ENDOV_HUMAN - dbPTM
ENDOV_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENDOV_HUMAN
UniProt AC Q8N8Q3
Protein Name Endonuclease V
Gene Name ENDOV
Organism Homo sapiens (Human).
Sequence Length 282
Subcellular Localization Cytoplasm. Nucleus, nucleolus.
Protein Description Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures..
Protein Sequence MALEAAGGPPEETLSLWKREQARLKAHVVDRDTEAWQRDPAFSGLQRVGGVDVSFVKGDSVRACASLVVLSFPELEVVYEESRMVSLTAPYVSGFLAFREVPFLLELVQQLREKEPGLMPQVLLVDGNGVLHHRGFGVACHLGVLTDLPCVGVAKKLLQVDGLENNALHKEKIRLLQTRGDSFPLLGDSGTVLGMALRSHDRSTRPLYISVGHRMSLEAAVRLTCCCCRFRIPEPVRQADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESSALC
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
18UbiquitinationEETLSLWKREQARLK
HHHHHHHHHHHHHHH
51.88-
25UbiquitinationKREQARLKAHVVDRD
HHHHHHHHCEEECCC
30.78-
57UbiquitinationGVDVSFVKGDSVRAC
CEEEEEECCHHHHHH
55.802190698
57 (in isoform 3)Ubiquitination-55.8021906983
57 (in isoform 2)Ubiquitination-55.8021906983
57 (in isoform 1)Ubiquitination-55.8021906983
86PhosphorylationYEESRMVSLTAPYVS
EEECCEEECCCCCCC
15.6228122231
88PhosphorylationESRMVSLTAPYVSGF
ECCEEECCCCCCCCC
20.3428122231
146PhosphorylationACHLGVLTDLPCVGV
CHHHCCCCCCCCHHH
32.84-
156UbiquitinationPCVGVAKKLLQVDGL
CCHHHHHHHHHCCCC
44.70-
170UbiquitinationLENNALHKEKIRLLQ
CCCCCHHHHHHHHHH
62.65-
172UbiquitinationNNALHKEKIRLLQTR
CCCHHHHHHHHHHHC
37.62-
178PhosphorylationEKIRLLQTRGDSFPL
HHHHHHHHCCCCCCC
36.27-
182PhosphorylationLLQTRGDSFPLLGDS
HHHHCCCCCCCCCCC
31.43-
198MethylationTVLGMALRSHDRSTR
CHHHHHHHCCCCCCC
23.54-
198DimethylationTVLGMALRSHDRSTR
CHHHHHHHCCCCCCC
23.54-
202MethylationMALRSHDRSTRPLYI
HHHHCCCCCCCCEEE
34.21-
202DimethylationMALRSHDRSTRPLYI
HHHHCCCCCCCCEEE
34.21-
230 (in isoform 3)Phosphorylation-5.3225159151
233 (in isoform 3)Phosphorylation-35.2725627689
244 (in isoform 3)Phosphorylation-34.7925849741
250PhosphorylationSREHIRKSLGLPGPP
CHHHHHHHCCCCCCC
20.1623403867
258PhosphorylationLGLPGPPTPRSPKAQ
CCCCCCCCCCCCCCC
34.1725159151
261PhosphorylationPGPPTPRSPKAQRPV
CCCCCCCCCCCCCCC
31.7725159151
278PhosphorylationPKGDSGESSALC---
CCCCCCCCCCCC---
25.16-
279PhosphorylationKGDSGESSALC----
CCCCCCCCCCC----
22.43-

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 ENDOV_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENDOV_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 ENDOV_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBS2_HUMANBBS2physical
26186194
VWA8_HUMANVWA8physical
26186194
TCPB_HUMANCCT2physical
26186194
ANR40_HUMANANKRD40physical
26186194
PHLP_HUMANPDCLphysical
26186194
SPS2_HUMANSEPHS2physical
26186194
RNF31_HUMANRNF31physical
26186194
T22D3_HUMANTSC22D3physical
26186194
APAF_HUMANAPAF1physical
26186194
SPS2_HUMANSEPHS2physical
28514442
APAF_HUMANAPAF1physical
28514442
RNF31_HUMANRNF31physical
28514442
VWA8_HUMANVWA8physical
28514442
T22D3_HUMANTSC22D3physical
28514442
ANR40_HUMANANKRD40physical
28514442
PHLP_HUMANPDCLphysical
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.
Regulatory Network of ENDOV_HUMAN

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Related Literatures of Post-Translational Modification

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