RNH2B_HUMAN
ID RNH2B_HUMAN Reviewed; 312 AA.
AC Q5TBB1; G3XAJ1; Q05DR2; Q6PK48; Q9HAF7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ribonuclease H2 subunit B;
DE Short=RNase H2 subunit B;
DE AltName: Full=Aicardi-Goutieres syndrome 2 protein;
DE Short=AGS2;
DE AltName: Full=Deleted in lymphocytic leukemia 8;
DE AltName: Full=Ribonuclease HI subunit B;
GN Name=RNASEH2B; Synonyms=DLEU8;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Corcoran M.M.;
RT "DLEU8, a novel conserved gene located in the CLL 13q14 deletion locus.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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.M., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-308 (ISOFORM 1).
RC TISSUE=Skin;
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY MASS
RP 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 [8]
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., Buerckstuemmer 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-233, SUBUNIT, FUNCTION, AND
RP CHARACTERIZATION OF VARIANTS AGS2 LEU-73; SER-83; ARG-86 AND HIS-219.
RX PubMed=21177858; DOI=10.1074/jbc.m110.181974;
RA Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J., Nowotny M.;
RT "The structural and biochemical characterization of human RNase H2 complex
RT reveals the molecular basis for substrate recognition and Aicardi-Goutieres
RT syndrome defects.";
RL J. Biol. Chem. 286:10540-10550(2011).
RN [13]
RP VARIANTS AGS2 ARG-60; ARG-86; THR-162; ILE-163; THR-177; GLY-185 AND
RP HIS-219, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RNASEH2A AND
RP RNASEH2C.
RX PubMed=16845400; DOI=10.1038/ng1842;
RA Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E.,
RA Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P.,
RA Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E.,
RA Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H.,
RA Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y.,
RA Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A., Stephenson J.B.P.,
RA Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T., Weschke B., Woods C.G.,
RA Lebon P., Bonthron D.T., Ponting C.P., Jackson A.P.;
RT "Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-
RT Goutieres syndrome and mimic congenital viral brain infection.";
RL Nat. Genet. 38:910-916(2006).
RN [14]
RP VARIANTS AGS2 HIS-43; ARG-60; LEU-73; SER-83; ARG-86; PHE-138; ILE-159;
RP THR-162; ILE-163; THE-177; MET-183; GLY-185 AND HIS-219.
RX PubMed=17846997; DOI=10.1086/521373;
RA Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J.,
RA Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P., Benko W.S.,
RA Bergmann C., Bertini E., Biancheri R., Blair E.M., Blau N., Bonthron D.T.,
RA Briggs T., Brueton L.A., Brunner H.G., Burke C.J., Carr I.M.,
RA Carvalho D.R., Chandler K.E., Christen H.J., Corry P.C., Cowan F.M.,
RA Cox H., D'Arrigo S., Dean J., De Laet C., De Praeter C., Dery C.,
RA Ferrie C.D., Flintoff K., Frints S.G., Garcia-Cazorla A., Gener B.,
RA Goizet C., Goutieres F., Green A.J., Guet A., Hamel B.C., Hayward B.E.,
RA Heiberg A., Hennekam R.C., Husson M., Jackson A.P., Jayatunga R.,
RA Jiang Y.H., Kant S.G., Kao A., King M.D., Kingston H.M., Klepper J.,
RA van der Knaap M.S., Kornberg A.J., Kotzot D., Kratzer W., Lacombe D.,
RA Lagae L., Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H.,
RA Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D., McClure J.P.,
RA McWilliam R., Melancon S.B., Mewasingh L.D., Moutard M.L., Nischal K.K.,
RA Ostergaard J.R., Prendiville J., Rasmussen M., Rogers R.C., Roland D.,
RA Rosser E.M., Rostasy K., Roubertie A., Sanchis A., Schiffmann R.,
RA Scholl-Burgi S., Seal S., Shalev S.A., Corcoles C.S., Sinha G.P., Soler D.,
RA Spiegel R., Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L.,
RA Tomlin P., Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N.,
RA Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B., Whiteford M.L.,
RA Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S., Fazzi E., Lebon P.,
RA Crow Y.J.;
RT "Clinical and molecular phenotype of Aicardi-Goutieres syndrome.";
RL Am. J. Hum. Genet. 81:713-725(2007).
RN [15]
RP VARIANTS AGS2 THR-177 AND PRO-229.
RX PubMed=20131292; DOI=10.1002/art.27367;
RA Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K., Hunger S.,
RA Borozdin W., Mah J.K., Ungerath K., Walkenhorst H., Richardt H.H.,
RA Buckard J., Bevot A., Siegel C., von Stuelpnagel C., Ikonomidou C.,
RA Thomas K., Proud V., Niemann F., Wieczorek D., Haeusler M., Niggemann P.,
RA Baltaci V., Conrad K., Lebon P., Lee-Kirsch M.A.;
RT "Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-
RT Goutieres syndrome.";
RL Arthritis Rheum. 62:1469-1477(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:16845400, ECO:0000269|PubMed:21177858}.
