KH_dom IPR004088 KH_dom_type_1 IPR036612 KH_dom_type_1_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF05641 Agenet, 1 hit PF16098 FXMR_C2, 1 hit PF12235 FXMRP1_C_core, 1 hit PF00013 KH_1, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00322 KH, 2 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54791 SSF54791, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51641 AGENET_LIKE, 2 hits PS50084 KH_TYPE_1, 2 hits |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | FMR1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q06787Primary (citable) accession number: Q06787 Secondary accession number(s): A6NNH4 , D3DWT0, D3DWT1, D3DWT2, G8JL90, Q16578, Q5PQZ6, Q99054 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
| Last sequence update: | June 1, 1994 | |
| Last modified: | July 18, 2018 | |
| This is version 199 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/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
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
