Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Fragile X mental retardation syndrome-related protein 1  

UniProtKB / Swiss-Prot ID :  FXR1_HUMAN

Gene Name (Synonyms) : 
FXR1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs (By similarity). 

Protein Sequence MAELTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSR...
Predicted Secondary Structure CCCEEEEEECCCCCCHHHHHHHHHHCCEEEEEECCCCCCCCCCCCCCCCCCCCCCHHHHCCCCEEEEEEC...
Protein Variant
LocationDescription
233A -> T (in a breast cancer sample;somatic mutation).
429D -> N (in dbSNP:rs1051080). VAR_016077
614A -> V (in dbSNP:rs11499). VAR_014890
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAELTV
---CCCEEE
22.10UniProtKB
Link-
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PPDIKKEIS
CCCCHHHHC
52.30Phosphositeplus
Link-
83Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)WWLAKVRMM
HHHHHHHHH
28.36Phosphositeplus
Link-
246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQARKVPGV
HHHHCCCCC
56.66Phosphositeplus
Link
265PhosphotyrosineTFRIYGESA
CEEEECCCH
15.58Phosphositeplus
Link
268PhosphoserineIYGESADAV
EECCCHHHH
27.38Phosphositeplus
Link
273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ADAVKKARG
HHHHHHHHH
42.30Phosphositeplus
Link
310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIVDKSGVV
HHHHHCCEE
37.91Phosphositeplus
Link-
325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DNENKLPRE
CCCCCCCCC
54.40Phosphositeplus
Link-
3685-methylarginineLRMERLQID
HHHHHHHHH
23.66HPRD
Link-
401PhosphothreonineSGYGTNSEL
CCCCCCCCC
27.39HPRD
Link-
401PhosphothreonineSGYGTNSEL
CCCCCCCCC
27.39SysPTM
Link-
403PhosphoserineYGTNSELSN
CCCCCCCCC
39.49HPRD
Link-
403PhosphoserineYGTNSELSN
CCCCCCCCC
39.49SysPTM
Link-
406PhosphoserineNSELSNPSE
CCCCCCCCC
42.52HPRD
Link-
406PhosphoserineNSELSNPSE
CCCCCCCCC
42.52PhosphoELM
Link-
406PhosphoserineNSELSNPSE
CCCCCCCCC
42.52Phosphositeplus
Link-
406PhosphoserineNSELSNPSE
CCCCCCCCC
42.52SysPTM
Link-
406Phosphoserine.NSELSNPSE
CCCCCCCCC
42.52UniProtKB
Link-
409PhosphoserineLSNPSETES
CCCCCCCCC
62.49HPRD
Link-
409PhosphoserineLSNPSETES
CCCCCCCCC
62.49HPRD
Link-
409PhosphoserineLSNPSETES
CCCCCCCCC
62.49PhosphoELM
Link-
409PhosphoserineLSNPSETES
CCCCCCCCC
62.49Phosphositeplus
Link-
409PhosphoserineLSNPSETES
CCCCCCCCC
62.49SysPTM
Link-
409Phosphoserine.LSNPSETES
CCCCCCCCC
62.49UniProtKB
Link-
411PhosphothreonineNPSETESER
CCCCCCCHH
49.50HPRD
Link-
411PhosphothreonineNPSETESER
CCCCCCCHH
49.50SysPTM
Link-
413PhosphoserineSETESERKD
CCCCCHHHC
50.55HPRD
Link-
413PhosphoserineSETESERKD
CCCCCHHHC
50.55SysPTM
Link-
420PhosphoserineKDELSDWSL
HCCCCCEEE
34.68HPRD
Link-
420PhosphoserineKDELSDWSL
HCCCCCEEE
34.68Phosphositeplus
Link-
423PhosphoserineLSDWSLAGE
CCCEEECCC
17.21HPRD
Link-
423PhosphoserineLSDWSLAGE
CCCEEECCC
17.21Phosphositeplus
Link-
432PhosphoserineDDRDSRHQR
CCCCCCHHH
32.34HPRD
Link-
4455-methylarginineRPGGRGRSV
CCCCCCCCC
43.18HPRD
Link-
4455-methylarginineRPGGRGRSV
CCCCCCCCC
43.18SysPTM
Link-
445N2,N2-dimethylarginineRPGGRGRSV
CCCCCCCCC
43.18MeMo
Link-
445N2,N2-dimethylarginineRPGGRGRSV
CCCCCCCCC
43.18Phosphositeplus
Link-
445Omega-N-methylated arginine.RPGGRGRSV
CCCCCCCCC
43.18UniProtKB
Link-
4535-methylarginineVSGGRGRGG
