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Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Dendritic cell-derived IFNG-induced protein) (DCIP) (Monocyte protein 5) (MOP-5) (SAM domain and HD domain-containing protein 1)

 SAMH1_HUMAN             Reviewed;         626 AA.
Q9Y3Z3; B4E2A5; E1P5V2; Q5JXG8; Q8N491; Q9H004; Q9H005; Q9H3U9;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
18-JUL-2018, entry version 171.
RecName: Full=Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 {ECO:0000305};
Short=dNTPase {ECO:0000305};
EC=3.1.5.- {ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:26101257, ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200};
AltName: Full=Dendritic cell-derived IFNG-induced protein {ECO:0000303|PubMed:11064105};
Short=DCIP {ECO:0000303|PubMed:11064105};
AltName: Full=Monocyte protein 5 {ECO:0000303|Ref.2};
Short=MOP-5 {ECO:0000303|Ref.2};
AltName: Full=SAM domain and HD domain-containing protein 1 {ECO:0000305};
Short=hSAMHD1 {ECO:0000303|PubMed:29379009};
Name=SAMHD1 {ECO:0000312|HGNC:HGNC:15925};
Synonyms=MOP5 {ECO:0000303|Ref.2};
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), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Brain;
PubMed=11064105; DOI=10.1016/S0165-2478(00)00276-5;
Li N., Zhang W., Cao X.;
"Identification of human homologue of mouse IFN-gamma induced protein
from human dendritic cells.";
Immunol. Lett. 74:221-224(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Platelet;
Takayama K., Yoshimoto M.;
"Molecular and biological characterization of a novel monocyte
protein, MOP-5.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Trachea;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[8]
PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18546154; DOI=10.1002/pmic.200700954;
Liao W., Bao Z., Cheng C., Mok Y.-K., Wong W.S.;
"Dendritic cell-derived interferon-gamma-induced protein mediates
tumor necrosis factor-alpha stimulation of human lung fibroblasts.";
Proteomics 8:2640-2650(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
INVOLVEMENT IN AGS5.
PubMed=20842748; DOI=10.1002/humu.21357;
Thiele H., du Moulin M., Barczyk K., George C., Schwindt W.,
Nurnberg G., Frosch M., Kurlemann G., Roth J., Nurnberg P., Rutsch F.;
"Cerebral arterial stenoses and stroke: novel features of Aicardi-
Goutieres syndrome caused by the Arg164X mutation in SAMHD1 are
associated with altered cytokine expression.";
Hum. Mutat. 31:E1836-E1850(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
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).
[18]
FUNCTION, INTERACTION WITH HIV-2 VIRUS PROTEIN VPX (MICROBIAL
INFECTION), UBIQUITINATION (MICROBIAL INFECTION), AND MUTAGENESIS OF
206-HIS-ASP-207.
PubMed=21613998; DOI=10.1038/nature10117;
Laguette N., Sobhian B., Casartelli N., Ringeard M., Chable-Bessia C.,
Segeral E., Yatim A., Emiliani S., Schwartz O., Benkirane M.;
"SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction
factor counteracted by Vpx.";
Nature 474:654-657(2011).
[19]
FUNCTION, INTERACTION WITH HIV-2 VIRUS PROTEIN VPX (MICROBIAL
INFECTION), AND UBIQUITINATION (MICROBIAL INFECTION).
PubMed=21720370; DOI=10.1038/nature10195;
Hrecka K., Hao C., Gierszewska M., Swanson S.K., Kesik-Brodacka M.,
Srivastava S., Florens L., Washburn M.P., Skowronski J.;
"Vpx relieves inhibition of HIV-1 infection of macrophages mediated by
the SAMHD1 protein.";
Nature 474:658-661(2011).
[20]
SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).
PubMed=23092512; DOI=10.1186/1742-4690-9-86;
Welbourn S., Miyagi E., White T.E., Diaz-Griffero F., Strebel K.;
"Identification and characterization of naturally occurring splice
variants of SAMHD1.";
Retrovirology 9:86-86(2012).
[21]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-592, AND
MUTAGENESIS OF 206-HIS-ASP-207 AND THR-592.
PubMed=23602554; DOI=10.1016/j.celrep.2013.03.017;
Cribier A., Descours B., Valadao A.L., Laguette N., Benkirane M.;
"Phosphorylation of SAMHD1 by cyclin A2/CDK1 regulates its restriction
activity toward HIV-1.";
Cell Rep. 3:1036-1043(2013).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS AGS5
PRO-123; HIS-143; GLN-145; TYR-167; ASN-201; SER-209; VAL-254 AND
HIS-290.
PubMed=24035396; DOI=10.1016/j.celrep.2013.08.019;
Zhao K., Du J., Han X., Goodier J.L., Li P., Zhou X., Wei W.,
Evans S.L., Li L., Zhang W., Cheung L.E., Wang G., Kazazian H.H. Jr.,
Yu X.F.;
"Modulation of LINE-1 and Alu/SVA retrotransposition by Aicardi-
Goutieres syndrome-related SAMHD1.";
Cell Rep. 4:1108-1115(2013).
[23]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION,
PHOSPHORYLATION AT THR-592, AND MUTAGENESIS OF THR-592 AND PRO-593.
PubMed=23601106; DOI=10.1016/j.chom.2013.03.005;
White T.E., Brandariz-Nunez A., Valle-Casuso J.C., Amie S.,
Nguyen L.A., Kim B., Tuzova M., Diaz-Griffero F.;
"The retroviral restriction ability of SAMHD1, but not its
deoxynucleotide triphosphohydrolase activity, is regulated by
phosphorylation.";
Cell Host Microbe 13:441-451(2013).
[24]
FUNCTION.
PubMed=23364794; DOI=10.1074/jbc.M112.431148;
Beloglazova N., Flick R., Tchigvintsev A., Brown G., Popovic A.,
Nocek B., Yakunin A.F.;
"Nuclease activity of the human SAMHD1 protein implicated in the
Aicardi-Goutieres syndrome and HIV-1 restriction.";
J. Biol. Chem. 288:8101-8110(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-93 AND THR-592,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23858451; DOI=10.1073/pnas.1312033110;
Franzolin E., Pontarin G., Rampazzo C., Miazzi C., Ferraro P.,
Palumbo E., Reichard P., Bianchi V.;
"The deoxynucleotide triphosphohydrolase SAMHD1 is a major regulator
of DNA precursor pools in mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 110:14272-14277(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-592, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
FUNCTION, AND MUTAGENESIS OF ASP-137; ASP-207 AND ASP-311.
PubMed=25038827; DOI=10.1038/nm.3626;
Ryoo J., Choi J., Oh C., Kim S., Seo M., Kim S.Y., Seo D., Kim J.,
White T.E., Brandariz-Nunez A., Diaz-Griffero F., Yun C.H.,
Hollenbaugh J.A., Kim B., Baek D., Ahn K.;
"The ribonuclease activity of SAMHD1 is required for HIV-1
restriction.";
Nat. Med. 20:936-941(2014).
[29]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 206-HIS-ASP-207;
ASP-207; ARG-451; GLN-548 AND THR-592.
