RNH1_HUMAN - dbPTM
RNH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNH1_HUMAN
UniProt AC O60930
Protein Name Ribonuclease H1
Gene Name RNASEH1
Organism Homo sapiens (Human).
Sequence Length 286
Subcellular Localization Cytoplasm .
Protein Description Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. [PubMed: 10497183 Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II]
Protein Sequence MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
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
22PhosphorylationALPCRRGSRGFGMFY
HCCCCCCCCCCCCEE
27.67-
52MethylationECRAQVDRFPAARFK
HHHHHHCCCCHHHHH
40.36115491333
59UbiquitinationRFPAARFKKFATEDE
CCCHHHHHHCCCHHH
41.23-
60UbiquitinationFPAARFKKFATEDEA
CCHHHHHHCCCHHHH
37.20-
73UbiquitinationEAWAFVRKSASPEVS
HHHHHHHHCCCCCCC
45.10-
74PhosphorylationAWAFVRKSASPEVSE
HHHHHHHCCCCCCCC
24.3429255136
76PhosphorylationAFVRKSASPEVSEGH
HHHHHCCCCCCCCCC
28.7829255136
80PhosphorylationKSASPEVSEGHENQH
HCCCCCCCCCCCCCC
35.8829255136
91PhosphorylationENQHGQESEAKASKR
CCCCCCCCHHHHHHH
34.6623403867
119UbiquitinationEPYAKHMKPSVEPAP
CHHHHHCCCCCCCCC
33.58-
175MethylationHPLNVGIRLPGRQTN
CCCCEEEECCCCCCC
28.9754558823
192UbiquitinationAEIHAACKAIEQAKT
HHHHHHHHHHHHHHH
47.90-
198UbiquitinationCKAIEQAKTQNINKL
HHHHHHHHHCCCCEE
50.79-
232PhosphorylationWKKNGWKTSAGKEVI
HHHCCCCCCCCCEEC
19.8020860994
233PhosphorylationKKNGWKTSAGKEVIN
HHCCCCCCCCCEECC
31.1520860994
236UbiquitinationGWKTSAGKEVINKED
CCCCCCCCEECCHHH
48.82-
241UbiquitinationAGKEVINKEDFVALE
CCCEECCHHHHHHHH
47.76-

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 RNH1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNH1_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 RNH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM9S1_HUMANTM9SF1physical
21988832

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 RNH1_HUMAN

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Related Literatures of Post-Translational Modification

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