UniProt Accession

 RNH2B_HUMAN; Q5TBB1; Q6PK48; Q9HAF7 

Genbank Protein ID

 AY764036; AK021774; AK223340; AL137881; BC001397; BC007332; BC010174 

Genbank Nucleotide ID

 AAX13343.1; BAB13892.1; BAD97060.1; CAI13913.1; AAH01397.1; AAH07332.1; AAH10174.1 

Protein Name

 Ribonuclease H2 subunit B 

Protein Synonyms/Alias

 RNase H2 subunit B; Aicardi-Goutieres syndrome 2 protein; AGS2; Deleted in lymphocytic leukemia 8; Ribonuclease HI subunit B 

Gene Name

 RNASEH2B 

Gene Synonyms/Alias

 DLEU8 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
145	LHHVTEEKGNPEIDN	ubiquitination	[1]
153	GNPEIDNKKYYKYSK	ubiquitination	[1]
154	NPEIDNKKYYKYSKE	ubiquitination	[1]
170	TLKWLEKKVNQTVAA	ubiquitination	[1]
179	NQTVAALKTNNVNVS	ubiquitination	[1]
204	GDQASTDKEEDYIRY	ubiquitination	[1]
222	LISDYIPKELSDDLS	ubiquitination	[1]
230	ELSDDLSKYLKLPEP	ubiquitination	[1, 2]
250	NPPSKKIKLSDEPVE	ubiquitination	[1]
259	SDEPVEAKEDYTKFN	ubiquitination	[1, 3]
264	EAKEDYTKFNTKDLK	acetylation	[4]
284	SKMTAAQKALAKVDK	ubiquitination	[1]
295	KVDKSGMKSIDTFFG	acetylation	[3, 4]
295	KVDKSGMKSIDTFFG	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional 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. 

Sequence Annotation

 MOD_RES 295 295 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Aicardi-Goutieres syndrome; Complete proteome; Disease mutation; Nucleus; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 312 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:HPA.
 GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
 GO:0006401; P:RNA catabolic process; IDA:UniProtKB. 

Interpro

 IPR019024; RNase_H2_suB. 

Pfam

 PF09468; RNase_H2-Ydr279 

SMART

  

PROSITE

  

PRINTS