Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  RING finger protein 113A  

UniProtKB / Swiss-Prot ID :  R113A_HUMAN

Gene Name (Synonyms) : 
RNF113A, RNF113, ZNF183  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MAEQLSPGKAVDQVCTFLFKKPGRKGAAGRRKRPACDPEPGESGSSSDEGCTVVRPEKKRVTHNPMIQKT...
Predicted Secondary Structure CCCCCCCCCCCCCEEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEECCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEQLS
---CCCCCC
17.16UniProtKB
Link-
6PhosphoserineAEQLSPGKA
CCCCCCCCC
31.16HPRD
Link-
6PhosphoserineAEQLSPGKA
CCCCCCCCC
31.16Phosphositeplus
Link-
6Phosphoserine.AEQLSPGKA
CCCCCCCCC
31.16UniProtKB
Link-
43PhosphoserineEPGESGSSS
CCCCCCCCC
50.30HPRD
Link-
43PhosphoserineEPGESGSSS
CCCCCCCCC
50.30PhosphoELM
Link-
43PhosphoserineEPGESGSSS
CCCCCCCCC
50.30Phosphositeplus
Link-
43PhosphoserineEPGESGSSS
CCCCCCCCC
50.30SysPTM
Link-
43Phosphoserine.EPGESGSSS
CCCCCCCCC
50.30UniProtKB
Link-
45PhosphoserineGESGSSSDE
CCCCCCCCC
35.63HPRD
Link-
45PhosphoserineGESGSSSDE
CCCCCCCCC
35.63PhosphoELM
Link-
45PhosphoserineGESGSSSDE
CCCCCCCCC
35.63Phosphositeplus
Link-
45PhosphoserineGESGSSSDE
CCCCCCCCC
35.63SysPTM
Link-
45Phosphoserine.GESGSSSDE
CCCCCCCCC
35.63UniProtKB
Link-
46PhosphoserineESGSSSDEG
CCCCCCCCC
45.38HPRD
Link-
46PhosphoserineESGSSSDEG
CCCCCCCCC
45.38PhosphoELM
Link-
46PhosphoserineESGSSSDEG
CCCCCCCCC
45.38Phosphositeplus
Link-
46PhosphoserineESGSSSDEG
CCCCCCCCC
45.38SysPTM
Link-
46Phosphoserine.ESGSSSDEG
CCCCCCCCC
45.38UniProtKB
Link-
47PhosphoserineSGSSSDEGC
CCCCCCCCC
41.18HPRD
Link-
47PhosphoserineSGSSSDEGC
CCCCCCCCC
41.18PhosphoELM
Link-
47PhosphoserineSGSSSDEGC
CCCCCCCCC
41.18Phosphositeplus
Link-
47PhosphoserineSGSSSDEGC
CCCCCCCCC
41.18SysPTM
Link-
47Phosphoserine.SGSSSDEGC
CCCCCCCCC
41.18UniProtKB
Link-
52PhosphothreonineDEGCTVVRP
CCCCCEECC
32.65HPRD
Link-
52PhosphothreonineDEGCTVVRP
CCCCCEECC
32.65SysPTM
Link-
52Phosphothreonine.DEGCTVVRP
CCCCCEECC
32.65UniProtKB
Link-
80PhosphotyrosineQKAAYGDLS
HHHHHCCCC
18.94HPRD
Link-
80PhosphotyrosineQKAAYGDLS
HHHHHCCCC
18.94PhosphoELM
Link-
80PhosphotyrosineQKAAYGDLS
HHHHHCCCC
18.94Phosphositeplus
Link-
80Phosphotyrosine.QKAAYGDLS
HHHHHCCCC
18.94UniProtKB
Link-
84PhosphoserineYGDLSSEEE
HCCCCCCCC
40.21HPRD
Link-
84PhosphoserineYGDLSSEEE
HCCCCCCCC
40.21PhosphoELM
Link-
84PhosphoserineYGDLSSEEE
HCCCCCCCC
40.21Phosphositeplus
Link-
84PhosphoserineYGDLSSEEE
HCCCCCCCC
40.21SysPTM
Link-
84Phosphoserine.YGDLSSEEE
HCCCCCCCC
40.21UniProtKB
Link-
85PhosphoserineGDLSSEEEE
CCCCCCCCC
57.22HPRD
Link-
85PhosphoserineGDLSSEEEE
CCCCCCCCC
57.22PhosphoELM
Link-
85PhosphoserineGDLSSEEEE
CCCCCCCCC
57.22Phosphositeplus
Link-
85PhosphoserineGDLSSEEEE
CCCCCCCCC
57.22SysPTM
Link-
85Phosphoserine.GDLSSEEEE
CCCCCCCCC
57.22UniProtKB
Link-
100PhosphotyrosineLGVVYKSTR
HHHHHHCCC
9.23HPRD
Link-
249PhosphotyrosineEDENYEVGS
CCCCEECCH
15.22HPRD
Link-
249PhosphotyrosineEDENYEVGS
CCCCEECCH
15.22Phosphositeplus
Link-
253PhosphoserineYEVGSDDEE
EECCHHHHC
47.25HPRD
Link-
253PhosphoserineYEVGSDDEE
EECCHHHHC
47.25PhosphoELM
Link-
253PhosphoserineYEVGSDDEE
EECCHHHHC
47.25Phosphositeplus
Link-
253PhosphoserineYEVGSDDEE
EECCHHHHC
47.25SysPTM
Link-
253Phosphoserine.YEVGSDDEE
EECCHHHHC
47.25UniProtKB
Link-
329PhosphoserineEGGASDLPE
CCCCCCCCC
42.85Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
OMIM disease
300953Trichothiodystrophy 5, non-photosensitive (TTD5)
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures