Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Non-secretory ribonuclease  

UniProtKB / Swiss-Prot ID :  RNAS2_HUMAN

Gene Name (Synonyms) : 
RNASE2, EDN, RNS2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Lysosome (Probable). Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. 

Protein Function :  This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities. 

Protein Sequence MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTF...
Predicted Secondary Structure CCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCHHHHHHHHCCCCCCHHHHHHHHCCCCCCCCCCCEEEE...
Protein Variant
LocationDescription
100H -> Q (in dbSNP:rs8012891). VAR_059820
156H -> N (probably inactive). VAR_013150
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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
Protein Variant
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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
34C-linked (Man)PQFTWAQWF
CCCCHHHHH
6.42HPRD
Link
34C-linked (Man)PQFTWAQWF
CCCCHHHHH
6.42OGlycBase
Link
34C-linked (Man)./FTId=CAR_000004.PQFTWAQWF
CCCCHHHHH
6.42UniProtKB
Link
44N-linked (Glc...)TQHINMTSQ
HHCCCCCCH
26.09OGlycBase
Link
44N-linked (GlcNAc...).TQHINMTSQ
HHCCCCCCH
26.09UniProtKB
Link
60Nitrated tyrosine.VINNYQRRC
CCCCCCCCC
10.02UniProtKB
Link
84N-linked (Glc...)NVCGNPNMT
HHHCCCCCC
21.46HPRD
Link
86N-linked (Glc...)CGNPNMTCP
HCCCCCCCC
42.25OGlycBase
Link
86N-linked (GlcNAc...).CGNPNMTCP
HCCCCCCCC
42.25UniProtKB
Link
92N-linked (Glc...)TCPSNKTRK
CCCCCCCCC
34.56OGlycBase
Link
92N-linked (GlcNAc...).TCPSNKTRK
CCCCCCCCC
34.56UniProtKB
Link
111N-linked (Glc...)LIHCNLTTP
EEEEEECCC
26.68OGlycBase
Link
111N-linked (GlcNAc...).LIHCNLTTP
EEEEEECCC
26.68UniProtKB
Link
119N-linked (Glc...)PSPQNISNC
CCCCCCCCC
42.94OGlycBase
Link
119N-linked (GlcNAc...).PSPQNISNC
CCCCCCCCC
42.94UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ANGI_HUMANENSP00000303276STRING
RINI_HUMANENSP00000303276STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.";
Hofsteenge J., Mueller D.R., de Beer T., Loeffler A., Richter W.J.,Vliegenthart J.F.G.;
Biochemistry 33:13524-13530(1994).
Cited for: GLYCOSYLATION AT TRP-34.
"Recognition signal for C-mannosylation of Trp-7 in RNase 2 consistsof sequence Trp-x-x-Trp.";
Krieg J., Hartmann S., Vicentini A., Glasner W., Hess D.,Hofsteenge J.;
Mol. Biol. Cell 9:301-309(1998).
Cited for: GLYCOSYLATION AT TRP-34.
Nitration
ReferencePubMed
"Post-translational tyrosine nitration of eosinophil granule toxinsmediated by eosinophil peroxidase.";
Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N.,Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H.,Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M.,Doering G.;
J. Biol. Chem. 283:28629-28640(2008).
Cited for: NITRATION AT TYR-60.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures