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Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1)

 SAMH1_MOUSE             Reviewed;         658 AA.
Q60710; E9Q0K6; F8WJE0; Q3U5X2; Q543A4; Q91VK8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-JUL-2018, sequence version 3.
13-FEB-2019, entry version 156.
RecName: Full=Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 {ECO:0000305};
Short=dNTPase {ECO:0000305};
EC=3.1.5.- {ECO:0000269|PubMed:29379009};
AltName: Full=Interferon-gamma-inducible protein Mg11 {ECO:0000303|PubMed:7884320};
AltName: Full=SAM domain and HD domain-containing protein 1 {ECO:0000305};
Short=mSAMHD1 {ECO:0000303|PubMed:29379009};
Name=Samhd1 {ECO:0000312|MGI:MGI:1927468};
Synonyms=Mg11 {ECO:0000303|PubMed:7884320};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-658 (ISOFORM 1).
TISSUE=Macrophage;
PubMed=7884320;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"Cloning and characterization of a novel cDNA that is IFN-gamma-
induced in mouse peritoneal macrophages and encodes a putative GTP-
binding protein.";
J. Leukoc. Biol. 57:477-483(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-658 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Ovary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-658 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-52 AND THR-634,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
INDUCTION.
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-52; SER-55;
THR-56 AND THR-634, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23972988; DOI=10.1016/j.celrep.2013.07.037;
Behrendt R., Schumann T., Gerbaulet A., Nguyen L.A., Schubert N.,
Alexopoulou D., Berka U., Lienenklaus S., Peschke K., Gibbert K.,
Wittmann S., Lindemann D., Weiss S., Dahl A., Naumann R., Dittmer U.,
Kim B., Mueller W., Gramberg T., Roers A.;
"Mouse SAMHD1 has antiretroviral activity and suppresses a spontaneous
cell-intrinsic antiviral response.";
Cell Rep. 4:689-696(2013).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND ALTERNATIVE SPLICING (ISOFORMS 1
AND 2).
PubMed=23872947; DOI=10.1038/emboj.2013.163;
Rehwinkel J., Maelfait J., Bridgeman A., Rigby R., Hayward B.,
Liberatore R.A., Bieniasz P.D., Towers G.J., Moita L.F., Crow Y.J.,
Bonthron D.T., Reis e Sousa C.;
"SAMHD1-dependent retroviral control and escape in mice.";
EMBO J. 32:2454-2462(2013).
[11]
FUNCTION, PHOSPHORYLATION AT THR-634, AND MUTAGENESIS OF THR-634.
PubMed=26667483; DOI=10.1186/s12977-015-0229-6;
Wittmann S., Behrendt R., Eissmann K., Volkmann B., Thomas D.,
Ebert T., Cribier A., Benkirane M., Hornung V., Bouzas N.F.,
Gramberg T.;
"Phosphorylation of murine SAMHD1 regulates its antiretroviral
activity.";
Retrovirology 12:103-103(2015).
[12]
FUNCTION.
PubMed=29669924; DOI=10.1073/pnas.1719771115;
Thientosapol E.S., Bosnjak D., Durack T., Stevanovski I.,
van Geldermalsen M., Holst J., Jahan Z., Shepard C., Weninger W.,
Kim B., Brink R., Jolly C.J.;
"SAMHD1 enhances immunoglobulin hypermutation by promoting
transversion mutation.";
Proc. Natl. Acad. Sci. U.S.A. 115:4921-4926(2018).
[13] {ECO:0000244|PDB:6BRG, ECO:0000244|PDB:6BRH, ECO:0000244|PDB:6BRK}
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
DGTP, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, ACTIVITY REGULATION, AND
MUTAGENESIS OF PHE-109; PHE-112 AND ARG-143.
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).
-!- FUNCTION: Isoform 1: 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 (By similarity).
