RB12B_HUMAN - dbPTM
RB12B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB12B_HUMAN
UniProt AC Q8IXT5
Protein Name RNA-binding protein 12B
Gene Name RBM12B
Organism Homo sapiens (Human).
Sequence Length 1001
Subcellular Localization
Protein Description
Protein Sequence MAVVIRLLGLPFIAGPVDIRHFFTGLTIPDGGVHIIGGEIGEAFIIFATDEDARRAISRSGGFIKDSSVELFLSSKAEMQKTIEMKRTDRVGRGRPGSGTSGVDSLSNFIESVKEEASNSGYGSSINQDAGFHTNGTGHGNLRPRKTRPLKAENPYLFLRGLPYLVNEDDVRVFFSGLCVDGVIFLKHHDGRNNGDAIVKFASCVDASGGLKCHRSFMGSRFIEVMQGSEQQWIEFGGNAVKEGDVLRRSEEHSPPRGINDRHFRKRSHSKSPRRTRSRSPLGFYVHLKNLSLSIDERDLRNFFRGTDLTDEQIRFLYKDENRTRYAFVMFKTLKDYNTALSLHKTVLQYRPVHIDPISRKQMLKFIARYEKKRSGSLERDRPGHVSQKYSQEGNSGQKLCIYIRNFPFDVTKVEVQKFFADFLLAEDDIYLLYDDKGVGLGEALVKFKSEEQAMKAERLNRRRFLGTEVLLRLISEAQIQEFGVNFSVMSSEKMQARSQSRERGDHSHLFDSKDPPIYSVGAFENFRHQLEDLRQLDNFKHPQRDFRQPDRHPPEDFRHSSEDFRFPPEDFRHSPEDFRRPREEDFRRPSEEDFRRPWEEDFRRPPEDDFRHPREEDWRRPLEEDWRRPLEEDFRRSPTEDFRQLPEEDFRQPPEEDLRWLPEEDFRRPPEEDWRRPPEEDFRRPLQGEWRRPPEDDFRRPPEEDFRHSPEEDFRQSPQEHFRRPPQEHFRRPPPEHFRRPPPEHFRRPPPEHFRRPPPEHFRRPPPEHFRRPPPEHFRRPPQEHFRRPPQEHFRRSREEDFRHPPDEDFRGPPDEDFRHPPDEDFRSPQEEDFRCPSDEDFRQLPEEDLREAPEEDPRLPDNFRPPGEDFRSPPDDFRSHRPFVNFGRPEGGKFDFGKHNMGSFPEGRFMPDPKINCGSGRVTPIKIMNLPFKANVNEILDFFHGYRIIPDSVSIQYNEQGLPTGEAIVAMINYNEAMAAIKDLNDRPVGPRKVKLTLL
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
67PhosphorylationSGGFIKDSSVELFLS
CCCCCCCCHHHHHHC		31.1430266825
68PhosphorylationGGFIKDSSVELFLSS
CCCCCCCHHHHHHCC		29.7330266825
74PhosphorylationSSVELFLSSKAEMQK
CHHHHHHCCHHHHHH		23.5822210691
75PhosphorylationSVELFLSSKAEMQKT
HHHHHHCCHHHHHHH		37.7221406692
82PhosphorylationSKAEMQKTIEMKRTD
CHHHHHHHHHEECCC		12.79-
98PhosphorylationVGRGRPGSGTSGVDS
CCCCCCCCCCCCHHH		41.3929255136
100PhosphorylationRGRPGSGTSGVDSLS
CCCCCCCCCCHHHHH		24.8130266825
101PhosphorylationGRPGSGTSGVDSLSN
CCCCCCCCCHHHHHH		40.1030266825
105PhosphorylationSGTSGVDSLSNFIES
CCCCCHHHHHHHHHH		31.1530266825
107PhosphorylationTSGVDSLSNFIESVK
CCCHHHHHHHHHHHH		33.3830266825
112PhosphorylationSLSNFIESVKEEASN
HHHHHHHHHHHHHHH		33.4020068231
114SumoylationSNFIESVKEEASNSG
HHHHHHHHHHHHHCC		60.1528112733
122PhosphorylationEEASNSGYGSSINQD
HHHHHCCCCCCCCCC		17.4128555341
124PhosphorylationASNSGYGSSINQDAG
HHHCCCCCCCCCCCC		21.4027251275
125PhosphorylationSNSGYGSSINQDAGF
HHCCCCCCCCCCCCC		22.6128555341
151SumoylationPRKTRPLKAENPYLF
CCCCCCCCCCCCEEE		57.2328112733
151AcetylationPRKTRPLKAENPYLF
CCCCCCCCCCCCEEE		57.2326051181
151SumoylationPRKTRPLKAENPYLF
CCCCCCCCCCCCEEE		57.23-
156PhosphorylationPLKAENPYLFLRGLP
CCCCCCCEEEECCCC		22.97-
160MethylationENPYLFLRGLPYLVN
CCCEEEECCCCCCCC		36.95115490523
164PhosphorylationLFLRGLPYLVNEDDV
EEECCCCCCCCCCCE		28.4628152594
208PhosphorylationFASCVDASGGLKCHR
