RBM47_HUMAN - dbPTM
RBM47_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM47_HUMAN
UniProt AC A0AV96
Protein Name RNA-binding protein 47
Gene Name RBM47
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY
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
42PhosphorylationLLALMERTGYSMVQE
HHHHHHHHCCCCCHH		27.4521659604
44PhosphorylationALMERTGYSMVQENG
HHHHHHCCCCCHHCC		7.9321659604
45PhosphorylationLMERTGYSMVQENGQ
HHHHHCCCCCHHCCC		17.5221659604
55PhosphorylationQENGQRKYGGPPPGW
HHCCCCCCCCCCCCC		29.51-
77AcetylationGCEVFVGKIPRDVYE
CCEEEEECCCCCHHH		44.2126051181
77UbiquitinationGCEVFVGKIPRDVYE
CCEEEEECCCCCHHH		44.21-
121 (in isoform 2)Ubiquitination-39.3121890473
121 (in isoform 1)Ubiquitination-39.3121890473
121UbiquitinationAFVMYCHKHEAKRAV
EEEEEECHHHHHHHH		39.3121890473
134PhosphorylationAVRELNNYEIRPGRL
HHHHHHCCCCCCCCE		16.2020068231
201PhosphorylationRGFAFVEYESHRAAA
CCEEEEEEHHHHHHH		19.89-
263MethylationETTEDTIKKSFGQFN
ECCHHHHHHHCCCCC		44.45-
263"N6,N6-dimethyllysine"ETTEDTIKKSFGQFN
ECCHHHHHHHCCCCC		44.45-
263UbiquitinationETTEDTIKKSFGQFN
ECCHHHHHHHCCCCC		44.45-
264UbiquitinationTTEDTIKKSFGQFNP
CCHHHHHHHCCCCCC		47.3633845483
265PhosphorylationTEDTIKKSFGQFNPG
CHHHHHHHCCCCCCC		29.6127499020
283PhosphorylationRVKKIRDYAFVHFTS
HHHHHCCEEEEEEEC		7.65-
3212-HydroxyisobutyrylationTLAKPVDKEQYSRYQ
EEECCCCHHHHHHHH		47.12-
332MethylationSRYQKAARGGGAAEA
HHHHHHHCCCCHHHH		49.5024129315
379DimethylationFVKAGSIRGRGRGAA
EEECCCCCCCCCCCC		30.38-
379MethylationFVKAGSIRGRGRGAA
EEECCCCCCCCCCCC		30.38116195813
381DimethylationKAGSIRGRGRGAAGN
ECCCCCCCCCCCCCC		23.06-
381MethylationKAGSIRGRGRGAAGN
ECCCCCCCCCCCCCC		23.0654558651
383DimethylationGSIRGRGRGAAGNRA
CCCCCCCCCCCCCCC		30.16-
383MethylationGSIRGRGRGAAGNRA
CCCCCCCCCCCCCCC		30.1654558663
385 (in isoform 2)Phosphorylation-15.7224719451
394Asymmetric dimethylarginineGNRAPGPRGSYLGGY
CCCCCCCCCCCCCCC		53.24-
394MethylationGNRAPGPRGSYLGGY
CCCCCCCCCCCCCCC		53.2424129315
396PhosphorylationRAPGPRGSYLGGYSA
CCCCCCCCCCCCCCC		20.6124719451
405MethylationLGGYSAGRGIYSRYH
CCCCCCCCCHHHCCC		28.2224129315
405Asymmetric dimethylarginineLGGYSAGRGIYSRYH
CCCCCCCCCHHHCCC		28.22-
409PhosphorylationSAGRGIYSRYHEGKG
CCCCCHHHCCCCCCC		25.1724719451
410MethylationAGRGIYSRYHEGKGK
CCCCHHHCCCCCCCC		21.6154558669
421UbiquitinationGKGKQQEKGYELVPN
CCCCCCCCCCEECCC		63.5633845483
453PhosphorylationIPAIGAQYSMFPAAP
ECCCCCCEECCCCCC		11.1125627689
454PhosphorylationPAIGAQYSMFPAAPA
CCCCCCEECCCCCCC		11.2324719451
506PhosphorylationAAAAVIPTVSTPPPF
HHHHHCCCCCCCCCC		18.9028348404
508PhosphorylationAAVIPTVSTPPPFQG
HHHCCCCCCCCCCCC		37.3628348404
509PhosphorylationAVIPTVSTPPPFQGR
HHCCCCCCCCCCCCC		35.1628348404
519PhosphorylationPFQGRPITPVYTVAP
CCCCCCCCCEEEECC		14.9125849741
522PhosphorylationGRPITPVYTVAPNVQ
CCCCCCEEEECCCCE		9.1923917254
533PhosphorylationPNVQRIPTAGIYGAS
CCCEECCCCCCCCCC		34.8321945579
537PhosphorylationRIPTAGIYGASYVPF
ECCCCCCCCCCCCCC		13.0121945579
540PhosphorylationTAGIYGASYVPFAAP
CCCCCCCCCCCCCCC		23.4621945579
541PhosphorylationAGIYGASYVPFAAPA
CCCCCCCCCCCCCCC		16.1721945579
554PhosphorylationPATATIATLQKNAAA
CCCCHHHHHHHHHHH		26.35-
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 RBM47_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM47_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 RBM47_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CA094_HUMANC1orf94physical
25416956
HSFY1_HUMANHSFY1physical
25416956
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 RBM47_HUMAN

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Related Literatures of Post-Translational Modification

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