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Q9Y3Z3

- SAMH1_HUMAN

UniProt

Q9Y3Z3 - SAMH1_HUMAN

Protein

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene

SAMHD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (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.4 Publications

    Catalytic activityi

    dNTP + H2O = Deoxynucleoside + triphosphate.2 Publications

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161dGTP 1
    Binding sitei119 – 1191dGTP 2; via amide nitrogen; shared with neighboring subunit
    Binding sitei149 – 1491Substrate
    Binding sitei164 – 1641Substrate
    Metal bindingi167 – 1671Zinc; via tele nitrogen2 Publications
    Metal bindingi206 – 2061Zinc; via tele nitrogen2 Publications
    Metal bindingi207 – 2071Zinc2 Publications
    Binding sitei210 – 2101Substrate
    Active sitei233 – 23311 Publication
    Metal bindingi311 – 3111Zinc2 Publications
    Binding sitei315 – 3151Substrate
    Binding sitei319 – 3191Substrate
    Binding sitei333 – 3331dGTP 2
    Binding sitei358 – 3581dGTP 2
    Binding sitei366 – 3661Substrate
    Binding sitei376 – 3761dGTP 2; shared with neighboring subunit
    Binding sitei377 – 3771dGTP 2; shared with neighboring subunit
    Binding sitei451 – 4511dGTP 1; shared with neighboring subunit
    Binding sitei455 – 4551dGTP 1; shared with neighboring subunit
    Binding sitei523 – 5231dGTP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 1459dGTP 1
    Nucleotide bindingi352 – 3543dGTP 2

    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. protein binding Source: IntAct
    6. RNA binding Source: UniProtKB
    7. 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. immune response Source: UniProtKB
    5. innate immune response Source: UniProtKB-KW
    6. protein homotetramerization Source: UniProtKB
    7. 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):
    Dendritic cell-derived IFNG-induced protein
    Short name:
    DCIP
    Monocyte protein 5
    Short name:
    MOP-5
    SAM domain and HD domain-containing protein 1
    Gene namesi
    Name:SAMHD1
    Synonyms:MOP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15925. SAMHD1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. intracellular Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231H → P in AGS5. 1 Publication
    VAR_058481
    Natural varianti143 – 1431R → C in AGS5. 1 Publication
    VAR_058482
    Natural varianti143 – 1431R → H in AGS5. 1 Publication
    VAR_058483
    Natural varianti145 – 1451R → Q in AGS5. 1 Publication
    VAR_058484
    Natural varianti167 – 1671H → Y in AGS5. 1 Publication
    VAR_070633
    Natural varianti201 – 2011I → N in AGS5 and CHBL2. 2 Publications
    VAR_058485
    Natural varianti209 – 2091G → S in AGS5. 1 Publication
    VAR_058486
    Natural varianti254 – 2541M → V in AGS5. 1 Publication
    VAR_058487
    Natural varianti290 – 2901R → H in AGS5. 1 Publication
    VAR_070634
    Natural varianti369 – 3691L → S in AGS5. 1 Publication
    VAR_058488
    Natural varianti385 – 3851M → V in AGS5. 1 Publication
    VAR_058489
    Chilblain lupus 2 (CHBL2) [MIM:614415]: A rare cutaneous form of lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure at temperatures less than 10 degrees centigrade.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011I → N in AGS5 and CHBL2. 2 Publications
    VAR_058485