PubMed=26101257; DOI=10.1093/nar/gkv633;
Seamon K.J., Sun Z., Shlyakhtenko L.S., Lyubchenko Y.L., Stivers J.T.;
"SAMHD1 is a single-stranded nucleic acid binding protein with no
active site-associated nuclease activity.";
Nucleic Acids Res. 43:6486-6499(2015).
[30]
FUNCTION.
PubMed=27477283; DOI=10.1016/j.celrep.2016.07.002;
Maelfait J., Bridgeman A., Benlahrech A., Cursi C., Rehwinkel J.;
"Restriction by SAMHD1 limits cGAS/STING-dependent innate and adaptive
immune responses to HIV-1.";
Cell Rep. 16:1492-1501(2016).
[31]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MRE11 AND RBBP8, AND
MUTAGENESIS OF 206-HIS-ASP-207.
PubMed=28834754; DOI=10.1016/j.celrep.2017.08.008;
Daddacha W., Koyen A.E., Bastien A.J., Head P.E., Dhere V.R.,
Nabeta G.N., Connolly E.C., Werner E., Madden M.Z., Daly M.B.,
Minten E.V., Whelan D.R., Schlafstein A.J., Zhang H., Anand R.,
Doronio C., Withers A.E., Shepard C., Sundaram R.K., Deng X.,
Dynan W.S., Wang Y., Bindra R.S., Cejka P., Rothenberg E.,
Doetsch P.W., Kim B., Yu D.S.;
"SAMHD1 promotes DNA end resection to facilitate DNA repair by
homologous recombination.";
Cell Rep. 20:1921-1935(2017).
[32]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS
AGS5 PRO-123; CYS-143; HIS-143; GLN-145; TYR-167; ASN-201; SER-209;
VAL-254; HIS-290; SER-369; VAL-385 AND THR-448, AND MUTAGENESIS OF
ARG-226; ASP-311 AND GLN-548.
PubMed=28229507; DOI=10.1002/humu.23201;
White T.E., Brandariz-Nunez A., Martinez-Lopez A., Knowlton C.,
Lenzi G., Kim B., Ivanov D., Diaz-Griffero F.;
"A SAMHD1 mutation associated with Aicardi-Goutieres Syndrome
uncouples the ability of SAMHD1 to restrict HIV-1 from its ability to
downmodulate type I interferon in humans.";
Hum. Mutat. 38:658-668(2017).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467; LYS-469; LYS-492 AND
LYS-622, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-592.
PubMed=29610582; DOI=10.1186/s13100-018-0116-5;
Herrmann A., Wittmann S., Thomas D., Shepard C.N., Kim B.,
Ferreiros N., Gramberg T.;
"The SAMHD1-mediated block of LINE-1 retroelements is regulated by
phosphorylation.";
Mob. DNA 9:11-11(2018).
[35]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH
MRE11, PHOSPHORYLATION AT THR-592, MUTAGENESIS OF LYS-312; TYR-315 AND
THR-592, VARIANT AGS5 548-GLN--MET-626 DEL, AND CHARACTERIZATION OF
VARIANT AGS5 548-GLN--MET-626 DEL.
PubMed=29670289; DOI=10.1038/s41586-018-0050-1;
Coquel F., Silva M.J., Techer H., Zadorozhny K., Sharma S.,
Nieminuszczy J., Mettling C., Dardillac E., Barthe A., Schmitz A.L.,
Promonet A., Cribier A., Sarrazin A., Niedzwiedz W., Lopez B.,
Costanzo V., Krejci L., Chabes A., Benkirane M., Lin Y.L., Pasero P.;
"SAMHD1 acts at stalled replication forks to prevent interferon
induction.";
Nature 557:57-61(2018).
[36]
DOMAIN, AND MUTAGENESIS OF LEU-77; CYS-80 AND HIS-111.
PubMed=29379009; DOI=10.1038/s41467-017-02783-8;
Buzovetsky O., Tang C., Knecht K.M., Antonucci J.M., Wu L., Ji X.,
Xiong Y.;
"The SAM domain of mouse SAMHD1 is critical for its activation and
regulation.";
Nat. Commun. 9:411-411(2018).
[37]
STRUCTURE BY NMR OF 23-118.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the N-terminal SAM-domain of the SAM domain and
HD domain containing protein 1 (dendritic cell-derived IFNG-induced
protein) (DCIP) (monocyte protein 5) (MOP-5).";
Submitted (JUL-2007) to the PDB data bank.
[38]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 120-626, CATALYTIC ACTIVITY,
ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE, ENZYME
REGULATION, UBIQUITINATION (MICROBIAL INFECTION), AND FUNCTION.
PubMed=22056990; DOI=10.1038/nature10623;
Goldstone D.C., Ennis-Adeniran V., Hedden J.J., Groom H.C., Rice G.I.,
Christodoulou E., Walker P.A., Kelly G., Haire L.F., Yap M.W.,
de Carvalho L.P., Stoye J.P., Crow Y.J., Taylor I.A., Webb M.;
"HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate
triphosphohydrolase.";
Nature 480:379-382(2011).
[39]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 109-626 IN COMPLEX WITH ATP;
GTP AND ZINC, SUBUNIT, ENZYME REGULATION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF ASP-137; GLN-142; ARG-145; ARG-333 AND ARG-451.
PubMed=24217394; DOI=10.1038/ncomms3722;
Zhu C., Gao W., Zhao K., Qin X., Zhang Y., Peng X., Zhang L., Dong Y.,
Zhang W., Li P., Wei W., Gong Y., Yu X.F.;
"Structural insight into dGTP-dependent activation of tetrameric
SAMHD1 deoxynucleoside triphosphate triphosphohydrolase.";
Nat. Commun. 4:2722-2722(2013).
[40]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP
AND ZINC, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF GLN-149;
206-HIS-ASP-207; LYS-312; TYR-315; ASP-319; ASP-330; ARG-333; ARG-352;
ASN-358; ASP-361; HIS-364; ARG-366; HIS-370; TYR-374; 376-HIS-LYS-377;
LYS-534; VAL-537 AND LEU-540, AND COFACTOR.
PubMed=24141705; DOI=10.1038/nsmb.2692;
Ji X., Wu Y., Yan J., Mehrens J., Yang H., DeLucia M., Hao C.,
Gronenborn A.M., Skowronski J., Ahn J., Xiong Y.;
"Mechanism of allosteric activation of SAMHD1 by dGTP.";
Nat. Struct. Mol. Biol. 20:1304-1309(2013).
[41] {ECO:0000244|PDB:4QFX, ECO:0000244|PDB:4QFY, ECO:0000244|PDB:4QFZ, ECO:0000244|PDB:4QG0, ECO:0000244|PDB:4QG1, ECO:0000244|PDB:4QG2, ECO:0000244|PDB:4QG4}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP
AND ZINC, COFACTOR, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF
ASP-137; GLN-142; ARG-145; GLN-149; HIS-210; HIS-215; HIS-233;
ASP-330; ASN-358 AND GLN-375.