CCCCCCCCC
34.85HPRD
Link-
477PhosphotyrosineDSNPYSLLD
CCCCCCCCC
19.05HPRD
Link-
477PhosphotyrosineDSNPYSLLD
CCCCCCCCC
19.05Phosphositeplus
Link-
477PhosphotyrosineDSNPYSLLD
CCCCCCCCC
19.05SysPTM
Link-
477Phosphotyrosine.DSNPYSLLD
CCCCCCCCC
19.05UniProtKB
Link-
483PhosphothreonineLLDNTESDQ
CCCCCCCCC
36.21HPRD
Link-
483PhosphothreonineLLDNTESDQ
CCCCCCCCC
36.21PhosphoELM
Link-
483PhosphothreonineLLDNTESDQ
CCCCCCCCC
36.21Phosphositeplus
Link-
485PhosphoserineDNTESDQTA
CCCCCCCCC
32.74HPRD
Link-
485PhosphoserineDNTESDQTA
CCCCCCCCC
32.74PhosphoELM
Link-
485PhosphoserineDNTESDQTA
CCCCCCCCC
32.74Phosphositeplus
Link-
485PhosphoserineDNTESDQTA
CCCCCCCCC
32.74SysPTM
Link-
488PhosphothreonineESDQTADTD
CCCCCCCCC
31.34HPRD
Link-
488PhosphothreonineESDQTADTD
CCCCCCCCC
31.34PhosphoELM
Link-
488PhosphothreonineESDQTADTD
CCCCCCCCC
31.34SysPTM
Link-
491PhosphothreonineQTADTDASE
CCCCCCCCC
30.88HPRD
Link-
491PhosphothreonineQTADTDASE
CCCCCCCCC
30.88PhosphoELM
Link-
494PhosphoserineDTDASESHH
CCCCCCCCC
42.30HPRD
Link-
494PhosphoserineDTDASESHH
CCCCCCCCC
42.30PhosphoELM
Link-
494PhosphoserineDTDASESHH
CCCCCCCCC
42.30SysPTM
Link-
500PhosphothreonineSHHSTNRRR
CCCCHHHHH
28.52HPRD
Link-
500PhosphothreonineSHHSTNRRR
CCCCHHHHH
28.52PhosphoELM
Link-
511PhosphothreonineRRRRTDEDA
CCCCCCCCC
41.76Phosphositeplus
Link-
524Phosphoserine.GMTESDTAS
CCCCCCCCC
30.97UniProtKB
Link-
528Phosphoserine.SDTASVNEN
CCCCCCCCC
27.80UniProtKB
Link-
585PhosphoserineNGPTSASGD
CCCCCCCCC
24.46Phosphositeplus
Link-
587PhosphoserinePTSASGDDI
CCCCCCCHH
42.39HPRD
Link-
587PhosphoserinePTSASGDDI
CCCCCCCHH
42.39Phosphositeplus
Link-
587Phosphoserine.PTSASGDDI
CCCCCCCHH
42.39UniProtKB
Link-
597PhosphothreonineKLQRTPGEE
CCCCCCCHH
23.76HPRD
Link-
597PhosphothreonineKLQRTPGEE
CCCCCCCHH
23.76Phosphositeplus
Link-
611PhosphothreonineKEENTQEAA
HHCCHHHHH
30.94Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PRS23_HUMANphysical interactionMINT-63255MINT16169070
GBP7_HUMANphysical interactionMINT-64925MINT16169070
ERG28_HUMANphysical interactionMINT-64928MINT16169070
LC7L2_HUMANphysical interactionMINT-64929MINT16169070
ERG28_HUMANphysical interactionEBI-730036
intact16169070
LC7L2_HUMANphysical interactionEBI-730039
intact16169070
RIF1_HUMANphysical interactionEBI-730042
intact16169070
DPYL1_HUMANphysical interactionEBI-731992
intact16169070
GBP2_HUMANphysical interactionEBI-731995
intact16169070
K1377_HUMANphysical interactionEBI-731998
intact16169070
FMR1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02892HPRD7489725
8668200
10527928
FXR1_HUMANin vitro
in vivo
HPRD:02892HPRD7489725
ERG28_HUMANyeast 2-hybridHPRD:02892HPRD16169070
PRS23_HUMANyeast 2-hybridHPRD:02892HPRD16169070
LC7L2_HUMANyeast 2-hybridHPRD:02892HPRD16169070
CA103_HUMANyeast 2-hybridHPRD:02892HPRD16169070
K1377_HUMANyeast 2-hybridHPRD:02892HPRD16169070
NR1H4_HUMANENSP00000350170STRING
FXR2_HUMANENSP00000350170STRING
CYFP1_HUMANENSP00000350170STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-445, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409; SER-524;SER-528 AND SER-587, AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-477, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures