RNH2B_MOUSE
ID RNH2B_MOUSE Reviewed; 308 AA.
AC Q80ZV0; Q9D014;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ribonuclease H2 subunit B;
DE Short=RNase H2 subunit B;
DE AltName: Full=Deleted in lymphocytic leukemia 8 homolog;
DE AltName: Full=Ribonuclease HI subunit B;
GN Name=Rnaseh2b; Synonyms=Dleu8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=19923215; DOI=10.1074/jbc.m109.059048;
RA Shaban N.M., Harvey S., Perrino F.W., Hollis T.;
RT "The structure of the mammalian RNase H2 complex provides insight into
RT RNA.NA hybrid processing to prevent immune dysfunction.";
RL J. Biol. Chem. 285:3617-3624(2010).
CC -!- FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that
CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC replication, possibly by mediating the removal of lagging-strand
CC Okazaki fragment RNA primers during DNA replication. Mediates the
CC excision of single ribonucleotides from DNA:RNA duplexes.
CC {ECO:0000269|PubMed:19923215}.
CC -!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
CC catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and
CC RNASEH2C. {ECO:0000269|PubMed:19923215}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK011914; BAB27913.1; -; mRNA.
DR EMBL; AK082752; BAC38602.1; -; mRNA.
DR EMBL; BC047997; AAH47997.1; -; mRNA.
DR CCDS; CCDS27189.1; -.
DR RefSeq; NP_080277.1; NM_026001.2.
DR PDB; 3KIO; X-ray; 2.90 A; B=1-308.
DR PDB; 3P5J; X-ray; 2.90 A; B=1-308.
DR PDBsum; 3KIO; -.
DR PDBsum; 3P5J; -.
DR AlphaFoldDB; Q80ZV0; -.
DR SMR; Q80ZV0; -.
DR BioGRID; 211980; 4.
DR ComplexPortal; CPX-2875; RNase H2 complex.
DR STRING; 10090.ENSMUSP00000022499; -.
DR iPTMnet; Q80ZV0; -.
DR PhosphoSitePlus; Q80ZV0; -.
DR EPD; Q80ZV0; -.
DR MaxQB; Q80ZV0; -.
DR PaxDb; Q80ZV0; -.
DR PeptideAtlas; Q80ZV0; -.
DR PRIDE; Q80ZV0; -.
DR ProteomicsDB; 300430; -.
DR Antibodypedia; 42315; 204 antibodies from 21 providers.
DR Ensembl; ENSMUST00000022499; ENSMUSP00000022499; ENSMUSG00000021932.
DR GeneID; 67153; -.
DR KEGG; mmu:67153; -.
DR UCSC; uc007ugl.1; mouse.
DR CTD; 79621; -.
DR MGI; MGI:1914403; Rnaseh2b.
DR VEuPathDB; HostDB:ENSMUSG00000021932; -.
DR eggNOG; KOG4705; Eukaryota.
DR GeneTree; ENSGT00390000011439; -.
DR HOGENOM; CLU_059802_0_0_1; -.
DR InParanoid; Q80ZV0; -.
DR OMA; MACDIVG; -.
DR OrthoDB; 1092212at2759; -.
DR PhylomeDB; Q80ZV0; -.
DR TreeFam; TF105250; -.
DR BioGRID-ORCS; 67153; 20 hits in 75 CRISPR screens.
DR EvolutionaryTrace; Q80ZV0; -.
DR PRO; PR:Q80ZV0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80ZV0; protein.
DR Bgee; ENSMUSG00000021932; Expressed in undifferentiated genital tubercle and 244 other tissues.
DR ExpressionAtlas; Q80ZV0; baseline and differential.
DR Genevisible; Q80ZV0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0009259; P:ribonucleotide metabolic process; IMP:MGI.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR CDD; cd09270; RNase_H2-B; 1.
DR DisProt; DP01594; -.
DR InterPro; IPR040456; RNase_H2_suB.
DR InterPro; IPR019024; RNase_H2_suB_wHTH.
DR InterPro; IPR041195; Rnh202_N.
DR PANTHER; PTHR13383; PTHR13383; 1.
DR Pfam; PF09468; RNase_H2-Ydr279; 1.
DR Pfam; PF17745; Ydr279_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5TBB1"
FT CHAIN 2..308
FT /note="Ribonuclease H2 subunit B"
FT /id="PRO_0000248379"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5TBB1"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5TBB1"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TBB1"
FT CONFLICT 239
FT /note="T -> P (in Ref. 2; AAH47997)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:3KIO"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:3P5J"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:3KIO"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3P5J"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3P5J"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3P5J"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:3KIO"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3KIO"
SQ SEQUENCE 308 AA; 34729 MW; 937DC1BBBA4D6C6A CRC64;
MAGGRDRGDL AARQLVFLLP EHLKDASKKK KKSSLLFVKL ANPHSGEGAT YLIDMCLQQL
FEIKVFKEKH HSWFINQSVQ SGGLLHFATP MDPLFLLLHY LLKAGKEGKY QPLDQVVVDD
TFPDCTLLLR FPELEKSLRH VTEEKEVNSK KYYKYSSEKT LKWLEKKVNQ TVVALKANNV
NVGARVQSSA YFSGGQVSRD KEEDYVRYAH GLISDYIPKE LSDDLSKFLK LPEPPASLTN
PPSKKLKLSD EPVEAKEDYT KFNTKDLKTG KKNSKMTAAQ KALAKVDKSG MKSIDAFFGA
KNKKTGKI
