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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) (hSAMHD1)

 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.
22-APR-2020, entry version 187.
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, ACTIVITY 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, ACTIVITY 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]
SUBCELLULAR LOCATION, AND INTERACTION WITH CD81.
PubMed=28871089; DOI=10.1038/s41564-017-0019-0;
Rocha-Perugini V., Suarez H., Alvarez S., Lopez-Martin S., Lenzi G.M.,
Vences-Catalan F., Levy S., Kim B., Munoz-Fernandez M.A.,
Sanchez-Madrid F., Yanez-Mo M.;
"CD81 association with SAMHD1 enhances HIV-1 reverse transcription by
increasing dNTP levels.";
Nat. Microbiol. 2:1513-1522(2017).
[34]
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).
[35]
FUNCTION, ACTIVITY 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).
[36]
FUNCTION, ACTIVITY 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).
[37]
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).
[38]
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.
[39]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 120-626, CATALYTIC ACTIVITY,
ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE, ACTIVITY
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).
[40]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 109-626 IN COMPLEX WITH ATP; GTP
AND ZINC, SUBUNIT, ACTIVITY 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).
[41]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP AND
ZINC, SUBUNIT, ACTIVITY 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).
[42] {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, ACTIVITY 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).
[43]
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).
[44]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP,
SUBUNIT, AND ACTIVITY 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).
[45] {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 ACTIVITY 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).
[46] {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, ACTIVITY
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).
[47] {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,
ACTIVITY 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).
[48]
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).
[49]
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).
[50]
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).
[51]
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:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
deoxyribonucleoside + H(+) + triphosphate; Xref=Rhea:RHEA:46148,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036,
ChEBI:CHEBI:18274, ChEBI:CHEBI:61560;
Evidence={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};
-!- ACTIVITY 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). Interacts (via its C-terminus) with CD81.
{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:28871089,
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:
Q9Y3Z3; Q9Y3Z3; NbExp=7; IntAct=EBI-1054601, EBI-1054601;
Q9Y3Z3; O75923: DYSF; NbExp=2; IntAct=EBI-1054601, EBI-2799016;
Q9Y3Z3; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-1054601, EBI-354956;
Q9Y3Z3; 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,
ECO:0000269|PubMed:28871089}. 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;
Name=4; Synonyms=delta14;
IsoId=Q9Y3Z3-4; Sequence=VSP_046562;
-!- 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. {ECO:0000269|PubMed:21204240}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- MISCELLANEOUS: [Isoform 3]: Catalytically inactive. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 4]: Catalytically inactive. {ECO:0000305}.
-!- 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]
CCDS; CCDS86953.1; -. [Q9Y3Z3-4]
PIR; T08686; T08686.
RefSeq; NP_056289.2; NM_015474.3. [Q9Y3Z3-1]
RefSeq; XP_005260441.1; XM_005260384.3.
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.
PDB; 6CM2; X-ray; 2.14 A; A/B/C/D=113-626.
PDB; 6DW3; X-ray; 2.20 A; A/B/C/D=113-626.
PDB; 6DW4; X-ray; 1.99 A; A/B/C/D=113-626.
PDB; 6DW5; X-ray; 1.93 A; A/B/C/D=113-626.
PDB; 6DW7; X-ray; 2.50 A; A/B/C/D=113-626.
PDB; 6DWD; X-ray; 1.70 A; A/B/C/D=113-626.
PDB; 6DWJ; X-ray; 2.50 A; A/B/C/D=113-626.
PDB; 6DWK; X-ray; 2.30 A; A/B/C/D=113-626.
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; -.
PDBsum; 6CM2; -.
PDBsum; 6DW3; -.
PDBsum; 6DW4; -.
PDBsum; 6DW5; -.
PDBsum; 6DW7; -.
PDBsum; 6DWD; -.
PDBsum; 6DWJ; -.
PDBsum; 6DWK; -.
SMR; Q9Y3Z3; -.
BioGrid; 117436; 95.
