HUMAN:FMR1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	FMR1
Protein Name(s)	Fragile X mental retardation protein 1 FMRP Protein FMR-1
External Links
UniProt	Q06787
EMBL	L29074 L29074 L29074 L29074 L29074 L29074 KJ534836 CH471171 CH471171 CH471171 CH471171 CH471171 CH471171 BC086957 M67468 X69962 S65791 L19476 L19477 L19478 L19479 L19480 L19481 L19482 L19483 L19484 L19485 L19486 L19487 L19488 L19489 L19490 L19491 L19492 L19493 S76590
CCDS	CCDS14682.1 CCDS55519.1 CCDS76039.1
PIR	I68614 S45243
RefSeq	NP_001172004.1 NP_001172005.1 NP_001172010.1 NP_001172011.1 NP_002015.1
UniGene	Hs.103183
PDB	2BKD 2FMR 2LA5 2QND
PDBsum	2BKD 2FMR 2LA5 2QND
DisProt	DP00134
ProteinModelPortal	Q06787
SMR	Q06787
BioGrid	108619
DIP	DIP-29022N DIP-29509N
IntAct	Q06787
MINT	MINT-108156
STRING	9606.ENSP00000359506
PhosphoSite	Q06787
DMDM	544328
MaxQB	Q06787
PaxDb	Q06787
PRIDE	Q06787
Ensembl	ENST00000218200 ENST00000370470 ENST00000370475 ENST00000440235
GeneID	2332
KEGG	hsa:2332
UCSC	uc004fck.4 uc010nst.3 uc022cge.1
CTD	2332
GeneCards	GC0XP146993
GeneReviews	FMR1
HGNC	HGNC:3775
HPA	CAB012444 HPA050118
MIM	300623 300624 309550 311360
neXtProt	NX_Q06787
Orphanet	908 93256 619 261483
PharmGKB	PA28191
eggNOG	NOG75351
GeneTree	ENSGT00390000017033
HOVERGEN	HBG005739
InParanoid	Q06787
KO	K15516
OMA	KAWQGMV
PhylomeDB	Q06787
TreeFam	TF105427
ChiTaRS	FMR1
EvolutionaryTrace	Q06787
GeneWiki	FMR1
GenomeRNAi	2332
NextBio	9465
PRO	PR:Q06787
Proteomes	UP000005640
Bgee	Q06787
CleanEx	HS_FMR1
ExpressionAtlas	Q06787
Genevestigator	Q06787
GO	GO:0044297 GO:0005737 GO:0036464 GO:0010494 GO:0043198 GO:0043197 GO:0016020 GO:0005874 GO:0005845 GO:0071598 GO:0005730 GO:0005654 GO:0005844 GO:0045202 GO:0003729 GO:0044822 GO:0003723 GO:0007417 GO:0051028 GO:0045947
Gene3D	3.30.1370.10
InterPro	IPR008395 IPR022034 IPR004087 IPR004088
Pfam	PF05641 PF12235 PF00013
SMART	SM00322
SUPFAM	SSF54791
PROSITE	PS51641 PS50084