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371D → A: Impairs homotetramerization and nearly abolishes enzyme activity. 1 Publication
    Mutagenesisi142 – 1421Q → E: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-145. 1 Publication
    Mutagenesisi145 – 1451R → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-145. 1 Publication
    Mutagenesisi149 – 1491Q → A: Abolishes enzyme activity; when associated with A-319. 1 Publication
    Mutagenesisi206 – 2072HD → RN: Abolishes zinc binding and enzyme activity.
    Mutagenesisi312 – 3121K → A: Abolishes enzyme activity; when associated with A-315 and A-366.
    Mutagenesisi315 – 3151Y → A: Abolishes enzyme activity; when associated with A-312 and A-366.
    Mutagenesisi319 – 3191D → A: Abolishes enzyme activity; when associated with A-149. 1 Publication
    Mutagenesisi330 – 3301D → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-358. 1 Publication
    Mutagenesisi333 – 3331R → E: Decreases enzyme activity. Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-451. 2 Publications
    Mutagenesisi352 – 3521R → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-376 and A-377. 1 Publication
    Mutagenesisi358 – 3581N → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-330. 1 Publication
    Mutagenesisi361 – 3611D → R: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-364. 1 Publication
    Mutagenesisi364 – 3641H → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with R-361. 1 Publication
    Mutagenesisi366 – 3661R → A: Abolishes enzyme activity; when associated with A-312 and A-315. 1 Publication
    Mutagenesisi370 – 3701H → A: Abolishes enzyme activity; when associated with G-374. 1 Publication
    Mutagenesisi374 – 3741Y → G: Abolishes enzyme activity; when associated with A-370. 1 Publication
    Mutagenesisi376 – 3761H → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-377.
    Mutagenesisi377 – 3771K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-376.
    Mutagenesisi451 – 4511R → E: Impairs homotetramerization and abolishes enzyme activity. 1 Publication
    Mutagenesisi534 – 5341K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and D-540. 1 Publication
    Mutagenesisi537 – 5371V → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-534 and D-540. 1 Publication
    Mutagenesisi540 – 5401L → D: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and A-534. 1 Publication
    Mutagenesisi609 – 6091R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication
    Mutagenesisi617 – 6171R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication
    Mutagenesisi622 – 6221K → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication

    Keywords - Diseasei

    Aicardi-Goutieres syndrome, Disease mutation

    Organism-specific databases

    MIMi612952. phenotype.
    614415. phenotype.
    Orphaneti51. Aicardi-Goutieres syndrome.
    90280. Chilblain lupus.
    PharmGKBiPA34938.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 626626Deoxynucleoside triphosphate triphosphohydrolase SAMHD1PRO_0000153732Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei18 – 181PhosphoserineBy similarity
    Modified residuei21 – 211PhosphothreonineBy similarity
    Modified residuei592 – 5921Phosphothreonine5 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.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y3Z3.
    PaxDbiQ9Y3Z3.
    PeptideAtlasiQ9Y3Z3.
    PRIDEiQ9Y3Z3.

    PTM databases

    PhosphoSiteiQ9Y3Z3.

    Expressioni

    Tissue specificityi

    Expressed in heart, skeletal muscle, spleen, liver, small intestine, placenta, lung and peripheral blood leukocytes. No expression is seen in brain and thymus.1 Publication

    Inductioni

    By IFNG/IFN-gamma. Up-regulated in TNF treated lung fibroblasts.2 Publications

    Gene expression databases

    ArrayExpressiQ9Y3Z3.
    BgeeiQ9Y3Z3.
    CleanExiHS_SAMHD1.
    GenevestigatoriQ9Y3Z3.

    Organism-specific databases

    HPAiHPA047072.

    Interactioni

    Subunit structurei

    Homodimer. Homotetramer; in dGTP-bound form. After HIV infection, interacts (via C-terminus) with a ubiquitin-protein ligase complex containing VPRBP and the viral accessory protein Vpx.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DYSFO759232EBI-1054601,EBI-2799016
    TIRAPP587532EBI-1054601,EBI-528644

    Protein-protein interaction databases

    BioGridi117436. 42 interactions.
    DIPiDIP-50704N.
    IntActiQ9Y3Z3. 8 interactions.
    MINTiMINT-2823520.
    STRINGi9606.ENSP00000262878.

    Structurei

    Secondary structure

    1
    626
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 443
    Helixi46 – 5712
    Helixi62 – 709
    Turni75 – 806
    Helixi83 – 886
    Helixi94 – 10815
    Turni109 – 1124
    Beta strandi116 – 1205
    Turni121 – 1233
    Beta strandi124 – 1285
    Helixi130 – 1367
    Helixi139 – 1424
    Helixi143 – 1464
    Beta strandi147 – 1504
    Helixi151 – 1555
    Helixi164 – 18522
    Helixi187 – 1893
    Helixi193 – 20513
    Turni206 – 2094
    Turni212 – 2143
    Helixi215 – 2195
    Helixi221 – 2255
    Helixi233 – 24715
    Helixi250 – 2567
    Helixi261 – 27313
    Beta strandi288 – 2903
    Helixi292 – 2998
    Beta strandi300 – 3023
    Turni304 – 3063
    Helixi310 – 32314
    Helixi331 – 3366
    Beta strandi338 – 3436
    Beta strandi346 – 3527
    Helixi353 – 3553
    Helixi356 – 37217
    Turni373 – 3753
    Helixi377 – 39317
    Turni394 – 3963
    Helixi402 – 4043
    Turni409 – 4113
    Helixi412 – 4143
    Helixi416 – 4194
    Helixi425 – 4328
    Helixi436 – 4383
    Helixi439 – 44911
    Beta strandi455 – 4606
    Helixi470 – 4756
    Helixi476 – 4827
    Helixi495 – 4973
    Beta strandi498 – 50912
    Helixi514 – 5174
    Beta strandi519 – 5224
    Beta strandi525 – 5306
    Helixi534 – 5363
    Beta strandi539 – 5413
    Beta strandi545 – 55511
    Helixi559 – 57618
    Helixi584 – 5874
    Turni589 – 5913
    Helixi592 – 5943
    Turni596 – 5983
    Helixi611 – 6133
    Helixi617 – 6226