PubMed=25288794; DOI=10.1074/jbc.M114.591958;
Koharudin L.M., Wu Y., DeLucia M., Mehrens J., Gronenborn A.M.,
Ahn J.;
"Structural basis of allosteric activation of sterile alpha motif and
histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside
triphosphates.";
J. Biol. Chem. 289:32617-32627(2014).
[42]
X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 582-626 IN COMPLEX WITH
DCAF1 AND SIMIAN IMMUNODEFICIENCY VIRUS PROTEIN VPX, UBIQUITINATION
(MICROBIAL INFECTION), FUNCTION, AND MUTAGENESIS OF ARG-609; ARG-617
AND LYS-622.
PubMed=24336198; DOI=10.1038/nature12815;
Schwefel D., Groom H.C., Boucherit V.C., Christodoulou E.,
Walker P.A., Stoye J.P., Bishop K.N., Taylor I.A.;
"Structural basis of lentiviral subversion of a cellular protein
degradation pathway.";
Nature 505:234-238(2014).
[43]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP,
SUBUNIT, AND ENZYME REGULATION.
PubMed=25267621; DOI=10.1073/pnas.1412289111;
Ji X., Tang C., Zhao Q., Wang W., Xiong Y.;
"Structural basis of cellular dNTP regulation by SAMHD1.";
Proc. Natl. Acad. Sci. U.S.A. 111:E4305-E4314(2014).
[44] {ECO:0000244|PDB:4RXO, ECO:0000244|PDB:4RXP, ECO:0000244|PDB:4RXQ, ECO:0000244|PDB:4RXR, ECO:0000244|PDB:4RXS}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 109-626 IN COMPLEX WITH GTP
AND ZINC, COFACTOR, SUBUNIT, AND ENZYME REGULATION.
PubMed=25760601; DOI=10.1107/S1399004714027527;
Zhu C.F., Wei W., Peng X., Dong Y.H., Gong Y., Yu X.F.;
"The mechanism of substrate-controlled allosteric regulation of SAMHD1
activated by GTP.";
Acta Crystallogr. D 71:516-524(2015).
[45] {ECO:0000244|PDB:4ZWE, ECO:0000244|PDB:4ZWG}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 113-626 OF MUTANT GLU-592 IN
COMPLEX WITH GTP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME
REGULATION, PHOSPHORYLATION AT THR-592, AND MUTAGENESIS OF THR-592.
PubMed=26294762; DOI=10.1074/jbc.M115.677435;
Tang C., Ji X., Wu L., Xiong Y.;
"Impaired dNTPase activity of SAMHD1 by phosphomimetic mutation of
Thr-592.";
J. Biol. Chem. 290:26352-26359(2015).
[46] {ECO:0000244|PDB:5AO0, ECO:0000244|PDB:5AO1, ECO:0000244|PDB:5AO2, ECO:0000244|PDB:5AO3, ECO:0000244|PDB:5AO4}
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 115-583 OF MUTANT ALA-164 IN
COMPLEX WITH GTP AND IRON, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
SUBUNIT, ENZYME REGULATION, PHOSPHORYLATION AT THR-592, AND
MUTAGENESIS OF ARG-143; ARG-145; ARG-164; HIS-167; HIS-206; ASP-207;
HIS-233; ASP-311; TYR-315; HIS-321; ARG-372 AND THR-592.
PubMed=26431200; DOI=10.1371/JOURNAL.PPAT.1005194;
Arnold L.H., Groom H.C., Kunzelmann S., Schwefel D., Caswell S.J.,
Ordonez P., Mann M.C., Rueschenbaum S., Goldstone D.C., Pennell S.,
Howell S.A., Stoye J.P., Webb M., Taylor I.A., Bishop K.N.;
"Phospho-dependent Regulation of SAMHD1 Oligomerisation Couples
Catalysis and Restriction.";
PLoS Pathog. 11:e1005194-e1005194(2015).
[47]
VARIANTS AGS5 PRO-123; CYS-143; HIS-143; GLN-145; ASN-201; SER-209;
VAL-254; SER-369 AND VAL-385, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19525956; DOI=10.1038/ng.373;
Rice G.I., Bond J., Asipu A., Brunette R.L., Manfield I.W., Carr I.M.,
Fuller J.C., Jackson R.M., Lamb T., Briggs T.A., Ali M., Gornall H.,
Couthard L.R., Aeby A., Attard-Montalto S.P., Bertini E., Bodemer C.,
Brockmann K., Brueton L.A., Corry P.C., Desguerre I., Fazzi E.,
Cazorla A.G., Gener B., Hamel B.C.J., Heiberg A., Hunter M.,
van der Knaap M.S., Kumar R., Lagae L., Landrieu P.G., Lourenco C.M.,
Marom D., McDermott M.F., van der Merwe W., Orcesi S.,
Prendiville J.S., Rasmussen M., Shalev S.A., Soler D.M., Shinawi M.,
Spiegel R., Tan T.Y., Vanderver A., Wakeling E.L., Wassmer E.,
Whittaker E., Lebon P., Stetson D.B., Bonthron D.T., Crow Y.J.;
"Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as
regulator of the innate immune response.";
Nat. Genet. 41:829-832(2009).
[48]
VARIANTS AGS5 TYR-167 AND HIS-290.
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).
[49]
VARIANT CHBL2 ASN-201.
PubMed=21204240; DOI=10.1002/ajmg.a.33778;
Ravenscroft J.C., Suri M., Rice G.I., Szynkiewicz M., Crow Y.J.;
"Autosomal dominant inheritance of a heterozygous mutation in SAMHD1
causing familial chilblain lupus.";
Am. J. Med. Genet. A 155:235-237(2011).
[50]
VARIANTS AGS5 120-ASP--HIS-123 DEL; PRO-123; HIS-143; ASN-201;
VAL-254; VAL-385 AND THR-448.
PubMed=24183309; DOI=10.1016/S1474-4422(13)70258-8;
Rice G.I., Forte G.M., Szynkiewicz M., Chase D.S., Aeby A.,
Abdel-Hamid M.S., Ackroyd S., Allcock R., Bailey K.M., Balottin U.,
Barnerias C., Bernard G., Bodemer C., Botella M.P., Cereda C.,
Chandler K.E., Dabydeen L., Dale R.C., De Laet C., De Goede C.G.,
Del Toro M., Effat L., Enamorado N.N., Fazzi E., Gener B., Haldre M.,
Lin J.P., Livingston J.H., Lourenco C.M., Marques W. Jr., Oades P.,
Peterson P., Rasmussen M., Roubertie A., Schmidt J.L., Shalev S.A.,
Simon R., Spiegel R., Swoboda K.J., Temtamy S.A., Vassallo G.,
Vilain C.N., Vogt J., Wermenbol V., Whitehouse W.P., Soler D.,
Olivieri I., Orcesi S., Aglan M.S., Zaki M.S., Abdel-Salam G.M.,
Vanderver A., Kisand K., Rozenberg F., Lebon P., Crow Y.J.;
"Assessment of interferon-related biomarkers in Aicardi-Goutieres
syndrome associated with mutations in TREX1, RNASEH2A, RNASEH2B,
RNASEH2C, SAMHD1, and ADAR: a case-control study.";
Lancet Neurol. 12:1159-1169(2013).
