FMR1_HUMAN - dbPTM
FMR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMR1_HUMAN
UniProt AC Q06787
Protein Name Synaptic functional regulator FMR1 {ECO:0000305}
Gene Name FMR1 {ECO:0000312|HGNC:HGNC:3775}
Organism Homo sapiens (Human).
Sequence Length 632
Subcellular Localization Nucleus . Nucleus, nucleolus . Chromosome, centromere . Chromosome . Cytoplasm . Cytoplasm, perinuclear region . Cytoplasm, Cytoplasmic ribonucleoprotein granule . Perikaryon . Cell projection . Cell projection, axon . Cell projection, dendrite . Cell pro
Protein Description Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. [PubMed: 16631377]
Protein Sequence MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
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
1Acetylation-------MEELVVEV
-------CCEEEEEE		9.0122814378
11PhosphorylationLVVEVRGSNGAFYKA
EEEEEECCCCHHHHE		22.8628348404
17AcetylationGSNGAFYKAFVKDVH
CCCCHHHHEEEEECC		28.9726051181
74AcetylationVYSRANEKEPCCWWL
EEECCCCCCCCHHHE		67.7626051181
74UbiquitinationVYSRANEKEPCCWWL
EEECCCCCCCCHHHE		67.7632015554
83AcetylationPCCWWLAKVRMIKGE
CCHHHEEEEEECCCE		28.3626051181
103PhosphorylationYAACDATYNEIVTIE
EEEECCCCCEEEEHH		16.72-
122PhosphorylationVNPNKPATKDTFHKI
CCCCCCCCCCCCCCC		37.6720860994
123UbiquitinationNPNKPATKDTFHKIK
CCCCCCCCCCCCCCC		57.8024816145
130AcetylationKDTFHKIKLDVPEDL
CCCCCCCCCCCCHHH		43.3625953088
130UbiquitinationKDTFHKIKLDVPEDL
CCCCCCCCCCCCHHH		43.3632015554
143UbiquitinationDLRQMCAKEAAHKDF
HHHHHHHHHHHHHHH		42.8529967540
191PhosphorylationLIDMHFRSLRTKLSL
HHHHHHHHHHHHHHH		22.6630631047
207UbiquitinationMRNEEASKQLESSRQ
HCCHHHHHHHHHHHH		66.9824816145
246UbiquitinationANIQQARKVPGVTAI
CCHHHHHCCCCCEEE		56.6623000965
295MalonylationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC		24.1726320211
295UbiquitinationVPRNLVGKVIGKNGK
CCHHHHHHHHCCCCC		24.1733845483
302AcetylationKVIGKNGKLIQEIVD
HHHCCCCCCHHHHHC		52.3825953088
302UbiquitinationKVIGKNGKLIQEIVD
HHHCCCCCCHHHHHC		52.3829967540
310UbiquitinationLIQEIVDKSGVVRVR
CHHHHHCCCCCEEEE		37.9123000965
324UbiquitinationRIEAENEKNVPQEEE
EEEEECCCCCCCHHH		74.8724816145
337PhosphorylationEEIMPPNSLPSNNSR
HHCCCCCCCCCCCCC		47.6425159151
340PhosphorylationMPPNSLPSNNSRVGP
CCCCCCCCCCCCCCC		54.6728176443
343PhosphorylationNSLPSNNSRVGPNAP
CCCCCCCCCCCCCCC		32.3728176443
353UbiquitinationGPNAPEEKKHLDIKE
CCCCCHHHCCCCCCC		43.7832015554
359AcetylationEKKHLDIKENSTHFS
HHCCCCCCCCCCCCC		50.9726051181
359UbiquitinationEKKHLDIKENSTHFS
HHCCCCCCCCCCCCC		50.9732015554
366PhosphorylationKENSTHFSQPNSTKV
CCCCCCCCCCCCHHC		36.8026425664
366 (in isoform 11)Phosphorylation-36.8025627689
366 (in isoform 2)Phosphorylation-36.8025627689
366 (in isoform 8)Phosphorylation-36.8025627689
366 (in isoform 9)Phosphorylation-36.8025627689
370PhosphorylationTHFSQPNSTKVQRVL
CCCCCCCCHHCEEEE		35.9720068231
370 (in isoform 11)Phosphorylation-35.9725159151
370 (in isoform 2)Phosphorylation-35.9725159151
370 (in isoform 8)Phosphorylation-35.9725159151
370 (in isoform 9)Phosphorylation-35.9725159151
