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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)DescriptionActionsGraphical viewLength
Metal bindingi34Divalent metal cationCurated1
Metal bindingi35Divalent metal cationCurated1
Metal bindingi142Divalent metal cationCurated1

GO - Molecular functioni

GO - Biological processi

  • DNA replication, removal of RNA primer Source: GO_Central
  • mismatch repair Source: MGI
  • RNA catabolic process Source: UniProtKB
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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
Mutagenesisi34D → N: Loss of enzyme activity. 1 Publication1
Mutagenesisi35E → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi37G → S: Strongly reduced in vitro enzyme activity. 1 Publication1
Mutagenesisi142D → N: Loss of enzyme activity. 1 Publication1
Mutagenesisi170D → N: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001117111 – 301Ribonuclease H2 subunit AAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei217PhosphothreonineBy similarity1
Modified residuei258PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CWY8.
MaxQBiQ9CWY8.
PaxDbiQ9CWY8.
PeptideAtlasiQ9CWY8.
PRIDEiQ9CWY8.

PTM databases

iPTMnetiQ9CWY8.
PhosphoSitePlusiQ9CWY8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000052926.
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

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Helixi7 – 9Combined sources3
Beta strandi11 – 17Combined sources7
Helixi23 – 26Combined sources4
Beta strandi29 – 36Combined sources8
Beta strandi41 – 43Combined sources3
Beta strandi45 – 53Combined sources9
Helixi54 – 59Combined sources6
Helixi60 – 64Combined sources5
Helixi73 – 85Combined sources13
Turni86 – 89Combined sources4
Beta strandi91 – 97Combined sources7
Helixi99 – 106Combined sources8
Beta strandi108 – 110Combined sources3
Helixi114 – 131Combined sources18
Beta strandi136 – 142Combined sources7
Helixi148 – 156Combined sources9
Beta strandi161 – 166Combined sources6
Helixi169 – 171Combined sources3
Helixi174 – 200Combined sources27
Beta strandi209 – 211Combined sources3
Helixi215 – 222Combined sources8
Turni227 – 229Combined sources3
Helixi240 – 249Combined sources10
Beta strandi253 – 255Combined sources3
Helixi287 – 293Combined sources7
Beta strandi295 – 297Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9CWY8.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase HII family. Eukaryotic subfamily.Curated

Phylogenomic databases

eggNOGiKOG2299. Eukaryota.
COG0164. LUCA.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiQ9CWY8.
KOiK10743.
OMAiREECRFF.
OrthoDBiEOG091G0E06.
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)DescriptionActionsGraphical viewLength
Sequence conflicti132Q → R in BAB26828 (PubMed:16141072).Curated1

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.
XP_011246799.1. XM_011248497.2.
XP_011246800.1. XM_011248498.2.
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.
XP_011246799.1. XM_011248497.2.
XP_011246800.1. XM_011248498.2.
UniGeneiMm.182470.

3D structure databases

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000105358.

PTM databases

iPTMnetiQ9CWY8.
PhosphoSitePlusiQ9CWY8.

Proteomic databases

EPDiQ9CWY8.
MaxQBiQ9CWY8.
PaxDbiQ9CWY8.
PeptideAtlasiQ9CWY8.
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

eggNOGiKOG2299. Eukaryota.
COG0164. LUCA.
GeneTreeiENSGT00390000010768.
HOGENOMiHOG000100290.
HOVERGENiHBG023585.
InParanoidiQ9CWY8.
KOiK10743.
OMAiREECRFF.
OrthoDBiEOG091G0E06.
PhylomeDBiQ9CWY8.
TreeFamiTF314302.

Enzyme and pathway databases

BRENDAi3.1.26.4. 3474.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000052926.
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...

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: November 2, 2016
This is version 125 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

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 one 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.