-!- FUNCTION: Protein that acts both as a host restriction factor
involved in defense response to virus and as a regulator of DNA
end resection at stalled replication forks (PubMed:19525956,
PubMed:21613998, PubMed:21720370, PubMed:23602554,
PubMed:23601106, PubMed:22056990, PubMed:24336198,
PubMed:26294762, PubMed:26431200, PubMed:28229507,
PubMed:28834754, PubMed:29670289). Has deoxynucleoside
triphosphate (dNTPase) activity, which is required to restrict
infection by viruses, such as HIV-1: dNTPase activity reduces
cellular dNTP levels to levels too low for retroviral reverse
transcription to occur, blocking early-stage virus replication in
dendritic and other myeloid cells (PubMed:19525956,
PubMed:21613998, PubMed:21720370, PubMed:23602554,
PubMed:23601106, PubMed:23364794, PubMed:25038827,
PubMed:26101257, PubMed:22056990, PubMed:24336198,
PubMed:28229507, PubMed:26294762, PubMed:26431200). Likewise,
suppresses LINE-1 retrotransposon activity (PubMed:24035396,
PubMed:29610582, PubMed:24217394). Not able to restrict infection
by HIV-2 virus; because restriction activity is counteracted by
HIV-2 viral protein Vpx (PubMed:21613998, PubMed:21720370). In
addition to virus restriction, dNTPase activity acts as a
regulator of DNA precursor pools by regulating dNTP pools
(PubMed:23858451). Phosphorylation at Thr-592 acts as a switch to
control dNTPase-dependent and -independent functions: it inhibits
dNTPase activity and ability to restrict infection by viruses,
while it promotes DNA end resection at stalled replication forks
(PubMed:23602554, PubMed:23601106, PubMed:29610582,
PubMed:29670289). Functions during S phase at stalled DNA
replication forks to promote the resection of gapped or reversed
forks: acts by stimulating the exonuclease activity of MRE11,
activating the ATR-CHK1 pathway and allowing the forks to restart
replication (PubMed:29670289). Its ability to promote degradation
of nascent DNA at stalled replication forks is required to prevent
induction of type I interferons, thereby preventing chronic
inflammation (PubMed:27477283, PubMed:29670289). Ability to
promote DNA end resection at stalled replication forks is
independent of dNTPase activity (PubMed:29670289). Enhances
immunoglobulin hypermutation in B-lymphocytes by promoting
transversion mutation (By similarity).
{ECO:0000250|UniProtKB:Q60710, ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:21613998, ECO:0000269|PubMed:21720370,
ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:23364794,
ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:23858451, ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:24336198,
ECO:0000269|PubMed:25038827, ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:27477283, ECO:0000269|PubMed:28229507,
ECO:0000269|PubMed:28834754, ECO:0000269|PubMed:29610582,
ECO:0000269|PubMed:29670289}.
-!- CATALYTIC ACTIVITY: dNTP + H(2)O = Deoxynucleoside + triphosphate.
{ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:23601106,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200};
-!- ENZYME REGULATION: Allosterically activated and regulated via the
combined actions of GTP and dNTPs (dATP, dGTP, dTTP and dCTP):
Allosteric site 1 binds GTP, while allosteric site 2 binds dNTP
(PubMed:25288794, PubMed:25267621, PubMed:25760601). Allosteric
activation promotes the formation of highly active homotetramers
(PubMed:22056990, PubMed:24141705, PubMed:24217394,
PubMed:25288794, PubMed:25267621, PubMed:25760601).
Phosphorylation at Thr-592 impairs homotetramerization, thereby
inhibiting dNTPase activity, leading to reduced ability to
restrict infection by viruses (PubMed:23602554, PubMed:23601106,
PubMed:26294762, PubMed:26431200, PubMed:29610582,
PubMed:29670289). {ECO:0000269|PubMed:22056990,
ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:24141705, ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:29610582,
ECO:0000269|PubMed:29670289}.
-!- SUBUNIT: Homodimer; in absence of GTP and dNTP (PubMed:24141705,
PubMed:24217394, PubMed:28229507, PubMed:25760601). Homotetramer;
in GTP- and dNTP-bound form (PubMed:23601106, PubMed:26101257,
PubMed:24141705, PubMed:24217394, PubMed:28229507,
PubMed:26294762, PubMed:26431200, PubMed:25288794,
PubMed:25267621, PubMed:25760601). Interacts with MRE11; leading
to stimulate the exonuclease activity of MRE11 (PubMed:28834754,
PubMed:29670289). Interacts with RBBP8/CtIP (PubMed:28834754).
{ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26101257, ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:28229507,
ECO:0000269|PubMed:28834754, ECO:0000269|PubMed:29670289}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-2 viral protein
Vpx; promoting interaction with a E3 ubiquitin-protein ligase
complex containing DCAF1, leading to subsequent ubiquitination and
degradation of SAMHD1. {ECO:0000269|PubMed:21613998,
ECO:0000269|PubMed:21720370, ECO:0000269|PubMed:24336198}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-1054601, EBI-1054601;
O75923:DYSF; NbExp=2; IntAct=EBI-1054601, EBI-2799016;
P58753:TIRAP; NbExp=2; IntAct=EBI-1054601, EBI-528644;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:23092512, ECO:0000269|PubMed:23858451,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:28229507}.
Chromosome {ECO:0000269|PubMed:28834754}. Note=Localizes to sites
of DNA double-strand breaks in response to DNA damage.
{ECO:0000269|PubMed:28834754}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y3Z3-1; Sequence=Displayed;
Name=3; Synonyms=delta8-9;
IsoId=Q9Y3Z3-3; Sequence=VSP_046561;
Note=Catalytically inactive.;
Name=4; Synonyms=delta14;
IsoId=Q9Y3Z3-4; Sequence=VSP_046562;
Note=Catalytically inactive.;
-!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, spleen,
liver, small intestine, placenta, lung and peripheral blood
leukocytes (PubMed:11064105). No expression is seen in brain and
thymus (PubMed:11064105). {ECO:0000269|PubMed:11064105}.
-!- INDUCTION: By IFNG/IFN-gamma. Up-regulated in TNF treated lung
fibroblasts. {ECO:0000269|PubMed:11064105,
ECO:0000269|PubMed:18546154}.
-!- DOMAIN: In human, and in contrast to mouse protein, the SAM domain
is not required for deoxynucleoside triphosphate (dNTPase)
activity and ability to restrict infection by viruses.
{ECO:0000269|PubMed:29379009}.
-!- PTM: Phosphorylation at Thr-592 by CDK1 acts as a switch to
control deoxynucleoside triphosphate (dNTPase)-dependent and
-independent functions (PubMed:29670289). Phosphorylation at Thr-
592 takes place in cycling cells: it reduces the stability of the
homotetramer, impairing the dNTPase activity and subsequent
ability to restrict infection by viruses (PubMed:23602554,
PubMed:23601106, PubMed:26294762, PubMed:26431200). It also
inhibits ability to suppress LINE-1 retrotransposon activity
(PubMed:29610582). In contrast, phosphorylation at Thr-592
promotes DNA end resection at stalled replication forks in
response to DNA damage (PubMed:29670289).
{ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:26294762, ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:29610582, ECO:0000269|PubMed:29670289}.
