R113A_HUMAN - dbPTM
R113A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID R113A_HUMAN
UniProt AC O15541
Protein Name RING finger protein 113A
Gene Name RNF113A
Organism Homo sapiens (Human).
Sequence Length 343
Subcellular Localization
Protein Description
Protein Sequence MAEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKTRDSGKQKAAYGDLSSEEEEENEPESLGVVYKSTRSAKPVGPEDMGATAVYELDTEKERDAQAIFERSQKIQEELRGKEDDKIYRGINNYQKYMKPKDTSMGNASSGMVRKGPIRAPEHLRATVRWDYQPDICKDYKETGFCGFGDSCKFLHDRSDYKHGWQIERELDEGRYGVYEDENYEVGSDDEEIPFKCFICRQSFQNPVVTKCRHYFCESCALQHFRTTPRCYVCDQQTNGVFNPAKELIAKLEKHRATGEGGASDLPEDPDEDAIPIT
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
2Acetylation------MAEQLSPGK
------CCCCCCCCH		17.1621406692
6Phosphorylation--MAEQLSPGKAVDQ
--CCCCCCCCHHHHH		31.1629255136
16PhosphorylationKAVDQVCTFLFKKPG
HHHHHHHHHHCCCCC		25.2328464451
43PhosphorylationCDPEPGESGSSSDEG
CCCCCCCCCCCCCCC		50.3021955146
45PhosphorylationPEPGESGSSSDEGCT
CCCCCCCCCCCCCCC		35.6321955146
46PhosphorylationEPGESGSSSDEGCTV
CCCCCCCCCCCCCCE		45.3821955146
47PhosphorylationPGESGSSSDEGCTVV
CCCCCCCCCCCCCEE		41.1821955146
52PhosphorylationSSSDEGCTVVRPEKK
CCCCCCCCEECCCCC		32.6521955146
62PhosphorylationRPEKKRVTHNPMIQK
CCCCCCCCCCCCCHH		21.7028555341
73PhosphorylationMIQKTRDSGKQKAAY
CCHHCHHCCCCCCCC		44.6026074081
80PhosphorylationSGKQKAAYGDLSSEE
CCCCCCCCCCCCCHH		18.9420201521
84PhosphorylationKAAYGDLSSEEEEEN
CCCCCCCCCHHHHHC		40.2120201521
85PhosphorylationAAYGDLSSEEEEENE
CCCCCCCCHHHHHCC		57.2220201521
95PhosphorylationEEENEPESLGVVYKS
HHHCCCHHHCEEEEE		40.9323927012
100PhosphorylationPESLGVVYKSTRSAK
CHHHCEEEEECCCCC		9.2323927012
102PhosphorylationSLGVVYKSTRSAKPV
HHCEEEEECCCCCCC		16.0326074081
103PhosphorylationLGVVYKSTRSAKPVG
HCEEEEECCCCCCCC		25.2126074081
105PhosphorylationVVYKSTRSAKPVGPE
EEEEECCCCCCCCHH		40.5126074081
107AcetylationYKSTRSAKPVGPEDM
EEECCCCCCCCHHHC		41.2923954790
107SumoylationYKSTRSAKPVGPEDM
EEECCCCCCCCHHHC		41.29-
107SumoylationYKSTRSAKPVGPEDM
EEECCCCCCCCHHHC		41.29-
117PhosphorylationGPEDMGATAVYELDT
CHHHCCCEEEEECCC		15.7821945579
120PhosphorylationDMGATAVYELDTEKE
HCCCEEEEECCCCHH		14.3321945579
124PhosphorylationTAVYELDTEKERDAQ
EEEEECCCCHHHHHH		62.6721945579
126UbiquitinationVYELDTEKERDAQAI
EEECCCCHHHHHHHH		61.2124816145
137PhosphorylationAQAIFERSQKIQEEL
HHHHHHHHHHHHHHH		28.7328555341
139SumoylationAIFERSQKIQEELRG
HHHHHHHHHHHHHCC		47.83-
139UbiquitinationAIFERSQKIQEELRG
HHHHHHHHHHHHHCC		47.8329967540
139SumoylationAIFERSQKIQEELRG
HHHHHHHHHHHHHCC		47.83-
147UbiquitinationIQEELRGKEDDKIYR
HHHHHCCCCCCHHHH		52.0829967540
151SumoylationLRGKEDDKIYRGINN
HCCCCCCHHHHHHHH		54.69-
151SumoylationLRGKEDDKIYRGINN
HCCCCCCHHHHHHHH		54.69-
153PhosphorylationGKEDDKIYRGINNYQ
CCCCCHHHHHHHHHH		14.4522817900
159PhosphorylationIYRGINNYQKYMKPK
HHHHHHHHHHHCCCC		11.24-
161SumoylationRGINNYQKYMKPKDT
HHHHHHHHHCCCCCC		36.63-
161AcetylationRGINNYQKYMKPKDT
HHHHHHHHHCCCCCC		36.6325953088
