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Ribonuclease H2 subunit B (RNase H2 subunit B) (Aicardi-Goutieres syndrome 2 protein) (AGS2) (Deleted in lymphocytic leukemia 8) (Ribonuclease HI subunit B)

 RNH2B_HUMAN             Reviewed;         312 AA.
Q5TBB1; G3XAJ1; Q05DR2; Q6PK48; Q9HAF7;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 1.
05-DEC-2018, entry version 121.
RecName: Full=Ribonuclease H2 subunit B;
Short=RNase H2 subunit B;
AltName: Full=Aicardi-Goutieres syndrome 2 protein;
Short=AGS2;
AltName: Full=Deleted in lymphocytic leukemia 8;
AltName: Full=Ribonuclease HI subunit B;
Name=RNASEH2B; Synonyms=DLEU8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Corcoran M.M.;
"DLEU8, a novel conserved gene located in the CLL 13q14 deletion
locus.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-308 (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 14-233, SUBUNIT, FUNCTION,
AND CHARACTERIZATION OF VARIANTS AGS2 LEU-73; SER-83; ARG-86 AND
HIS-219.
PubMed=21177858; DOI=10.1074/jbc.M110.181974;
Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J.,
Nowotny M.;
"The structural and biochemical characterization of human RNase H2
complex reveals the molecular basis for substrate recognition and
Aicardi-Goutieres syndrome defects.";
J. Biol. Chem. 286:10540-10550(2011).
[13]
VARIANTS AGS2 ARG-60; ARG-86; THR-162; ILE-163; THR-177; GLY-185 AND
HIS-219, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RNASEH2A
AND RNASEH2C.
PubMed=16845400; DOI=10.1038/ng1842;
Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E.,
Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P.,
Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E.,
Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H.,
Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y.,
Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A.,
Stephenson J.B.P., Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T.,
Weschke B., Woods C.G., Lebon P., Bonthron D.T., Ponting C.P.,
Jackson A.P.;
"Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-
Goutieres syndrome and mimic congenital viral brain infection.";
Nat. Genet. 38:910-916(2006).
[14]
VARIANTS AGS2 HIS-43; ARG-60; LEU-73; SER-83; ARG-86; PHE-138;
ILE-159; THR-162; ILE-163; THE-177; MET-183; GLY-185 AND HIS-219.
PubMed=17846997; DOI=10.1086/521373;
Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J.,
Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P.,
Benko W.S., Bergmann C., Bertini E., Biancheri R., Blair E.M.,
Blau N., Bonthron D.T., Briggs T., Brueton L.A., Brunner H.G.,
Burke C.J., Carr I.M., Carvalho D.R., Chandler K.E., Christen H.J.,
Corry P.C., Cowan F.M., Cox H., D'Arrigo S., Dean J., De Laet C.,
De Praeter C., Dery C., Ferrie C.D., Flintoff K., Frints S.G.,
Garcia-Cazorla A., Gener B., Goizet C., Goutieres F., Green A.J.,
Guet A., Hamel B.C., Hayward B.E., Heiberg A., Hennekam R.C.,
Husson M., Jackson A.P., Jayatunga R., Jiang Y.H., Kant S.G., Kao A.,
King M.D., Kingston H.M., Klepper J., van der Knaap M.S.,
Kornberg A.J., Kotzot D., Kratzer W., Lacombe D., Lagae L.,
Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H.,
Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D.,
McClure J.P., McWilliam R., Melancon S.B., Mewasingh L.D.,
Moutard M.L., Nischal K.K., Ostergaard J.R., Prendiville J.,
Rasmussen M., Rogers R.C., Roland D., Rosser E.M., Rostasy K.,
Roubertie A., Sanchis A., Schiffmann R., Scholl-Burgi S., Seal S.,
Shalev S.A., Corcoles C.S., Sinha G.P., Soler D., Spiegel R.,
Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L., Tomlin P.,
Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N.,
Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B.,
Whiteford M.L., Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S.,
Fazzi E., Lebon P., Crow Y.J.;
"Clinical and molecular phenotype of Aicardi-Goutieres syndrome.";
Am. J. Hum. Genet. 81:713-725(2007).
[15]
VARIANTS AGS2 THR-177 AND PRO-229.
PubMed=20131292; DOI=10.1002/art.27367;
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K.,
Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H.,
Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C.,
Ikonomidou C., Thomas K., Proud V., Niemann F., Wieczorek D.,
Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P.,
Lee-Kirsch M.A.;
"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-
Goutieres syndrome.";
Arthritis Rheum. 62:1469-1477(2010).
-!- FUNCTION: Non catalytic subunit of RNase H2, 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. {ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:21177858}.