-!- PTM: (Microbial infection) Ubiquitinated following interaction
with HIV-2 viral protein Vpx; Vpx promotes interaction and with a
DCX (DDB1-CUL4-X-box) E3 ubiquitin ligase, leading to proteasomal
degradation. {ECO:0000269|PubMed:21613998,
ECO:0000269|PubMed:21720370, ECO:0000269|PubMed:22056990,
ECO:0000269|PubMed:24336198}.
-!- DISEASE: Aicardi-Goutieres syndrome 5 (AGS5) [MIM:612952]: 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:19525956, ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:20842748, ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309, ECO:0000269|PubMed:28229507,
ECO:0000269|PubMed:29670289}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Chilblain lupus 2 (CHBL2) [MIM:614415]: A rare cutaneous
form of lupus erythematosus. Affected individuals present with
painful bluish-red papular or nodular lesions of the skin in acral
locations precipitated by cold and wet exposure at temperatures
less than 10 degrees centigrade. {ECO:0000269|PubMed:21204240}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000305}.
-!- CAUTION: Was intially thought to be allosterically stimulated by
dGTP (PubMed:22056990, PubMed:24141705, PubMed:24217394). However,
it was later shown that it is allosterically activated and
regulated via the combined actions of GTP and dNTPs (dATP, dGTP,
dTTP and dCTP), which bind two separate binding sites
(PubMed:25288794, PubMed:25267621, PubMed:25760601).
{ECO:0000269|PubMed:22056990, ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794, ECO:0000269|PubMed:25760601}.
-!- CAUTION: Phosphorylation at Thr-592 was initially thought to
impair ability to restrict infection by viruses without affecting
the deoxynucleoside triphosphate (dNTPase) activity
(PubMed:23601106). However, it was later shown that
phosphorylation reduces the stability of the homotetramer, leading
to impair the dNTPase activity (PubMed:26294762, PubMed:26431200).
{ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
-!- CAUTION: Was initially thought to have 3'-5' exonuclease activity,
acting on single-stranded RNA (PubMed:23364794, PubMed:25038827).
A publication also reported some DNA 3'-5' exonuclease activity
(PubMed:23364794). However, it was later shown that SAMHD1 does
not possess DNA and/or RNA exonuclease activities and that these
activities are due to contamination during the purification
process that can be removed after chromatography steps
(PubMed:26101257). The exonuclease activity observed was maybe due
to the presence of MRE11 during the purification steps
(PubMed:29670289). {ECO:0000269|PubMed:23364794,
ECO:0000269|PubMed:25038827, ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:29670289}.
-!- SEQUENCE CAUTION:
Sequence=BAG65067.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF228421; AAF32407.1; -; mRNA.
EMBL; AB013847; BAB18916.1; -; mRNA.
EMBL; AL050267; CAB43368.1; -; mRNA.
EMBL; AK027811; BAB55386.1; -; mRNA.
EMBL; AK304187; BAG65067.1; ALT_SEQ; mRNA.
EMBL; AL079335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76090.1; -; Genomic_DNA.
EMBL; CH471077; EAW76091.1; -; Genomic_DNA.
EMBL; BC036450; AAH36450.1; -; mRNA.
CCDS; CCDS13288.1; -. [Q9Y3Z3-1]
PIR; T08686; T08686.
RefSeq; NP_056289.2; NM_015474.3. [Q9Y3Z3-1]
RefSeq; XP_005260441.1; XM_005260384.3. [Q9Y3Z3-4]
UniGene; Hs.580681; -.
PDB; 2E8O; NMR; -; A=23-118.
PDB; 3U1N; X-ray; 3.10 A; A/B/C/D=120-626.
PDB; 4BZB; X-ray; 1.83 A; A/B/C/D=113-626.
PDB; 4BZC; X-ray; 2.88 A; A/B/C/D=113-626.
PDB; 4CC9; X-ray; 2.47 A; C=582-626.
PDB; 4MZ7; X-ray; 1.80 A; A/B=109-626.
PDB; 4Q7H; X-ray; 2.59 A; A/B/C/D=109-626.
PDB; 4QFX; X-ray; 2.20 A; A/B/C/D=113-626.
PDB; 4QFY; X-ray; 2.10 A; A/B/C/D=113-626.
PDB; 4QFZ; X-ray; 2.30 A; A/B/C/D=113-626.
PDB; 4QG0; X-ray; 2.30 A; A/B/C/D=113-626.
PDB; 4QG1; X-ray; 2.20 A; A/B/C/D=113-626.
PDB; 4QG2; X-ray; 2.25 A; A/B/C/D=113-626.
PDB; 4QG4; X-ray; 2.10 A; A/B/C/D=113-626.
PDB; 4RXO; X-ray; 2.60 A; A/B/C/D=109-626.
PDB; 4RXP; X-ray; 2.10 A; A/B=109-626.
PDB; 4RXQ; X-ray; 2.10 A; A/B=109-626.
PDB; 4RXR; X-ray; 2.12 A; A/B=109-626.
PDB; 4RXS; X-ray; 2.20 A; A/B=109-626.
PDB; 4TNP; X-ray; 2.00 A; A/B/C/D=113-626.
PDB; 4TNQ; X-ray; 2.55 A; A/B/C/D=113-626.
PDB; 4TNR; X-ray; 2.75 A; A/B/C/D=113-626.
PDB; 4TNX; X-ray; 2.31 A; A/B/C/D=113-626.
PDB; 4TNY; X-ray; 2.60 A; A/B/C/D=113-626.
PDB; 4TNZ; X-ray; 2.38 A; A/B/C/D=113-626.
PDB; 4TO0; X-ray; 2.30 A; A/B/C/D=113-626.
PDB; 4TO1; X-ray; 2.55 A; A/B/C/D=113-626.
PDB; 4TO2; X-ray; 2.27 A; A/B/C/D=113-626.
PDB; 4TO3; X-ray; 2.20 A; A/B/C/D=113-626.
PDB; 4TO4; X-ray; 2.10 A; A/B/C/D=113-626.
PDB; 4TO5; X-ray; 2.80 A; A/B/C/D=113-626.
PDB; 4TO6; X-ray; 2.33 A; A/B/C/D=113-626.
PDB; 4ZWE; X-ray; 2.81 A; A/B/C/D=113-626.
PDB; 4ZWG; X-ray; 2.30 A; A/B/C/D=113-626.
PDB; 5AO0; X-ray; 3.73 A; A/B=41-583.
PDB; 5AO1; X-ray; 2.54 A; A/B/C/D=115-583.
PDB; 5AO2; X-ray; 2.97 A; A/B/C/D=115-583.
PDB; 5AO3; X-ray; 3.00 A; A/B/C/D=115-626.
PDB; 5AO4; X-ray; 3.70 A; A/B/C/D=115-626.
PDBsum; 2E8O; -.
PDBsum; 3U1N; -.
PDBsum; 4BZB; -.
PDBsum; 4BZC; -.
PDBsum; 4CC9; -.
PDBsum; 4MZ7; -.
PDBsum; 4Q7H; -.
PDBsum; 4QFX; -.
PDBsum; 4QFY; -.
PDBsum; 4QFZ; -.
PDBsum; 4QG0; -.
PDBsum; 4QG1; -.
PDBsum; 4QG2; -.
