RNAS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNAS1_HUMAN
• UniProt AC: P07998
• Protein Name: Ribonuclease pancreatic
• Gene Name: RNASE1
• Organism: Homo sapiens (Human).
• Sequence Length: 156
• Subcellular Localization: Secreted.
• Protein Description: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA..
• Protein Sequence: MALEKSLVRLLLLVLILLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSSSTYCNQMMRRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQGNCYKSNSSMHITDCRLTNGSRYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST

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
26	Phosphorylation	VLGWVQPSLGKESRA HHHHHCHHCCHHHHH	32.44	24114839
49	Phosphorylation	DSDSSPSSSSTYCNQ CCCCCCCCHHHHHHH	31.52	-
62	N-linked_Glycosylation	NQMMRRRNMTQGRCK HHHHHHCCCCCCCCC	35.72	12626415
62	N-linked_Glycosylation	NQMMRRRNMTQGRCK HHHHHHCCCCCCCCC	35.72	12626415
92	Phosphorylation	VCFQEKVTCKNGQGN EEEEEEEEEECCCCC	28.91	29978859
104	N-linked_Glycosylation	QGNCYKSNSSMHITD CCCCEECCCCCEEEE	33.67	12626415
104	N-linked_Glycosylation	QGNCYKSNSSMHITD CCCCEECCCCCEEEE	33.67	12626415
115	Phosphorylation	HITDCRLTNGSRYPN EEEEEECCCCCCCCC	20.41	30576142
116	N-linked_Glycosylation	ITDCRLTNGSRYPNC EEEEECCCCCCCCCC	51.54	12626415
116	N-linked_Glycosylation	ITDCRLTNGSRYPNC EEEEECCCCCCCCCC	51.54	12626415
120	Phosphorylation	RLTNGSRYPNCAYRT ECCCCCCCCCCCCCC	10.65	30576142

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

Oops, there are no upstream regulatory protein records of RNAS1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNAS1_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 RNAS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RINI_HUMAN	RNH1	physical	28514442
BUD31_HUMAN	BUD31	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
ASHWN_HUMAN	C2orf49	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

N-linked Glycosylation

"Differences in glycosylation pattern of human secretoryribonucleases.";
Beintema J.J., Blank A., Schieven G.L., Dekker C.A., Sorrentino S.,Libonati M.;
Biochem. J. 255:501-505(1988).
Cited for: PROTEIN SEQUENCE OF 29-156, AND GLYCOSYLATION AT ASN-62; ASN-104 ANDASN-116.
PubMed: 3202829