Has deoxynucleoside triphosphate (dNTPase) activity, which is
required to restrict infection by viruses: 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:23972988,
PubMed:23872947, PubMed:26667483, PubMed:29379009). Likewise,
suppresses LINE-1 retrotransposon activity (PubMed:26667483). In
addition to virus restriction, dNTPase activity acts as a
regulator of DNA precursor pools by regulating dNTP pools (By
similarity). Phosphorylation at Thr-634 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
(By similarity). 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 (By similarity). 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 (By similarity). Ability to promote DNA end resection
at stalled replication forks is independent of dNTPase activity
(By similarity). Enhances immunoglobulin hypermutation in B-
lymphocytes by promoting transversion mutation (PubMed:29669924).
{ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:23872947,
ECO:0000269|PubMed:23972988, ECO:0000269|PubMed:26667483,
ECO:0000269|PubMed:29379009, ECO:0000269|PubMed:29669924}.
-!- 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:29379009};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9Y3Z3};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y3Z3};
-!- 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.
Allosteric activation promotes the formation of highly active
homotetramers. Isoform 1: Phosphorylation at Thr-634 impairs
homotetramerization, thereby inhibiting dNTPase activity, leading
to reduced ability to restrict infection by viruses.
{ECO:0000305|PubMed:29379009}.
-!- SUBUNIT: Homodimer; in absence of GTP and dNTP (By similarity).
Homotetramer; in GTP- and dNTP-bound form (PubMed:29379009).
Interacts with MRE11; leading to stimulate the exonuclease
activity of MRE11 (By similarity). Interacts with RBBP8/CtIP (By
similarity). {ECO:0000250|UniProtKB:Q9Y3Z3,
ECO:0000269|PubMed:29379009}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}.
Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites
of DNA double-strand breaks in response to DNA damage.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q60710-1; Sequence=Displayed;
Name=2;
IsoId=Q60710-2; Sequence=VSP_059661;
-!- INDUCTION: By interferon alpha, beta and gamma (IFN-alpha, IFN-
beta and IFN-gamma). {ECO:0000269|PubMed:19525956}.
-!- DOMAIN: In mouse, the SAM domain is required for deoxynucleoside
triphosphate (dNTPase) activity and ability to restrict infection
by viruses. It acts by capping allosteric sites.
{ECO:0000269|PubMed:29379009}.
-!- PTM: Isoform 1: Phosphorylation at Thr-634 by CDK1 acts as a
switch to control deoxynucleoside triphosphate (dNTPase)-dependent
and -independent functions (PubMed:26667483) (By similarity).
Phosphorylation at Thr-634 takes place in cycling cells: it
reduces the stability of the homotetramer, impairing the dNTPase
activity and subsequent ability to restrict infection by viruses
(Probable). It also inhibits ability to suppress LINE-1
retrotransposon activity (PubMed:26667483). In contrast,
phosphorylation at Thr-634 promotes DNA end resection at stalled
replication forks in response to DNA damage (By similarity).
{ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:26667483,
ECO:0000305|PubMed:26667483}.
-!- PTM: Isoform 2: Not phosphorylated by CDK1 at the C-terminus.
{ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile but show
increased cellular dNTP concentrations and impaired ability to
restrict retroviral replication in lymphocytes, macrophages and
dendritic cells (PubMed:23972988). Mice also diplay interferon
(IFN)-beta-dependent transcriptional up-regulation of type I IFN-
inducible genes in various cell types indicative of spontaneous
IFN production (PubMed:23972988, PubMed:23872947).
{ECO:0000269|PubMed:23872947, ECO:0000269|PubMed:23972988}.
-!- SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA66219.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA66219.1; Type=Frameshift; Positions=607; Evidence={ECO:0000305};
Sequence=AAH12721.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH67198.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC35801.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE30313.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE31954.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U15635; AAA66219.1; ALT_SEQ; mRNA.
EMBL; AK054490; BAC35801.1; ALT_INIT; mRNA.
EMBL; AK151335; BAE30313.1; ALT_INIT; mRNA.
EMBL; AK153390; BAE31954.1; ALT_INIT; mRNA.
