FXR1_HUMAN - dbPTM
FXR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FXR1_HUMAN
UniProt AC P51114
Protein Name Fragile X mental retardation syndrome-related protein 1
Gene Name FXR1
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Cytoplasm .
Protein Description 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 MAELTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESADAVKKARGFLEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDDISKLQRTPGEEKINTLKEENTQEAAVLNGVS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAELTVEVR
------CCEEEEEEE
22.1022814378
11PhosphorylationLTVEVRGSNGAFYKG
EEEEEECCCCCEEEC
22.8628348404
17AcetylationGSNGAFYKGFIKDVH
CCCCCEEECEEEEEC
40.6726051181
17UbiquitinationGSNGAFYKGFIKDVH
CCCCCEEECEEEEEC
40.67-
56SumoylationLPPPPDIKKEISEGD
CCCCCCCCCCCCCCC
52.3028112733
56UbiquitinationLPPPPDIKKEISEGD
CCCCCCCCCCCCCCC
52.3021906983
56 (in isoform 1)Ubiquitination-52.3021906983
56 (in isoform 2)Ubiquitination-52.3021906983
57UbiquitinationPPPPDIKKEISEGDE
CCCCCCCCCCCCCCE
61.69-
60PhosphorylationPDIKKEISEGDEVEV
CCCCCCCCCCCEEEE
36.3028985074
68PhosphorylationEGDEVEVYSRANDQE
CCCEEEEEECCCCCC
4.4825147952
77GlutathionylationRANDQEPCGWWLAKV
CCCCCCCCHHEEEEE
7.5822555962
83AcetylationPCGWWLAKVRMMKGE
CCHHEEEEEEHHCCC
28.3626051181
83UbiquitinationPCGWWLAKVRMMKGE
CCHHEEEEEEHHCCC
28.3683
83 (in isoform 1)Ubiquitination-28.3621906983
83 (in isoform 2)Ubiquitination-28.3621906983
92PhosphorylationRMMKGEFYVIEYAAC
EHHCCCEEEEEEEEE
9.0126552605
96PhosphorylationGEFYVIEYAACDATY
CCEEEEEEEEECCCC
6.5926552605
102PhosphorylationEYAACDATYNEIVTF
EEEEECCCCCEEEEE
17.3926552605
103PhosphorylationYAACDATYNEIVTFE
EEEECCCCCEEEEEE
16.7226552605
108PhosphorylationATYNEIVTFERLRPV
CCCCEEEEEEEECCC
25.9926552605
119UbiquitinationLRPVNQNKTVKKNTF
ECCCCCCCCCCCCCE
44.95-
128UbiquitinationVKKNTFFKCTVDVPE
CCCCCEEEEEEECCH
25.46-
148UbiquitinationCANENAHKDFKKAVG
HHCCCHHHHHHHHHH
63.55-
161 (in isoform 3)Ubiquitination-17.6921906983
179UbiquitinationSASEATVKRVNILSD
ECCHHCHHHHHHCCH
46.39-
188 (in isoform 3)Ubiquitination-24.0721906983
190MethylationILSDMHLRSIRTKLM
HCCHHHHHHHHHHHH
18.50-
191PhosphorylationLSDMHLRSIRTKLML
CCHHHHHHHHHHHHH
23.84-
194PhosphorylationMHLRSIRTKLMLMSR
HHHHHHHHHHHHHHC
27.1926552605
195AcetylationHLRSIRTKLMLMSRN
HHHHHHHHHHHHHCC
23.2725953088
195UbiquitinationHLRSIRTKLMLMSRN
HHHHHHHHHHHHHCC
23.27-
200PhosphorylationRTKLMLMSRNEEATK
HHHHHHHHCCHHHHH
28.1728851738
206PhosphorylationMSRNEEATKHLECTK
HHCCHHHHHHHHHHH
23.4426552605
207AcetylationSRNEEATKHLECTKQ
HCCHHHHHHHHHHHH
53.9225953088
207UbiquitinationSRNEEATKHLECTKQ
HCCHHHHHHHHHHHH
53.92-
213UbiquitinationTKHLECTKQLAAAFH
HHHHHHHHHHHHHHC
55.78-
225 (in isoform 3)Ubiquitination-7.2421906983
236PhosphorylationLMGLAIGTHGSNIQQ
HHHHHCCCCCCCHHH
19.5620873877
239PhosphorylationLAIGTHGSNIQQARK
HHCCCCCCCHHHHHC
24.1320873877
240 (in isoform 3)Ubiquitination-40.4521906983
246UbiquitinationSNIQQARKVPGVTAI
CCHHHHHCCCCEEEE
56.6621906983
246 (in isoform 1)Ubiquitination-56.6621906983
246 (in isoform 2)Ubiquitination-56.6621906983
265PhosphorylationDTGTFRIYGESADAV
CCCEEEEEECCHHHH
15.5828152594
268PhosphorylationTFRIYGESADAVKKA
EEEEEECCHHHHHHH
27.3828152594
273UbiquitinationGESADAVKKARGFLE
ECCHHHHHHHHHHHH
42.3021906983
273 (in isoform 1)Ubiquitination-42.3021906983
273 (in isoform 2)Ubiquitination-42.3021906983
274UbiquitinationESADAVKKARGFLEF
CCHHHHHHHHHHHHH
36.40-
295AcetylationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC
24.1725953088
295MalonylationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC
24.1726320211
295UbiquitinationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC
24.17-
302AcetylationKVIGKNGKVIQEIVD
HHHCCCCCEEEEEEC
45.6325953088
302UbiquitinationKVIGKNGKVIQEIVD
HHHCCCCCEEEEEEC
45.63-
310AcetylationVIQEIVDKSGVVRVR
EEEEEECCCCCEEEE
37.9126051181
310UbiquitinationVIQEIVDKSGVVRVR
EEEEEECCCCCEEEE
37.9121906983
310 (in isoform 1)Ubiquitination-37.9121906983
310 (in isoform 2)Ubiquitination-37.9121906983
324 (in isoform 3)Phosphorylation-58.3718669648
325AcetylationIEGDNENKLPREDGM
EECCCCCCCCCCCCC
54.4026051181
325UbiquitinationIEGDNENKLPREDGM
EECCCCCCCCCCCCC
54.402190698
325 (in isoform 1)Ubiquitination-54.4021906983
325 (in isoform 2)Ubiquitination-54.4021906983
353PhosphorylationNVQVLLEYHIAYLKE
CHHHHHHHHHHHHHH
9.8622817900
357PhosphorylationLLEYHIAYLKEVEQL
HHHHHHHHHHHHHHH
20.0822817900
360MethylationYHIAYLKEVEQLRME
HHHHHHHHHHHHHHH
49.0115782174
365MethylationLKEVEQLRMERLQID
HHHHHHHHHHHHCHH
25.30-
368MethylationVEQLRMERLQIDEQL
HHHHHHHHHCHHHHH
23.6615782174
376MethylationLQIDEQLRQIGSRSY
HCHHHHHHHHCCCCC
26.26-
386MethylationGSRSYSGRGRGRRGP
CCCCCCCCCCCCCCC
26.20-
395PhosphorylationRGRRGPNYTSGYGTN
CCCCCCCCCCCCCCC
12.8625850435
396PhosphorylationGRRGPNYTSGYGTNS
CCCCCCCCCCCCCCC
23.4723401153
397PhosphorylationRRGPNYTSGYGTNSE
CCCCCCCCCCCCCCC
21.4723927012
399PhosphorylationGPNYTSGYGTNSELS
CCCCCCCCCCCCCCC
22.1223927012
401PhosphorylationNYTSGYGTNSELSNP
CCCCCCCCCCCCCCC
27.3923927012
403PhosphorylationTSGYGTNSELSNPSE
CCCCCCCCCCCCCCC
39.4923927012
406PhosphorylationYGTNSELSNPSETES
CCCCCCCCCCCCCHH
42.5223927012
409PhosphorylationNSELSNPSETESERK
CCCCCCCCCCHHHHH
62.4923927012
411PhosphorylationELSNPSETESERKDE
CCCCCCCCHHHHHHH
49.5030278072
413PhosphorylationSNPSETESERKDELS
CCCCCCHHHHHHHHC
50.5523927012
416UbiquitinationSETESERKDELSDWS
CCCHHHHHHHHCHHH
52.05-
420PhosphorylationSERKDELSDWSLAGE
HHHHHHHCHHHHCCC
34.6830266825
423PhosphorylationKDELSDWSLAGEDDR