DIP; DIP-50704N; -.
IntAct; Q9Y3Z3; 47.
MINT; Q9Y3Z3; -.
STRING; 9606.ENSP00000262878; -.
CarbonylDB; Q9Y3Z3; -.
iPTMnet; Q9Y3Z3; -.
PhosphoSitePlus; Q9Y3Z3; -.
BioMuta; SAMHD1; -.
DMDM; 22257047; -.
CPTAC; CPTAC-945; -.
EPD; Q9Y3Z3; -.
jPOST; Q9Y3Z3; -.
MassIVE; Q9Y3Z3; -.
PaxDb; Q9Y3Z3; -.
PeptideAtlas; Q9Y3Z3; -.
PRIDE; Q9Y3Z3; -.
ProteomicsDB; 86088; -. [Q9Y3Z3-1]
Antibodypedia; 26616; 414 antibodies.
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; -.
GeneCards; SAMHD1; -.
GeneReviews; SAMHD1; -.
HGNC; HGNC:15925; SAMHD1.
HPA; ENSG00000101347; Low tissue specificity.
MalaCards; SAMHD1; -.
MIM; 606754; gene.
MIM; 612952; phenotype.
MIM; 614415; phenotype.
neXtProt; NX_Q9Y3Z3; -.
OpenTargets; ENSG00000101347; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
Orphanet; 481662; Familial Chilblain lupus.
PharmGKB; PA34938; -.
eggNOG; KOG2681; Eukaryota.
eggNOG; COG1078; LUCA.
GeneTree; ENSGT00390000013867; -.
HOGENOM; CLU_026821_1_2_1; -.
InParanoid; Q9Y3Z3; -.
KO; K22544; -.
OMA; WSHVWDS; -.
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; -.
Pharos; Q9Y3Z3; Tbio.
PRO; PR:Q9Y3Z3; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; Q9Y3Z3; protein.
Bgee; ENSG00000101347; Expressed in bronchial epithelial cell and 233 other tissues.
ExpressionAtlas; Q9Y3Z3; baseline and differential.
Genevisible; Q9Y3Z3; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
GO; GO:0032567; F:dGTP binding; IDA:UniProtKB.
GO; GO:0008832; F:dGTPase activity; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0046061; P:dATP catabolic process; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0009264; P:deoxyribonucleotide catabolic process; IDA:UniProtKB.
GO; GO:0006203; P:dGTP catabolic process; IDA:UniProtKB.
GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IDA:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISS:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.150.50; -; 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;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
DNA replication; GTP-binding; Host-virus interaction; Hydrolase; Immunity;
Innate immunity; Isopeptide bond; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
CHAIN 1..626
/note="Deoxynucleoside triphosphate triphosphohydrolase
SAMHD1"
/id="PRO_0000153732"
DOMAIN 45..110
/note="SAM"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
DOMAIN 164..316
/note="HD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
NP_BIND 137..145
/note="GTP"
/evidence="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
/note="dNTP"
/evidence="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
/note="Substrate binding"
/evidence="ECO:0000269|PubMed:24141705"
REGION 370..375
/note="Substrate binding"
/evidence="ECO:0000269|PubMed:24141705"
ACT_SITE 233
/evidence="ECO:0000305|PubMed:22056990"
METAL 167
/note="Zinc; via tele nitrogen"
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200"
METAL 206
/note="Zinc; via tele nitrogen"
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200"
METAL 207
/note="Zinc"
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200"
METAL 311
/note="Zinc"
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394, ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:25760601, ECO:0000269|PubMed:26431200"
BINDING 116
/note="GTP"
/evidence="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
/note="dNTP; via amide nitrogen; shared with neighboring
subunit"
/evidence="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
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 164
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 210
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 315
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 319
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 333
/note="dNTP"
/evidence="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
/note="dNTP"
/evidence="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
/note="Substrate"
/evidence="ECO:0000269|PubMed:24141705"
BINDING 376
/note="dNTP; shared with neighboring subunit"
/evidence="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
/note="dNTP; shared with neighboring subunit"
/evidence="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
/note="GTP; shared with neighboring subunit"