EMBL; AL669828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012721; AAH12721.1; ALT_INIT; mRNA.
EMBL; BC067198; AAH67198.1; ALT_INIT; mRNA.
CCDS; CCDS16973.2; -. [Q60710-1]
CCDS; CCDS50783.1; -. [Q60710-2]
PIR; I49127; I49127.
RefSeq; NP_001132992.1; NM_001139520.1. [Q60710-2]
RefSeq; NP_061339.3; NM_018851.3. [Q60710-1]
UniGene; Mm.248478; -.
UniGene; Mm.468781; -.
PDB; 6BRG; X-ray; 3.50 A; A/B/C/D=1-658.
PDB; 6BRH; X-ray; 3.40 A; A/B=1-658.
PDB; 6BRK; X-ray; 3.50 A; A=1-658.
PDBsum; 6BRG; -.
PDBsum; 6BRH; -.
PDBsum; 6BRK; -.
ProteinModelPortal; Q60710; -.
SMR; Q60710; -.
BioGrid; 207791; 11.
IntAct; Q60710; 3.
MINT; Q60710; -.
STRING; 10090.ENSMUSP00000059717; -.
CarbonylDB; Q60710; -.
iPTMnet; Q60710; -.
PhosphoSitePlus; Q60710; -.
SwissPalm; Q60710; -.
EPD; Q60710; -.
jPOST; Q60710; -.
MaxQB; Q60710; -.
PaxDb; Q60710; -.
PeptideAtlas; Q60710; -.
PRIDE; Q60710; -.
DNASU; 56045; -.
Ensembl; ENSMUST00000057725; ENSMUSP00000059717; ENSMUSG00000027639. [Q60710-1]
Ensembl; ENSMUST00000088523; ENSMUSP00000085880; ENSMUSG00000027639. [Q60710-2]
GeneID; 56045; -.
KEGG; mmu:56045; -.
CTD; 25939; -.
MGI; MGI:1927468; Samhd1.
eggNOG; KOG2681; Eukaryota.
eggNOG; COG1078; LUCA.
GeneTree; ENSGT00390000013867; -.
HOGENOM; HOG000264286; -.
HOVERGEN; HBG054208; -.
InParanoid; Q60710; -.
KO; K22544; -.
OrthoDB; 835545at2759; -.
PhylomeDB; Q60710; -.
TreeFam; TF316113; -.
Reactome; R-MMU-8956319; Nucleobase catabolism.
ChiTaRS; Samhd1; mouse.
PMAP-CutDB; Q60710; -.
PRO; PR:Q60710; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027639; Expressed in 267 organ(s), highest expression level in decidua.
ExpressionAtlas; Q60710; baseline and differential.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0032567; F:dGTP binding; ISS: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; ISO:MGI.
GO; GO:0003676; F:nucleic acid binding; ISS:UniProtKB.
GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0046061; P:dATP catabolic process; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0009264; P:deoxyribonucleotide catabolic process; ISS:UniProtKB.
GO; GO:0006203; P:dGTP catabolic process; ISS:UniProtKB.
GO; GO:0110025; P:DNA strand resection involved in replication fork processing; ISS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:UniProtKB.
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; Allosteric enzyme; Alternative splicing;
Antiviral defense; Chromosome; Complete proteome; 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 1 658 Deoxynucleoside triphosphate
triphosphohydrolase SAMHD1.
/FTId=PRO_0000153733.
DOMAIN 77 142 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 196 348 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
NP_BIND 169 177 GTP. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
NP_BIND 395 397 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
REGION 341 347 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
REGION 413 418 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
ACT_SITE 265 265 {ECO:0000250|UniProtKB:Q9Y3Z3}.