371PhosphorylationHFSQPNSTKVQRVLV
CCCCCCCHHCEEEEE		41.7020068231
372UbiquitinationFSQPNSTKVQRVLVA
CCCCCCHHCEEEEEE		35.8732015554
381PhosphorylationQRVLVASSVVAGESQ
EEEEEEEEHHCCCCC		15.7528555341
448PhosphorylationLRQIGASSRPPPNRT
HHHHCCCCCCCCCCC		48.5520068231
460PhosphorylationNRTDKEKSYVTDDGQ
CCCCCCCCEECCCCC		26.40-
461PhosphorylationRTDKEKSYVTDDGQG
CCCCCCCEECCCCCC		20.5922817900
463PhosphorylationDKEKSYVTDDGQGMG
CCCCCEECCCCCCCC		21.82-
463 (in isoform 8)Methylation-21.82-
469SulfoxidationVTDDGQGMGRGSRPY
ECCCCCCCCCCCCCC		2.2521406390
471DimethylationDDGQGMGRGSRPYRN
CCCCCCCCCCCCCCC		30.90-
471MethylationDDGQGMGRGSRPYRN
CCCCCCCCCCCCCCC		30.90-
474MethylationQGMGRGSRPYRNRGH
CCCCCCCCCCCCCCC		34.78-
477MethylationGRGSRPYRNRGHGRR
CCCCCCCCCCCCCCC		29.11-
479PhosphorylationGSRPYRNRGHGRRGP
CCCCCCCCCCCCCCC		29.5032142685
488PhosphorylationHGRRGPGYTSGTNSE
CCCCCCCCCCCCCCC		10.8121955146
489PhosphorylationGRRGPGYTSGTNSEA
CCCCCCCCCCCCCCC		26.9621955146
490PhosphorylationRRGPGYTSGTNSEAS
CCCCCCCCCCCCCCC		34.8321955146
492PhosphorylationGPGYTSGTNSEASNA
CCCCCCCCCCCCCCC		35.0330108239
494PhosphorylationGYTSGTNSEASNASE
CCCCCCCCCCCCCCC		34.0830108239
497PhosphorylationSGTNSEASNASETES
CCCCCCCCCCCCCCC		28.9530108239
500PhosphorylationNSEASNASETESDHR
CCCCCCCCCCCCCCC		49.6721955146
500 (in isoform 7)Phosphorylation-49.6721406692
502PhosphorylationEASNASETESDHRDE
CCCCCCCCCCCCCHH		37.9921955146
502 (in isoform 7)Phosphorylation-37.9921406692
504PhosphorylationSNASETESDHRDELS
CCCCCCCCCCCHHHC		46.2521955146
504 (in isoform 7)Phosphorylation-46.2521406692
506 (in isoform 11)Phosphorylation-48.66-
508 (in isoform 11)Phosphorylation-58.74-
511PhosphorylationSDHRDELSDWSLAPT
CCCCHHHCCCCCCCC		34.6821955146
514PhosphorylationRDELSDWSLAPTEEE
CHHHCCCCCCCCHHH		21.4630108239
518PhosphorylationSDWSLAPTEEERESF
CCCCCCCCHHHHHHH		50.8830108239
524PhosphorylationPTEEERESFLRRGDG
CCHHHHHHHHHCCCC		35.4821406692
524 (in isoform 7)Phosphorylation-35.4821406692
527 (in isoform 10)Phosphorylation-38.23-
529 (in isoform 10)Phosphorylation-34.98-
534MethylationRRGDGRRRGGGGRGQ
HCCCCCCCCCCCCCC		46.91-
539MethylationRRRGGGGRGQGGRGR
CCCCCCCCCCCCCCC		37.22-
544MethylationGGRGQGGRGRGGGFK
CCCCCCCCCCCCCCC		38.1616922515
546MethylationRGQGGRGRGGGFKGN
CCCCCCCCCCCCCCC		38.94-
552 (in isoform 6)Phosphorylation-40.3021815630
556 (in isoform 2)Phosphorylation-23.2621815630
556 (in isoform 6)Phosphorylation-23.2625627689
557 (in isoform 6)Phosphorylation-43.8221815630
558 (in isoform 6)Phosphorylation-42.5525627689
560 (in isoform 2)Phosphorylation-48.2925627689
561 (in isoform 2)Phosphorylation-56.0721815630
561 (in isoform 6)Phosphorylation-56.0727732954
562 (in isoform 2)Phosphorylation-34.0725627689
565 (in isoform 2)Phosphorylation-42.5427732954
565 (in isoform 4)Phosphorylation-42.5421815630
569 (in isoform 4)Phosphorylation-22.3825627689
570 (in isoform 4)Phosphorylation-44.1421815630
571 (in isoform 4)Phosphorylation-38.9325627689
574PhosphorylationREAKGRTTDGSLQIR
CCCCCCCCCCCEEEE		36.6828348404
574 (in isoform 4)Phosphorylation-36.6827732954
