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Q60710

- SAMH1_MOUSE

UniProt

Q60710 - SAMH1_MOUSE

Protein

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene

Samhd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (13 Aug 2002)
      Previous versions | rss
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    Functioni

    Host restriction nuclease that blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May function by reducing the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. May play a role in mediating proinflammatory responses to TNF-alpha signaling By similarity.By similarity

    Catalytic activityi

    dNTP + H2O = Deoxynucleoside + triphosphate.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Allosterically stimulated by dGTP which binds in a cleft at the interface of the homodimer and promotes the formation of highly active homotetramers. Each allosteric site binds two molecules of dGTP (dGTP1 and dGTP 2) between adjoining subunits. Not activated by dATP, dCTP and dTTP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171dGTP 1By similarity
    Binding sitei120 – 1201dGTP 2; via amide nitrogen; shared with neighboring subunitBy similarity
    Binding sitei150 – 1501SubstrateBy similarity
    Binding sitei165 – 1651SubstrateBy similarity
    Metal bindingi168 – 1681Zinc; via tele nitrogenBy similarity
    Metal bindingi207 – 2071Zinc; via tele nitrogenBy similarity
    Metal bindingi208 – 2081ZincBy similarity
    Binding sitei211 – 2111SubstrateBy similarity
    Active sitei234 – 2341By similarity
    Metal bindingi312 – 3121ZincBy similarity
    Binding sitei316 – 3161SubstrateBy similarity
    Binding sitei320 – 3201SubstrateBy similarity
    Binding sitei334 – 3341dGTP 2By similarity
    Binding sitei370 – 3701dGTP 2By similarity
    Binding sitei378 – 3781SubstrateBy similarity
    Binding sitei388 – 3881dGTP 2; shared with neighboring subunitBy similarity
    Binding sitei389 – 3891dGTP 2; shared with neighboring subunitBy similarity
    Binding sitei463 – 4631dGTP 1; shared with neighboring subunitBy similarity
    Binding sitei467 – 4671dGTP 1; shared with neighboring subunitBy similarity
    Binding sitei534 – 5341dGTP 2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi138 – 1469dGTPBy similarity
    Nucleotide bindingi138 – 1469dGTP 1By similarity
    Nucleotide bindingi364 – 3663dGTP 2By similarity

    GO - Molecular functioni

    1. dGTPase activity Source: UniProtKB
    2. dGTP binding Source: UniProtKB
    3. nucleic acid binding Source: UniProtKB
    4. phosphoric diester hydrolase activity Source: InterPro
    5. RNA binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. dATP catabolic process Source: UniProtKB
    2. defense response to virus Source: UniProtKB
    3. dGTP catabolic process Source: UniProtKB
    4. innate immune response Source: UniProtKB-KW
    5. regulation of innate immune response Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC:3.1.5.-)
    Short name:
    dNTPase
    Alternative name(s):
    Interferon-gamma-inducible protein Mg11
    SAM domain and HD domain-containing protein 1
    Gene namesi
    Name:Samhd1
    Synonyms:Mg11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1927468. Samhd1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 627627Deoxynucleoside triphosphate triphosphohydrolase SAMHD1PRO_0000153733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei18 – 181Phosphoserine1 Publication
    Modified residuei21 – 211Phosphothreonine1 Publication
    Modified residuei603 – 6031Phosphothreonine2 Publications

    Post-translational modificationi

    Ubiquitinated and targeted for proteasomal degradation by a DCX (DDB1-CUL4-X-box) E3 ubiquitin ligase with the help of the viral accessory protein Vpx.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ60710.
    PaxDbiQ60710.
    PRIDEiQ60710.

    PTM databases

    PhosphoSiteiQ60710.

    Miscellaneous databases

    PMAP-CutDBQ60710.

    Expressioni

    Inductioni

    By interferon alpha, beta and gamma (IFN-alpha, IFN-beta and IFN-gamma).1 Publication

    Gene expression databases

    ArrayExpressiQ60710.
    BgeeiQ60710.
    CleanExiMM_SAMHD1.
    GenevestigatoriQ60710.