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0035613	RNA stem-loop binding	PMID:15805463^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:8156595^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1990812	growth cone filopodium	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0032433	filopodium tip	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
involved_in	GO:0060998	regulation of dendritic spine development	PMID:16631377^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051489	regulation of filopodium assembly	PMID:16631377^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003730	mRNA 3'-UTR binding	PMID:17417632^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060964	regulation of gene silencing by miRNA	PMID:25464849^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0002151	G-quadruplex RNA binding	PMID:25464849^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902416	positive regulation of mRNA binding	PMID:25464849^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:25464849^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:1900453	negative regulation of long-term synaptic depression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:0007215	glutamate receptor signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
enables	GO:0030371	translation repressor activity	PMID:11157796^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:11157796^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11157796^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1902737	dendritic filopodium	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:15380484^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	PMID:15380484^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	PMID:15380484^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:15380484^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18936162^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:18936162^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:18936162^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:9659908^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9659908^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043679	axon terminus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:19097999^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:19097999^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:19097999^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:25225333^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q99959)	Seeded From UniProt	complete
part_of	GO:1990124	messenger ribonucleoprotein complex	PMID:25225333^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1902373	negative regulation of mRNA catabolic process	PMID:25225333^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q99959)	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:10496225^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
part_of	GO:0005844	polysome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
enables	GO:1990825	sequence-specific mRNA binding	PMID:23235829^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
colocalizes_with	GO:0032797	SMN complex	PMID:18093976^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:18093976^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:18093976^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:18093976^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:16571602^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:16571602^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16571602^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002092	positive regulation of receptor internalization	PMID:25561520^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:25561520^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:25561520^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0098908	regulation of neuronal action potential	PMID:25561520^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:25561520^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9JIN6	F		Seeded From UniProt	complete
enables	GO:0002151	G-quadruplex RNA binding	PMID:18653529^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000381	regulation of alternative mRNA splicing, via spliceosome	PMID:18653529^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:7489725^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:7489725^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007215	glutamate receptor signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	P		Seeded From UniProt	complete
part_of	GO:0010369	chromocenter	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	F		Seeded From UniProt	complete
involved_in	GO:0072711	cellular response to hydroxyurea	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
enables	GO:0035064	methylated histone binding	PMID:24813610^[19]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0033129	positive regulation of histone phosphorylation	PMID:24813610^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001022	positive regulation of response to DNA damage stimulus	PMID:24813610^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:24813610^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:9659908^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:7688265^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0034046	poly(G) binding	PMID:7688265^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0031369	translation initiation factor binding	PMID:24658146^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55010	F		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	PMID:24658146^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05388	F		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:24658146^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:24658146^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15381419^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:15381419^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005844	polysome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0097386	glial cell projection	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	C		Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:19166269^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070840	dynein complex binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	F		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	F		Seeded From UniProt	complete
involved_in	GO:0060999	positive regulation of dendritic spine development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:0051491	positive regulation of filopodium assembly	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:0051028	mRNA transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
part_of	GO:1902737	dendritic filopodium	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
enables	GO:0035613	RNA stem-loop binding	PMID:19166269^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0048027	mRNA 5'-UTR binding	PMID:19166269^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0071598	neuronal ribonucleoprotein granule	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
