RNH2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNH2C_HUMAN
• UniProt AC: Q8TDP1
• Protein Name: Ribonuclease H2 subunit C
• Gene Name: RNASEH2C
• Organism: Homo sapiens (Human).
• Sequence Length: 164
• Subcellular Localization: Nucleus .
• Protein Description: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes..
• Protein Sequence: MESGDEAAIERHRVHLRSATLRDAVPATLHLLPCEVAVDGPAPVGRFFTPAIRQGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSMGKPDPLRDSGTDDQEEEPLERDFDRFIGATANFSRFTLWGLETIPGPDAKVRGALTWPSLAAAIHAQVPED

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
1	Acetylation	-------MESGDEAA -------CCCCCHHH	9.26	22223895
3	Phosphorylation	-----MESGDEAAIE -----CCCCCHHHHH	50.69	23401153
34	Glutathionylation	ATLHLLPCEVAVDGP CEEEEEEEEEEECCC	7.10	22555962
62	Phosphorylation	GPEGLEVSFRGRCLR CCCCEEEEEECEECC	10.39	27251275
64	Methylation	EGLEVSFRGRCLRGE CCEEEEEECEECCCC	24.92	18958555
92	Phosphorylation	VTEEKKVSMGKPDPL EECCEEECCCCCCCC	30.60	25159151
95	Acetylation	EKKVSMGKPDPLRDS CEEECCCCCCCCCCC	37.29	26822725
102	Phosphorylation	KPDPLRDSGTDDQEE CCCCCCCCCCCCCCC	36.84	28348404
104	Phosphorylation	DPLRDSGTDDQEEEP CCCCCCCCCCCCCCC	40.11	28348404
114	Methylation	QEEEPLERDFDRFIG CCCCCHHHCHHHHHH	58.54	115491355
143	Ubiquitination	TIPGPDAKVRGALTW ECCCCCCEECCCCCH	39.58	21890473
143	Sumoylation	TIPGPDAKVRGALTW ECCCCCCEECCCCCH	39.58	-
143 (in isoform 1)	Ubiquitination	-	39.58	21890473

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

Oops, there are no upstream regulatory protein records of RNH2C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNH2C_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 RNH2C_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of RNH2C_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 610329: Aicardi-Goutieres syndrome 3 (AGS3)
• 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

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
PubMed: 19413330