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Q9CWY8 (RNH2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease H2 subunit A

Short name=RNase H2 subunit A
EC=3.1.26.4
Alternative name(s):
Ribonuclease HI large subunit
Short name=RNase HI large subunit
Ribonuclease HI subunit A
Gene names
Name:Rnaseh2a
Synonyms:Rnasehi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. Ref.4

Cofactor

Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding By similarity. Ref.4

Subunit structure

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. Ref.4

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the RNase HII family. Eukaryotic subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 301301Ribonuclease H2 subunit A
PRO_0000111711

Sites

Metal binding341Divalent metal cation Probable
Metal binding351Divalent metal cation Probable
Metal binding1421Divalent metal cation Probable

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2171Phosphothreonine By similarity
Modified residue2581Phosphoserine Ref.3

Experimental info

Mutagenesis341D → N: Loss of enzyme activity. Ref.4
Mutagenesis351E → A: Loss of enzyme activity. Ref.4
Mutagenesis371G → S: Strongly reduced in vitro enzyme activity. Ref.4
Mutagenesis1421D → N: Loss of enzyme activity. Ref.4
Mutagenesis1701D → N: Loss of enzyme activity. Ref.4
Sequence conflict1321Q → R in BAB26828. Ref.1

Secondary structure

................................................... 301
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CWY8 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: 3B95211289847CBC

FASTA30133,513
        10         20         30         40         50         60 
MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC YCPLSRLADL 

        70         80         90        100        110        120 
EALKVADSKT LTENERERLF AKMEEDGDFV GWALDVLSPN LISTSMLGRV KYNLNSLSHD 

       130        140        150        160        170        180 
TAAGLIQYAL DQNVNVTQVF VDTVGMPETY QARLQQHFPG IEVTVKAKAD SLFPVVSAAS 

       190        200        210        220        230        240 
IFAKVARDKA VKNWQFVENL QDLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS 

       250        260        270        280        290        300 
TAQAILEKEA EDVIWEDSEA EEDPERPGKI TSYFSQGPQT CRPQAPHRYF QERGLEAASS 


L 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic stem cell and Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction."
Shaban N.M., Harvey S., Perrino F.W., Hollis T.
J. Biol. Chem. 285:3617-3624(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF ASP-34; GLU-35; GLY-37; ASP-142 AND ASP-170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010292 mRNA. Translation: BAB26828.1.
AK146518 mRNA. Translation: BAE27230.1.
BC038158 mRNA. Translation: AAH38158.1.
RefSeqNP_081463.1. NM_027187.3.
UniGeneMm.182470.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90A1-301[»]
3P5JX-ray2.90A1-301[»]
ProteinModelPortalQ9CWY8.
SMRQ9CWY8. Positions 1-301.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CWY8.

Proteomic databases

PaxDbQ9CWY8.
PRIDEQ9CWY8.

Protocols and materials databases

DNASU69724.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.
GeneID69724.
KEGGmmu:69724.
UCSCuc009mok.1. mouse.

Organism-specific databases

CTD10535.
MGIMGI:1916974. Rnaseh2a.

Phylogenomic databases

eggNOGCOG0164.
GeneTreeENSGT00390000010768.
HOGENOMHOG000100290.
HOVERGENHBG023585.
InParanoidQ9CWY8.
KOK10743.
OMAGPPEKYQ.
OrthoDBEOG7KM5T4.
PhylomeDBQ9CWY8.
TreeFamTF314302.

Gene expression databases

ArrayExpressQ9CWY8.
BgeeQ9CWY8.
CleanExMM_RNASEH2A.
GenevestigatorQ9CWY8.

Family and domain databases

Gene3D1.10.10.460. 1 hit.
3.30.420.10. 1 hit.
InterProIPR004649. RNase_H2_suA.
IPR001352. RNase_HII/HIII.
IPR024567. RNase_HII/HIII_dom.
IPR023160. RNase_HII_hlx-loop-hlx_cap_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERPTHR10954. PTHR10954. 1 hit.
PfamPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00729. TIGR00729. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRNASEH2A. mouse.
EvolutionaryTraceQ9CWY8.
NextBio330190.
PROQ9CWY8.
SOURCESearch...

Entry information

Entry nameRNH2A_MOUSE
AccessionPrimary (citable) accession number: Q9CWY8
Secondary accession number(s): Q8CHY8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot