RBM12_HUMAN - dbPTM
RBM12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM12_HUMAN
UniProt AC Q9NTZ6
Protein Name RNA-binding protein 12
Gene Name RBM12
Organism Homo sapiens (Human).
Sequence Length 932
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MAVVIRLQGLPIVAGTMDIRHFFSGLTIPDGGVHIVGGELGEAFIVFATDEDARLGMMRTGGTIKGSKVTLLLSSKTEMQNMIELSRRRFETANLDIPPANASRSGPPPSSGMSSRVNLPTTVSNFNNPSPSVVTATTSVHESNKNIQTFSTASVGTAPPNMGASFGSPTFSSTVPSTASPMNTVPPPPIPPIPAMPSLPPMPSIPPIPVPPPVPTLPPVPPVPPIPPVPSVPPMTPLPPMSGMPPLNPPPVAPLPAGMNGSGAPMNLNNNLNPMFLGPLNPVNPIQMNSQSSVKPLPINPDDLYVSVHGMPFSAMENDVRDFFHGLRVDAVHLLKDHVGRNNGNGLVKFLSPQDTFEALKRNRMLMIQRYVEVSPATERQWVAAGGHITFKQNMGPSGQTHPPPQTLPRSKSPSGQKRSRSRSPHEAGFCVYLKGLPFEAENKHVIDFFKKLDIVEDSIYIAYGPNGKATGEGFVEFRNEADYKAALCRHKQYMGNRFIQVHPITKKGMLEKIDMIRKRLQNFSYDQREMILNPEGDVNSAKVCAHITNIPFSITKMDVLQFLEGIPVDENAVHVLVDNNGQGLGQALVQFKNEDDARKSERLHRKKLNGREAFVHVVTLEDMREIEKNPPAQGKKGLKMPVPGNPAVPGMPNAGLPGVGLPSAGLPGAGLPSTGLPGSAITSAGLPGAGMPSAGIPSAGGEEHAFLTVGSKEANNGPPFNFPGNFGGSNAFGPPIPPPGLGGGAFGDARPGMPSVGNSGLPGLGLDVPGFGGGPNNLSGPSGFGGGPQNFGNGPGSLGGPPGFGSGPPGLGSAPGHLGGPPAFGPGPGPGPGPGPIHIGGPPGFASSSGKPGPTVIKVQNMPFTVSIDEILDFFYGYQVIPGSVCLKYNEKGMPTGEAMVAFESRDEATAAVIDLNDRPIGSRKVKLVLG
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
16PhosphorylationGLPIVAGTMDIRHFF
CCCEEEEEEEHHHHH		11.26-
17SulfoxidationLPIVAGTMDIRHFFS
CCEEEEEEEHHHHHC		3.8421406390
67PhosphorylationTGGTIKGSKVTLLLS
CCCEECCCEEEEEEC		20.96-
67O-linked_GlycosylationTGGTIKGSKVTLLLS
CCCEECCCEEEEEEC		20.9630059200
70PhosphorylationTIKGSKVTLLLSSKT
EECCCEEEEEECCCH		18.54-
77PhosphorylationTLLLSSKTEMQNMIE
EEEECCCHHHHHHHH		38.34-
111PhosphorylationRSGPPPSSGMSSRVN
CCCCCCCCCCCCCCC		44.27-
111O-linked_GlycosylationRSGPPPSSGMSSRVN
CCCCCCCCCCCCCCC		44.2730059200
121O-linked_GlycosylationSSRVNLPTTVSNFNN
CCCCCCCCCHHCCCC		42.8930059200
122O-linked_GlycosylationSRVNLPTTVSNFNNP
CCCCCCCCHHCCCCC		21.7230059200
124O-linked_GlycosylationVNLPTTVSNFNNPSP
CCCCCCHHCCCCCCC		33.3430059200
130PhosphorylationVSNFNNPSPSVVTAT
HHCCCCCCCCCEEEE		31.7527050516
130O-linked_GlycosylationVSNFNNPSPSVVTAT
HHCCCCCCCCCEEEE		31.7530059200
132O-linked_GlycosylationNFNNPSPSVVTATTS
CCCCCCCCCEEEEEE		33.2930059200
135O-linked_GlycosylationNPSPSVVTATTSVHE
CCCCCCEEEEEEEEC		19.0130059200
137O-linked_GlycosylationSPSVVTATTSVHESN
CCCCEEEEEEEECCC		15.3930059200
138O-linked_GlycosylationPSVVTATTSVHESNK
CCCEEEEEEEECCCC		26.7030059200
139O-linked_GlycosylationSVVTATTSVHESNKN
CCEEEEEEEECCCCC		19.6830059200
143O-linked_GlycosylationATTSVHESNKNIQTF
EEEEEECCCCCCEEE		37.9230059200
149O-linked_GlycosylationESNKNIQTFSTASVG
CCCCCCEEEEECCCC		18.7630059200
295SumoylationMNSQSSVKPLPINPD
CCCCCCCCCCCCCHH		42.67-
3362-HydroxyisobutyrylationVDAVHLLKDHVGRNN
HHHHHHHHHHCCCCC		52.74-
336UbiquitinationVDAVHLLKDHVGRNN
HHHHHHHHHHCCCCC		52.7433845483
349UbiquitinationNNGNGLVKFLSPQDT
CCCCCCEEECCHHHH		45.7021890473
352PhosphorylationNGLVKFLSPQDTFEA
CCCEEECCHHHHHHH		24.5325159151
356PhosphorylationKFLSPQDTFEALKRN
EECCHHHHHHHHHHC		20.3720068231
361UbiquitinationQDTFEALKRNRMLMI
HHHHHHHHHCCEEEE		55.4632142685
361AcetylationQDTFEALKRNRMLMI
HHHHHHHHHCCEEEE		55.4624846347
371PhosphorylationRMLMIQRYVEVSPAT
CEEEEEEEEECCCCC		5.6528152594
375PhosphorylationIQRYVEVSPATERQW
EEEEEECCCCCCCEE		8.7029255136
378PhosphorylationYVEVSPATERQWVAA
EEECCCCCCCEEEEE		34.7829255136
395SulfoxidationHITFKQNMGPSGQTH
EEEEECCCCCCCCCC		8.4921406390
398PhosphorylationFKQNMGPSGQTHPPP
EECCCCCCCCCCCCC		37.4926074081
401PhosphorylationNMGPSGQTHPPPQTL
CCCCCCCCCCCCCCC		39.6226074081
407PhosphorylationQTHPPPQTLPRSKSP
CCCCCCCCCCCCCCC		44.4926074081
411PhosphorylationPPQTLPRSKSPSGQK
CCCCCCCCCCCCCCC		35.2326699800
413PhosphorylationQTLPRSKSPSGQKRS
CCCCCCCCCCCCCCC		26.0827422710
415PhosphorylationLPRSKSPSGQKRSRS
CCCCCCCCCCCCCCC		62.0328176443
420PhosphorylationSPSGQKRSRSRSPHE
CCCCCCCCCCCCHHC		41.4623401153
422PhosphorylationSGQKRSRSRSPHEAG
CCCCCCCCCCHHCCC		38.0522167270
424PhosphorylationQKRSRSRSPHEAGFC
CCCCCCCCHHCCCEE		31.6722167270
433PhosphorylationHEAGFCVYLKGLPFE
HCCCEEEEECCCCCC		12.1320164059
444UbiquitinationLPFEAENKHVIDFFK
CCCCCCCHHHHHHHH		30.6523000965
444AcetylationLPFEAENKHVIDFFK
CCCCCCCHHHHHHHH		30.6527452117
4442-HydroxyisobutyrylationLPFEAENKHVIDFFK
CCCCCCCHHHHHHHH		30.65-
451UbiquitinationKHVIDFFKKLDIVED
HHHHHHHHHCCCCCC		53.0433845483
451AcetylationKHVIDFFKKLDIVED
HHHHHHHHHCCCCCC		53.0419608861
485UbiquitinationFRNEADYKAALCRHK
ECCHHHHHHHHHHCH		27.9433845483
485AcetylationFRNEADYKAALCRHK
ECCHHHHHHHHHHCH		27.9423749302
485MethylationFRNEADYKAALCRHK
ECCHHHHHHHHHHCH		27.9482987705
4852-HydroxyisobutyrylationFRNEADYKAALCRHK
ECCHHHHHHHHHHCH		27.94-
506PhosphorylationFIQVHPITKKGMLEK
EEEEEECCCCCHHHH		31.0229209046
507UbiquitinationIQVHPITKKGMLEKI
EEEEECCCCCHHHHH		48.3129967540
513AcetylationTKKGMLEKIDMIRKR
CCCCHHHHHHHHHHH		39.7926822725
525PhosphorylationRKRLQNFSYDQREMI
HHHHHCCCCCCCCCC		35.0428796482
526PhosphorylationKRLQNFSYDQREMIL
HHHHCCCCCCCCCCC		16.3826462736
531SulfoxidationFSYDQREMILNPEGD
CCCCCCCCCCCCCCC		4.6221406390
554PhosphorylationHITNIPFSITKMDVL
HHHCCCCCEEHHHHH		24.8025627689
593SumoylationGQALVQFKNEDDARK
HHHHHEECCHHHHHH		42.19-
629UbiquitinationEDMREIEKNPPAQGK
HHHHHHHHCCCCCCC		79.1529967540
636AcetylationKNPPAQGKKGLKMPV
HCCCCCCCCCCCCCC		31.4325953088
893UbiquitinationVCLKYNEKGMPTGEA
EEEEECCCCCCCCEE		57.80-
893AcetylationVCLKYNEKGMPTGEA
EEEEECCCCCCCCEE		57.8025953088
897PhosphorylationYNEKGMPTGEAMVAF
ECCCCCCCCEEEEEE		38.4726552605
906PhosphorylationEAMVAFESRDEATAA
EEEEEEECCCCCCEE		38.2826552605
920MethylationAVIDLNDRPIGSRKV
EEEECCCCCCCCCEE		24.54115490499
924PhosphorylationLNDRPIGSRKVKLVL
CCCCCCCCCEEEEEC		29.6428555341
925MethylationNDRPIGSRKVKLVLG
CCCCCCCCEEEEECC		42.44115490507
926MethylationDRPIGSRKVKLVLG-
CCCCCCCEEEEECC-		45.48115490515
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 RBM12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM12_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 RBM12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDHF2_HUMANSDHAF2physical
22939629
BIN1_HUMANBIN1physical
22863883
GMPPB_HUMANGMPPBphysical
22863883
GLCNE_HUMANGNEphysical
22863883
RBGPR_HUMANRAB3GAP2physical
22863883
UBE4B_HUMANUBE4Bphysical
22863883
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 RBM12_HUMAN

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Related Literatures of Post-Translational Modification
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-420; SER-422 ANDSER-424, AND MASS 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-424, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-420; SER-422AND SER-424, 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-420; SER-422 ANDSER-424, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-526, AND MASSSPECTROMETRY.

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