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Q9CWY8

- RNH2A_MOUSE

UniProt

Q9CWY8 - RNH2A_MOUSE

Protein

Ribonuclease H2 subunit A

Gene

Rnaseh2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (10 Jan 2006)
      Previous versions | rss
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    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

    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.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

    1. metal ion binding Source: UniProtKB-KW
    2. RNA binding Source: InterPro
    3. RNA-DNA hybrid ribonuclease activity Source: UniProtKB

    GO - Biological processi

    1. mismatch repair Source: MGI
    2. RNA catabolic process Source: UniProtKB
    3. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    Metal-binding

    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: Chromosome 8

    Organism-specific databases

    MGIiMGI:1916974. Rnaseh2a.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. ribonuclease H2 complex Source: UniProtKB

    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

    ArrayExpressiQ9CWY8.
    BgeeiQ9CWY8.
    CleanExiMM_RNASEH2A.
    GenevestigatoriQ9CWY8.

    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

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiGPPEKYQ.
    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

    MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC    50
    YCPLSRLADL EALKVADSKT LTENERERLF AKMEEDGDFV GWALDVLSPN 100
    LISTSMLGRV KYNLNSLSHD TAAGLIQYAL DQNVNVTQVF VDTVGMPETY 150
    QARLQQHFPG IEVTVKAKAD SLFPVVSAAS IFAKVARDKA VKNWQFVENL 200
    QDLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS TAQAILEKEA 250
    EDVIWEDSEA EEDPERPGKI TSYFSQGPQT CRPQAPHRYF QERGLEAASS 300
    L 301
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010292 mRNA. Translation: BAB26828.1 .
    AK146518 mRNA. Translation: BAE27230.1 .
    BC038158 mRNA. Translation: AAH38158.1 .
    CCDSi CCDS22486.1.
    RefSeqi NP_081463.1. NM_027187.3.
    UniGenei Mm.182470.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KIO X-ray 2.90 A 1-301 [» ]
    3P5J X-ray 2.90 A 1-301 [» ]
    ProteinModelPortali Q9CWY8.
    SMRi Q9CWY8. Positions 1-301.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9CWY8.

    Proteomic databases

    MaxQBi Q9CWY8.
    PaxDbi Q9CWY8.
    PRIDEi Q9CWY8.

    Protocols and materials databases

    DNASUi 69724.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000109736 ; ENSMUSP00000105358 ; ENSMUSG00000052926 .
    ENSMUST00000109738 ; ENSMUSP00000105360 ; ENSMUSG00000052926 .
    ENSMUST00000147812 ; ENSMUSP00000120374 ; ENSMUSG00000052926 .
    GeneIDi 69724.
    KEGGi mmu:69724.
    UCSCi uc009mok.1. mouse.

    Organism-specific databases

    CTDi 10535.
    MGIi MGI:1916974. Rnaseh2a.

    Phylogenomic databases

    eggNOGi COG0164.
    GeneTreei ENSGT00390000010768.
    HOGENOMi HOG000100290.
    HOVERGENi HBG023585.
    InParanoidi Q9CWY8.
    KOi K10743.
    OMAi GPPEKYQ.
    OrthoDBi EOG7KM5T4.
    PhylomeDBi Q9CWY8.
    TreeFami TF314302.

    Miscellaneous databases

    ChiTaRSi RNASEH2A. mouse.
    EvolutionaryTracei Q9CWY8.
    NextBioi 330190.
    PROi Q9CWY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CWY8.
    Bgeei Q9CWY8.
    CleanExi MM_RNASEH2A.
    Genevestigatori Q9CWY8.

    Family and domain databases

    Gene3Di 1.10.10.460. 1 hit.
    3.30.420.10. 1 hit.
    InterProi 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 ]
    PANTHERi PTHR10954. PTHR10954. 1 hit.
    Pfami PF01351. RNase_HII. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    TIGRFAMsi TIGR00729. TIGR00729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 105 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