{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9Y3Z3","secondaryAccessions":["B4E2A5","E1P5V2","Q5JXG8","Q8N491","Q9H004","Q9H005","Q9H3U9"],"uniProtkbId":"SAMH1_HUMAN","entryAudit":{"firstPublicDate":"2002-08-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-08-13","entryVersion":217,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22069334"}],"value":"Deoxynucleoside triphosphate triphosphohydrolase SAMHD1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"dNTPase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"}],"value":"3.1.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11064105"}],"value":"Dendritic cell-derived IFNG-induced protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11064105"}],"value":"DCIP"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.2"}],"value":"Monocyte protein 5"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.2"}],"value":"MOP-5"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"SAM domain and HD domain-containing protein 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29379009"}],"value":"hSAMHD1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:15925"}],"value":"SAMHD1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.2"}],"value":"MOP5"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60710"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19525956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21613998"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21720370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23364794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23602554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23858451"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24035396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25038827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26101257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27477283"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28229507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29610582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"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:22056990, PubMed:23601106, PubMed:23602554, 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:22056990, PubMed:23364794, PubMed:23601106, PubMed:23602554, PubMed:24336198, PubMed:25038827, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:24035396, PubMed:24217394, PubMed:29610582). 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:23601106, PubMed:23602554, 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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside + triphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46148"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:18274"},{"database":"ChEBI","id":"CHEBI:61560"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26101257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29610582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46149"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dATP + H2O = 2'-deoxyadenosine + triphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67648"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17256"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:61404"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29610582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67649"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dCTP + H2O = 2'-deoxycytidine + triphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:80083"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15698"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:61481"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:80084"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dGTP + H2O = 2'-deoxyguanosine + triphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17172"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:61429"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:15194"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTTP + H2O = thymidine + triphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:80079"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:18036"},{"database":"ChEBI","id":"CHEBI:37568"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:80080"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4BZB"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"}],"value":"Binds 1 Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22069334"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25267621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25288794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25760601"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29610582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"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:22069334, PubMed:25267621, PubMed:25288794, PubMed:25760601). Allosteric activation promotes the formation of highly active homotetramers (PubMed:22056990, PubMed:24141705, PubMed:24217394, PubMed:25267621, PubMed:25288794, PubMed:25760601). Phosphorylation at Thr-592 impairs homotetramerization, thereby inhibiting dNTPase activity, leading to reduced ability to restrict infection by viruses (PubMed:23601106, PubMed:26294762, PubMed:26431200, PubMed:29610582, PubMed:29670289)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25267621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25288794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25760601"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26101257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28229507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28871089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"Homodimer; in absence of GTP and dNTP (PubMed:24141705, PubMed:24217394, PubMed:25760601, PubMed:28229507). Homotetramer; in GTP- and dNTP-bound form (PubMed:23601106, PubMed:24141705, PubMed:24217394, PubMed:25267621, PubMed:25288794, PubMed:25760601, PubMed:26101257, PubMed:26294762, PubMed:26431200, PubMed:28229507). 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"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21613998"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21720370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336198"}],"value":"(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"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9Y3Z3","intActId":"EBI-1054601"},"interactantTwo":{"uniProtKBAccession":"Q08380","geneName":"LGALS3BP","intActId":"EBI-354956"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9Y3Z3","intActId":"EBI-1054601"},"interactantTwo":{"uniProtKBAccession":"Q9Y3Z3","geneName":"SAMHD1","intActId":"EBI-1054601"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9Y3Z3","intActId":"EBI-1054601"},"interactantTwo":{"uniProtKBAccession":"P58753","geneName":"TIRAP","intActId":"EBI-528644"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"}],"value":"Localizes to sites of DNA double-strand breaks in response to DNA damage"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19525956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23092512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23858451"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24035396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28229507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28871089"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9Y3Z3-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"3"},"synonyms":[{"value":"delta8-9"}],"isoformIds":["Q9Y3Z3-3"],"sequenceIds":["VSP_046561"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"synonyms":[{"value":"delta14"}],"isoformIds":["Q9Y3Z3-4"],"sequenceIds":["VSP_046562"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11064105"}],"value":"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)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11064105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18546154"}],"value":"By IFNG/IFN-gamma. Up-regulated in TNF treated lung fibroblasts"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29379009"}],"value":"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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23602554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29610582"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"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:23601106, PubMed:23602554, PubMed:26294762, PubMed:26431200, PubMed:31291580). 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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31291580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31548682"}],"value":"(Microbial infection) Phosphorylation at Thr-592 by Epstein-Barr virus kinase BGLF4 and human cytomegalovirus/HCMV UL97 leads to a reduced level of dCTPase and dTTPase activity and the loss of viral restriction"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21613998"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21720370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24336198"}],"value":"(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"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Aicardi-Goutieres syndrome 5","diseaseAccession":"DI-02499","acronym":"AGS5","description":"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.","diseaseCrossReference":{"database":"MIM","id":"612952"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19525956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20131292"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20842748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24035396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24183309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28229507"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Chilblain lupus 2","diseaseAccession":"DI-03338","acronym":"CHBL2","description":"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.","diseaseCrossReference":{"database":"MIM","id":"614415"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21204240"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Catalytically inactive"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Catalytically inactive"}],"commentType":"MISCELLANEOUS","molecule":"Isoform 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SAMHD1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22056990"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24141705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24217394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25267621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25288794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25760601"}],"value":"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:25267621, PubMed:25288794, PubMed:25760601)"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23601106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26294762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26431200"}],"value":"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)"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23364794"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25038827"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26101257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"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)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"BAG65067.1","note":"Unlikely isoform. 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