CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001261
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease H2 subunit A 
Protein Synonyms/Alias
 RNase H2 subunit A; Aicardi-Goutieres syndrome 4 protein; AGS4; RNase H(35); Ribonuclease HI large subunit; RNase HI large subunit; Ribonuclease HI subunit A 
Gene Name
 RNASEH2A 
Gene Synonyms/Alias
 RNASEHI; RNHIA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26PVPAVCRKEPCVLGVubiquitination[1, 2]
64LADLEALKVADSKTLubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
69ALKVADSKTLLESERubiquitination[1, 2, 4, 5]
165PGIEVTVKAKADALYubiquitination[1, 4]
167IEVTVKAKADALYPVubiquitination[1, 2, 5, 6, 7]
183SAASICAKVARDQAVubiquitination[1]
192ARDQAVKKWQFVEKLubiquitination[1]
198KKWQFVEKLQDLDTDubiquitination[1, 4, 5, 8]
215SGYPNDPKTKAWLKEubiquitination[2, 4, 5]
217YPNDPKTKAWLKEHVubiquitination[1]
221PKTKAWLKEHVEPVFubiquitination[1, 2, 3, 4, 5, 8, 9]
247TAQTILEKEAEDVIWubiquitination[1, 4]
267ENQEGLRKITSYFLNubiquitination[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] 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]
 [3] 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]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Catalytic subunit of RNase HII, 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
 METAL 34 34 Divalent metal cation (By similarity).
 METAL 35 35 Divalent metal cation (By similarity).
 METAL 141 141 Divalent metal cation (By similarity).
 MOD_RES 204 204 Phosphothreonine.
 MOD_RES 216 216 Phosphothreonine.
 MOD_RES 257 257 Phosphoserine (By similarity).  
Keyword
 3D-structure; Aicardi-Goutieres syndrome; Complete proteome; Disease mutation; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 299 AA 
Protein Sequence
MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC YCPLPRLADL 60
EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL ISTSMLGRVK YNLNSLSHDT 120
ATGLIQYALD QGVNVTQVFV DTVGMPETYQ ARLQQSFPGI EVTVKAKADA LYPVVSAASI 180
CAKVARDQAV KKWQFVEKLQ DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT 240
AQTILEKEAE DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL 299 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004523; F:ribonuclease H activity; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0006260; P:DNA replication; TAS:UniProtKB.
 GO:0006401; P:RNA catabolic process; IDA:UniProtKB. 
Interpro
 IPR004649; RNase_H2_suA.
 IPR001352; RNase_HII/HIII.
 IPR024567; RNase_HII/HIII_dom.
 IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
 IPR012337; RNaseH-like_dom. 
Pfam
 PF01351; RNase_HII 
SMART
  
PROSITE
  
PRINTS