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E8ONMR-A23-118[»]
    3U1NX-ray3.10A/B/C/D120-626[»]
    4BZBX-ray1.83A/B/C/D113-626[»]
    4BZCX-ray2.88A/B/C/D113-626[»]
    4CC9X-ray2.47C582-626[»]
    4MZ7X-ray1.80A/B109-626[»]
    ProteinModelPortaliQ9Y3Z3.
    SMRiQ9Y3Z3. Positions 24-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3Z3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 11066SAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini164 – 319156HDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni309 – 3157Substrate binding
    Regioni370 – 3756Substrate binding

    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.
    HOVERGENiHBG054208.
    InParanoidiQ9Y3Z3.
    OMAiGNIIEIM.
    OrthoDBiEOG7SJD4J.
    PhylomeDBiQ9Y3Z3.
    TreeFamiTF316113.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y3Z3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV    50
    CSFLRRGGFE EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL 100
    LSYIQRLVQI HVDTMKVIND PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL 150
    GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH ALGEKQPELQ ISERDVLCVQ 200
    IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM FEHLINSNGI 250
    KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI 300
    VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC 350
    ARDKEVGNLY DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT 400
    GAGGKKYRIS TAIDDMEAYT KLTDNIFLEI LYSTDPKLKD AREILKQIEY 450
    RNLFKYVGET QPTGQIKIKR EDYESLPKEV ASAKPKVLLD VKLKAEDFIV 500
    DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL LPEKFAEQLI 550
    RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND 600
    STSVQNPTRL REASKSRVQL FKDDPM 626
    Length:626
    Mass (Da):72,201
    Last modified:August 13, 2002 - v2
    Checksum:i559CB6BB029E6558
    GO
    Isoform 2 (identifier: Q9Y3Z3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         113-136: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:602
    Mass (Da):69,444
    Checksum:i1C1BEBBF78784F57
    GO
    Isoform 3 (identifier: Q9Y3Z3-3) [UniParc]FASTAAdd to Basket

    Also known as: delta8-9

    The sequence of this isoform differs from the canonical sequence as follows:
         285-354: Missing.

    Note: Catalytically inactive.

    Show »
    Length:556
    Mass (Da):63,676
    Checksum:iD9C169FB9758B462
    GO
    Isoform 4 (identifier: Q9Y3Z3-4) [UniParc]FASTAAdd to Basket

    Also known as: delta14

    The sequence of this isoform differs from the canonical sequence as follows:
         502-536: Missing.

    Note: Catalytically inactive.

    Show »
    Length:591
    Mass (Da):68,122
    Checksum:iE31590B50311FD5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti394 – 3941D → G in AAF32407. (PubMed:11064105)Curated
    Sequence conflicti394 – 3941D → G in CAB43368. (PubMed:11230166)Curated
    Sequence conflicti404 – 4041G → E in AAH36450. (PubMed:15489334)Curated
    Sequence conflicti494 – 4941K → E in AAF32407. (PubMed:11064105)Curated
    Sequence conflicti494 – 4941K → E in CAB43368. (PubMed:11230166)Curated
    Sequence conflicti546 – 5461A → V in AAH36450. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti123 – 1231H → P in AGS5. 1 Publication
    VAR_058481
    Natural varianti143 – 1431R → C in AGS5. 1 Publication
    VAR_058482
    Natural varianti143 – 1431R → H in AGS5. 1 Publication
    VAR_058483
    Natural varianti145 – 1451R → Q in AGS5. 1 Publication
    VAR_058484
    Natural varianti167 – 1671H → Y in AGS5. 1 Publication
    VAR_070633
    Natural varianti201 – 2011I → N in AGS5 and CHBL2. 2 Publications
    VAR_058485
    Natural varianti209 – 2091G → S in AGS5. 1 Publication
    VAR_058486
    Natural varianti254 – 2541M → V in AGS5. 1 Publication
    VAR_058487
    Natural varianti290 – 2901R → H in AGS5. 1 Publication
    VAR_070634
    Natural varianti369 – 3691L → S in AGS5. 1 Publication
    VAR_058488
    Natural varianti385 – 3851M → V in AGS5. 1 Publication
    VAR_058489