577PhosphorylationKGRTTDGSLQIRVDC
CCCCCCCCEEEEEEC		21.6528348404
577 (in isoform 7)Phosphorylation-21.6521815630
581 (in isoform 7)Phosphorylation-12.7825627689
582 (in isoform 7)Phosphorylation-11.9921815630
583 (in isoform 7)Phosphorylation-21.4125627689
586 (in isoform 7)Phosphorylation-53.0027732954
594PhosphorylationERSVHTKTLQNTSSE
CEEEEEEEEECCCCH		34.4328102081
598PhosphorylationHTKTLQNTSSEGSRL
EEEEEECCCCHHHCC		22.2228985074
599PhosphorylationTKTLQNTSSEGSRLR
EEEEECCCCHHHCCC		33.6621815630
600PhosphorylationKTLQNTSSEGSRLRT
EEEECCCCHHHCCCC		43.8921815630
603PhosphorylationQNTSSEGSRLRTGKD
ECCCCHHHCCCCCCC		24.8825159151
620PhosphorylationQKKEKPDSVDGQQPL
CCCCCCCCCCCCCCC		30.5421815630
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
500SPhosphorylationKinaseCSNK2A1P68400
GPS
500SPhosphorylationKinaseRPS6KB1P23443
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
500SPhosphorylation

12446764
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 FMR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
11367701
NUFP1_HUMANNUFIP1physical
10556305
NUFP2_HUMANNUFIP2physical
12837692
FXR1_HUMANFXR1physical
8668200
FXR2_HUMANFXR2physical
8668200
CYFP1_HUMANCYFIP1physical
11438699
CYFP2_HUMANCYFIP2physical
11438699
FMR1_HUMANFMR1physical
10567518
FXR2_HUMANFXR2physical
10567518
NUCL_HUMANNCLphysical
10567518
FXR2_HUMANFXR2physical
7489725
FMR1_HUMANFMR1physical
7489725
FXR1_HUMANFXR1physical
7489725
TDRD3_HUMANTDRD3physical
18664458
FXR1_HUMANFXR1physical
24778252
FXR2_HUMANFXR2physical
24778252
POTEE_HUMANPOTEEphysical
24778252
RANB9_HUMANRANBP9physical
15381419
FXR2_HUMANFXR2physical
24722188
INCA1_HUMANINCA1physical
24722188
MEOX1_HUMANMEOX1physical
24722188
SPAG5_HUMANSPAG5physical
24722188
FSD2_HUMANFSD2physical
24722188
CHIP_HUMANSTUB1physical
25268320
FXR2_HUMANFXR2physical
25416956
FSD2_HUMANFSD2physical
25416956
FXR1_HUMANFXR1physical
26186194
BCL7B_HUMANBCL7Bphysical
26186194
KBTB2_HUMANKBTBD2physical
26186194
NCK1_HUMANNCK1physical
26344197
FZR1_HUMANFZR1physical
25913861
KBTB2_HUMANKBTBD2physical
28514442
LG3BP_HUMANLGALS3BPphysical
28514442
BCL7B_HUMANBCL7Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300624Fragile X syndrome (FRAX)
300623Fragile X tremor/ataxia syndrome (FXTAS)
300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems. {ECO
Premature ovarian failure 1 (POF1) [ DISEASE
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FMR1_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardationprotein.";
Dolzhanskaya N., Merz G., Denman R.B.;
Biochemistry 45:10385-10393(2006).
Cited for: METHYLATION AT ARG-544, AND MUTAGENESIS OF ARG-544 AND ARG-546.
Phosphorylation
ReferencePubMed
"Casein kinase II phosphorylates the fragile X mental retardationprotein and modulates its biological properties.";
Siomi M.C., Higashijima K., Ishizuka A., Siomi H.;
Mol. Cell. Biol. 22:8438-8447(2002).
Cited for: PHOSPHORYLATION AT SER-500, AND MUTAGENESIS OF SER-500.

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