    Interactioni

    Subunit structurei

    Homodimer. Homotetramer; in dGTP-bound form By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ60710. 2 interactions.
    MINTiMINT-4133768.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60710.
    SMRiQ60710. Positions 24-608.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 11166SAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini165 – 320156HDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni310 – 3167Substrate bindingBy similarity
    Regioni382 – 3876Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the SAMHD1 family.Curated
    Contains 1 HD domain.Curated
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1078.
    HOGENOMiHOG000264286.
    HOVERGENiHBG054208.
    InParanoidiQ543A4.
    PhylomeDBiQ60710.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    1.10.3210.10. 2 hits.
    InterProiIPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    [Graphical view]
    PfamiPF01966. HD. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    SMARTiSM00471. HDc. 1 hit.
    SM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    PROSITEiPS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60710-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSAPLEQPA KRPRCDGSPR TPPSTPPATA NLSADDDFQN TDLRTWEPED    50
    VCSFLENRGF REKKVLDIFR DNKIAGSFLP FLDEDRLEDL GVSSLEERKK 100
    MIECIQQLSQ SRIDLMKVFN DPIHGHIEFH PLLIRIIDTP QFQRLRYIKQ 150
    LGGGYYVFPG ASHNRFEHSL GVGYLAGCLV RALAEKQPEL QISERDILCV 200
    QIAGLCHDLG HGPFSHMFDG RFIPRARPEK KWKHEQGSIE MFEHLVNSNE 250
    LKLVMKNYGL VPEEDITFIK EQIMGPPITP VKDSLWPYKG RPATKSFLYE 300
    IVSNKRNGID VDKWDYFARD CHHLGIQNNF DYKRFIKFAR ICEVEYKVKE 350
    DKTYIRKVKH ICSREKEVGN LYDMFHTRNC LHRRAYQHKI SNLIDIMITD 400
    AFLKADPYVE ITGTAGKKFR ISTAIDDMEA FTKLTDNIFL EVLHSTDPQL 450
    SEAQSILRNI ECRNLYKYLG ETQPKREKIR KEEYERLPQE VAKAKPEKAP 500
    DVELKAEDFI VDVINVDYGM EDKNPIDRVH FYCKSNSKQA VRINKEQVSQ 550
    LLPEKFAEQL IRVYCKKKDG KSLDAAGKHF VQWCALRDFT KPQDGDIIAP 600
    LITPLKWNNK TSSCLQEVSK VKTCLKF 627
    Length:627
    Mass (Da):72,650
    Last modified:August 13, 2002 - v2
    Checksum:iC68BB653C3F4B17C
    GO

    Sequence cautioni

    The sequence AAA66219.1 differs from that shown. Reason: Frameshift at position 576.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti340 – 3401R → L in BAE31954. (PubMed:16141072)Curated
    Sequence conflicti340 – 3401R → L in BAE30313. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15635 mRNA. Translation: AAA66219.1. Frameshift.
    AK054490 mRNA. Translation: BAC35801.1.
    AK151335 mRNA. Translation: BAE30313.1.
    AK153390 mRNA. Translation: BAE31954.1.
    AL669828 Genomic DNA. Translation: CAM15970.1.
    BC012721 mRNA. Translation: AAH12721.1.
    BC067198 mRNA. Translation: AAH67198.1.
    PIRiI49127.
    RefSeqiNP_001132992.1. NM_001139520.1.
    NP_061339.3. NM_018851.3.
    UniGeneiMm.248478.
    Mm.468781.

    Genome annotation databases

    GeneIDi56045.
    KEGGimmu:56045.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15635 mRNA. Translation: AAA66219.1 . Frameshift.
    AK054490 mRNA. Translation: BAC35801.1 .
    AK151335 mRNA. Translation: BAE30313.1 .
    AK153390 mRNA. Translation: BAE31954.1 .
    AL669828 Genomic DNA. Translation: CAM15970.1 .
    BC012721 mRNA. Translation: AAH12721.1 .
    BC067198 mRNA. Translation: AAH67198.1 .
    PIRi I49127.
    RefSeqi NP_001132992.1. NM_001139520.1.
    NP_061339.3. NM_018851.3.
    UniGenei Mm.248478.
    Mm.468781.

    3D structure databases

    ProteinModelPortali Q60710.
    SMRi Q60710. Positions 24-608.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q60710. 2 interactions.
    MINTi MINT-4133768.

    PTM databases

    PhosphoSitei Q60710.

    Proteomic databases

    MaxQBi Q60710.
    PaxDbi Q60710.
    PRIDEi Q60710.

    Protocols and materials databases

    DNASUi 56045.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 56045.
    KEGGi mmu:56045.

    Organism-specific databases

    CTDi 25939.
    MGIi MGI:1927468. Samhd1.

    Phylogenomic databases

    eggNOGi COG1078.
    HOGENOMi HOG000264286.
    HOVERGENi HBG054208.
    InParanoidi Q543A4.
    PhylomeDBi Q60710.

    Miscellaneous databases

    ChiTaRSi SAMHD1. mouse.
    NextBioi 311816.
    PMAP-CutDB Q60710.
    PROi Q60710.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60710.
    Bgeei Q60710.
    CleanExi MM_SAMHD1.
    Genevestigatori Q60710.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    1.10.3210.10. 2 hits.
    InterProi IPR003607. HD/PDEase_dom.
    IPR006674. HD_domain.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    [Graphical view ]
    Pfami PF01966. HD. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    SMARTi SM00471. HDc. 1 hit.
    SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    PROSITEi PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel cDNA that is IFN-gamma-induced in mouse peritoneal macrophages and encodes a putative GTP-binding protein."
      Lafuse W.P., Brown D., Castle L., Zwilling B.S.
      J. Leukoc. Biol. 57:477-483(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    2. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Ovary.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Mammary gland.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-21 AND THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as regulator of the innate immune response."
      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.
      Nat. Genet. 41:829-832(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiSAMH1_MOUSE
    AccessioniPrimary (citable) accession number: Q60710
    Secondary accession number(s): Q3U5X2, Q543A4, Q91VK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3