involved_in	GO:2000766	negative regulation of cytoplasmic translation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:0098586	cellular response to virus	PMID:24514761^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901254	positive regulation of intracellular transport of viral material	PMID:24514761^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044830	modulation by host of viral RNA genome replication	PMID:24514761^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0019034	viral replication complex	PMID:24514761^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0098793	presynapse	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
part_of	GO:0019897	extrinsic component of plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
involved_in	GO:1901800	positive regulation of proteasomal protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
involved_in	GO:2000301	negative regulation of synaptic vesicle exocytosis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	P		Seeded From UniProt	complete
involved_in	GO:1901386	negative regulation of voltage-gated calcium channel activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	P		Seeded From UniProt	complete
involved_in	GO:0046928	regulation of neurotransmitter secretion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q80WE1	P		Seeded From UniProt	complete
enables	GO:1990825	sequence-specific mRNA binding	PMID:12927206^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0033592	RNA strand annealing activity	PMID:17057366^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0035197	siRNA binding	PMID:17057366^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0035198	miRNA binding	PMID:17057366^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2000637	positive regulation of gene silencing by miRNA	PMID:17057366^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[27]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:15121898^[28]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000031)	Seeded From UniProt	complete
involved_in	GO:0045947	negative regulation of translational initiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[29]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[30]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005845	mRNA cap binding complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35922	C		Seeded From UniProt	complete
involved_in	GO:2001022	positive regulation of response to DNA damage stimulus	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318101 UniProtKB:Q06787	P		Seeded From UniProt	complete
involved_in	GO:1905244	regulation of modification of synaptic structure	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN000063980	P		Seeded From UniProt	complete
part_of	GO:1902737	dendritic filopodium	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318101 RGD:2623	C		Seeded From UniProt	complete
involved_in	GO:0099578	regulation of translation at postsynapse, modulating synaptic transmission	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN000063980	P		Seeded From UniProt	complete
part_of	GO:0098793	presynapse	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318101	C		Seeded From UniProt	complete
part_of	GO:0071598	neuronal ribonucleoprotein granule	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 MGI:MGI:95564 PANTHER:PTN000063980 RGD:2623	C		Seeded From UniProt	complete
involved_in	GO:0060998	regulation of dendritic spine development	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN000063980 UniProtKB:Q06787	P		Seeded From UniProt	complete
involved_in	GO:0051489	regulation of filopodium assembly	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318101 UniProtKB:Q06787	P		Seeded From UniProt	complete
involved_in	GO:0048814	regulation of dendrite morphogenesis	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 PANTHER:PTN000063980	P		Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318100 UniProtKB:Q06787	P		Seeded From UniProt	complete
enables	GO:0045182	translation regulator activity	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 PANTHER:PTN001318100	F		Seeded From UniProt	complete
part_of	GO:0044326	dendritic spine neck	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001318101 RGD:2623	C		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318100	P		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN000063980 RGD:2623	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 PANTHER:PTN000063980 RGD:2623	C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001318100 UniProtKB:P51114 UniProtKB:P51116 UniProtKB:Q06787	F		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318100 RGD:2623 UniProtKB:Q06787	C		Seeded From UniProt	complete
part_of	GO:0035770	ribonucleoprotein granule	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN001318100	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001318101 RGD:2623 UniProtKB:Q06787	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN000063980 RGD:2623	C		Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN001318100	P		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000063980 RGD:2623	C		Seeded From UniProt	complete
involved_in	GO:0008089	anterograde axonal transport	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN000063980	P		Seeded From UniProt	complete
involved_in	GO:0007417	central nervous system development	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN000063980	P		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:1346074 MGI:MGI:95564 PANTHER:PTN001318100 RGD:2623 UniProtKB:Q06787	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0028734 MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN001318100 UniProtKB:P51116 UniProtKB:Q06787	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN001318100 RGD:2623 UniProtKB:Q06787 Xenbase:XB-GENE-1004708 Xenbase:XB-GENE-977113	C		Seeded From UniProt	complete
enables	GO:0003730	mRNA 3'-UTR binding	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104860 MGI:MGI:95564 PANTHER:PTN001318100 UniProtKB:Q06787	F		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318100 RGD:2623 UniProtKB:Q06787	F		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001318101 RGD:2623	P		Seeded From UniProt	complete
involved_in	GO:0000381	regulation of alternative mRNA splicing, via spliceosome	PMID:21873635^[31]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95564 PANTHER:PTN001318101 UniProtKB:Q06787	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21446998^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q06787	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17850748^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q06787	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904115	axon cytoplasm	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008089	C		Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004087	F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004088 InterPro:IPR022034 InterPro:IPR036612	F		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040148	F		Seeded From UniProt	complete
involved_in	GO:0006417	regulation of translation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040148	P		Seeded From UniProt	complete
enables	GO:0034046	poly(G) binding	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015030	Cajal body	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0015030	Cajal body	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034046	poly(G) binding	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24204304^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:10888599^[35]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:7692601^[36]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:8156595^[2]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
colocalizes_with	GO:0042788	polysomal ribosome	PMID:12837692^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16407062^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:16407062^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770 UniProtKB-SubCell:SL-0258	C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0771 UniProtKB-SubCell:SL-0261	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966 UniProtKB-SubCell:SL-0280	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
involved_in	GO:0006417	regulation of translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0810	P		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0137 UniProtKB-SubCell:SL-0047	C		Seeded From UniProt	complete
involved_in	GO:0031047	gene silencing by RNA	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0943	P		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	C		Seeded From UniProt	complete
involved_in	GO:0051028	mRNA transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0509	P		Seeded From UniProt	complete
involved_in	GO:0007399	nervous system development	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0524	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0508	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0045211	postsynaptic membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0628 UniProtKB-SubCell:SL-0219	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0197	C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0284	C		Seeded From UniProt	complete
part_of	GO:0015030	Cajal body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0031	C		Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0496	C		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0495	C		Seeded From UniProt	complete
part_of	GO:0042734	presynaptic membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0222	C		Seeded From UniProt	complete
part_of	GO:0032433	filopodium tip	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0470	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0288	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0279	C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0283	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Darnell, JC et al. (2005) Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes. Genes Dev. 19 903-18 PubMed GONUTS page
↑ ^2.0 ^2.1 Siomi, H et al. (1994) 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. Cell 77 33-9 PubMed GONUTS page
↑ ^3.0 ^3.1 Antar, LN et al. () Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses. Mol. Cell. Neurosci. 32 37-48 PubMed GONUTS page
↑ Zalfa, F et al. (2007) A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability. Nat. Neurosci. 10 578-87 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Kenny, PJ et al. (2014) MOV10 and FMRP regulate AGO2 association with microRNA recognition elements. Cell Rep 9 1729-1741 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Laggerbauer, B et al. (2001) Evidence that fragile X mental retardation protein is a negative regulator of translation. Hum. Mol. Genet. 10 329-38 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Schrier, M et al. (2004) Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells. Exp. Neurol. 189 343-53 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Kim, M et al. (2009) Fragile X mental retardation protein FMRP binds mRNAs in the nucleus. Mol. Cell. Biol. 29 214-28 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Feng, Y et al. (1997) FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell 1 109-18 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Fähling, M et al. (2009) Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein. J. Biol. Chem. 284 4255-66 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Fischer-Kešo, R et al. (2014) Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins. Mol. Cell. Biol. 34 4244-56 PubMed GONUTS page
↑ Adinolfi, S et al. (1999) Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. RNA 5 1248-58 PubMed GONUTS page
↑ Ascano, M Jr et al. (2012) FMRP targets distinct mRNA sequence elements to regulate protein expression. Nature 492 382-6 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Piazzon, N et al. (2008) In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein. J. Biol. Chem. 283 5598-610 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Davidovic, L et al. (2006) The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons. Hum. Mol. Genet. 15 1525-38 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 Myrick, LK et al. (2015) Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures. Proc. Natl. Acad. Sci. U.S.A. 112 949-56 PubMed GONUTS page
↑ ^17.0 ^17.1 Didiot, MC et al. (2008) The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer. Nucleic Acids Res. 36 4902-12 PubMed GONUTS page
↑ ^18.0 ^18.1 Zhang, Y et al. (1995) The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14 5358-66 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Alpatov, R et al. (2014) A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response. Cell 157 869-81 PubMed GONUTS page
↑ ^20.0 ^20.1 Siomi, H et al. (1993) The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 74 291-8 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Taha, MS et al. (2014) Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin. PLoS ONE 9 e91465 PubMed GONUTS page
↑ ^22.0 ^22.1 Menon, RP et al. (2004) The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J. Mol. Biol. 343 43-53 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Bechara, EG et al. (2009) A novel function for fragile X mental retardation protein in translational activation. PLoS Biol. 7 e16 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 Zhou, Z et al. (2014) Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus. Nat Commun 5 3259 PubMed GONUTS page
↑ Chen, L et al. (2003) The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences. Neuroscience 120 1005-17 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 Plante, I et al. (2006) Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs. J. Biomed. Biotechnol. 2006 64347 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ ^31.00 ^31.01 ^31.02 ^31.03 ^31.04 ^31.05 ^31.06 ^31.07 ^31.08 ^31.09 ^31.10 ^31.11 ^31.12 ^31.13 ^31.14 ^31.15 ^31.16 ^31.17 ^31.18 ^31.19 ^31.20 ^31.21 ^31.22 ^31.23 ^31.24 ^31.25 ^31.26 ^31.27 ^31.28 ^31.29 ^31.30 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Sjekloća, L et al. (2011) On the aggregation properties of FMRP--a link with the FXTAS syndrome? FEBS J. 278 1912-21 PubMed GONUTS page
↑ Valverde, R et al. (2007) Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein. Structure 15 1090-8 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 ^34.3 ^34.4 ^34.5 ^34.6 ^34.7 ^34.8 ^34.9 Dury, AY et al. (2013) Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies. PLoS Genet. 9 e1003890 PubMed GONUTS page
↑ Tamanini, F et al. (2000) The fragile X-related proteins FXR1P and FXR2P contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins. Hum. Mol. Genet. 9 1487-93 PubMed GONUTS page
↑ Ashley, CT Jr et al. (1993) FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262 563-6 PubMed GONUTS page
↑ Bardoni, B et al. (2003) 82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization. Hum. Mol. Genet. 12 1689-98 PubMed GONUTS page
↑ ^38.0 ^38.1 Ramos, A et al. (2006) The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction. Structure 14 21-31 PubMed GONUTS page