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:21177858}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TBB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TBB1-2; Sequence=VSP_054039, VSP_054040;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16845400}.
CC -!- DISEASE: Aicardi-Goutieres syndrome 2 (AGS2) [MIM:610181]: A form of
CC Aicardi-Goutieres syndrome, a genetically heterogeneous disease
CC characterized by cerebral atrophy, leukoencephalopathy, intracranial
CC calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis,
CC increased CSF alpha-interferon, and negative serologic investigations
CC for common prenatal infection. Clinical features as thrombocytopenia,
CC hepatosplenomegaly and elevated hepatic transaminases along with
CC intermittent fever may erroneously suggest an infective process. Severe
CC neurological dysfunctions manifest in infancy as progressive
CC microcephaly, spasticity, dystonic posturing and profound psychomotor
CC retardation. Death often occurs in early childhood.
CC {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:17846997,
CC ECO:0000269|PubMed:20131292, ECO:0000269|PubMed:21177858}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01397.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH07332.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH10174.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY764036; AAX13343.1; -; mRNA.
DR EMBL; AK021774; BAB13892.1; -; mRNA.
DR EMBL; AK223340; BAD97060.1; -; mRNA.
DR EMBL; AL137881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08864.1; -; Genomic_DNA.
DR EMBL; BC001397; AAH01397.1; ALT_SEQ; mRNA.
DR EMBL; BC005088; AAH05088.1; -; mRNA.
DR EMBL; BC007332; AAH07332.1; ALT_SEQ; mRNA.
DR EMBL; BC010174; AAH10174.1; ALT_SEQ; mRNA.
DR CCDS; CCDS45047.1; -. [Q5TBB1-2]
DR CCDS; CCDS9425.1; -. [Q5TBB1-1]
DR RefSeq; NP_001135751.1; NM_001142279.2. [Q5TBB1-2]
DR RefSeq; NP_078846.2; NM_024570.3. [Q5TBB1-1]
DR PDB; 3P56; X-ray; 4.06 A; B/E=2-226.
DR PDB; 3P87; X-ray; 2.99 A; G/H/I/J/K/L=290-312.
DR PDB; 3PUF; X-ray; 3.10 A; B/E/H/K/N/Q=14-233.
DR PDBsum; 3P56; -.
DR PDBsum; 3P87; -.
DR PDBsum; 3PUF; -.
DR AlphaFoldDB; Q5TBB1; -.
DR SMR; Q5TBB1; -.
DR BioGRID; 122751; 48.
DR ComplexPortal; CPX-745; RNase H2 complex.
DR IntAct; Q5TBB1; 34.
DR MINT; Q5TBB1; -.
DR STRING; 9606.ENSP00000337623; -.
DR iPTMnet; Q5TBB1; -.
DR PhosphoSitePlus; Q5TBB1; -.
DR BioMuta; RNASEH2B; -.
DR DMDM; 74745929; -.
DR EPD; Q5TBB1; -.
DR jPOST; Q5TBB1; -.
DR MassIVE; Q5TBB1; -.
DR MaxQB; Q5TBB1; -.
DR PaxDb; Q5TBB1; -.
DR PeptideAtlas; Q5TBB1; -.
DR PRIDE; Q5TBB1; -.
DR ProteomicsDB; 33763; -.
DR ProteomicsDB; 64894; -. [Q5TBB1-1]
DR Antibodypedia; 42315; 204 antibodies from 21 providers.
DR DNASU; 79621; -.
DR Ensembl; ENST00000336617.8; ENSP00000337623.2; ENSG00000136104.21. [Q5TBB1-1]
DR Ensembl; ENST00000422660.6; ENSP00000389877.1; ENSG00000136104.21. [Q5TBB1-2]
DR GeneID; 79621; -.
DR KEGG; hsa:79621; -.
DR MANE-Select; ENST00000336617.8; ENSP00000337623.2; NM_024570.4; NP_078846.2.
DR UCSC; uc001vfa.4; human. [Q5TBB1-1]
DR CTD; 79621; -.
DR DisGeNET; 79621; -.
DR GeneCards; RNASEH2B; -.
DR GeneReviews; RNASEH2B; -.
DR HGNC; HGNC:25671; RNASEH2B.
DR HPA; ENSG00000136104; Tissue enhanced (lymphoid).
DR MalaCards; RNASEH2B; -.
DR MIM; 610181; phenotype.
DR MIM; 610326; gene.
DR neXtProt; NX_Q5TBB1; -.
