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Protein Page:
FMR1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: RNA-binding; Translation; Nucleolus
Chromosomal Location of Human Ortholog: Xq27.3
Cellular Component: axon; cell projection; chromocenter; chromosome; cytoplasm; dendrite; dendritic spine; extrinsic to plasma membrane; filopodium tip; growth cone; membrane; mRNA cap complex; nerve terminal; neuron projection; nucleolus; nucleoplasm; nucleus; perikaryon; perinuclear region of cytoplasm; polysomal ribosome; polysome; postsynaptic density; ribonucleoprotein complex; SMN complex; synapse
Molecular Function: chromatin binding; dynein binding; identical protein binding; methylated histone residue binding; microtubule binding; miRNA binding; mRNA 3'-UTR binding; mRNA 5'-UTR binding; mRNA binding; poly(rG) binding; poly(U) binding; protein binding; protein heterodimerization activity; protein homodimerization activity; ribosome binding; RNA binding; RNA strand annealing activity; siRNA binding; translation initiation factor binding; translation repressor activity
Biological Process: glutamate signaling pathway; mRNA transport; negative regulation of translation; negative regulation of translational initiation; positive regulation of filopodium formation; positive regulation of histone phosphorylation; positive regulation of receptor internalization; positive regulation of translation; regulation of alternative nuclear mRNA splicing, via spliceosome; regulation of filopodium formation; regulation of mRNA stability; regulation of neurotransmitter secretion; response to DNA damage stimulus
Disease: Fragile X Mental Retardation Syndrome; Fragile X Tremor/ataxia Syndrome; Premature Ovarian Failure 1
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.
Download PyMol Script
Download ChimeraX Script


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Sites Implicated In
neural plasticity: S500‑p
translation, inhibited: S500‑p
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



 LTP 

LTP: 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.


 HTP 

HTP: 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 T122‑p VNPNKPAtKDTFHKI
0 1 K130 KDTFHKIKLDVPEDL
0 1 K143 DLRQMCAKEAAHKDF
0 1 K295 VPRNLVGKVIGKNGK
0 1 K310 LIQEIVDKSGVVRVR
0 1 N336 EEEIMPPNsLPSNNS
0 2 S337‑p EEIMPPNsLPSNNSR
0 1 P347 SNNSRVGPNAPEEKK
0 1 A349 NSRVGPNAPEEKKHL
0 1 P350 SRVGPNAPEEKKHLD
0 2 S370‑p THFSQPNsTKVQRVL
0 1 S460‑p NRTDKEKsyVtDDGQ
0 1 Y461‑p RTDKEKsyVtDDGQG
0 15 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
16 3 S500‑p NSEASNAsETESDHR
1 1 S511‑p SDHRDELsDWSLAPT
2 0 R534 RRGDGRRRGGGGRGQ
2 0 R539 RRRGGGGRGQGGrGr
0 1 R539 RRRGGGGRGQGGrGr
4 0 R544‑me GGRGQGGrGrGGGFK
5 0 R546‑me RGQGGrGrGGGFKGN
0 1 T594 ERSVHTKTLQNtSSE
0 1 T598‑p HTKTLQNtSSEGSRL
0 3 S620‑p QKKEKPDsVDGQQPL
0 1 - gap
0 1 - gap
  FMR1 iso2  
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLDVPEDL
K143 DLRQMCAKEAAHKDF
K295 VPRNLVGKVIGKNGK
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370 THFSQPNSTKVQRGM
S439 NRTDKEKSYVTDDGQ
Y440 RTDKEKSYVTDDGQG
T442 DKEKSYVTDDGQGMG
R450 DDGQGMGRGSRPYRN
R450 DDGQGMGRGSRPYRN
R453 QGMGRGSRPYRNRGH
R456 GRGSRPYRNRGHGRR
S476 SGTNSEASNASETES
S479 NSEASNASETESDHR
S490 SDHRDELSDWSLAPT
R513 RRGDGRRRGGGGRGQ
R518 RRRGGGGRGQGGRGR
R518 RRRGGGGRGQGGRGR
R523 GGRGQGGRGRGGGFK
R525 RGQGGRGRGGGFKGN
S556 KGRTTDGSLQNTSSE
T560 TDGSLQNTSSEGSRL
S582 QKKEKPDSVDGQQPL
- gap
- gap
  FMR1 iso3  
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLDVPEDL
K143 DLRQMCAKEAAHKDF
K295 VPRNLVGKVIGKNGK
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370 THFSQPNSTKVQRVL
S460 NRTDKEKSYVTDDGQ
Y461 RTDKEKSYVTDDGQG
T463 DKEKSYVTDDGQGMG
R471 DDGQGMGRGSRPYRN
R471 DDGQGMGRGSRPYRN
R474 QGMGRGSRPYRNRGH
R477 GRGSRPYRNRGHGRR
- gap
- gap
S499 SDHRDELSDWSLAPT
R522 RRGDGRRRGGGGRGQ
R527 RRRGGGGRGQGGRGR
R527 RRRGGGGRGQGGRGR
R532 GGRGQGGRGRGGGFK
R534 RGQGGRGRGGGFKGN
T582 ERSVHTKTLQNTSSE
T586 HTKTLQNTSSEGSRL
S608 QKKEKPDSVDGQQPL
- gap
- gap
  FMR1 iso6  
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLDVPEDL
K143 DLRQMCAKEAAHKDF
K295 VPRNLVGKVIGKNGK
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
- gap
- gap
- gap
- gap
S527‑p IVTRRKRsQtAWMVS
T529‑p TRRKRsQtAWMVSNH
  FMR1 iso7  
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLDVPEDL
K143 DLRQMCAKEAAHKDF
K295 VPRNLVGKVIGKNGK
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370 THFSQPNSTKVQRVL
S460 NRTDKEKSYVTDDGQ
Y461 RTDKEKSYVTDDGQG
T463 DKEKSYVTDDGQGMG
R471 DDGQGMGRGSRPYRN
R471 DDGQGMGRGSRPYRN
R474 QGMGRGSRPYRNRGH
R477 GRGSRPYRNRGHGRR
S497 SGTNSEASNASETES
S500 NSEASNASETESDHR
S511 SDHRDELSDWSLAPT
R534 RRGDGRRRGGGGRGQ
R539 RRRGGGGRGQGGRGR
R539 RRRGGGGRGQGGRGR
R544 GGRGQGGRGRGGGFK
R546 RGQGGRGRGGGFKGN
S577‑p KGRTTDGsLQNTSSE
T581 TDGsLQNTSSEGSRL
S603 QKKEKPDSVDGQQPL
- gap
- gap
  FMR1 iso8  
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLDVPEDL
K143 DLRQMCAKEAAHKDF
K295 VPRNLVGKVIGKNGK
K310 LIQEIVDKSGVVRVR
N336 EEEIMPPNSLPSNNS
S337 EEIMPPNSLPSNNSR
P347 SNNSRVGPNAPEEKK
A349 NSRVGPNAPEEKKHL
P350 SRVGPNAPEEKKHLD
S370‑p THFSQPNsTKVQRGM
S439 NRTDKEKSYVTDDGQ
Y440 RTDKEKSYVTDDGQG
T442 DKEKSYVTDDGQGMG
R450 DDGQGMGRGSRPYRN
R450 DDGQGMGRGSRPYRN
R453 QGMGRGSRPYRNRGH
R456 GRGSRPYRNRGHGRR
- gap
- gap
- gap
R488 RRGDGRRRGGGGRGQ
R493 RRRGGGGRGQGGRGR
R493 RRRGGGGRGQGGRGR
R498 GGRGQGGRGRGGGFK
R500 RGQGGRGRGGGFKGN
T548 ERSVHTKTLQNTSSE
T552 HTKTLQNTSSEGSRL
S574 QKKEKPDSVDGQQPL
- gap
- gap
  mouse