HHHHCHHHHCCCCCC
17.2130266825
432PhosphorylationAGEDDRDSRHQRDSR
CCCCCCCCCHHHHCC
32.3430266825
438PhosphorylationDSRHQRDSRRRPGGR
CCCHHHHCCCCCCCC
29.85-
445DimethylationSRRRPGGRGRSVSGG
CCCCCCCCCCCCCCC
43.18-
445MethylationSRRRPGGRGRSVSGG
CCCCCCCCCCCCCCC
43.1815782174
447MethylationRRPGGRGRSVSGGRG
CCCCCCCCCCCCCCC
32.31-
448PhosphorylationRPGGRGRSVSGGRGR
CCCCCCCCCCCCCCC
24.3729496963
450PhosphorylationGGRGRSVSGGRGRGG
CCCCCCCCCCCCCCC
36.4630177828
453DimethylationGRSVSGGRGRGGPRG
CCCCCCCCCCCCCCC
34.85-
453MethylationGRSVSGGRGRGGPRG
CCCCCCCCCCCCCCC
34.8515782174
455DimethylationSVSGGRGRGGPRGGK
CCCCCCCCCCCCCCC
45.60-
455MethylationSVSGGRGRGGPRGGK
CCCCCCCCCCCCCCC
45.60-
459DimethylationGRGRGGPRGGKSSIS
CCCCCCCCCCCCCHH
70.53-
459MethylationGRGRGGPRGGKSSIS
CCCCCCCCCCCCCHH
70.53-
462"N6,N6-dimethyllysine"RGGPRGGKSSISSVL
CCCCCCCCCCHHHHH
43.80-
462MethylationRGGPRGGKSSISSVL
CCCCCCCCCCHHHHH
43.8023748837
463O-linked_GlycosylationGGPRGGKSSISSVLK
CCCCCCCCCHHHHHC
35.8623301498
463PhosphorylationGGPRGGKSSISSVLK
CCCCCCCCCHHHHHC
35.8621945579
464PhosphorylationGPRGGKSSISSVLKD
CCCCCCCCHHHHHCC
29.9421945579
466PhosphorylationRGGKSSISSVLKDPD
CCCCCCHHHHHCCCC
19.1521945579
467PhosphorylationGGKSSISSVLKDPDS
CCCCCHHHHHCCCCC
29.7821945579
470AcetylationSSISSVLKDPDSNPY
CCHHHHHCCCCCCCC
66.1326051181
470UbiquitinationSSISSVLKDPDSNPY
CCHHHHHCCCCCCCC
66.13-
474PhosphorylationSVLKDPDSNPYSLLD
HHHCCCCCCCCCCCC
45.1321945579
477PhosphorylationKDPDSNPYSLLDNTE
CCCCCCCCCCCCCCC
19.0521945579
478PhosphorylationDPDSNPYSLLDNTES
CCCCCCCCCCCCCCC
24.5821945579
483PhosphorylationPYSLLDNTESDQTAD
CCCCCCCCCCCCCCC
36.2121945579
485PhosphorylationSLLDNTESDQTADTD
CCCCCCCCCCCCCCC
32.7421945579
488PhosphorylationDNTESDQTADTDASE
CCCCCCCCCCCCHHH
31.3421945579
491PhosphorylationESDQTADTDASESHH
CCCCCCCCCHHHCHH
30.8821945579
494PhosphorylationQTADTDASESHHSTN
CCCCCCHHHCHHHHH
42.3021945579
496PhosphorylationADTDASESHHSTNRR
CCCCHHHCHHHHHHH
24.8121945579
499PhosphorylationDASESHHSTNRRRRS
CHHHCHHHHHHHHHH
23.1921945579
500PhosphorylationASESHHSTNRRRRSR
HHHCHHHHHHHHHHH
28.5221945579
506PhosphorylationSTNRRRRSRRRRTDE
HHHHHHHHHHCCCCC
28.47-
511PhosphorylationRRSRRRRTDEDAVLM
HHHHHCCCCCCCEEC
41.7628985074
511 (in isoform 2)Phosphorylation-41.7627273156
522PhosphorylationAVLMDGMTESDTASV
CEECCCCCHHHCCCC
37.56-
522 (in isoform 2)Phosphorylation-37.5630266825
524PhosphorylationLMDGMTESDTASVNE
ECCCCCHHHCCCCCC
30.9728985074
524 (in isoform 2)Phosphorylation-30.9730266825
526PhosphorylationDGMTESDTASVNENG
CCCCHHHCCCCCCCC
30.0628985074
526 (in isoform 2)Phosphorylation-30.0630266825
528PhosphorylationMTESDTASVNENGLV
CCHHHCCCCCCCCCE
27.8019690332
528 (in isoform 2)Phosphorylation-27.8030266825
540PhosphorylationGLVTVADYISRAESQ
CCEEHHHHHHHHHHH