/evidence="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
/note="GTP; shared with neighboring subunit"
/evidence="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
/note="dNTP"
/evidence="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
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:19413330, ECO:0000269|Ref.8"
MOD_RES 18
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q60710"
MOD_RES 21
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q60710"
MOD_RES 25
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q60710"
MOD_RES 33
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 93
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 592
/note="Phosphothreonine; by CDK1"
/evidence="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
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 469
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 492
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 622
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 285..354
/note="Missing (in isoform 3)"
/evidence="ECO:0000305"
/id="VSP_046561"
VAR_SEQ 502..536
/note="Missing (in isoform 4)"
/evidence="ECO:0000305"
/id="VSP_046562"
VARIANT 120..123
/note="Missing (in AGS5)"
/evidence="ECO:0000269|PubMed:24183309"
/id="VAR_078239"
VARIANT 123
/note="H -> P (in AGS5; loss of oligomerization; decreased
ability to restrict LINE-1 retrotransposon activity;
dbSNP:rs121434520)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507"
/id="VAR_058481"
VARIANT 143
/note="R -> C (in AGS5; loss of oligomerization;
dbSNP:rs387906948)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:28229507"
/id="VAR_058482"
VARIANT 143
/note="R -> H (in AGS5; loss of oligomerization; decreased
ability to restrict LINE-1 retrotransposon activity;
dbSNP:rs369035155)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507"
/id="VAR_058483"
VARIANT 145
/note="R -> Q (in AGS5; loss of oligomerization; decreased
ability to restrict LINE-1 retrotransposon activity;
dbSNP:rs515726145)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:28229507"
/id="VAR_058484"
VARIANT 167
/note="H -> Y (in AGS5; loss of function in defense
response to virus; loss of oligomerization; decreased
ability to restrict LINE-1 retrotransposon activity)"
/evidence="ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:28229507"
/id="VAR_070633"
VARIANT 201
/note="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)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:21204240, ECO:0000269|PubMed:24035396,
ECO:0000269|PubMed:24183309, ECO:0000269|PubMed:28229507"
/id="VAR_058485"
VARIANT 209
/note="G -> S (in AGS5; does not affect oligomerization;
decreased ability to restrict LINE-1 retrotransposon
activity; does not affect localization to nucleus;
dbSNP:rs121434516)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:28229507"
/id="VAR_058486"
VARIANT 254
/note="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)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507"
/id="VAR_058487"
VARIANT 290
/note="R -> H (in AGS5; loss of oligomerization; decreased
ability to restrict LINE-1 retrotransposon activity;
dbSNP:rs559553527)"
/evidence="ECO:0000269|PubMed:20131292,
ECO:0000269|PubMed:24035396, ECO:0000269|PubMed:28229507"
/id="VAR_070634"
VARIANT 369
/note="L -> S (in AGS5; loss of function in defense
response to virus; decreased oligomerization;
dbSNP:rs515726139)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:28229507"
/id="VAR_058488"
VARIANT 385
/note="M -> V (in AGS5; loss of function in defense
response to virus; loss of oligomerization;
dbSNP:rs515726140)"
/evidence="ECO:0000269|PubMed:19525956,
ECO:0000269|PubMed:24183309, ECO:0000269|PubMed:28229507"
/id="VAR_058489"
VARIANT 448
/note="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)"
/evidence="ECO:0000269|PubMed:24183309,
ECO:0000269|PubMed:28229507"
/id="VAR_078240"
VARIANT 548..626
/note="Missing (in AGS5; Does not affect dNTP regulation,
while affecting ability to promote DNA end resection at
stalled replication forks)"
/evidence="ECO:0000269|PubMed:29670289"
/id="VAR_080530"
MUTAGEN 77
/note="L->F: Increased stability of the tetramer and
increased deoxynucleoside triphosphate (dNTPase) activity;
when associated with F-77 and F-80 and R-111."
/evidence="ECO:0000269|PubMed:29379009"
MUTAGEN 80
/note="C->F: Increased stability of the tetramer and
increased deoxynucleoside triphosphate (dNTPase) activity;
when associated with F-77 and R-111."
/evidence="ECO:0000269|PubMed:29379009"
MUTAGEN 111
/note="H->R: Increased stability of the tetramer and
increased deoxynucleoside triphosphate (dNTPase) activity;
when associated with F-77 and F-80."
/evidence="ECO:0000269|PubMed:29379009"
MUTAGEN 137
/note="D->A: Impairs homotetramerization and nearly
abolishes dNTPase activity."
/evidence="ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25038827, ECO:0000269|PubMed:25288794"
MUTAGEN 142
/note="Q->E,A: Impairs homotetramerization and nearly
abolishes dNTPase activity; when associated with K-145."
/evidence="ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:25288794"
MUTAGEN 143
/note="R->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 145
/note="R->A: Impairs homotetramerization and nearly
abolishes dNTPase activity. Abolished ability to restrict
infection by viruses."
/evidence="ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:26431200"
MUTAGEN 145
/note="R->K: Impairs homotetramerization and nearly
abolishes dNTPase activity; when associated with E-145."
/evidence="ECO:0000269|PubMed:24217394"
MUTAGEN 149
/note="Q->A: Abolished dNTPase activity without affecting
homotetramerization. Abolished dNTPase activity; when
associated with A-319."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794"
MUTAGEN 164
/note="R->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 167
/note="H->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 206..207
/note="HD->RN: Abolishes zinc binding and dNTPase activity.
Does not affect ability to promote DNA end resection at
stalled replication forks."
/evidence="ECO:0000269|PubMed:21613998,
ECO:0000269|PubMed:23602554, ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:26101257, ECO:0000269|PubMed:28834754"
MUTAGEN 206
/note="H->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 207
/note="D->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 207
/note="D->N,A: Loss of dNTPase activity."
/evidence="ECO:0000269|PubMed:25038827,
ECO:0000269|PubMed:26101257"
MUTAGEN 210
/note="H->A: Abolished dNTPase activity without affecting
homotetramerization."
/evidence="ECO:0000269|PubMed:25288794"
MUTAGEN 215
/note="H->A: Abolished dNTPase activity without affecting
homotetramerization."
/evidence="ECO:0000269|PubMed:25288794"
MUTAGEN 226
/note="R->G: Loss of function in defense response to
virus."
/evidence="ECO:0000269|PubMed:28229507"
MUTAGEN 233
/note="H->A: Abolished dNTPase activity without affecting
homotetramerization. Abolished ability to restrict
infection by viruses."
/evidence="ECO:0000269|PubMed:25288794,
ECO:0000269|PubMed:26431200"
MUTAGEN 311
/note="D->A: Loss of function in defense response to virus.
Loss of dNTPase activity. Does not affect oligomerization."
/evidence="ECO:0000269|PubMed:25038827,
ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:28229507"
MUTAGEN 312
/note="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."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:29670289"
MUTAGEN 315
/note="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."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:26431200, ECO:0000269|PubMed:29670289"
MUTAGEN 319
/note="D->A: Abolishes dNTPase activity; when associated
with A-149."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 321
/note="H->A: Abolished ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 330
/note="D->A: Impaired homotetramerization and slightly
reduced dNTPase activity. Impaired homotetramerization and
reduced dNTPase activity; when associated with A-358."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794"
MUTAGEN 333
/note="R->E: Decreases dNTPase activity. Impairs
homotetramerization and nearly abolishes dNTPase activity;
when associated with E-451."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:24217394"
MUTAGEN 352
/note="R->A: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-376 and A-377."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 358
/note="N->A: Impaired homotetramerization and slightly
reduced dNTPase activity. Impaired homotetramerization and
reduced dNTPase activity A-330."