PDBsum; 4QG4; -.
PDBsum; 4RXO; -.
PDBsum; 4RXP; -.
PDBsum; 4RXQ; -.
PDBsum; 4RXR; -.
PDBsum; 4RXS; -.
PDBsum; 4TNP; -.
PDBsum; 4TNQ; -.
PDBsum; 4TNR; -.
PDBsum; 4TNX; -.
PDBsum; 4TNY; -.
PDBsum; 4TNZ; -.
PDBsum; 4TO0; -.
PDBsum; 4TO1; -.
PDBsum; 4TO2; -.
PDBsum; 4TO3; -.
PDBsum; 4TO4; -.
PDBsum; 4TO5; -.
PDBsum; 4TO6; -.
PDBsum; 4ZWE; -.
PDBsum; 4ZWG; -.
PDBsum; 5AO0; -.
PDBsum; 5AO1; -.
PDBsum; 5AO2; -.
PDBsum; 5AO3; -.
PDBsum; 5AO4; -.
ProteinModelPortal; Q9Y3Z3; -.
SMR; Q9Y3Z3; -.
BioGrid; 117436; 73.
DIP; DIP-50704N; -.
IntAct; Q9Y3Z3; 30.
STRING; 9606.ENSP00000262878; -.
CarbonylDB; Q9Y3Z3; -.
iPTMnet; Q9Y3Z3; -.
PhosphoSitePlus; Q9Y3Z3; -.
BioMuta; SAMHD1; -.
DMDM; 22257047; -.
EPD; Q9Y3Z3; -.
PaxDb; Q9Y3Z3; -.
PeptideAtlas; Q9Y3Z3; -.
PRIDE; Q9Y3Z3; -.
ProteomicsDB; 86088; -.
DNASU; 25939; -.
Ensembl; ENST00000262878; ENSP00000262878; ENSG00000101347. [Q9Y3Z3-4]
Ensembl; ENST00000646066; ENSP00000495432; ENSG00000101347. [Q9Y3Z3-3]
Ensembl; ENST00000646673; ENSP00000493536; ENSG00000101347. [Q9Y3Z3-1]
Ensembl; ENST00000646869; ENSP00000495667; ENSG00000101347. [Q9Y3Z3-1]
GeneID; 25939; -.
KEGG; hsa:25939; -.
UCSC; uc002xgh.3; human. [Q9Y3Z3-1]
CTD; 25939; -.
DisGeNET; 25939; -.
EuPathDB; HostDB:ENSG00000101347.8; -.
GeneCards; SAMHD1; -.
GeneReviews; SAMHD1; -.
HGNC; HGNC:15925; SAMHD1.
HPA; HPA047072; -.
MalaCards; SAMHD1; -.
MIM; 606754; gene.
MIM; 612952; phenotype.
MIM; 614415; phenotype.
neXtProt; NX_Q9Y3Z3; -.
OpenTargets; ENSG00000101347; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
Orphanet; 90280; Chilblain lupus.
PharmGKB; PA34938; -.
eggNOG; KOG2681; Eukaryota.
eggNOG; COG1078; LUCA.
GeneTree; ENSGT00390000013867; -.
HOVERGEN; HBG054208; -.
InParanoid; Q9Y3Z3; -.
KO; K22544; -.
OMA; EVKWTHE; -.
OrthoDB; EOG091G060J; -.
PhylomeDB; Q9Y3Z3; -.
TreeFam; TF316113; -.
Reactome; R-HSA-8956319; Nucleobase catabolism.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SIGNOR; Q9Y3Z3; -.
ChiTaRS; SAMHD1; human.
EvolutionaryTrace; Q9Y3Z3; -.
GeneWiki; SAMHD1; -.
GenomeRNAi; 25939; -.
PRO; PR:Q9Y3Z3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101347; -.
CleanEx; HS_SAMHD1; -.
Genevisible; Q9Y3Z3; HS.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032567; F:dGTP binding; IDA:UniProtKB.
GO; GO:0008832; F:dGTPase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003676; F:nucleic acid binding; IDA:UniProtKB.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0016793; F:triphosphoric monoester hydrolase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046061; P:dATP catabolic process; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0009264; P:deoxyribonucleotide catabolic process; TAS:Reactome.
GO; GO:0006203; P:dGTP catabolic process; IDA:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00077; HDc; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
Pfam; PF01966; HD; 1.
Pfam; PF07647; SAM_2; 1.
SMART; SM00471; HDc; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS51831; HD; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aicardi-Goutieres syndrome;
Allosteric enzyme; Alternative splicing; Antiviral defense;
Chromosome; Complete proteome; Direct protein sequencing;
Disease mutation; DNA damage; DNA repair; DNA replication;
GTP-binding; Hydrolase; Immunity; Innate immunity; Isopeptide bond;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 626 Deoxynucleoside triphosphate
triphosphohydrolase SAMHD1.
/FTId=PRO_0000153732.
DOMAIN 45 110 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 164 316 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
NP_BIND 137 145 GTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
NP_BIND 352 354 dNTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
REGION 309 315 Substrate binding.
{ECO:0000269|PubMed:24141705}.
REGION 370 375 Substrate binding.
{ECO:0000269|PubMed:24141705}.
ACT_SITE 233 233 {ECO:0000305|PubMed:22056990}.
METAL 167 167 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26431200}.
METAL 206 206 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26431200}.
METAL 207 207 Zinc. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26431200}.
METAL 311 311 Zinc. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26431200}.
BINDING 116 116 GTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 119 119 dNTP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 149 149 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 164 164 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 210 210 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 315 315 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 319 319 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 333 333 dNTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 358 358 dNTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 366 366 Substrate. {ECO:0000269|PubMed:24141705}.
BINDING 376 376 dNTP; shared with neighboring subunit.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 377 377 dNTP; shared with neighboring subunit.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 451 451 GTP; shared with neighboring subunit.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 455 455 GTP; shared with neighboring subunit.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
BINDING 523 523 dNTP. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25267621,
ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.8}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000250|UniProtKB:Q60710}.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60710}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60710}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 592 592 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:23601106,
ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:29610582,
ECO:0000269|PubMed:29670289}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 622 622 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 285 354 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046561.
VAR_SEQ 502 536 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_046562.
VARIANT 120 123 Missing (in AGS5).
{ECO:0000269|PubMed:24183309}.
/FTId=VAR_078239.
VARIANT 123 123 H -> P (in AGS5; loss of oligomerization;
decreased ability to restrict LINE-1
retrotransposon activity;
dbSNP:rs121434520).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058481.
VARIANT 143 143 R -> C (in AGS5; loss of oligomerization;
dbSNP:rs387906948).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058482.
VARIANT 143 143 R -> H (in AGS5; loss of oligomerization;
decreased ability to restrict LINE-1
retrotransposon activity;
dbSNP:rs369035155).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058483.
VARIANT 145 145 R -> Q (in AGS5; loss of oligomerization;
decreased ability to restrict LINE-1
retrotransposon activity;
dbSNP:rs515726145).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058484.
VARIANT 167 167 H -> Y (in AGS5; loss of function in
defense response to virus; loss of
oligomerization; decreased ability to
restrict LINE-1 retrotransposon
activity). {ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_070633.