DR OpenTargets; ENSG00000136104; -.
DR Orphanet; 51; Aicardi-Goutieres syndrome.
DR PharmGKB; PA162401418; -.
DR VEuPathDB; HostDB:ENSG00000136104; -.
DR eggNOG; KOG4705; Eukaryota.
DR GeneTree; ENSGT00390000011439; -.
DR HOGENOM; CLU_059802_0_0_1; -.
DR InParanoid; Q5TBB1; -.
DR OMA; MACDIVG; -.
DR PhylomeDB; Q5TBB1; -.
DR TreeFam; TF105250; -.
DR BioCyc; MetaCyc:HS13612-MON; -.
DR BRENDA; 3.1.26.4; 2681.
DR PathwayCommons; Q5TBB1; -.
DR SignaLink; Q5TBB1; -.
DR BioGRID-ORCS; 79621; 101 hits in 1082 CRISPR screens.
DR ChiTaRS; RNASEH2B; human.
DR EvolutionaryTrace; Q5TBB1; -.
DR GenomeRNAi; 79621; -.
DR Pharos; Q5TBB1; Tbio.
DR PRO; PR:Q5TBB1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5TBB1; protein.
DR Bgee; ENSG00000136104; Expressed in calcaneal tendon and 160 other tissues.
DR ExpressionAtlas; Q5TBB1; baseline and differential.
DR Genevisible; Q5TBB1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0009259; P:ribonucleotide metabolic process; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR CDD; cd09270; RNase_H2-B; 1.
DR IDEAL; IID00600; -.
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; Aicardi-Goutieres syndrome;
KW Alternative splicing; Disease variant; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..312
FT /note="Ribonuclease H2 subunit B"
FT /id="PRO_0000248378"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 248..257
FT /note="KIKLSDEPVE -> MAAQRQKRGK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054039"
FT VAR_SEQ 258..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054040"
FT VARIANT 43
FT /note="P -> H (in AGS2; dbSNP:rs79564863)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070611"
FT VARIANT 60
FT /note="L -> R (in AGS2; heterozygous compound with T-177;
FT dbSNP:rs75325951)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027280"
FT VARIANT 73
FT /note="W -> L (in AGS2; reduces stability of the RNase
FT complex; dbSNP:rs78071087)"
FT /evidence="ECO:0000269|PubMed:17846997,
FT ECO:0000269|PubMed:21177858"
FT /id="VAR_070612"
FT VARIANT 83
FT /note="G -> S (in AGS2; reduces stability of the RNase
FT complex; dbSNP:rs76158094)"
FT /evidence="ECO:0000269|PubMed:17846997,
FT ECO:0000269|PubMed:21177858"
FT /id="VAR_070613"
FT VARIANT 86
FT /note="H -> R (in AGS2; heterozygous compound with T-177;
FT reduces stability of the RNase complex; dbSNP:rs77931005)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997, ECO:0000269|PubMed:21177858"
FT /id="VAR_027281"
FT VARIANT 138
FT /note="L -> F (in AGS2; dbSNP:rs78705382)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070614"
FT VARIANT 159
FT /note="S -> I (in AGS2; dbSNP:rs76219783)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070615"
FT VARIANT 162
FT /note="K -> T (in AGS2; dbSNP:rs75971463)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027282"
FT VARIANT 163
FT /note="T -> I (in AGS2; heterozygous compound with T-177;
FT dbSNP:rs79310911)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027283"
FT VARIANT 177
FT /note="A -> T (in AGS2; frequent mutation;
FT dbSNP:rs75184679)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:20131292"
FT /id="VAR_027284"
FT VARIANT 183
FT /note="V -> M (in AGS2; dbSNP:rs77377571)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070616"
FT VARIANT 185
FT /note="V -> G (in AGS2; dbSNP:rs74555752)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027285"
FT VARIANT 219
FT /note="Y -> H (in AGS2; heterozygous compound with a
FT nonsense mutation; reduces stability of the RNase complex;
FT dbSNP:rs77391331)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997, ECO:0000269|PubMed:21177858"
FT /id="VAR_027286"
FT VARIANT 229
FT /note="S -> P (in AGS2; dbSNP:rs768565639)"
FT /evidence="ECO:0000269|PubMed:20131292"
FT /id="VAR_070617"
FT CONFLICT 61
FT /note="F -> L (in Ref. 1; AAX13343 and 2; BAB13892)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="N -> K (in Ref. 6; AAH05088)"
FT /evidence="ECO:0000305"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3PUF"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:3PUF"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:3PUF"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 160..181
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:3PUF"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3P87"
SQ SEQUENCE 312 AA; 35139 MW; 98B1A8E073A50D68 CRC64;
MAAGVDCGDG VGARQHVFLV SEYLKDASKK 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