-!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B
and RNASEH2C. {ECO:0000269|PubMed:21177858}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5TBB1-1; Sequence=Displayed;
Name=2;
IsoId=Q5TBB1-2; Sequence=VSP_054039, VSP_054040;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:16845400}.
-!- DISEASE: Aicardi-Goutieres syndrome 2 (AGS2) [MIM:610181]: A form
of Aicardi-Goutieres syndrome, a genetically heterogeneous disease
characterized by cerebral atrophy, leukoencephalopathy,
intracranial calcifications, chronic cerebrospinal fluid (CSF)
lymphocytosis, increased CSF alpha-interferon, and negative
serologic investigations for common prenatal infection. Clinical
features as thrombocytopenia, hepatosplenomegaly and elevated
hepatic transaminases along with intermittent fever may
erroneously suggest an infective process. Severe neurological
dysfunctions manifest in infancy as progressive microcephaly,
spasticity, dystonic posturing and profound psychomotor
retardation. Death often occurs in early childhood.
{ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:20131292, ECO:0000269|PubMed:21177858}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the RNase H2 subunit B family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01397.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH07332.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH10174.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AY764036; AAX13343.1; -; mRNA.
EMBL; AK021774; BAB13892.1; -; mRNA.
EMBL; AK223340; BAD97060.1; -; mRNA.
EMBL; AL137881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08864.1; -; Genomic_DNA.
EMBL; BC001397; AAH01397.1; ALT_SEQ; mRNA.
EMBL; BC005088; AAH05088.1; -; mRNA.
EMBL; BC007332; AAH07332.1; ALT_SEQ; mRNA.
EMBL; BC010174; AAH10174.1; ALT_SEQ; mRNA.
CCDS; CCDS45047.1; -. [Q5TBB1-2]
CCDS; CCDS9425.1; -. [Q5TBB1-1]
RefSeq; NP_001135751.1; NM_001142279.2. [Q5TBB1-2]
RefSeq; NP_078846.2; NM_024570.3. [Q5TBB1-1]
UniGene; Hs.306291; -.
PDB; 3P56; X-ray; 4.06 A; B/E=2-226.
PDB; 3P87; X-ray; 2.99 A; G/H/I/J/K/L=290-312.
PDB; 3PUF; X-ray; 3.10 A; B/E/H/K/N/Q=14-233.
PDBsum; 3P56; -.
PDBsum; 3P87; -.
PDBsum; 3PUF; -.
ProteinModelPortal; Q5TBB1; -.
SMR; Q5TBB1; -.
BioGrid; 122751; 41.
IntAct; Q5TBB1; 31.
STRING; 9606.ENSP00000337623; -.
iPTMnet; Q5TBB1; -.
PhosphoSitePlus; Q5TBB1; -.
BioMuta; RNASEH2B; -.
DMDM; 74745929; -.
EPD; Q5TBB1; -.
MaxQB; Q5TBB1; -.
PaxDb; Q5TBB1; -.
PeptideAtlas; Q5TBB1; -.
PRIDE; Q5TBB1; -.
ProteomicsDB; 64894; -.
DNASU; 79621; -.
Ensembl; ENST00000336617; ENSP00000337623; ENSG00000136104. [Q5TBB1-1]
Ensembl; ENST00000422660; ENSP00000389877; ENSG00000136104. [Q5TBB1-2]
GeneID; 79621; -.
KEGG; hsa:79621; -.
UCSC; uc001vfa.4; human. [Q5TBB1-1]
CTD; 79621; -.
DisGeNET; 79621; -.
EuPathDB; HostDB:ENSG00000136104.18; -.
GeneCards; RNASEH2B; -.
GeneReviews; RNASEH2B; -.
HGNC; HGNC:25671; RNASEH2B.
HPA; HPA040084; -.
HPA; HPA041469; -.
MalaCards; RNASEH2B; -.
MIM; 610181; phenotype.
MIM; 610326; gene.
neXtProt; NX_Q5TBB1; -.
OpenTargets; ENSG00000136104; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
PharmGKB; PA162401418; -.
eggNOG; KOG4705; Eukaryota.
eggNOG; ENOG410YS7I; LUCA.
GeneTree; ENSGT00390000011439; -.
HOVERGEN; HBG056010; -.
InParanoid; Q5TBB1; -.
KO; K10744; -.
OMA; RMACDIV; -.
PhylomeDB; Q5TBB1; -.
TreeFam; TF105250; -.
BioCyc; MetaCyc:HS13612-MONOMER; -.
BRENDA; 3.1.26.4; 2681.
ChiTaRS; RNASEH2B; human.