VARIANT 201 201 I -> N (in AGS5 and CHBL2; loss of
function in defense response to virus;
decreased oligomerization; decreased
ability to restrict LINE-1
retrotransposon activity;
dbSNP:rs138603088).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:21204240,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058485.
VARIANT 209 209 G -> S (in AGS5; does not affect
oligomerization; decreased ability to
restrict LINE-1 retrotransposon activity;
does not affect localization to nucleus;
dbSNP:rs121434516).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058486.
VARIANT 254 254 M -> V (in AGS5; loss of function in
defense response to virus; does not
affect oligomerization; decreased ability
to restrict LINE-1 retrotransposon
activity; dbSNP:rs121434521).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058487.
VARIANT 290 290 R -> H (in AGS5; loss of oligomerization;
decreased ability to restrict LINE-1
retrotransposon activity;
dbSNP:rs559553527).
{ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_070634.
VARIANT 369 369 L -> S (in AGS5; loss of function in
defense response to virus; decreased
oligomerization; dbSNP:rs515726139).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058488.
VARIANT 385 385 M -> V (in AGS5; loss of function in
defense response to virus; loss of
oligomerization; dbSNP:rs515726140).
{ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_058489.
VARIANT 448 448 I -> T (in AGS5; loss of function in
defense response to virus; decreased
oligomerization; does not affect
localization to nucleus; novel
localization to the cytoplasm;
dbSNP:rs774964432).
{ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507}.
/FTId=VAR_078240.
VARIANT 548 626 Missing (in AGS5; Does not affect dNTP
regulation, while affecting ability to
promote DNA end resection at stalled
replication forks).
{ECO:0000269|PubMed:29670289}.
/FTId=VAR_080530.
MUTAGEN 77 77 L->F: Increased stability of the tetramer
and increased deoxynucleoside
triphosphate (dNTPase) activity; when
associated with F-77 and F-80 and R-111.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 80 80 C->F: Increased stability of the tetramer
and increased deoxynucleoside
triphosphate (dNTPase) activity; when
associated with F-77 and R-111.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 111 111 H->R: Increased stability of the tetramer
and increased deoxynucleoside
triphosphate (dNTPase) activity; when
associated with F-77 and F-80.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 137 137 D->A: Impairs homotetramerization and
nearly abolishes dNTPase activity.
{ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25038827,
ECO:0000269|PubMed:25288794}.
MUTAGEN 142 142 Q->E,A: Impairs homotetramerization and
nearly abolishes dNTPase activity; when
associated with K-145.
{ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794}.
MUTAGEN 143 143 R->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 145 145 R->A: Impairs homotetramerization and
nearly abolishes dNTPase activity.
Abolished ability to restrict infection
by viruses. {ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:26431200}.
MUTAGEN 145 145 R->K: Impairs homotetramerization and
nearly abolishes dNTPase activity; when
associated with E-145.
{ECO:0000269|PubMed:24217394}.
MUTAGEN 149 149 Q->A: Abolished dNTPase activity without
affecting homotetramerization. Abolished
dNTPase activity; when associated with A-
319. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794}.
MUTAGEN 164 164 R->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 167 167 H->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 206 207 HD->RN: Abolishes zinc binding and
dNTPase activity. Does not affect ability
to promote DNA end resection at stalled
replication forks.
{ECO:0000269|PubMed:21613998,
ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:28834754}.
MUTAGEN 206 206 H->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 207 207 D->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 207 207 D->N,A: Loss of dNTPase activity.
{ECO:0000269|PubMed:25038827,
ECO:0000269|PubMed:26101257}.
MUTAGEN 210 210 H->A: Abolished dNTPase activity without
affecting homotetramerization.
{ECO:0000269|PubMed:25288794}.
MUTAGEN 215 215 H->A: Abolished dNTPase activity without
affecting homotetramerization.
{ECO:0000269|PubMed:25288794}.
MUTAGEN 226 226 R->G: Loss of function in defense
response to virus.
{ECO:0000269|PubMed:28229507}.
MUTAGEN 233 233 H->A: Abolished dNTPase activity without
affecting homotetramerization. Abolished
ability to restrict infection by viruses.
{ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:26431200}.
MUTAGEN 311 311 D->A: Loss of function in defense
response to virus. Loss of dNTPase
activity. Does not affect
oligomerization.
{ECO:0000269|PubMed:25038827,
ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:28229507}.
MUTAGEN 312 312 K->A: Abolishes dNTPase activity; when
associated with A-315 and A-366. Does not
affect ability to promote DNA end
resection at stalled replication forks;
when associated with A-315.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:29670289}.
MUTAGEN 315 315 Y->A: Abolished ability to restrict
infection by viruses. Abolishes dNTPase
activity; when associated with A-312 and
A-366. Does not affect ability to promote
DNA end resection at stalled replication
forks; when associated with A-312.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:29670289}.
MUTAGEN 319 319 D->A: Abolishes dNTPase activity; when
associated with A-149.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 321 321 H->A: Abolished ability to restrict
infection by viruses.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 330 330 D->A: Impaired homotetramerization and
slightly reduced dNTPase activity.
Impaired homotetramerization and reduced
dNTPase activity; when associated with A-
358. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794}.
MUTAGEN 333 333 R->E: Decreases dNTPase activity. Impairs
homotetramerization and nearly abolishes
dNTPase activity; when associated with E-
451. {ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394}.
MUTAGEN 352 352 R->A: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-376 and A-377.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 358 358 N->A: Impaired homotetramerization and
slightly reduced dNTPase activity.
Impaired homotetramerization and reduced
dNTPase activity A-330.
{ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794}.
MUTAGEN 361 361 D->R: Impairs homotetramerization and
nearly abolishes dNTPase activity; when
associated with K-364.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 364 364 H->K: Impairs homotetramerization and
nearly abolishes dNTPase activity; when
associated with R-361.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 366 366 R->A: Abolishes dNTPase activity; when
associated with A-312 and A-315.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 370 370 H->A: Abolishes dNTPase activity; when
associated with G-374.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 372 372 R->D: Abolished homotetramerization and
dNTPase activity.
{ECO:0000269|PubMed:26431200}.
MUTAGEN 374 374 Y->G: Abolishes dNTPase activity; when
associated with A-370.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 375 375 Q->A: Abolished dNTPase activity without
affecting homotetramerization.
{ECO:0000269|PubMed:25288794}.
MUTAGEN 376 376 H->A: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-352 and A-377.
MUTAGEN 377 377 K->A: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-352 and A-376.
MUTAGEN 451 451 R->E: Impairs homotetramerization and
abolishes dNTPase activity.
{ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:26101257}.
MUTAGEN 534 534 K->A: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-537 and D-540.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 537 537 V->A: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-534 and D-540.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 540 540 L->D: Impairs homotetramerization and
abolishes dNTPase activity; when
associated with A-537 and A-534.
{ECO:0000269|PubMed:24141705}.
MUTAGEN 548 548 Q->A: Loss of function in defense
response to virus. Does not affect
oligomerization. Retains dNTPase
activity. {ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:28229507}.
MUTAGEN 592 592 T->A,V: Impaired ability to promote DNA
end resection at stalled replication
forks. Promotes dNTPase activity and
ability to restrict infection by viruses.