ECCEEECCCCCEECH		29.0025159151
212AcetylationVDASGGLKCHRSFMG
EECCCCCEECHHHHC		31.1319814673
250PhosphorylationEGDVLRRSEEHSPPR
CCCCCCCCCCCCCCC		40.6829255136
254PhosphorylationLRRSEEHSPPRGIND
CCCCCCCCCCCCCCH		39.6229255136
268PhosphorylationDRHFRKRSHSKSPRR
HHHHHHHCCCCCCCC		34.8430576142
270PhosphorylationHFRKRSHSKSPRRTR
HHHHHCCCCCCCCCC		35.7530576142
272PhosphorylationRKRSHSKSPRRTRSR
HHHCCCCCCCCCCCC		27.0130576142
276PhosphorylationHSKSPRRTRSRSPLG
CCCCCCCCCCCCCCC		33.9925159151
278PhosphorylationKSPRRTRSRSPLGFY
CCCCCCCCCCCCCEE		36.1822167270
280PhosphorylationPRRTRSRSPLGFYVH
CCCCCCCCCCCEEEE		26.2329255136
285PhosphorylationSRSPLGFYVHLKNLS
CCCCCCEEEEEEEEE		5.7828176443
292PhosphorylationYVHLKNLSLSIDERD
EEEEEEEEEECCHHH		29.4823403867
294PhosphorylationHLKNLSLSIDERDLR
EEEEEEEECCHHHHH		25.3123403867
318PhosphorylationDEQIRFLYKDENRTR
HHHHHHEEECCCCCE		17.4328152594
319AcetylationEQIRFLYKDENRTRY
HHHHHEEECCCCCEE		61.7919608861
326PhosphorylationKDENRTRYAFVMFKT
ECCCCCEEEEEEEEC		12.0920090780
335SumoylationFVMFKTLKDYNTALS
EEEEECHHHHHHHHH		64.5028112733
335UbiquitinationFVMFKTLKDYNTALS
EEEEECHHHHHHHHH		64.5029967540
345AcetylationNTALSLHKTVLQYRP
HHHHHHCHHHHHHCC		45.6926051181
346PhosphorylationTALSLHKTVLQYRPV
HHHHHCHHHHHHCCC		18.72-
350PhosphorylationLHKTVLQYRPVHIDP
HCHHHHHHCCCCCCC		16.8420090780
369MethylationQMLKFIARYEKKRSG
HHHHHHHHHHHHCCC		35.0124390031
369DimethylationQMLKFIARYEKKRSG
HHHHHHHHHHHHCCC		35.01-
370PhosphorylationMLKFIARYEKKRSGS
HHHHHHHHHHHCCCC		24.07-
375PhosphorylationARYEKKRSGSLERDR
HHHHHHCCCCCCCCC		41.4326055452
377PhosphorylationYEKKRSGSLERDRPG
HHHHCCCCCCCCCCC		28.4423401153
387PhosphorylationRDRPGHVSQKYSQEG
CCCCCCCCCCCCCCC		18.4523403867
389UbiquitinationRPGHVSQKYSQEGNS
CCCCCCCCCCCCCCC		39.0929967540
390PhosphorylationPGHVSQKYSQEGNSG
CCCCCCCCCCCCCCC		14.1430108239
391PhosphorylationGHVSQKYSQEGNSGQ
CCCCCCCCCCCCCCC		28.8828348404
396PhosphorylationKYSQEGNSGQKLCIY
CCCCCCCCCCEEEEE		54.1529496963
431PhosphorylationLLAEDDIYLLYDDKG
HCCCCCEEEEECCCC		9.54-
434PhosphorylationEDDIYLLYDDKGVGL
CCCEEEEECCCCCCH		21.36-
4472-HydroxyisobutyrylationGLGEALVKFKSEEQA
CHHHHHHHCCCHHHH		48.18-
449SumoylationGEALVKFKSEEQAMK
HHHHHHCCCHHHHHH		51.76-
449SumoylationGEALVKFKSEEQAMK
HHHHHHCCCHHHHHH		51.76-
499PhosphorylationSEKMQARSQSRERGD
HHHHHHHHHHHCCCC		35.2129496963
501PhosphorylationKMQARSQSRERGDHS
HHHHHHHHHCCCCCC		37.0429496963
508PhosphorylationSRERGDHSHLFDSKD
HHCCCCCCCCCCCCC		26.9928796482
513PhosphorylationDHSHLFDSKDPPIYS
CCCCCCCCCCCCCEE		31.4628796482
514SumoylationHSHLFDSKDPPIYSV
CCCCCCCCCCCCEEC		75.8928112733
514UbiquitinationHSHLFDSKDPPIYSV
CCCCCCCCCCCCEEC		75.8929967540
519PhosphorylationDSKDPPIYSVGAFEN
CCCCCCCEECCHHHC		11.7721945579
520PhosphorylationSKDPPIYSVGAFENF
