RNT2_HUMAN - dbPTM
RNT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNT2_HUMAN
UniProt AC O00584
Protein Name Ribonuclease T2
Gene Name RNASET2
Organism Homo sapiens (Human).
Sequence Length 256
Subcellular Localization Secreted. Lysosome lumen. Endoplasmic reticulum lumen. Subcellular fractionation of transfected ovarian cancer cells reveals full-length RNASET2 in the endoplasmic reticulum fraction and the 2 smaller RNASET2 proteolytic products in the lysosome frac
Protein Description Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism..
Protein Sequence MRPAALRGALLGCLCLALLCLGGADKRLRDNHEWKKLIMVQHWPETVCEKIQNDCRDPPDYWTIHGLWPDKSEGCNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTCAAQVDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQCLPPSQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVWLANGAAESRGLRVCEDGPVFYPPPKKTKH
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
76N-linked_GlycosylationPDKSEGCNRSWPFNL
CCCCCCCCCCCCCCH
52.4522735700
103O-linked_GlycosylationYWPDVIHSFPNRSRF
HCCHHHHHCCCCHHH
31.1332574038
106N-linked_GlycosylationDVIHSFPNRSRFWKH
HHHHHCCCCHHHHHC
53.1822735700
112AcetylationPNRSRFWKHEWEKHG
CCCHHHHHCHHHHHC
29.0026822725
130PhosphorylationAQVDALNSQKKYFGR
HHHHHHHHCHHHHCC
44.2024247654
157UbiquitinationVLLKLGIKPSINYYQ
HHHHHCCCCCCCEEE
30.802189047
157 (in isoform 1)Ubiquitination-30.8021890473
159PhosphorylationLKLGIKPSINYYQVA
HHHCCCCCCCEEEEC
20.6123898821
162PhosphorylationGIKPSINYYQVADFK
CCCCCCCEEEECCHH
8.1323898821
163PhosphorylationIKPSINYYQVADFKD
CCCCCCEEEECCHHH
7.6323898821
212N-linked_GlycosylationKQDQQLQNCTEPGEQ
HHHHHHHCCCCCCCC
43.1822735700
214PhosphorylationDQQLQNCTEPGEQPS
HHHHHCCCCCCCCCC
53.4128674419
221PhosphorylationTEPGEQPSPKQEVWL
CCCCCCCCCHHHEEE
44.4128674419
235PhosphorylationLANGAAESRGLRVCE
ECCCCHHHCCCEECC
27.2426270265

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 RNT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNT2_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 RNT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUCB2_HUMANSUCLG2physical
22939629
TRAF2_HUMANTRAF2physical
24457966
PDIA5_HUMANPDIA5physical
26186194
FBX2_HUMANFBXO2physical
26186194
PDIA5_HUMANPDIA5physical
28514442
FBX2_HUMANFBXO2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612951Leukoencephalopathy, cystic, without megalencephaly (LCWM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNT2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP