Q9CWY8 (RNH2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribonuclease H2 complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 301

301

Ribonuclease H2 subunit A

PRO_0000111711

Sites

Metal binding

34

1

Divalent metal cation Probable

Metal binding

35

1

Divalent metal cation Probable

Metal binding

142

1

Divalent metal cation Probable

Amino acid modifications

Modified residue

217

1

Phosphothreonine By similarity

Modified residue

258

1

Phosphoserine Ref.3

Experimental info

Mutagenesis

34

1

D → N: Loss of enzyme activity. Ref.4

Mutagenesis

35

1

E → A: Loss of enzyme activity. Ref.4

Mutagenesis

37

1

G → S: Strongly reduced in vitro enzyme activity. Ref.4

Mutagenesis

142

1

D → N: Loss of enzyme activity. Ref.4

Mutagenesis

170

1

D → N: Loss of enzyme activity. Ref.4

Sequence conflict

132

1

Q → R in BAB26828. Ref.1

Secondary structure

1

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301

Helix Strand Turn

Details...

Turn

3 – 6

4

Helix

7 – 9

3

Beta strand

11 – 17

7

Helix

23 – 26

4

Beta strand

29 – 36

8

Beta strand

41 – 43

3

Beta strand

45 – 53

9

Helix

54 – 59

6

Helix

60 – 64

5

Helix

73 – 85

13

Turn

86 – 89

4

Beta strand

91 – 97

7

Helix

99 – 106

8

Beta strand

108 – 110

3

Helix

114 – 131

18

Beta strand

136 – 142

7

Helix

148 – 156

9

Beta strand

161 – 166

6

Helix

169 – 171

3

Helix

174 – 200

27

Beta strand

209 – 211

3

Helix

215 – 222

8

Turn

227 – 229

3

Helix

240 – 249

10

Beta strand

253 – 255

3

Helix

287 – 293

7

Beta strand

295 – 297

3

Sequences

	Sequence		Length	Mass (Da)
	Q9CWY8 [UniParc]. Last modified January 10, 2006. Version 2. Checksum: 3B95211289847CBC	FASTA	301	33,513
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, MASS SPECTROMETRY. Tissue: Melanoma.
[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.

IPI

IPI00229787.

RefSeq

NP_081463.1. NM_027187.3.

UniGene

Mm.182470.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KIO	X-ray	2.90	A	1-301	[»]
3P5J	X-ray	2.90	A	1-301	[»]

ProteinModelPortal

Q9CWY8.

SMR

Q9CWY8. Positions 1-301.

ModBase

Search...

PTM databases

PhosphoSite

Q9CWY8.

Proteomic databases

PaxDb

Q9CWY8.

PRIDE

Q9CWY8.

Protocols and materials databases

DNASU

69724.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.

GeneID

69724.

KEGG

mmu:69724.

UCSC

uc009mok.1. mouse.

Organism-specific databases

CTD

10535.

MGI

MGI:1916974. Rnaseh2a.

Phylogenomic databases

eggNOG

COG0164.

GeneTree

ENSGT00390000010768.

HOGENOM

HOG000100290.

HOVERGEN

HBG023585.

InParanoid

Q9CWY8.

KO

K10743.

OMA

WRTAQTI.

OrthoDB

EOG4PNXHM.

Gene expression databases

ArrayExpress

Q9CWY8.

Bgee

Q9CWY8.

CleanEx

MM_RNASEH2A.

Genevestigator

Q9CWY8.

GermOnline

ENSMUSG00000052926. Mus musculus.

Family and domain databases

Gene3D

1.10.10.460. 1 hit.

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.
[Graphical view]

PANTHER

PTHR10954. PTHR10954. 1 hit.

Pfam

PF01351. RNase_HII. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

TIGRFAMs

TIGR00729. TIGR00729. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RNASEH2A. mouse.

EvolutionaryTrace

Q9CWY8.

NextBio

330190.

SOURCE

Search...

Entry information

Entry name

RNH2A_MOUSE

Accession

Primary (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 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program