Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease H2 subunit A

Gene

Rnaseh2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.1 Publication

Cofactori

Mn2+By similarity, Mg2+By similarityNote: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Divalent metal cationCurated
Metal bindingi35 – 351Divalent metal cationCurated
Metal bindingi142 – 1421Divalent metal cationCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi3.1.26.4. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H2 subunit A (EC:3.1.26.4)
Short name:
RNase H2 subunit A
Alternative name(s):
Ribonuclease HI large subunit
Short name:
RNase HI large subunit
Ribonuclease HI subunit A
Gene namesi
Name:Rnaseh2a
Synonyms:Rnasehi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1916974. Rnaseh2a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341D → N: Loss of enzyme activity. 1 Publication
Mutagenesisi35 – 351E → A: Loss of enzyme activity. 1 Publication
Mutagenesisi37 – 371G → S: Strongly reduced in vitro enzyme activity. 1 Publication
Mutagenesisi142 – 1421D → N: Loss of enzyme activity. 1 Publication
Mutagenesisi170 – 1701D → N: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Ribonuclease H2 subunit APRO_0000111711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei217 – 2171PhosphothreonineBy similarity
Modified residuei258 – 2581Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CWY8.
PaxDbiQ9CWY8.
PRIDEiQ9CWY8.

PTM databases

PhosphoSiteiQ9CWY8.

Expressioni

Gene expression databases

BgeeiQ9CWY8.
CleanExiMM_RNASEH2A.
ExpressionAtlasiQ9CWY8. baseline and differential.
GenevisibleiQ9CWY8. MM.

Interactioni

Subunit structurei

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105358.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Helixi7 – 93Combined sources
Beta strandi11 – 177Combined sources
Helixi23 – 264Combined sources
Beta strandi29 – 368Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 539Combined sources
Helixi54 – 596Combined sources
Helixi60 – 645Combined sources
Helixi73 – 8513Combined sources
Turni86 – 894Combined sources
Beta strandi91 – 977Combined sources
Helixi99 – 1068Combined sources
Beta strandi108 – 1103Combined sources
Helixi114 – 13118Combined sources
Beta strandi136 – 1427Combined sources
Helixi148 – 1569Combined sources
Beta strandi161 – 1666Combined sources
Helixi169 – 1713Combined sources
Helixi174 – 20027Combined sources
Beta strandi209 – 2113Combined sources
Helixi215 – 2228Combined sources
Turni227 – 2293Combined sources
Helixi240 – 24910Combined sources
Beta strandi253 – 2553Combined sources
Helixi287 – 2937Combined sources
Beta strandi295 – 2973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90A1-301[»]
3P5JX-ray2.90A1-301[»]
ProteinModelPortaliQ9CWY8.
SMRiQ9CWY8. Positions 1-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CWY8.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase HII family. Eukaryotic subfamily.Curated

Phylogenomic databases

eggNOGiCOG0164.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiQ9CWY8.
KOiK10743.
OMAiVCAFAIE.
OrthoDBiEOG7KM5T4.
PhylomeDBiQ9CWY8.
TreeFamiTF314302.

Family and domain databases

Gene3Di1.10.10.460. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR004649. 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]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00729. TIGR00729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CWY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC
60 70 80 90 100
YCPLSRLADL EALKVADSKT LTENERERLF AKMEEDGDFV GWALDVLSPN
110 120 130 140 150
LISTSMLGRV KYNLNSLSHD TAAGLIQYAL DQNVNVTQVF VDTVGMPETY
160 170 180 190 200
QARLQQHFPG IEVTVKAKAD SLFPVVSAAS IFAKVARDKA VKNWQFVENL
210 220 230 240 250
QDLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS TAQAILEKEA
260 270 280 290 300
EDVIWEDSEA EEDPERPGKI TSYFSQGPQT CRPQAPHRYF QERGLEAASS

L
Length:301
Mass (Da):33,513
Last modified:January 10, 2006 - v2
Checksum:i3B95211289847CBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321Q → R in BAB26828 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010292 mRNA. Translation: BAB26828.1.
AK146518 mRNA. Translation: BAE27230.1.
BC038158 mRNA. Translation: AAH38158.1.
CCDSiCCDS22486.1.
RefSeqiNP_081463.1. NM_027187.3.
UniGeneiMm.182470.

Genome annotation databases

EnsembliENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.
GeneIDi69724.
KEGGimmu:69724.
UCSCiuc009mok.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010292 mRNA. Translation: BAB26828.1.
AK146518 mRNA. Translation: BAE27230.1.
BC038158 mRNA. Translation: AAH38158.1.
CCDSiCCDS22486.1.
RefSeqiNP_081463.1. NM_027187.3.
UniGeneiMm.182470.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90A1-301[»]
3P5JX-ray2.90A1-301[»]
ProteinModelPortaliQ9CWY8.
SMRiQ9CWY8. Positions 1-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105358.

PTM databases

PhosphoSiteiQ9CWY8.

Proteomic databases

MaxQBiQ9CWY8.
PaxDbiQ9CWY8.
PRIDEiQ9CWY8.

Protocols and materials databases

DNASUi69724.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.
GeneIDi69724.
KEGGimmu:69724.
UCSCiuc009mok.1. mouse.

Organism-specific databases

CTDi10535.
MGIiMGI:1916974. Rnaseh2a.

Phylogenomic databases

eggNOGiCOG0164.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiQ9CWY8.
KOiK10743.
OMAiVCAFAIE.
OrthoDBiEOG7KM5T4.
PhylomeDBiQ9CWY8.
TreeFamiTF314302.

Enzyme and pathway databases

BRENDAi3.1.26.4. 3474.

Miscellaneous databases

ChiTaRSiRnaseh2a. mouse.
EvolutionaryTraceiQ9CWY8.
NextBioi330190.
PROiQ9CWY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CWY8.
CleanExiMM_RNASEH2A.
ExpressionAtlasiQ9CWY8. baseline and differential.
GenevisibleiQ9CWY8. MM.

Family and domain databases

Gene3Di1.10.10.460. 1 hit.
3.30.420.10. 1 hit.
InterProiIPR004649. 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]
PANTHERiPTHR10954. PTHR10954. 1 hit.
PfamiPF01351. RNase_HII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00729. TIGR00729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiRNH2A_MOUSE
AccessioniPrimary (citable) accession number: Q9CWY8
Secondary accession number(s): Q8CHY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 10, 2006
Last modified: June 24, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.