/evidence="ECO:0000269|PubMed:24141705,
ECO:0000269|PubMed:25288794"
MUTAGEN 361
/note="D->R: Impairs homotetramerization and nearly
abolishes dNTPase activity; when associated with K-364."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 364
/note="H->K: Impairs homotetramerization and nearly
abolishes dNTPase activity; when associated with R-361."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 366
/note="R->A: Abolishes dNTPase activity; when associated
with A-312 and A-315."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 370
/note="H->A: Abolishes dNTPase activity; when associated
with G-374."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 372
/note="R->D: Abolished homotetramerization and dNTPase
activity."
/evidence="ECO:0000269|PubMed:26431200"
MUTAGEN 374
/note="Y->G: Abolishes dNTPase activity; when associated
with A-370."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 375
/note="Q->A: Abolished dNTPase activity without affecting
homotetramerization."
/evidence="ECO:0000269|PubMed:25288794"
MUTAGEN 376
/note="H->A: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-352 and A-377."
MUTAGEN 377
/note="K->A: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-352 and A-376."
MUTAGEN 451
/note="R->E: Impairs homotetramerization and abolishes
dNTPase activity."
/evidence="ECO:0000269|PubMed:24217394,
ECO:0000269|PubMed:26101257"
MUTAGEN 534
/note="K->A: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-537 and D-540."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 537
/note="V->A: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-534 and D-540."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 540
/note="L->D: Impairs homotetramerization and abolishes
dNTPase activity; when associated with A-537 and A-534."
/evidence="ECO:0000269|PubMed:24141705"
MUTAGEN 548
/note="Q->A: Loss of function in defense response to virus.
Does not affect oligomerization. Retains dNTPase activity."
/evidence="ECO:0000269|PubMed:26101257,
ECO:0000269|PubMed:28229507"
MUTAGEN 592
/note="T->A,V: Impaired ability to promote DNA end
resection at stalled replication forks. Promotes dNTPase
activity and ability to restrict infection by viruses."
/evidence="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
/note="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."
/evidence="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
/note="P->A: Promotes ability to restrict infection by
viruses."
/evidence="ECO:0000269|PubMed:23601106"
MUTAGEN 609
/note="R->A,E: Abolishes proteasomal degradation triggered
by the viral accessory protein vpx."
/evidence="ECO:0000269|PubMed:24336198"
MUTAGEN 617
/note="R->A,E: Abolishes proteasomal degradation triggered
by the viral accessory protein vpx."
/evidence="ECO:0000269|PubMed:24336198"
MUTAGEN 622
/note="K->A,E: Abolishes proteasomal degradation triggered
by the viral accessory protein vpx."
/evidence="ECO:0000269|PubMed:24336198"
CONFLICT 394
/note="D -> G (in Ref. 1; AAF32407 and 3; CAB43368)"
/evidence="ECO:0000305"
CONFLICT 404
/note="G -> E (in Ref. 7; AAH36450)"
/evidence="ECO:0000305"
CONFLICT 494
/note="K -> E (in Ref. 1; AAF32407 and 3; CAB43368)"
/evidence="ECO:0000305"
CONFLICT 546
/note="A -> V (in Ref. 7; AAH36450)"
/evidence="ECO:0000305"
HELIX 42..44
/evidence="ECO:0000244|PDB:2E8O"
HELIX 46..57
/evidence="ECO:0000244|PDB:2E8O"
HELIX 62..70
/evidence="ECO:0000244|PDB:2E8O"
TURN 75..80
/evidence="ECO:0000244|PDB:2E8O"
