FXR2_HUMAN - dbPTM
FXR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FXR2_HUMAN
UniProt AC P51116
Protein Name Fragile X mental retardation syndrome-related protein 2
Gene Name FXR2
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Cytoplasm.
Protein Description RNA-binding protein..
Protein Sequence MGGLASGGDVEPGLPVEVRGSNGAFYKGFVKDVHEDSVTIFFENNWQSERQIPFGDVRLPPPADYNKEITEGDEVEVYSRANEQEPCGWWLARVRMMKGDFYVIEYAACDATYNEIVTLERLRPVNPNPLATKGSFFKVTMAVPEDLREACSNENVHKEFKKALGANCIFLNITNSELFILSTTEAPVKRASLLGDMHFRSLRTKLLLMSRNEEATKHLETSKQLAAAFQEEFTVREDLMGLAIGTHGANIQQARKVPGVTAIELGEETCTFRIYGETPEACRQARSYLEFSEDSVQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRVEGDNDKKNPREEGMVPFIFVGTRENISNAQALLEYHLSYLQEVEQLRLERLQIDEQLRQIGLGFRPPGSGRGSGGSDKAGYSTDESSSSSLHATRTYGGSYGGRGRGRRTGGPAYGPSSDVSTASETESEKREEPNRAGPGDRDPPTRGEESRRRPTGGRGRGPPPAPRPTSRYNSSSISSVLKDPDSNPYSLLDTSEPEPPVDSEPGEPPPASARRRRSRRRRTDEDRTVMDGGLESDGPNMTENGLEDESRPQRRNRSRRRRNRGNRTDGSISGDRQPVTVADYISRAESQSRQRPPLERTKPSEDSLSGQKGDSVSKLPKGPSENGELSAPLELGSMVNGVS
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
6Phosphorylation--MGGLASGGDVEPG
--CCCCCCCCCCCCC		48.6420068231
21PhosphorylationLPVEVRGSNGAFYKG
CCEEEECCCCCEEEC		22.8628348404
26PhosphorylationRGSNGAFYKGFVKDV
ECCCCCEEECEEEEE		15.07-
27AcetylationGSNGAFYKGFVKDVH
CCCCCEEECEEEEEC		39.1426051181
27UbiquitinationGSNGAFYKGFVKDVH
CCCCCEEECEEEEEC		39.1432015554
70PhosphorylationADYNKEITEGDEVEV
CCCCCCCCCCCEEEE		34.70-
78PhosphorylationEGDEVEVYSRANEQE
CCCEEEEEECCCCCC		4.48-
113PhosphorylationYAACDATYNEIVTLE
EEEECCCCCCEEEEE		16.72-
1332-HydroxyisobutyrylationNPNPLATKGSFFKVT
CCCCCCCCCCEEEEE		47.12-
133UbiquitinationNPNPLATKGSFFKVT
CCCCCCCCCCEEEEE		47.1232015554
135PhosphorylationNPLATKGSFFKVTMA
CCCCCCCCEEEEEEE		29.1229970186
138UbiquitinationATKGSFFKVTMAVPE
CCCCCEEEEEEECCH		34.4832015554
192PhosphorylationEAPVKRASLLGDMHF
CCCCHHHHHCCCHHH		28.3222617229
205UbiquitinationHFRSLRTKLLLMSRN
HHHHHHHHHHHHHCC		30.6129967540
256UbiquitinationANIQQARKVPGVTAI
CCHHHHHCCCCEEEE		56.6623000965
270GlutathionylationIELGEETCTFRIYGE
EECCCCEEEEEEECC		3.7122555962
275PhosphorylationETCTFRIYGETPEAC
CEEEEEEECCCHHHH		12.4928152594
278PhosphorylationTFRIYGETPEACRQA
EEEEECCCHHHHHHH		23.2821815630
305UbiquitinationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC		24.17-
312UbiquitinationKVIGKNGKVIQEIVD
HHHCCCCCEEEEEEC		45.6332015554
320UbiquitinationVIQEIVDKSGVVRVR
EEEEEECCCCCEEEE		37.9123000965
334UbiquitinationRVEGDNDKKNPREEG
EEECCCCCCCCCCCC		61.7824816145
342SulfoxidationKNPREEGMVPFIFVG
CCCCCCCCCCEEEEE		3.8121406390
