RNH2A_HUMAN
ID RNH2A_HUMAN Reviewed; 299 AA.
AC O75792; B2RCY1; Q96F11;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ribonuclease H2 subunit A;
DE Short=RNase H2 subunit A;
DE EC=3.1.26.4;
DE AltName: Full=Aicardi-Goutieres syndrome 4 protein;
DE Short=AGS4;
DE AltName: Full=RNase H(35);
DE AltName: Full=Ribonuclease HI large subunit;
DE Short=RNase HI large subunit;
DE AltName: Full=Ribonuclease HI subunit A;
GN Name=RNASEH2A; Synonyms=RNASEHI, RNHIA;
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].
RX PubMed=9789007; DOI=10.1073/pnas.95.22.12872;
RA Frank P., Braunshofer-Reiter C., Wintersberger U., Grimm R., Buesen W.;
RT "Cloning of the cDNA encoding the large subunit of human RNase HI, a
RT homologue of the prokaryotic RNase HII.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12872-12877(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND THR-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-67; LYS-69; ASN-112; TYR-210 AND
RP THR-240.
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 [11]
RP VARIANT AGS4 SER-37, CHARACTERIZATION OF VARIANT AGS4 SER-37, FUNCTION, AND
RP INTERACTION WITH RNASEH2B AND 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 [12]
RP VARIANTS AGS4 SER-37; TRP-108; TRP-186; LEU-230; GLN-235; MET-240 AND
RP HIS-291, AND VARIANTS ASP-99; SER-202; GLU-205 AND GLY-260.
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 [13]
RP VARIANTS AGS4 2-TYR-PRO-3 AND TRP-186.
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: Catalytic subunit of RNase HII, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000269|PubMed:21177858};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000250};
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 -!- DISEASE: Aicardi-Goutieres syndrome 4 (AGS4) [MIM:610333]: 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}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000305}.
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DR EMBL; Z97029; CAB09725.1; -; mRNA.
DR EMBL; AK315327; BAG37728.1; -; mRNA.
DR EMBL; CH471106; EAW84313.1; -; Genomic_DNA.
DR EMBL; BC011748; AAH11748.1; -; mRNA.
DR CCDS; CCDS12282.1; -.
DR RefSeq; NP_006388.2; NM_006397.2.
DR PDB; 3P56; X-ray; 4.06 A; A/D=1-299.
DR PDB; 3PUF; X-ray; 3.10 A; A/D/G/J/M/P=1-299.
DR PDBsum; 3P56; -.
DR PDBsum; 3PUF; -.
DR AlphaFoldDB; O75792; -.
DR SMR; O75792; -.
DR BioGRID; 115789; 63.
DR ComplexPortal; CPX-745; RNase H2 complex.
DR IntAct; O75792; 38.
DR MINT; O75792; -.
DR STRING; 9606.ENSP00000221486; -.
DR GlyGen; O75792; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75792; -.
DR PhosphoSitePlus; O75792; -.
DR BioMuta; RNASEH2A; -.
DR EPD; O75792; -.
DR jPOST; O75792; -.
DR MassIVE; O75792; -.
DR MaxQB; O75792; -.
DR PaxDb; O75792; -.
DR PeptideAtlas; O75792; -.
DR PRIDE; O75792; -.
DR ProteomicsDB; 50197; -.
DR Antibodypedia; 13379; 185 antibodies from 28 providers.
DR CPTC; O75792; 1 antibody.
DR DNASU; 10535; -.
DR Ensembl; ENST00000221486.6; ENSP00000221486.4; ENSG00000104889.7.
DR GeneID; 10535; -.
DR KEGG; hsa:10535; -.
DR MANE-Select; ENST00000221486.6; ENSP00000221486.4; NM_006397.3; NP_006388.2.
DR UCSC; uc002mvg.2; human.
DR CTD; 10535; -.
DR DisGeNET; 10535; -.
DR GeneCards; RNASEH2A; -.
DR GeneReviews; RNASEH2A; -.
DR HGNC; HGNC:18518; RNASEH2A.
DR HPA; ENSG00000104889; Low tissue specificity.
DR MalaCards; RNASEH2A; -.
DR MIM; 606034; gene.