CCCCCCEECCHHHCH		18.1321945579
541SumoylationLRQLDNFKHPQRDFR
HHCCCCCCCCCCCCC		61.7128112733
561PhosphorylationPPEDFRHSSEDFRFP
CCCCCCCCCCCCCCC		31.0330266825
562PhosphorylationPEDFRHSSEDFRFPP
CCCCCCCCCCCCCCH		34.7530266825
575PhosphorylationPPEDFRHSPEDFRRP
CHHHHCCCHHHHCCC		26.2329255136
591PhosphorylationEEDFRRPSEEDFRRP
HHHCCCCCHHHHCCC		52.3830266825
638PhosphorylationLEEDFRRSPTEDFRQ
CHHHHHHCCCHHHHC		31.7329255136
640PhosphorylationEDFRRSPTEDFRQLP
HHHHHCCCHHHHCCC		49.8129255136
710PhosphorylationPEEDFRHSPEEDFRQ
CHHHHCCCCHHHHHC		29.7429255136
718PhosphorylationPEEDFRQSPQEHFRR
CHHHHHCCHHHHHCC		25.0529255136
732MethylationRPPQEHFRRPPPEHF
CCCHHHHCCCCCHHH		52.70-
733MethylationPPQEHFRRPPPEHFR
CCHHHHCCCCCHHHC		47.32-
740MethylationRPPPEHFRRPPPEHF
CCCCHHHCCCCCHHH		52.70-
741MethylationPPPEHFRRPPPEHFR
CCCHHHCCCCCHHHC		47.32-
748MethylationRPPPEHFRRPPPEHF
CCCCHHHCCCCCHHH		52.70-
749MethylationPPPEHFRRPPPEHFR
CCCHHHCCCCCHHHC		47.32-
756MethylationRPPPEHFRRPPPEHF
CCCCHHHCCCCCHHH		52.70-
757MethylationPPPEHFRRPPPEHFR
CCCHHHCCCCCHHHC		47.32-
764MethylationRPPPEHFRRPPPEHF
CCCCHHHCCCCCHHH		52.70-
765MethylationPPPEHFRRPPPEHFR
CCCHHHCCCCCHHHC		47.32-
772MethylationRPPPEHFRRPPPEHF
CCCCHHHCCCCCHHH		52.70-
773MethylationPPPEHFRRPPPEHFR
CCCHHHCCCCCHHHC		47.32-
788MethylationRPPQEHFRRPPQEHF
CCCHHHCCCCCHHHH		52.70-
798PhosphorylationPQEHFRRSREEDFRH
CHHHHHHHHHHHHCC		39.5223401153
829PhosphorylationPPDEDFRSPQEEDFR
CCCCCCCCCCHHHCC		30.8130266825
839PhosphorylationEEDFRCPSDEDFRQL
HHHCCCCCHHHHHHC		58.2023401153
874PhosphorylationPPGEDFRSPPDDFRS
CCCCCCCCCCCCHHC		40.5529255136
895AcetylationFGRPEGGKFDFGKHN
CCCCCCCCCCCCCCC		53.2519608861
895SumoylationFGRPEGGKFDFGKHN
CCCCCCCCCCCCCCC		53.2528112733
905PhosphorylationFGKHNMGSFPEGRFM
CCCCCCCCCCCCCCC		27.1925159151
916AcetylationGRFMPDPKINCGSGR
CCCCCCCCCCCCCCC		54.6626051181
921PhosphorylationDPKINCGSGRVTPIK
CCCCCCCCCCCCEEE		26.1525159151
925PhosphorylationNCGSGRVTPIKIMNL
CCCCCCCCEEEEECC		20.2425159151
948PhosphorylationILDFFHGYRIIPDSV
HHHHHCCCEECCCCE		7.06-
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 RB12B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB12B_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 RB12B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3A1_HUMANSF3A1physical
22939629
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 RB12B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-895, AND MASSSPECTROMETRY.
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 THR-276; SER-278; SER-280AND SER-575, 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-278; SER-280; SER-377;SER-575 AND SER-591, AND MASS SPECTROMETRY.

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