350PhosphorylationVPFIFVGTRENISNA
CCEEEEEECCCCCHH		29.52-
393MethylationRQIGLGFRPPGSGRG
HHCCCCCCCCCCCCC		34.40-
397PhosphorylationLGFRPPGSGRGSGGS
CCCCCCCCCCCCCCC		30.9629523821
399MethylationFRPPGSGRGSGGSDK
CCCCCCCCCCCCCCC		37.49-
401PhosphorylationPPGSGRGSGGSDKAG
CCCCCCCCCCCCCCC		38.3226055452
404PhosphorylationSGRGSGGSDKAGYST
CCCCCCCCCCCCCCC		39.1926055452
406UbiquitinationRGSGGSDKAGYSTDE
CCCCCCCCCCCCCCC		45.4633845483
409PhosphorylationGGSDKAGYSTDESSS
CCCCCCCCCCCCCCC		17.1622167270
410PhosphorylationGSDKAGYSTDESSSS
CCCCCCCCCCCCCCC		28.5922167270
411PhosphorylationSDKAGYSTDESSSSS
CCCCCCCCCCCCCCC		34.9922167270
414PhosphorylationAGYSTDESSSSSLHA
CCCCCCCCCCCCCEE		38.0322167270
415PhosphorylationGYSTDESSSSSLHAT
CCCCCCCCCCCCEEE		31.9922167270
416PhosphorylationYSTDESSSSSLHATR
CCCCCCCCCCCEEEE		32.9722167270
417PhosphorylationSTDESSSSSLHATRT
CCCCCCCCCCEEEEE		38.5822167270
418PhosphorylationTDESSSSSLHATRTY
CCCCCCCCCEEEEEC		26.5622167270
422PhosphorylationSSSSLHATRTYGGSY
CCCCCEEEEECCCCC		16.8823403867
424PhosphorylationSSLHATRTYGGSYGG
CCCEEEEECCCCCCC		23.3622468782
425PhosphorylationSLHATRTYGGSYGGR
CCEEEEECCCCCCCC		19.0527251275
428PhosphorylationATRTYGGSYGGRGRG
EEEECCCCCCCCCCC		19.0822468782
429PhosphorylationTRTYGGSYGGRGRGR
EEECCCCCCCCCCCC		27.2022468782
432MethylationYGGSYGGRGRGRRTG
CCCCCCCCCCCCCCC		27.54-
434MethylationGSYGGRGRGRRTGGP
CCCCCCCCCCCCCCC		33.80-
436MethylationYGGRGRGRRTGGPAY
CCCCCCCCCCCCCCC		31.46-
438PhosphorylationGRGRGRRTGGPAYGP
CCCCCCCCCCCCCCC		45.1624732914
443PhosphorylationRRTGGPAYGPSSDVS
CCCCCCCCCCCCCCC		32.4723927012
446PhosphorylationGGPAYGPSSDVSTAS
CCCCCCCCCCCCCCC		34.5023927012
447PhosphorylationGPAYGPSSDVSTASE
CCCCCCCCCCCCCCC		45.2023401153
450PhosphorylationYGPSSDVSTASETES
CCCCCCCCCCCCCHH		24.2023401153
451PhosphorylationGPSSDVSTASETESE
CCCCCCCCCCCCHHH		33.7730266825
453PhosphorylationSSDVSTASETESEKR
CCCCCCCCCCHHHHC		45.1819664994
455PhosphorylationDVSTASETESEKREE
CCCCCCCCHHHHCCC		42.1730266825
457PhosphorylationSTASETESEKREEPN
CCCCCCHHHHCCCCC		56.7023401153
459UbiquitinationASETESEKREEPNRA
CCCCHHHHCCCCCCC		74.5124816145
459AcetylationASETESEKREEPNRA
CCCCHHHHCCCCCCC		74.5126051181
488MethylationRRRPTGGRGRGPPPA
CCCCCCCCCCCCCCC		32.74-
490MethylationRPTGGRGRGPPPAPR
CCCCCCCCCCCCCCC		53.75-
499PhosphorylationPPPAPRPTSRYNSSS
CCCCCCCCCCCCCCC		27.4130266825
500PhosphorylationPPAPRPTSRYNSSSI
CCCCCCCCCCCCCCH		35.1430266825
502PhosphorylationAPRPTSRYNSSSISS
CCCCCCCCCCCCHHH		21.1126552605
504PhosphorylationRPTSRYNSSSISSVL
CCCCCCCCCCHHHHH		19.2729978859
505PhosphorylationPTSRYNSSSISSVLK