[PMID:15805463-1] Darnell, JC et al. (2005) Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes. Genes Dev. 19 903-18 PubMed GONUTS page

[PMID:8156595-2] 2.0 ^2.1 Siomi, H et al. (1994) 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. Cell 77 33-9 PubMed GONUTS page

[PMID:16631377-3] 3.0 ^3.1 Antar, LN et al. () Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses. Mol. Cell. Neurosci. 32 37-48 PubMed GONUTS page

[PMID:17417632-4] Zalfa, F et al. (2007) A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability. Nat. Neurosci. 10 578-87 PubMed GONUTS page

[PMID:25464849-5] 5.0 ^5.1 ^5.2 ^5.3 Kenny, PJ et al. (2014) MOV10 and FMRP regulate AGO2 association with microRNA recognition elements. Cell Rep 9 1729-1741 PubMed GONUTS page

[PMID:11157796-6] 6.0 ^6.1 ^6.2 Laggerbauer, B et al. (2001) Evidence that fragile X mental retardation protein is a negative regulator of translation. Hum. Mol. Genet. 10 329-38 PubMed GONUTS page

[PMID:15380484-7] 7.0 ^7.1 ^7.2 ^7.3 Schrier, M et al. (2004) Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells. Exp. Neurol. 189 343-53 PubMed GONUTS page

[PMID:18936162-8] 8.0 ^8.1 ^8.2 Kim, M et al. (2009) Fragile X mental retardation protein FMRP binds mRNAs in the nucleus. Mol. Cell. Biol. 29 214-28 PubMed GONUTS page

[PMID:9659908-9] 9.0 ^9.1 ^9.2 Feng, Y et al. (1997) FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell 1 109-18 PubMed GONUTS page

[PMID:19097999-10] 10.0 ^10.1 ^10.2 Fähling, M et al. (2009) Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein. J. Biol. Chem. 284 4255-66 PubMed GONUTS page

[PMID:25225333-11] 11.0 ^11.1 ^11.2 Fischer-Kešo, R et al. (2014) Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins. Mol. Cell. Biol. 34 4244-56 PubMed GONUTS page

[PMID:10496225-12] Adinolfi, S et al. (1999) Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. RNA 5 1248-58 PubMed GONUTS page

[PMID:23235829-13] Ascano, M Jr et al. (2012) FMRP targets distinct mRNA sequence elements to regulate protein expression. Nature 492 382-6 PubMed GONUTS page

[PMID:18093976-14] 14.0 ^14.1 ^14.2 ^14.3 Piazzon, N et al. (2008) In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein. J. Biol. Chem. 283 5598-610 PubMed GONUTS page

[PMID:16571602-15] 15.0 ^15.1 ^15.2 Davidovic, L et al. (2006) The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons. Hum. Mol. Genet. 15 1525-38 PubMed GONUTS page

[PMID:25561520-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 Myrick, LK et al. (2015) Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures. Proc. Natl. Acad. Sci. U.S.A. 112 949-56 PubMed GONUTS page

[PMID:18653529-17] 17.0 ^17.1 Didiot, MC et al. (2008) The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer. Nucleic Acids Res. 36 4902-12 PubMed GONUTS page

[PMID:7489725-18] 18.0 ^18.1 Zhang, Y et al. (1995) The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2. EMBO J. 14 5358-66 PubMed GONUTS page

[PMID:24813610-19] 19.0 ^19.1 ^19.2 ^19.3 Alpatov, R et al. (2014) A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response. Cell 157 869-81 PubMed GONUTS page

[PMID:7688265-20] 20.0 ^20.1 Siomi, H et al. (1993) The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 74 291-8 PubMed GONUTS page

[PMID:24658146-21] 21.0 ^21.1 ^21.2 ^21.3 Taha, MS et al. (2014) Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin. PLoS ONE 9 e91465 PubMed GONUTS page

[PMID:15381419-22] 22.0 ^22.1 Menon, RP et al. (2004) The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J. Mol. Biol. 343 43-53 PubMed GONUTS page

[PMID:19166269-23] 23.0 ^23.1 ^23.2 Bechara, EG et al. (2009) A novel function for fragile X mental retardation protein in translational activation. PLoS Biol. 7 e16 PubMed GONUTS page

[PMID:24514761-24] 24.0 ^24.1 ^24.2 ^24.3 Zhou, Z et al. (2014) Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus. Nat Commun 5 3259 PubMed GONUTS page

[PMID:12927206-25] Chen, L et al. (2003) The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences. Neuroscience 120 1005-17 PubMed GONUTS page

[PMID:17057366-26] 26.0 ^26.1 ^26.2 ^26.3 Plante, I et al. (2006) Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs. J. Biomed. Biotechnol. 2006 64347 PubMed GONUTS page

[PMID:19946888-27] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:15121898-28] Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page

[PMID:22658674-29] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:22681889-30] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:21873635-31] 31.00 ^31.01 ^31.02 ^31.03 ^31.04 ^31.05 ^31.06 ^31.07 ^31.08 ^31.09 ^31.10 ^31.11 ^31.12 ^31.13 ^31.14 ^31.15 ^31.16 ^31.17 ^31.18 ^31.19 ^31.20 ^31.21 ^31.22 ^31.23 ^31.24 ^31.25 ^31.26 ^31.27 ^31.28 ^31.29 ^31.30 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:21446998-32] Sjekloća, L et al. (2011) On the aggregation properties of FMRP--a link with the FXTAS syndrome? FEBS J. 278 1912-21 PubMed GONUTS page

[PMID:17850748-33] Valverde, R et al. (2007) Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein. Structure 15 1090-8 PubMed GONUTS page

[PMID:24204304-34] 34.0 ^34.1 ^34.2 ^34.3 ^34.4 ^34.5 ^34.6 ^34.7 ^34.8 ^34.9 Dury, AY et al. (2013) Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies. PLoS Genet. 9 e1003890 PubMed GONUTS page

[PMID:10888599-35] Tamanini, F et al. (2000) The fragile X-related proteins FXR1P and FXR2P contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins. Hum. Mol. Genet. 9 1487-93 PubMed GONUTS page

[PMID:7692601-36] Ashley, CT Jr et al. (1993) FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262 563-6 PubMed GONUTS page

[PMID:12837692-37] Bardoni, B et al. (2003) 82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization. Hum. Mol. Genet. 12 1689-98 PubMed GONUTS page

[PMID:16407062-38] 38.0 ^38.1 Ramos, A et al. (2006) The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction. Structure 14 21-31 PubMed GONUTS page

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