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Protein

Ribonuclease H2 subunit B

Gene

Rnaseh2b

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

Functioni

Non catalytic subunit of RNase H2, 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

GO - Molecular functioni

  • RNA-DNA hybrid ribonuclease activity Source: MGI

GO - Biological processi

  • in utero embryonic development Source: MGI
  • negative regulation of gene expression Source: MGI
  • positive regulation of fibroblast proliferation Source: MGI
  • regulation of DNA damage checkpoint Source: MGI
  • regulation of G2/M transition of mitotic cell cycle Source: MGI
  • ribonucleotide metabolic process Source: MGI
  • RNA catabolic process Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H2 subunit B
Short name:
RNase H2 subunit B
Alternative name(s):
Deleted in lymphocytic leukemia 8 homolog
Ribonuclease HI subunit B
Gene namesi
Name:Rnaseh2b
Synonyms:Dleu8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1914403. Rnaseh2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002483792 – 308Ribonuclease H2 subunit BAdd BLAST307

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei293PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ80ZV0.
MaxQBiQ80ZV0.
PaxDbiQ80ZV0.
PeptideAtlasiQ80ZV0.
PRIDEiQ80ZV0.

PTM databases

iPTMnetiQ80ZV0.
PhosphoSitePlusiQ80ZV0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021932.
CleanExiMM_RNASEH2B.
ExpressionAtlasiQ80ZV0. baseline and differential.
GenevisibleiQ80ZV0. 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.ENSMUSP00000022499.

Structurei

Secondary structure

1308
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 20Combined sources7
Helixi21 – 24Combined sources4
Beta strandi35 – 39Combined sources5
Turni43 – 46Combined sources4
Beta strandi50 – 57Combined sources8
Beta strandi61 – 66Combined sources6
Beta strandi72 – 81Combined sources10
Beta strandi85 – 94Combined sources10
Helixi95 – 97Combined sources3
Turni98 – 100Combined sources3
Turni101 – 104Combined sources4
Helixi125 – 129Combined sources5
Helixi134 – 138Combined sources5
Turni139 – 141Combined sources3
Helixi152 – 155Combined sources4
Helixi161 – 174Combined sources14
Turni175 – 179Combined sources5
Helixi205 – 214Combined sources10
Helixi218 – 220Combined sources3
Beta strandi221 – 226Combined sources6
Turni227 – 229Combined sources3
Helixi274 – 277Combined sources4
Turni278 – 280Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90B1-308[»]
3P5JX-ray2.90B1-308[»]
ProteinModelPortaliQ80ZV0.
SMRiQ80ZV0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80ZV0.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase H2 subunit B family.Curated

Phylogenomic databases

eggNOGiKOG4705. Eukaryota.
ENOG410YS7I. LUCA.
GeneTreeiENSGT00390000011439.
HOGENOMiHOG000006910.
HOVERGENiHBG056010.
InParanoidiQ80ZV0.
KOiK10744.
OMAiGARQHVF.
OrthoDBiEOG091G0M4Q.
PhylomeDBiQ80ZV0.
TreeFamiTF105250.

Family and domain databases

CDDicd09270. RNase_H2-B. 1 hit.
InterProiIPR019024. RNase_H2_suB.
[Graphical view]
PfamiPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80ZV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGRDRGDL AARQLVFLLP EHLKDASKKK KKSSLLFVKL ANPHSGEGAT
60 70 80 90 100
YLIDMCLQQL FEIKVFKEKH HSWFINQSVQ SGGLLHFATP MDPLFLLLHY
110 120 130 140 150
LLKAGKEGKY QPLDQVVVDD TFPDCTLLLR FPELEKSLRH VTEEKEVNSK
160 170 180 190 200
KYYKYSSEKT LKWLEKKVNQ TVVALKANNV NVGARVQSSA YFSGGQVSRD
210 220 230 240 250
KEEDYVRYAH GLISDYIPKE LSDDLSKFLK LPEPPASLTN PPSKKLKLSD
260 270 280 290 300
EPVEAKEDYT KFNTKDLKTG KKNSKMTAAQ KALAKVDKSG MKSIDAFFGA

KNKKTGKI
Length:308
Mass (Da):34,729
Last modified:September 5, 2006 - v2
Checksum:i937DC1BBBA4D6C6A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti239T → P in AAH47997 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011914 mRNA. Translation: BAB27913.1.
AK082752 mRNA. Translation: BAC38602.1.
BC047997 mRNA. Translation: AAH47997.1.
CCDSiCCDS27189.1.
RefSeqiNP_080277.1. NM_026001.2.
UniGeneiMm.26040.

Genome annotation databases

EnsembliENSMUST00000022499; ENSMUSP00000022499; ENSMUSG00000021932.
GeneIDi67153.
KEGGimmu:67153.
UCSCiuc007ugl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011914 mRNA. Translation: BAB27913.1.
AK082752 mRNA. Translation: BAC38602.1.
BC047997 mRNA. Translation: AAH47997.1.
CCDSiCCDS27189.1.
RefSeqiNP_080277.1. NM_026001.2.
UniGeneiMm.26040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90B1-308[»]
3P5JX-ray2.90B1-308[»]
ProteinModelPortaliQ80ZV0.
SMRiQ80ZV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022499.

PTM databases

iPTMnetiQ80ZV0.
PhosphoSitePlusiQ80ZV0.

Proteomic databases

EPDiQ80ZV0.
MaxQBiQ80ZV0.
PaxDbiQ80ZV0.
PeptideAtlasiQ80ZV0.
PRIDEiQ80ZV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022499; ENSMUSP00000022499; ENSMUSG00000021932.
GeneIDi67153.
KEGGimmu:67153.
UCSCiuc007ugl.1. mouse.

Organism-specific databases

CTDi79621.
MGIiMGI:1914403. Rnaseh2b.

Phylogenomic databases

eggNOGiKOG4705. Eukaryota.
ENOG410YS7I. LUCA.
GeneTreeiENSGT00390000011439.
HOGENOMiHOG000006910.
HOVERGENiHBG056010.
InParanoidiQ80ZV0.
KOiK10744.
OMAiGARQHVF.
OrthoDBiEOG091G0M4Q.
PhylomeDBiQ80ZV0.
TreeFamiTF105250.

Miscellaneous databases

EvolutionaryTraceiQ80ZV0.
PROiQ80ZV0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021932.
CleanExiMM_RNASEH2B.
ExpressionAtlasiQ80ZV0. baseline and differential.
GenevisibleiQ80ZV0. MM.

Family and domain databases

CDDicd09270. RNase_H2-B. 1 hit.
InterProiIPR019024. RNase_H2_suB.
[Graphical view]
PfamiPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNH2B_MOUSE
AccessioniPrimary (citable) accession number: Q80ZV0
Secondary accession number(s): Q9D014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 87 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.