7.34-
542PhosphorylationVTVADYISRAESQSR
EEHHHHHHHHHHHHH
21.1422496350
546PhosphorylationDYISRAESQSRQRNL
HHHHHHHHHHHHHCC
32.2526853621
557PhosphorylationQRNLPRETLAKNKKE
HHCCCHHHHHHCHHH
33.0428555341
565SulfoxidationLAKNKKEMAKDVIEE
HHHCHHHHHHHHHHH
8.4621406390
567AcetylationKNKKEMAKDVIEEHG
HCHHHHHHHHHHHHC
51.7425953088
576PhosphorylationVIEEHGPSEKAINGP
HHHHHCCCHHHCCCC
57.2126074081
578AcetylationEEHGPSEKAINGPTS
HHHCCCHHHCCCCCC
59.9323236377
584PhosphorylationEKAINGPTSASGDDI
HHHCCCCCCCCCCCH
38.0230266825
585PhosphorylationKAINGPTSASGDDIS
HHCCCCCCCCCCCHH
24.4630266825
587PhosphorylationINGPTSASGDDISKL
CCCCCCCCCCCHHHH
42.3930266825
592PhosphorylationSASGDDISKLQRTPG
CCCCCCHHHHCCCCC
34.0230266825
593AcetylationASGDDISKLQRTPGE
CCCCCHHHHCCCCCH
49.3126051181
597PhosphorylationDISKLQRTPGEEKIN
CHHHHCCCCCHHHHH
23.7625159151
605PhosphorylationPGEEKINTLKEENTQ
CCHHHHHHHCHHCHH
42.5524732914
607AcetylationEEKINTLKEENTQEA
HHHHHHHCHHCHHHH
62.0326051181
611PhosphorylationNTLKEENTQEAAVLN
HHHCHHCHHHHHHHC
30.9428112733

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
420SPhosphorylationKinasePAK1Q13153
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXO4Q9UKT5
PMID:29142209

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
445RMethylation

-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FXR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FMR1_HUMANFMR1physical
7489725
CYFP2_HUMANCYFIP2physical
11438699
DPYL1_HUMANCRMP1physical
16169070
GBP2_HUMANGBP2physical
16169070
CE126_HUMANKIAA1377physical
16169070
ERG28_HUMANC14orf1physical
16169070
LC7L2_HUMANLUC7L2physical
16169070
LRIF1_HUMANLRIF1physical
16169070
FXR2_HUMANFXR2physical
8668200
FXR2_HUMANFXR2physical
7489725
FXR1_HUMANFXR1physical
7489725
CAPR1_HUMANCAPRIN1physical
24778252
FMR1_HUMANFMR1physical
24778252
FXR2_HUMANFXR2physical
24778252
LRWD1_HUMANLRWD1physical
24778252
ORC2_HUMANORC2physical
24778252
RANB9_HUMANRANBP9physical
24778252
TDRD3_HUMANTDRD3physical
24778252
TOP3B_HUMANTOP3Bphysical
24778252
UBAP2_HUMANUBAP2physical
24778252
FBX4_HUMANFBXO4physical
29142209
SKP1_HUMANSKP1physical
29142209
CUL1_HUMANCUL1physical
29142209
RBX1_HUMANRBX1physical
29142209
GSK3B_HUMANGSK3Bphysical
29142209

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FXR1_HUMAN

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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
"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.
"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.
"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.
"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.
"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.

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