 
K17‑ub GSNGAFYkAFVKDVH
T122 VNPNKPATKDTFHKI
K130‑ub KDTFHKIkLEVPEDL
K143‑ac DLRQMCAkESAHKDF
K295‑ac VPRNLVGkVIGKNGK
K310‑ub LIQEIVDkSGVVRVR
S336 EEEIMPPSSLPSNNS
S337 EEIMPPSSLPSNNSR
P347 SNNSRVGPNSSEEKK
S349 NSRVGPNSSEEKKHL
S350 SRVGPNSSEEKKHLD
S369 THFSQPNSTKVQRVL
G459 NRTDKEKGYVtDDGQ
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‑me RRGDGRRrRGGGrGQ
R538‑me RRrRGGGrGQGGrGr
R538‑m1 RRrRGGGrGQGGrGr
R543‑me GGrGQGGrGrGGGFK
R545‑me rGQGGrGrGGGFKGN
S576 KGRTADGSLQSASSE
A580 ADGSLQSASSEGSRL
S602‑p QKKEKPDsVDGLQPL
- gap
- gap
  rat

 
K17 GSNGAFYKAFVKDVH
T122 VNPNKPATKDTFHKI
K130 KDTFHKIKLEVPEDL
K143 DLRQMCAKESAHKDF
K295 VPRNLVGKVIGKNGK
K310 LIQEIVDKSGVVRVR
S336‑p EEENLPPssLPSNNS
S337‑p EENLPPssLPSNNSR
S347‑p SNNSRVGsNssEEKK
S349‑p NSRVGsNssEEKKHL
S350‑p SRVGsNssEEKKHLD
S369 THFSQPNSTKVQRGM
G438 NRTDKEKGYVTDDGQ
Y439 RTDKEKGYVTDDGQG
T441 DKEKGYVTDDGQGMG
R449‑m1 DDGQGMGrGSRPYRN
R449 DDGQGMGRGSRPYRN
R452 QGMGrGSRPYRNRGH
R455 GrGSRPYRNRGHGRR
S475 SGTNSEASNAsETES
S478‑p NSEASNAsETESDHR
S489 SDHRDELSDWSLAPT
R512 RRGDGRRRGGGGRGQ
R517 RRRGGGGRGQGGRGR
R517 RRRGGGGRGQGGRGR
R522 GGRGQGGRGRGGGFK
R524 RGQGGRGRGGGFKGN
S555 KGRTTDGSLQSTSSE
T559 TDGSLQSTSSEGSRL
S581 QKKEKPDSVDGLQPL
- gap
- gap
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