CCCCCCCCCHHHHHC		28.2221815630
506PhosphorylationTSRYNSSSISSVLKD
CCCCCCCCHHHHHCC		26.7228348404
508PhosphorylationRYNSSSISSVLKDPD
CCCCCCHHHHHCCCC		19.1529978859
509PhosphorylationYNSSSISSVLKDPDS
CCCCCHHHHHCCCCC		29.7821815630
512UbiquitinationSSISSVLKDPDSNPY
CCHHHHHCCCCCCCC		66.13-
516PhosphorylationSVLKDPDSNPYSLLD
HHHCCCCCCCCCCCC		45.1321945579
519PhosphorylationKDPDSNPYSLLDTSE
CCCCCCCCCCCCCCC		19.0521945579
520PhosphorylationDPDSNPYSLLDTSEP
CCCCCCCCCCCCCCC		24.5821945579
524PhosphorylationNPYSLLDTSEPEPPV
CCCCCCCCCCCCCCC		34.6521945579
525PhosphorylationPYSLLDTSEPEPPVD
CCCCCCCCCCCCCCC		51.3121945579
533PhosphorylationEPEPPVDSEPGEPPP
CCCCCCCCCCCCCCC		46.0221945579
542PhosphorylationPGEPPPASARRRRSR
CCCCCCHHHHHHHHH		28.2521945579
548PhosphorylationASARRRRSRRRRTDE
HHHHHHHHHCCCCCC		28.47-
553PhosphorylationRRSRRRRTDEDRTVM
HHHHCCCCCCCCCCC		41.7623186163
557MethylationRRRTDEDRTVMDGGL
CCCCCCCCCCCCCCC		27.46-
558PhosphorylationRRTDEDRTVMDGGLE
CCCCCCCCCCCCCCC		32.2930266825
566PhosphorylationVMDGGLESDGPNMTE
CCCCCCCCCCCCCCC		53.5723927012
572PhosphorylationESDGPNMTENGLEDE
CCCCCCCCCCCCCCC		32.7030266825
580PhosphorylationENGLEDESRPQRRNR
CCCCCCCCCHHHHHH		62.6824732914
598PhosphorylationRRNRGNRTDGSISGD
HHHCCCCCCCCCCCC		49.0329255136
601PhosphorylationRGNRTDGSISGDRQP
CCCCCCCCCCCCCCC		19.1829255136
603PhosphorylationNRTDGSISGDRQPVT
CCCCCCCCCCCCCEE		36.0229255136
610PhosphorylationSGDRQPVTVADYISR
CCCCCCEEHHHHHHH		19.3629255136
610O-linked_GlycosylationSGDRQPVTVADYISR
CCCCCCEEHHHHHHH		19.3623301498
614PhosphorylationQPVTVADYISRAESQ
CCEEHHHHHHHHHHH		7.3423927012
616PhosphorylationVTVADYISRAESQSR
EEHHHHHHHHHHHHC		21.1423927012
620PhosphorylationDYISRAESQSRQRPP
HHHHHHHHHHCCCCC		32.2527422710
622PhosphorylationISRAESQSRQRPPLE
HHHHHHHHCCCCCCC		39.3926074081
631PhosphorylationQRPPLERTKPSEDSL
CCCCCCCCCCCCCCC		37.6226657352
634PhosphorylationPLERTKPSEDSLSGQ
CCCCCCCCCCCCCCC		56.4422985185
637PhosphorylationRTKPSEDSLSGQKGD
CCCCCCCCCCCCCCC		22.0023312004
639PhosphorylationKPSEDSLSGQKGDSV
CCCCCCCCCCCCCCC		43.0325159151
642AcetylationEDSLSGQKGDSVSKL
CCCCCCCCCCCCCCC		69.1126051181
645PhosphorylationLSGQKGDSVSKLPKG
CCCCCCCCCCCCCCC		36.6428555341
647PhosphorylationGQKGDSVSKLPKGPS
CCCCCCCCCCCCCCC		32.2121712546
654PhosphorylationSKLPKGPSENGELSA
CCCCCCCCCCCCCCC		52.9828348404
660PhosphorylationPSENGELSAPLELGS
CCCCCCCCCCHHHHC		24.4428102081
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

Oops, there are no upstream regulatory protein records of FXR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FXR2_HUMAN !!