161SumoylationRGINNYQKYMKPKDT
HHHHHHHHHCCCCCC		36.63-
162PhosphorylationGINNYQKYMKPKDTS
HHHHHHHHCCCCCCC		8.5428258704
166SumoylationYQKYMKPKDTSMGNA
HHHHCCCCCCCCCCC		69.03-
166SumoylationYQKYMKPKDTSMGNA
HHHHCCCCCCCCCCC		69.03-
168PhosphorylationKYMKPKDTSMGNASS
HHCCCCCCCCCCCCC		27.0920068231
169PhosphorylationYMKPKDTSMGNASSG
HCCCCCCCCCCCCCC		34.5225159151
174PhosphorylationDTSMGNASSGMVRKG
CCCCCCCCCCCEECC		31.27-
175PhosphorylationTSMGNASSGMVRKGP
CCCCCCCCCCEECCC		28.62-
180SumoylationASSGMVRKGPIRAPE
CCCCCEECCCCCCCH		58.59-
180SumoylationASSGMVRKGPIRAPE
CCCCCEECCCCCCCH		58.59-
192PhosphorylationAPEHLRATVRWDYQP
CCHHHCEEEECCCCC		12.27-
197PhosphorylationRATVRWDYQPDICKD
CEEEECCCCCCCCCC		18.2628796482
216PhosphorylationGFCGFGDSCKFLHDR
CCCCCCCCCCCCCCC		21.4224719451
227SumoylationLHDRSDYKHGWQIER
CCCCCCCCCCEEEEE		40.40-
227SumoylationLHDRSDYKHGWQIER
CCCCCCCCCCEEEEE		40.40-
241PhosphorylationRELDEGRYGVYEDEN
EEECCCCCEEEECCC		23.0728796482
244PhosphorylationDEGRYGVYEDENYEV
CCCCCEEEECCCCCC		17.1923927012
249PhosphorylationGVYEDENYEVGSDDE
EEEECCCCCCCCCCC		15.2223927012
253PhosphorylationDENYEVGSDDEEIPF
CCCCCCCCCCCCCCE		47.2525159151
268PhosphorylationKCFICRQSFQNPVVT
EEEEECHHCCCCHHH		14.9525159151
316SumoylationPAKELIAKLEKHRAT
HHHHHHHHHHHHHCC		50.62-
316SumoylationPAKELIAKLEKHRAT
HHHHHHHHHHHHHCC		50.62-
323PhosphorylationKLEKHRATGEGGASD
HHHHHHCCCCCCCCC		35.4025159151
329PhosphorylationATGEGGASDLPEDPD
CCCCCCCCCCCCCCC		42.8525159151
343PhosphorylationDEDAIPIT-------
CCCCCCCC-------		27.4921406692
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 R113A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of R113A_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 R113A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B2_HUMANSF3B2physical
22365833
CCAR1_HUMANCCAR1physical
22365833
RBM39_HUMANRBM39physical
22365833
ILF3_HUMANILF3physical
22365833
U520_HUMANSNRNP200physical
22365833
RED_HUMANIKphysical
22365833
CARME_HUMANC9orf41physical
28514442
ACSF4_HUMANAASDHphysical
28514442
CSK22_HUMANCSNK2A2physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300953Trichothiodystrophy 5, non-photosensitive (TTD5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of R113A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6; TYR-80; SER-84; SER-85 AND SER-253, AND MASSSPECTROMETRY.
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 SER-84 AND SER-253, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6; TYR-80; SER-84; SER-85 AND SER-253, AND MASSSPECTROMETRY.
"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-84; SER-85 AND SER-253,AND MASS SPECTROMETRY.
"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 TYR-80 AND SER-85, AND MASSSPECTROMETRY.
"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-43; SER-45; SER-46;SER-47; THR-52; SER-84; SER-85 AND SER-253, AND MASS SPECTROMETRY.

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