HELIX 83..88
/evidence="ECO:0000244|PDB:2E8O"
HELIX 94..108
/evidence="ECO:0000244|PDB:2E8O"
TURN 109..112
/evidence="ECO:0000244|PDB:2E8O"
STRAND 116..120
/evidence="ECO:0000244|PDB:6DWD"
TURN 121..123
/evidence="ECO:0000244|PDB:6DWD"
STRAND 124..128
/evidence="ECO:0000244|PDB:6DWD"
HELIX 130..136
/evidence="ECO:0000244|PDB:6DWD"
HELIX 139..142
/evidence="ECO:0000244|PDB:6DWD"
HELIX 143..146
/evidence="ECO:0000244|PDB:6DWD"
STRAND 147..150
/evidence="ECO:0000244|PDB:4QFY"
HELIX 151..155
/evidence="ECO:0000244|PDB:6DWD"
HELIX 164..185
/evidence="ECO:0000244|PDB:6DWD"
HELIX 187..189
/evidence="ECO:0000244|PDB:6DWD"
HELIX 193..205
/evidence="ECO:0000244|PDB:6DWD"
TURN 206..209
/evidence="ECO:0000244|PDB:6DWD"
TURN 212..214
/evidence="ECO:0000244|PDB:6DWD"
HELIX 215..219
/evidence="ECO:0000244|PDB:6DWD"
HELIX 221..225
/evidence="ECO:0000244|PDB:6DWD"
STRAND 227..229
/evidence="ECO:0000244|PDB:6CM2"
HELIX 233..247
/evidence="ECO:0000244|PDB:6DWD"
HELIX 250..256
/evidence="ECO:0000244|PDB:6DWD"
HELIX 261..273
/evidence="ECO:0000244|PDB:6DWD"
STRAND 288..290
/evidence="ECO:0000244|PDB:6DWD"
HELIX 292..299
/evidence="ECO:0000244|PDB:6DWD"
STRAND 300..302
/evidence="ECO:0000244|PDB:6DWD"
TURN 304..306
/evidence="ECO:0000244|PDB:6DWD"
HELIX 310..323
/evidence="ECO:0000244|PDB:6DWD"
HELIX 331..336
/evidence="ECO:0000244|PDB:6DWD"
STRAND 338..343
/evidence="ECO:0000244|PDB:6DWD"
STRAND 346..352
/evidence="ECO:0000244|PDB:6DWD"
HELIX 353..355
/evidence="ECO:0000244|PDB:6DWD"
HELIX 356..372
/evidence="ECO:0000244|PDB:6DWD"
TURN 373..375
/evidence="ECO:0000244|PDB:6DWD"
HELIX 377..393
/evidence="ECO:0000244|PDB:6DWD"
TURN 394..396
/evidence="ECO:0000244|PDB:6DWD"
HELIX 402..404
/evidence="ECO:0000244|PDB:6DWD"
TURN 409..411
/evidence="ECO:0000244|PDB:6DWD"
HELIX 412..414
/evidence="ECO:0000244|PDB:6DWD"
HELIX 416..419
/evidence="ECO:0000244|PDB:6DWD"
HELIX 425..432
/evidence="ECO:0000244|PDB:6DWD"
HELIX 436..438
/evidence="ECO:0000244|PDB:6DWD"
HELIX 439..450
/evidence="ECO:0000244|PDB:6DWD"
STRAND 455..460
/evidence="ECO:0000244|PDB:6DWD"
STRAND 463..465
/evidence="ECO:0000244|PDB:4ZWG"
HELIX 470..475
/evidence="ECO:0000244|PDB:6DWD"
HELIX 476..482
/evidence="ECO:0000244|PDB:6DWD"
HELIX 495..497
/evidence="ECO:0000244|PDB:6DWD"
STRAND 498..509
/evidence="ECO:0000244|PDB:6DWD"
HELIX 514..517
/evidence="ECO:0000244|PDB:6DWD"
STRAND 520..522
/evidence="ECO:0000244|PDB:6DWD"
STRAND 525..530
/evidence="ECO:0000244|PDB:6DWD"
HELIX 534..536
/evidence="ECO:0000244|PDB:6DWD"
STRAND 541..543
/evidence="ECO:0000244|PDB:6DWD"
STRAND 545..555
/evidence="ECO:0000244|PDB:6DWD"
HELIX 559..576
/evidence="ECO:0000244|PDB:6DWD"
HELIX 584..587
/evidence="ECO:0000244|PDB:6DWD"
TURN 589..591
/evidence="ECO:0000244|PDB:6DWD"
HELIX 592..594
/evidence="ECO:0000244|PDB:6DWD"
HELIX 596..598
/evidence="ECO:0000244|PDB:6DWD"
HELIX 611..613
/evidence="ECO:0000244|PDB:4CC9"
HELIX 617..622
/evidence="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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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1694: Pyrimidine metabolism
WP2218: sGC
WP1676: Non-homologous end-joining
WP1624: Bacterial secretion system
WP1650: Fluorobenzoate degradation
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1693: Purine metabolism
WP1659: Glycine, serine and threonine metabolism
WP232: G Protein Signaling Pathways
WP1665: Limonene and pinene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1493: Carbon assimilation C4 pathway
