ID A0A087WXR7_HUMAN Unreviewed; 282 AA.
AC A0A087WXR7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN Name=RNASEH2B {ECO:0000313|Ensembl:ENSP00000481236.3};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000481236.3, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000481236.3, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2] {ECO:0007829|PubMed:19608861}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [3] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5] {ECO:0000313|Ensembl:ENSP00000481236.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024778}.
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:0000256|ARBA:ARBA00011277}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit B family.
CC {ECO:0000256|ARBA:ARBA00009823}.
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DR EMBL; AL137881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Antibodypedia; 42315; 216 antibodies from 21 providers.
DR Ensembl; ENST00000611510.5; ENSP00000481236.3; ENSG00000136104.21.
DR Ensembl; ENST00000646709.1; ENSP00000495278.1; ENSG00000136104.21.
DR UCSC; uc058xcx.1; human.
DR HGNC; HGNC:25671; RNASEH2B.
DR VEuPathDB; HostDB:ENSG00000136104; -.
DR GeneTree; ENSGT00390000011439; -.
DR ChiTaRS; RNASEH2B; human.
DR Proteomes; UP000005640; Chromosome 13.
DR Bgee; ENSG00000136104; Expressed in calcaneal tendon and 162 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032299; C:ribonuclease H2 complex; IEA:InterPro.
DR CDD; cd09270; RNase_H2-B; 1.
DR Gene3D; 1.10.20.120; -; 1.
DR Gene3D; 2.20.25.530; -; 1.
DR InterPro; IPR040456; RNase_H2_suB.
DR InterPro; IPR019024; RNase_H2_suB_wHTH.
DR InterPro; IPR041195; Rnh202_N.
DR PANTHER; PTHR13383; RIBONUCLEASE H2 SUBUNIT B; 1.
DR PANTHER; PTHR13383:SF11; RIBONUCLEASE H2 SUBUNIT B; 1.
DR Pfam; PF09468; RNase_H2-Ydr279; 1.
DR Pfam; PF17745; Ydr279_N; 1.
PE 1: Evidence at protein level;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:A0A087WXR7,
KW ECO:0007829|MaxQB:A0A087WXR7};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 5..62
FT /note="Rnh202 triple barrel"
FT /evidence="ECO:0000259|Pfam:PF17745"
FT DOMAIN 65..198
FT /note="Ribonuclease H2 subunit B wHTH"
FT /evidence="ECO:0000259|Pfam:PF09468"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 32004 MW; 0515B473EB48F6EA CRC64;
MKNGLMFVKL VNPCSGEGAI YLFNMCLQQL FEVKVFKEKH HSWFINQSVQ SGGLLHFATP
VDPLFLLLHY LIKADKEGKF QPLDQVVVDN VFPNCILLLK LPGLEKLLHH VTEEKGNPEI
DNKKYYKYSK EKTLKWLEKK VNQTVAALKT NNVNVSSRVQ STAFFSGDQA STDKEEDYIR
YAHGLISDYI PKELSDDLSK YLKLPEPSAS LPNPPSKKIK LSDEPVEAKE DYTKFNTKDL
KTEKKNSKMT AAQKALAKVD KSGMKSIDTF FGVKNKKKIG KV
//