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 FXR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTN3_HUMANRTN3physical
16189514
KCTD4_HUMANKCTD4physical
16189514
RBPMS_HUMANRBPMSphysical
16189514
PSME3_HUMANPSME3physical
16189514
RALYL_HUMANRALYLphysical
16189514
THAP1_HUMANTHAP1physical
16189514
EAF6_HUMANMEAF6physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
CJ062_HUMANC10orf62physical
16189514
GKAP1_HUMANGKAP1physical
16189514
PRAF1_HUMANRABAC1physical
16189514
PUR6_HUMANPAICSphysical
16189514
LCMT1_HUMANLCMT1physical
16189514
KCNRG_HUMANKCNRGphysical
16189514
CACO2_HUMANCALCOCO2physical
16189514
T22D4_HUMANTSC22D4physical
16189514
KXDL1_HUMANKXD1physical
16189514
ZN451_HUMANZNF451physical
16189514
LDOC1_HUMANLDOC1physical
16189514
RBMX_HUMANRBMXphysical
16189514
MCRS1_HUMANMCRS1physical
16189514
TRI29_HUMANTRIM29physical
16189514
CCD33_HUMANCCDC33physical
16189514
RTN4_HUMANRTN4physical
16189514
AMOL2_HUMANAMOTL2physical
16189514
AR6P1_HUMANARL6IP1physical
16189514
MBIP1_HUMANMBIPphysical
16189514
RPIA_HUMANRPIAphysical
16189514
5NTC_HUMANNT5C2physical
16189514
SKT_HUMANKIAA1217physical
16189514
DPPA2_HUMANDPPA2physical
16189514
K1C20_HUMANKRT20physical
16189514
NECA2_HUMANNECAB2physical
16189514
SSA27_HUMANSSSCA1physical
16189514
FXR2_HUMANFXR2physical
16189514
ZBT8A_HUMANZBTB8Aphysical
16189514
FMR1_HUMANFMR1physical
8668200
CYFP1_HUMANCYFIP1physical
11438699
FXR1_HUMANFXR1physical
7489725
FMR1_HUMANFMR1physical
7489725
FXR2_HUMANFXR2physical
7489725
ZSCA1_HUMANZSCAN1physical
20211142
5NTC_HUMANNT5C2physical
19060904
PRAF1_HUMANRABAC1physical
19060904
EAF6_HUMANMEAF6physical
19060904
LDOC1_HUMANLDOC1physical
19060904
PUR6_HUMANPAICSphysical
19060904
MBIP1_HUMANMBIPphysical
19060904
AR6P1_HUMANARL6IP1physical
19060904
NDKA_HUMANNME1physical
19060904
PTPS_HUMANPTSphysical
19060904
TRI23_HUMANTRIM23physical
19060904
CAPR1_HUMANCAPRIN1physical
24778252
CPSF6_HUMANCPSF6physical
24778252
CPSF7_HUMANCPSF7physical
24778252
FMR1_HUMANFMR1physical
24778252
FXR1_HUMANFXR1physical
24778252
G3BP1_HUMANG3BP1physical
24778252
G3BP2_HUMANG3BP2physical
24778252
CPSF5_HUMANNUDT21physical
24778252
FXR2_HUMANFXR2physical
25416956
P121A_HUMANPOM121physical
25416956
MO4L1_HUMANMORF4L1physical
25416956
BAZ2B_HUMANBAZ2Bphysical
25416956
CDKL3_HUMANCDKL3physical
25416956
PAF1_HUMANPAF1physical
25416956
F90A1_HUMANFAM90A1physical
25416956
CEP55_HUMANCEP55physical
25416956
TB22B_HUMANTBC1D22Bphysical
25416956
NIF3L_HUMANNIF3L1physical
25416956
MMTA2_HUMANC1orf35physical
25416956
HMBX1_HUMANHMBOX1physical
25416956
CEP44_HUMANCEP44physical
25416956
PRAM_HUMANPRAM1physical
25416956
RM43_HUMANMRPL43physical
25416956
SYTL4_HUMANSYTL4physical
25416956
SYT6_HUMANSYT6physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
TGO1_HUMANMIA3physical
25416956
CJ062_HUMANC10orf62physical
25416956
BRCA1_HUMANBRCA1physical
25184681
P121A_HUMANPOM121physical
21516116
FMR1_HUMANFMR1physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
SNX1_HUMANSNX1physical
28514442
LG3BP_HUMANLGALS3BPphysical
28514442
BTBD1_HUMANBTBD1physical
28514442
FXR1_HUMANFXR1physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
NU214_HUMANNUP214physical
28514442
THUM3_HUMANTHUMPD3physical
28514442
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 FXR2_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-598; SER-601 ANDSER-603, 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 THR-598; SER-601 ANDSER-603, AND MASS SPECTROMETRY.
"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 THR-411; SER-525; SER-533;SER-566; THR-598; SER-601 AND SER-603, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-603, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; THR-455; THR-598;SER-601 AND SER-603, AND MASS 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-601 AND SER-603, ANDMASS 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-519, AND MASSSPECTROMETRY.

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