RNAS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNAS2_HUMAN
• UniProt AC: P10153
• Protein Name: Non-secretory ribonuclease
• Gene Name: RNASE2
• Organism: Homo sapiens (Human).
• Sequence Length: 161
• Subcellular Localization: Lysosome . Cytoplasmic granule. Matrix of eosinophil's large specific granule.
• Protein Description: 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: MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII

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
34	C-linked_Glycosylation	VKPPQFTWAQWFETQ CCCCCCCHHHHHEEE	6.42	7947762
34	C-linked_Glycosylation	VKPPQFTWAQWFETQ CCCCCCCHHHHHEEE	6.42	7947762
44	N-linked_Glycosylation	WFETQHINMTSQQCT HHEEECCCCCHHHHH	26.09	7947762
60	Nitrated tyrosine	AMQVINNYQRRCKNQ HHHHHHHHHHHHCCC	10.02	-
60	Nitration	AMQVINNYQRRCKNQ HHHHHHHHHHHHCCC	10.02	18694936
60	Nitration	AMQVINNYQRRCKNQ HHHHHHHHHHHHCCC	10.02	18694936
84	N-linked_Glycosylation	NVVNVCGNPNMTCPS CHHHHCCCCCCCCCC	21.46	-
84	N-linked_Glycosylation	NVVNVCGNPNMTCPS CHHHHCCCCCCCCCC	21.46	12578357
86	N-linked_Glycosylation	VNVCGNPNMTCPSNK HHHCCCCCCCCCCCC	42.25	7947762
92	N-linked_Glycosylation	PNMTCPSNKTRKNCH CCCCCCCCCCCCCCC	34.56	7947762
111	N-linked_Glycosylation	QVPLIHCNLTTPSPQ CCCEEEEECCCCCCC	26.68	7947762
119	N-linked_Glycosylation	LTTPSPQNISNCRYA CCCCCCCCCCCCEEC	42.94	7947762
150	Phosphorylation	QRRDPPQYPVVPVHL CCCCCCCCCCCCCCH	12.08	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RNAS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNAS2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RNAS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCP2_HUMAN	PCP2	physical	28514442

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.

Related Literatures of Post-Translational Modification

C-linked Glycosylation

"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.
PubMed: 9450956

"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.
PubMed: 7947762

Nitration

"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.
PubMed: 18694936