METAL 199 199 Zinc; via tele nitrogen.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 238 238 Zinc; via tele nitrogen.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 239 239 Zinc. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 343 343 Zinc. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 148 148 GTP. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 151 151 dNTP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 181 181 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 196 196 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 242 242 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 347 347 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 351 351 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 365 365 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 401 401 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 409 409 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 419 419 dNTP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 420 420 dNTP; shared with neighboring subunit.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 494 494 GTP; shared with neighboring subunit.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 498 498 GTP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 565 565 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 52 52 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 56 56 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 634 634 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:26667483}.
CROSSLNK 509 509 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y3Z3}.
VAR_SEQ 625 658 DGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLKF -> QCG
AGEMAEDPDSIPSTQQPHAAHNQL (in isoform 2).
/FTId=VSP_059661.
MUTAGEN 109 109 F->L: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with C-112 and H-143.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 112 112 F->C: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with L-109 and H-143.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 143 143 R->H: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with L-109 and C-112.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 634 634 T->A,V: Increased ability to restrict
LINE-1 retrotransposon activity.
{ECO:0000269|PubMed:26667483}.
MUTAGEN 634 634 T->E: Mimicks phosphorylation state,
reduced ability to restrict LINE-1
retrotransposon activity.
{ECO:0000269|PubMed:26667483}.
CONFLICT 371 371 R -> L (in Ref. 2; BAE31954/BAE30313).
{ECO:0000305}.
HELIX 79 88 {ECO:0000244|PDB:6BRH}.
HELIX 94 102 {ECO:0000244|PDB:6BRH}.
HELIX 107 112 {ECO:0000244|PDB:6BRH}.
HELIX 115 121 {ECO:0000244|PDB:6BRH}.
HELIX 128 138 {ECO:0000244|PDB:6BRH}.
HELIX 144 146 {ECO:0000244|PDB:6BRG}.
STRAND 148 152 {ECO:0000244|PDB:6BRH}.
TURN 153 155 {ECO:0000244|PDB:6BRH}.
STRAND 156 160 {ECO:0000244|PDB:6BRH}.
HELIX 162 168 {ECO:0000244|PDB:6BRH}.
HELIX 171 174 {ECO:0000244|PDB:6BRH}.
HELIX 175 178 {ECO:0000244|PDB:6BRH}.
HELIX 183 187 {ECO:0000244|PDB:6BRH}.
HELIX 196 217 {ECO:0000244|PDB:6BRH}.
HELIX 219 221 {ECO:0000244|PDB:6BRH}.
HELIX 225 236 {ECO:0000244|PDB:6BRH}.
TURN 237 241 {ECO:0000244|PDB:6BRH}.
HELIX 247 251 {ECO:0000244|PDB:6BRH}.
HELIX 253 257 {ECO:0000244|PDB:6BRH}.
STRAND 259 261 {ECO:0000244|PDB:6BRK}.
HELIX 265 279 {ECO:0000244|PDB:6BRH}.
HELIX 282 288 {ECO:0000244|PDB:6BRH}.
HELIX 293 305 {ECO:0000244|PDB:6BRH}.
STRAND 320 322 {ECO:0000244|PDB:6BRH}.
HELIX 324 331 {ECO:0000244|PDB:6BRH}.
TURN 336 339 {ECO:0000244|PDB:6BRH}.
HELIX 342 355 {ECO:0000244|PDB:6BRH}.
HELIX 363 368 {ECO:0000244|PDB:6BRH}.
STRAND 370 378 {ECO:0000244|PDB:6BRH}.
STRAND 386 394 {ECO:0000244|PDB:6BRH}.
HELIX 396 398 {ECO:0000244|PDB:6BRH}.
HELIX 399 415 {ECO:0000244|PDB:6BRH}.
TURN 416 418 {ECO:0000244|PDB:6BRH}.
HELIX 420 436 {ECO:0000244|PDB:6BRH}.
TURN 437 439 {ECO:0000244|PDB:6BRH}.
HELIX 445 447 {ECO:0000244|PDB:6BRH}.
TURN 452 454 {ECO:0000244|PDB:6BRH}.
HELIX 455 457 {ECO:0000244|PDB:6BRH}.
HELIX 459 462 {ECO:0000244|PDB:6BRH}.
HELIX 469 475 {ECO:0000244|PDB:6BRH}.
HELIX 479 481 {ECO:0000244|PDB:6BRH}.
HELIX 482 492 {ECO:0000244|PDB:6BRH}.
STRAND 498 503 {ECO:0000244|PDB:6BRH}.
STRAND 505 508 {ECO:0000244|PDB:6BRH}.
HELIX 514 517 {ECO:0000244|PDB:6BRH}.
HELIX 518 524 {ECO:0000244|PDB:6BRH}.
HELIX 537 539 {ECO:0000244|PDB:6BRH}.
STRAND 540 546 {ECO:0000244|PDB:6BRH}.
STRAND 590 597 {ECO:0000244|PDB:6BRH}.
HELIX 601 617 {ECO:0000244|PDB:6BRH}.
SEQUENCE 658 AA; 75893 MW; 8ED07CE9EB6239D6 CRC64;
MDSLLGCGVS AAAREPVPRY LTSQPRVSEV AMQSAPLEQP AKRPRCDGSP RTPPSTPPAT
ANLSADDDFQ NTDLRTWEPE DVCSFLENRG FREKKVLDIF RDNKIAGSFL PFLDEDRLED
LGVSSLEERK KMIECIQQLS QSRIDLMKVF NDPIHGHIEF HPLLIRIIDT PQFQRLRYIK
QLGGGYYVFP GASHNRFEHS LGVGYLAGCL VRALAEKQPE LQISERDILC VQIAGLCHDL
GHGPFSHMFD GRFIPRARPE KKWKHEQGSI EMFEHLVNSN ELKLVMKNYG LVPEEDITFI
KEQIMGPPIT PVKDSLWPYK GRPATKSFLY EIVSNKRNGI DVDKWDYFAR DCHHLGIQNN
FDYKRFIKFA RICEVEYKVK EDKTYIRKVK HICSREKEVG NLYDMFHTRN CLHRRAYQHK
ISNLIDIMIT DAFLKADPYV EITGTAGKKF RISTAIDDME AFTKLTDNIF LEVLHSTDPQ
LSEAQSILRN IECRNLYKYL GETQPKREKI RKEEYERLPQ EVAKAKPEKA PDVELKAEDF
IVDVINVDYG MEDKNPIDRV HFYCKSNSKQ AVRINKEQVS QLLPEKFAEQ LIRVYCKKKD
GKSLDAAGKH FVQWCALRDF TKPQDGDIIA PLITPLKWNN KTSSCLQEVS KVKTCLKF


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Gentaur; yes we can

Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1694: Pyrimidine metabolism
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[Samhd1 Mg11] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1)
[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] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-)
[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.-)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[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)
[MRE11 HNGS1 MRE11A] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[Tgtp1 Ifggb5 Irgb6 Mg21] T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)
[Cdk1 Cdc2 Cdc2a Cdkn1] 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)
[Mre11 Mre11a] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (MmMRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[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)
[Irgm1 Ifi1 Iigp3 Irgm] Immunity-related GTPase family M protein 1 (EC 3.6.5.-) (Interferon-inducible GTPase 3) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47) (LRG-47)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[Cdk1 Cdc2 Cdc2a Cdkn1] 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)
[CDK1 CDC2 CDKN1] 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)
[TIRAP MAL] Toll/interleukin-1 receptor domain-containing adapter protein (TIR domain-containing adapter protein) (Adaptor protein Wyatt) (MyD88 adapter-like protein) (MyD88-2)
[CDK1 CDC2 CDKN1] 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)
[IFI30 GILT IP30] Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Legumaturain)
[Mre11 Mre11a] Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)
[IFI16 IFNGIP1] Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)
[] 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)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); 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) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[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)]
[RSAD2 CIG5] Radical S-adenosyl methionine domain-containing protein 2 (Cytomegalovirus-induced gene 5 protein) (Viperin) (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p14); 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) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Ifitm3] Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1)

Bibliography :