DR MIM; 610333; phenotype.
DR neXtProt; NX_O75792; -.
DR OpenTargets; ENSG00000104889; -.
DR Orphanet; 51; Aicardi-Goutieres syndrome.
DR PharmGKB; PA38565; -.
DR VEuPathDB; HostDB:ENSG00000104889; -.
DR eggNOG; KOG2299; Eukaryota.
DR GeneTree; ENSGT00390000010768; -.
DR HOGENOM; CLU_036532_0_3_1; -.
DR InParanoid; O75792; -.
DR OMA; REECRFF; -.
DR OrthoDB; 1354466at2759; -.
DR PhylomeDB; O75792; -.
DR TreeFam; TF314302; -.
DR BioCyc; MetaCyc:HS02645-MON; -.
DR BRENDA; 3.1.26.4; 2681.
DR PathwayCommons; O75792; -.
DR SignaLink; O75792; -.
DR BioGRID-ORCS; 10535; 229 hits in 1086 CRISPR screens.
DR ChiTaRS; RNASEH2A; human.
DR EvolutionaryTrace; O75792; -.
DR GeneWiki; RNASEH2A; -.
DR GenomeRNAi; 10535; -.
DR Pharos; O75792; Tbio.
DR PRO; PR:O75792; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75792; protein.
DR Bgee; ENSG00000104889; Expressed in ganglionic eminence and 99 other tissues.
DR ExpressionAtlas; O75792; baseline and differential.
DR Genevisible; O75792; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IDA:MGI.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.10.460; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR IDEAL; IID00601; -.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00729; TIGR00729; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aicardi-Goutieres syndrome; Disease variant;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..299
FT /note="Ribonuclease H2 subunit A"
FT /id="PRO_0000111710"
FT DOMAIN 28..250
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWY8"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 2..3
FT /note="DL -> YP (in AGS4)"
FT /id="VAR_070623"
FT VARIANT 37
FT /note="G -> S (in AGS4; strongly impairs enzyme activity
FT but not interaction with RNASEH2B and RNASEH2C;
FT dbSNP:rs76857106)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027377"
FT VARIANT 99
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070624"
FT VARIANT 108
FT /note="R -> W (in AGS4; dbSNP:rs76436818)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070625"
FT VARIANT 186
FT /note="R -> W (in AGS4; dbSNP:rs77103971)"
FT /evidence="ECO:0000269|PubMed:17846997,
FT ECO:0000269|PubMed:20131292"
FT /id="VAR_070626"
FT VARIANT 202
FT /note="L -> S (in dbSNP:rs7247284)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_024617"
FT VARIANT 205
FT /note="D -> E (in dbSNP:rs62619782)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070627"
FT VARIANT 230
FT /note="F -> L (in AGS4; dbSNP:rs79767407)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070628"
FT VARIANT 235
FT /note="R -> Q (in AGS4; dbSNP:rs75718910)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070629"
FT VARIANT 240
FT /note="T -> M (in AGS4; dbSNP:rs79843600)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070630"
FT VARIANT 258
FT /note="A -> G (in dbSNP:rs15389)"
FT /id="VAR_027378"
FT VARIANT 260
FT /note="E -> G (in dbSNP:rs770898096)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070631"
FT VARIANT 291
FT /note="R -> H (in AGS4; dbSNP:rs75037667)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070632"
FT MUTAGEN 67
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT MUTAGEN 69
FT /note="K->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT MUTAGEN 112
FT /note="N->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT MUTAGEN 210
FT /note="Y->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT MUTAGEN 210
FT /note="Y->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT MUTAGEN 240
FT /note="T->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21177858"
FT CONFLICT 152
FT /note="R -> Q (in Ref. 1; CAB09725)"
FT /evidence="ECO:0000305"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3PUF"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3PUF"
SQ SEQUENCE 299 AA; 33395 MW; 34992FE85130157B CRC64;
MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC YCPLPRLADL
EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL ISTSMLGRVK YNLNSLSHDT
ATGLIQYALD QGVNVTQVFV DTVGMPETYQ ARLQQSFPGI EVTVKAKADA LYPVVSAASI
CAKVARDQAV KKWQFVEKLQ DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT
AQTILEKEAE DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL
