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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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 308307Ribonuclease H2 subunit BPRO_0000248379Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei292 – 2921N6-acetyllysineBy similarity
Modified residuei293 – 2931PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ80ZV0.
MaxQBiQ80ZV0.
PaxDbiQ80ZV0.
PeptideAtlasiQ80ZV0.
PRIDEiQ80ZV0.

PTM databases

iPTMnetiQ80ZV0.
PhosphoSiteiQ80ZV0.

Expressioni

Gene expression databases

BgeeiQ80ZV0.
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

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207Combined sources
Helixi21 – 244Combined sources
Beta strandi35 – 395Combined sources
Turni43 – 464Combined sources
Beta strandi50 – 578Combined sources
Beta strandi61 – 666Combined sources
Beta strandi72 – 8110Combined sources
Beta strandi85 – 9410Combined sources
Helixi95 – 973Combined sources
Turni98 – 1003Combined sources
Turni101 – 1044Combined sources
Helixi125 – 1295Combined sources
Helixi134 – 1385Combined sources
Turni139 – 1413Combined sources
Helixi152 – 1554Combined sources
Helixi161 – 17414Combined sources
Turni175 – 1795Combined sources
Helixi205 – 21410Combined sources
Helixi218 – 2203Combined sources
Beta strandi221 – 2266Combined sources
Turni227 – 2293Combined sources
Helixi274 – 2774Combined sources
Turni278 – 2803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90B1-308[»]
3P5JX-ray2.90B1-308[»]
ProteinModelPortaliQ80ZV0.
SMRiQ80ZV0. Positions 11-231.
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.
OMAiRMACDIV.
PhylomeDBiQ80ZV0.
TreeFamiTF105250.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391T → P in AAH47997 (PubMed:15489334).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90B1-308[»]
3P5JX-ray2.90B1-308[»]
ProteinModelPortaliQ80ZV0.
SMRiQ80ZV0. Positions 11-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022499.

PTM databases

iPTMnetiQ80ZV0.
PhosphoSiteiQ80ZV0.

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.
OMAiRMACDIV.
PhylomeDBiQ80ZV0.
TreeFamiTF105250.

Miscellaneous databases

EvolutionaryTraceiQ80ZV0.
PROiQ80ZV0.
SOURCEiSearch...

Gene expression databases

BgeeiQ80ZV0.
CleanExiMM_RNASEH2B.
ExpressionAtlasiQ80ZV0. baseline and differential.
GenevisibleiQ80ZV0. MM.

Family and domain databases

InterProiIPR019024. RNase_H2_suB.
[Graphical view]
PfamiPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]
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.
  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].
    Tissue: Limb.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  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, SUBUNIT.

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: July 6, 2016
This is version 85 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.