{ECO:0000269|PubMed:23601106,
ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:29610582,
ECO:0000269|PubMed:29670289}.
MUTAGEN 592 592 T->E: Mimicks phosphorylation state,
retains ability to promote DNA end
resection at stalled replication forks.
Induces large conformational changes that
impair homotetramerization, leading to
reduced dNTPase activity and decreased
ability to restrict infection by viruses.
{ECO:0000269|PubMed:23601106,
ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:26294762,
ECO:0000269|PubMed:26431200,
ECO:0000269|PubMed:29610582,
ECO:0000269|PubMed:29670289}.
MUTAGEN 593 593 P->A: Promotes ability to restrict
infection by viruses.
{ECO:0000269|PubMed:23601106}.
MUTAGEN 609 609 R->A,E: Abolishes proteasomal degradation
triggered by the viral accessory protein
vpx. {ECO:0000269|PubMed:24336198}.
MUTAGEN 617 617 R->A,E: Abolishes proteasomal degradation
triggered by the viral accessory protein
vpx. {ECO:0000269|PubMed:24336198}.
MUTAGEN 622 622 K->A,E: Abolishes proteasomal degradation
triggered by the viral accessory protein
vpx. {ECO:0000269|PubMed:24336198}.
CONFLICT 394 394 D -> G (in Ref. 1; AAF32407 and 3;
CAB43368). {ECO:0000305}.
CONFLICT 404 404 G -> E (in Ref. 7; AAH36450).
{ECO:0000305}.
CONFLICT 494 494 K -> E (in Ref. 1; AAF32407 and 3;
CAB43368). {ECO:0000305}.
CONFLICT 546 546 A -> V (in Ref. 7; AAH36450).
{ECO:0000305}.
HELIX 42 44 {ECO:0000244|PDB:2E8O}.
HELIX 46 57 {ECO:0000244|PDB:2E8O}.
HELIX 62 70 {ECO:0000244|PDB:2E8O}.
TURN 75 80 {ECO:0000244|PDB:2E8O}.
HELIX 83 88 {ECO:0000244|PDB:2E8O}.
HELIX 94 108 {ECO:0000244|PDB:2E8O}.
TURN 109 112 {ECO:0000244|PDB:2E8O}.
STRAND 116 120 {ECO:0000244|PDB:4MZ7}.
TURN 121 123 {ECO:0000244|PDB:4MZ7}.
STRAND 124 128 {ECO:0000244|PDB:4MZ7}.
HELIX 130 136 {ECO:0000244|PDB:4MZ7}.
HELIX 139 142 {ECO:0000244|PDB:4MZ7}.
HELIX 143 146 {ECO:0000244|PDB:4MZ7}.
STRAND 147 150 {ECO:0000244|PDB:4QFY}.
HELIX 151 155 {ECO:0000244|PDB:4MZ7}.
HELIX 164 185 {ECO:0000244|PDB:4MZ7}.
HELIX 187 189 {ECO:0000244|PDB:4MZ7}.
HELIX 193 205 {ECO:0000244|PDB:4MZ7}.
TURN 206 209 {ECO:0000244|PDB:4MZ7}.
TURN 212 214 {ECO:0000244|PDB:4MZ7}.
HELIX 215 219 {ECO:0000244|PDB:4MZ7}.
HELIX 221 225 {ECO:0000244|PDB:4MZ7}.
STRAND 226 229 {ECO:0000244|PDB:4TO6}.
HELIX 233 247 {ECO:0000244|PDB:4MZ7}.
HELIX 250 256 {ECO:0000244|PDB:4MZ7}.
HELIX 261 273 {ECO:0000244|PDB:4MZ7}.
STRAND 288 290 {ECO:0000244|PDB:4MZ7}.
HELIX 292 299 {ECO:0000244|PDB:4MZ7}.
STRAND 300 302 {ECO:0000244|PDB:4MZ7}.
TURN 304 306 {ECO:0000244|PDB:4MZ7}.
HELIX 310 323 {ECO:0000244|PDB:4MZ7}.
HELIX 331 336 {ECO:0000244|PDB:4MZ7}.
STRAND 338 343 {ECO:0000244|PDB:4MZ7}.
STRAND 346 352 {ECO:0000244|PDB:4MZ7}.
HELIX 353 355 {ECO:0000244|PDB:4MZ7}.
HELIX 356 372 {ECO:0000244|PDB:4MZ7}.
TURN 373 375 {ECO:0000244|PDB:4MZ7}.
HELIX 377 393 {ECO:0000244|PDB:4MZ7}.
TURN 394 396 {ECO:0000244|PDB:4MZ7}.
HELIX 402 404 {ECO:0000244|PDB:4MZ7}.
TURN 409 411 {ECO:0000244|PDB:4MZ7}.
HELIX 412 414 {ECO:0000244|PDB:4MZ7}.
HELIX 416 419 {ECO:0000244|PDB:4MZ7}.
HELIX 425 432 {ECO:0000244|PDB:4MZ7}.
HELIX 436 438 {ECO:0000244|PDB:4MZ7}.
HELIX 439 449 {ECO:0000244|PDB:4MZ7}.
STRAND 455 460 {ECO:0000244|PDB:4MZ7}.
STRAND 463 465 {ECO:0000244|PDB:4ZWG}.
HELIX 470 475 {ECO:0000244|PDB:4MZ7}.
HELIX 476 482 {ECO:0000244|PDB:4MZ7}.
HELIX 495 497 {ECO:0000244|PDB:4MZ7}.
STRAND 498 509 {ECO:0000244|PDB:4MZ7}.
HELIX 514 517 {ECO:0000244|PDB:4MZ7}.
STRAND 519 522 {ECO:0000244|PDB:4MZ7}.
STRAND 525 530 {ECO:0000244|PDB:4MZ7}.
HELIX 534 536 {ECO:0000244|PDB:4MZ7}.
STRAND 539 541 {ECO:0000244|PDB:4MZ7}.
STRAND 545 555 {ECO:0000244|PDB:4MZ7}.
HELIX 559 576 {ECO:0000244|PDB:4MZ7}.
HELIX 584 587 {ECO:0000244|PDB:4MZ7}.
TURN 589 591 {ECO:0000244|PDB:4MZ7}.
HELIX 592 594 {ECO:0000244|PDB:4MZ7}.
TURN 596 598 {ECO:0000244|PDB:4BZB}.
HELIX 611 613 {ECO:0000244|PDB:4CC9}.
HELIX 617 622 {ECO:0000244|PDB:4CC9}.
SEQUENCE 626 AA; 72201 MW; 559CB6BB029E6558 CRC64;
MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE
EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTMKVIND
PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH
ALGEKQPELQ ISERDVLCVQ IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM
FEHLINSNGI KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI
VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC ARDKEVGNLY
DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT GAGGKKYRIS TAIDDMEAYT
KLTDNIFLEI LYSTDPKLKD AREILKQIEY RNLFKYVGET QPTGQIKIKR EDYESLPKEV
ASAKPKVLLD VKLKAEDFIV DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL
LPEKFAEQLI RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND
STSVQNPTRL REASKSRVQL FKDDPM


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