WP731: Sterol regulatory element binding protein related
WP1566: Citrate cycle (TCA cycle)
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WP346: Protein Modifications
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Related Genes :
[SAMHD1 MOP5] 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) (hSAMHD1)
[Samhd1 Mg21] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1)
[samhd1] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-)
[SAMHD1] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-)
[SAMHD1 RCJMB04_17d8] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-)
[samhd1] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Zc3h12a Mcpip Mcpip1] Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)
[ARNTL BHLHE5 BMAL1 MOP3 PASD3] Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Basic-helix-loop-helix-PAS protein MOP3) (Brain and muscle ARNT-like 1) (Class E basic helix-loop-helix protein 5) (bHLHe5) (Member of PAS protein 3) (PAS domain-containing protein 3) (bHLH-PAS protein JAP3)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[TNFSF13B BAFF BLYS TALL1 TNFSF20 ZTNF4 UNQ401/PRO738] Tumor necrosis factor ligand superfamily member 13B (B lymphocyte stimulator) (BLyS) (B-cell-activating factor) (BAFF) (Dendritic cell-derived TNF-like molecule) (TNF- and APOL-related leukocyte expressed ligand 1) (TALL-1) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[hchA A8C65_13880 A9R57_25255 AMK83_16550 AWB10_10580 AWG90_013200 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI693_17820 CI694_25210 CIG45_02340 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO04_05510 DL800_09215 DLW88_16170 DND16_20085 DQE83_22775 DTL43_21780 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E4K55_17625 E5P22_21380 E5S46_06650 EAX79_27320 EC95NR1_00961 ED648_25045 EI028_00085 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC019_03873 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F18_11615 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FWK02_18105 FZ043_14730 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC10974_02300 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[CCL18 AMAC1 DCCK1 MIP4 PARC SCYA18] C-C motif chemokine 18 (Alternative macrophage activation-associated CC chemokine 1) (AMAC-1) (CC chemokine PARC) (Dendritic cell chemokine 1) (DC-CK1) (Macrophage inflammatory protein 4) (MIP-4) (Pulmonary and activation-regulated chemokine) (Small-inducible cytokine A18) [Cleaved into: CCL18(1-68); CCL18(3-69); CCL18(4-69)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[ZC3H12A MCPIP MCPIP1] Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)
[CD81 TAPA1 TSPAN28] CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (Tetraspanin-28) (Tspan-28) (CD antigen CD81)
[tubZ ATN07_33550 pBt156] Tubulin-like protein TubZ (EC 3.6.5.-) (FtsZ-like protein TubZ-Bt)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Cd81 Tapa1] CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (CD antigen CD81)
[Tgtp1 Ifggb5 Irgb6 Mg21] T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[CD209 CLEC4L] CD209 antigen (C-type lectin domain family 4 member L) (Dendritic cell-specific ICAM-3-grabbing non-integrin 1) (DC-SIGN) (DC-SIGN1) (CD antigen CD209)
[UL97] Serine/threonine protein kinase UL97 (EC 2.7.1.-) (Ganciclovir kinase) (HSRF3 protein)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

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