EvolutionaryTrace; Q5TBB1; -.
GenomeRNAi; 79621; -.
PRO; PR:Q5TBB1; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136104; Expressed in 179 organ(s), highest expression level in heart.
CleanEx; HS_RNASEH2B; -.
ExpressionAtlas; Q5TBB1; baseline and differential.
Genevisible; Q5TBB1; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0009259; P:ribonucleotide metabolic process; IBA:GO_Central.
GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
InterPro; IPR019024; RNase_H2_suB_wHTH.
Pfam; PF09468; RNase_H2-Ydr279; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aicardi-Goutieres syndrome;
Alternative splicing; Complete proteome; Disease mutation; Nucleus;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 312 Ribonuclease H2 subunit B.
/FTId=PRO_0000248378.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 295 295 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 248 257 KIKLSDEPVE -> MAAQRQKRGK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_054039.
VAR_SEQ 258 312 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054040.
VARIANT 43 43 P -> H (in AGS2; dbSNP:rs79564863).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070611.
VARIANT 60 60 L -> R (in AGS2; heterozygous compound
with T-177; dbSNP:rs75325951).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_027280.
VARIANT 73 73 W -> L (in AGS2; reduces stability of the
RNase complex; dbSNP:rs78071087).
{ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:21177858}.
/FTId=VAR_070612.
VARIANT 83 83 G -> S (in AGS2; reduces stability of the
RNase complex; dbSNP:rs76158094).
{ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:21177858}.
/FTId=VAR_070613.
VARIANT 86 86 H -> R (in AGS2; heterozygous compound
with T-177; reduces stability of the
RNase complex; dbSNP:rs77931005).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:21177858}.
/FTId=VAR_027281.
VARIANT 138 138 L -> F (in AGS2; dbSNP:rs78705382).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070614.
VARIANT 159 159 S -> I (in AGS2; dbSNP:rs76219783).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070615.
VARIANT 162 162 K -> T (in AGS2; dbSNP:rs75971463).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_027282.
VARIANT 163 163 T -> I (in AGS2; heterozygous compound
with T-177; dbSNP:rs79310911).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_027283.
VARIANT 177 177 A -> T (in AGS2; frequent mutation;
dbSNP:rs75184679).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:20131292}.
/FTId=VAR_027284.
VARIANT 183 183 V -> M (in AGS2; dbSNP:rs77377571).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070616.
VARIANT 185 185 V -> G (in AGS2; dbSNP:rs74555752).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_027285.
VARIANT 219 219 Y -> H (in AGS2; heterozygous compound
with a nonsense mutation; reduces
stability of the RNase complex;
dbSNP:rs77391331).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:21177858}.
/FTId=VAR_027286.
VARIANT 229 229 S -> P (in AGS2; dbSNP:rs768565639).
{ECO:0000269|PubMed:20131292}.
/FTId=VAR_070617.
CONFLICT 61 61 F -> L (in Ref. 1; AAX13343 and 2;
BAB13892). {ECO:0000305}.
CONFLICT 305 305 N -> K (in Ref. 6; AAH05088).
{ECO:0000305}.
STRAND 14 21 {ECO:0000244|PDB:3PUF}.
STRAND 36 41 {ECO:0000244|PDB:3PUF}.
TURN 43 45 {ECO:0000244|PDB:3PUF}.
STRAND 47 54 {ECO:0000244|PDB:3PUF}.
TURN 55 58 {ECO:0000244|PDB:3PUF}.
STRAND 59 66 {ECO:0000244|PDB:3PUF}.
STRAND 72 75 {ECO:0000244|PDB:3PUF}.
STRAND 78 81 {ECO:0000244|PDB:3PUF}.
STRAND 85 90 {ECO:0000244|PDB:3PUF}.
HELIX 94 107 {ECO:0000244|PDB:3PUF}.
HELIX 113 116 {ECO:0000244|PDB:3PUF}.
HELIX 123 130 {ECO:0000244|PDB:3PUF}.
HELIX 134 138 {ECO:0000244|PDB:3PUF}.
TURN 139 141 {ECO:0000244|PDB:3PUF}.
STRAND 142 145 {ECO:0000244|PDB:3PUF}.
STRAND 155 158 {ECO:0000244|PDB:3PUF}.
HELIX 160 181 {ECO:0000244|PDB:3PUF}.
HELIX 206 216 {ECO:0000244|PDB:3PUF}.
TURN 217 219 {ECO:0000244|PDB:3PUF}.
HELIX 222 230 {ECO:0000244|PDB:3PUF}.
HELIX 297 299 {ECO:0000244|PDB:3P87}.
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


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