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Protein Page:
FMR1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
FMR1 Translation repressor. Component of the CYFIP1-EIF4E- FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression. RNA- binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C). Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with CYFIP1 and CYFIP2. The interaction with brain cytoplasmic RNA 1 (BC1) increases binding affinity for the CYFIP1-EIF4E complex in the brain. Homooligomer. Found in a RNP granule complex with IGF2BP1. Directly interacts with SMN and TDRD3. Interacts with the SMN core complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Interacts with FXR1, FXR2, IGF2BP1, NUFIP1, NUFIP2, MCRS1 and RANBP9. Highest levels found in neurons, brain, testis, placenta and lymphocytes. Also expressed in epithelial tissues and at very low levels in glial cells. Belongs to the FMR1 family. 8 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Translation
Cellular Component: nucleoplasm; mRNA cap complex; polysomal ribosome; stress granule; cytoplasm; dendritic spine; nucleolus; synapse; dendritic shaft
Molecular Function: mRNA binding; protein binding; RNA binding
Biological Process: negative regulation of translational initiation; central nervous system development; mRNA transport
Reference #:  Q06787 (UniProtKB)
Alt. Names/Synonyms: FMR1; FMRP; fragile X mental retardation 1; Fragile X mental retardation 1 protein; FRAXA; MGC87458; POF; POF1; premature ovarian failure 1; Protein FMR-1
Gene Symbols: FMR1
Molecular weight: 71,174 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FMR1

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S511‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K17 GSNGAFYKAFVKDVH
0 1 K130 KDTFHKIKLDVPEDL
0 1 K310 LIQEIVDKSGVVRVR
0 1 N336 EEEIMPPNSLPSNNS
0 1 S337 EEIMPPNSLPSNNSR
0 1 P347 SNNSRVGPNAPEEKK
0 1 A349 NSRVGPNAPEEKKHL
0 1 P350 SRVGPNAPEEKKHLD
0 1 S370-p THFSQPNsTKVQRVL
0 2 Y461-p RTDKEKSyVtDDGQG
0 13 T463-p DKEKSyVtDDGQGMG
0 24 R471-m1 DDGQGMGrGSrPYrN
0 2 R471 DDGQGMGRGSrPYrN
0 6 R474-m1 QGMGrGSrPYrNRGH
0 1 R477-m1 GrGSrPYrNRGHGRR
0 1 S497 SGTNSEASNAsETES
10 1 S500-p NSEASNAsETESDHR
1 0 S511-p SDHRDELsDWSLAPT
2 0 R534 RRGDGRRRGGGGRGQ
2 0 R539 RRRGGGGRGQGGrGr
4 0 R544-m GGRGQGGrGrGGGFK
5 0 R546-m RGQGGrGrGGGFKGN
0 1 S620 QKKEKPDSVDGQQPL
  FMR1 iso6  
K17 GSNGAFYKAFVKDVH
K130 KDTFHKIKLDVPEDL
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370 THFSQPNSTKVQRVL
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  FMR1 iso7  
K17 GSNGAFYKAFVKDVH
K130 KDTFHKIKLDVPEDL
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370 THFSQPNSTKVQRVL
Y461 RTDKEKSYVTDDGQG
T463 DKEKSYVTDDGQGMG
R471 DDGQGMGRGSRPYRN
R471 DDGQGMGRGSRPYRN
R474 QGMGRGSRPYRNRGH
R477 GRGSRPYRNRGHGRR
S497 SGTNSEASNASETES
S500 NSEASNASETESDHR
S511 SDHRDELSDWSLAPT
R534 RRGDGRRRGGGGRGQ
R539 RRRGGGGRGQGGRGR
R544 GGRGQGGRGRGGGFK
R546 RGQGGRGRGGGFKGN
S603 QKKEKPDSVDGQQPL
  mouse

 
K17-u GSNGAFYkAFVKDVH
K130-u KDTFHKIkLEVPEDL
K310-u LIQEIVDkSGVVRVR
S336 EEEIMPPSSLPSNNS
S337 EEIMPPSSLPSNNSR
P347 SNNSRVGPNSSEEKK
S349 NSRVGPNSSEEKKHL
S350 SRVGPNSSEEKKHLD
S369 THFSQPNSTKVQRVL
Y460 RTDKEKGYVtDDGQG
T462-p DKEKGYVtDDGQGMG
R470-m1 DDGQGMGrGSrPYRN
R470-m2 DDGQGMGrGSrPYRN
R473-m1 QGMGrGSrPYRNRGH
R476 GrGSrPYRNRGHGRR
S496-p SGTNSEAsNAsETES
S499-p NSEAsNAsETESDHR
S510 SDHRDELSDWSLAPT
R533-m RRGDGRRrRGGGrGQ
R538-m RRrRGGGrGQGGrGr
R543-m GGrGQGGrGrGGGFK
R545-m rGQGGrGrGGGFKGN
S602-p QKKEKPDsVDGLQPL
  rat

 
K17 GSNGAFYKAFVKDVH
K130 KDTFHKIKLEVPEDL
K310 LIQEIVDKSGVVRVR
S336-p EEENLPPssLPSNNS
S337-p EENLPPssLPSNNSR
S347-p SNNSRVGsNssEEKK
S349-p NSRVGsNssEEKKHL
S350-p SRVGsNssEEKKHLD
S369 THFSQPNSTKVQRGM
Y439 RTDKEKGYVTDDGQG
T441 DKEKGYVTDDGQGMG
R449-m1 DDGQGMGrGSRPYRN
R449 DDGQGMGRGSRPYRN
R452 QGMGrGSRPYRNRGH
R455 GrGSRPYRNRGHGRR
S475 SGTNSEASNAsETES
S478-p NSEASNAsETESDHR
S489 SDHRDELSDWSLAPT
R512 RRGDGRRRGGGGRGQ
R517 RRRGGGGRGQGGRGR
R522 GGRGQGGRGRGGGFK
R524 RGQGGRGRGGGFKGN
S581 QKKEKPDSVDGLQPL
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