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei113 – 13624Missing in isoform 2. 1 PublicationVSP_037841Add
    BLAST
    Alternative sequencei285 – 35470Missing in isoform 3. CuratedVSP_046561Add
    BLAST
    Alternative sequencei502 – 53635Missing in isoform 4. CuratedVSP_046562Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF228421 mRNA. Translation: AAF32407.1.
    AB013847 mRNA. Translation: BAB18916.1.
    AL050267 mRNA. Translation: CAB43368.1.
    AK027811 mRNA. Translation: BAB55386.1.
    AK304187 mRNA. Translation: BAG65067.1.
    AL079335, AL365505 Genomic DNA. Translation: CAI42293.1.
    AL365505, AL079335 Genomic DNA. Translation: CAI95179.1.
    CH471077 Genomic DNA. Translation: EAW76090.1.
    CH471077 Genomic DNA. Translation: EAW76091.1.
    BC036450 mRNA. Translation: AAH36450.1.
    CCDSiCCDS13288.1. [Q9Y3Z3-1]
    PIRiT08686.
    RefSeqiNP_056289.2. NM_015474.3. [Q9Y3Z3-1]
    XP_005260441.1. XM_005260384.1. [Q9Y3Z3-4]
    UniGeneiHs.580681.

    Genome annotation databases

    EnsembliENST00000262878; ENSP00000262878; ENSG00000101347. [Q9Y3Z3-1]
    GeneIDi25939.
    KEGGihsa:25939.
    UCSCiuc002xgh.2. human. [Q9Y3Z3-1]

    Polymorphism databases

    DMDMi22257047.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF228421 mRNA. Translation: AAF32407.1 .
    AB013847 mRNA. Translation: BAB18916.1 .
    AL050267 mRNA. Translation: CAB43368.1 .
    AK027811 mRNA. Translation: BAB55386.1 .
    AK304187 mRNA. Translation: BAG65067.1 .
    AL079335 , AL365505 Genomic DNA. Translation: CAI42293.1 .
    AL365505 , AL079335 Genomic DNA. Translation: CAI95179.1 .
    CH471077 Genomic DNA. Translation: EAW76090.1 .
    CH471077 Genomic DNA. Translation: EAW76091.1 .
    BC036450 mRNA. Translation: AAH36450.1 .
    CCDSi CCDS13288.1. [Q9Y3Z3-1 ]
    PIRi T08686.
    RefSeqi NP_056289.2. NM_015474.3. [Q9Y3Z3-1 ]
    XP_005260441.1. XM_005260384.1. [Q9Y3Z3-4 ]
    UniGenei Hs.580681.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E8O NMR - A 23-118 [» ]
    3U1N X-ray 3.10 A/B/C/D 120-626 [» ]
    4BZB X-ray 1.83 A/B/C/D 113-626 [» ]
    4BZC X-ray 2.88 A/B/C/D 113-626 [» ]
    4CC9 X-ray 2.47 C 582-626 [» ]
    4MZ7 X-ray 1.80 A/B 109-626 [» ]
    ProteinModelPortali Q9Y3Z3.
    SMRi Q9Y3Z3. Positions 24-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117436. 42 interactions.
    DIPi DIP-50704N.
    IntActi Q9Y3Z3. 8 interactions.
    MINTi MINT-2823520.
    STRINGi 9606.ENSP00000262878.

    PTM databases

    PhosphoSitei Q9Y3Z3.

    Polymorphism databases

    DMDMi 22257047.

    Proteomic databases

    MaxQBi Q9Y3Z3.
    PaxDbi Q9Y3Z3.
    PeptideAtlasi Q9Y3Z3.
    PRIDEi Q9Y3Z3.

    Protocols and materials databases

    DNASUi 25939.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262878 ; ENSP00000262878 ; ENSG00000101347 . [Q9Y3Z3-1 ]
    GeneIDi 25939.
    KEGGi hsa:25939.
    UCSCi uc002xgh.2. human. [Q9Y3Z3-1 ]

    Organism-specific databases

    CTDi 25939.
    GeneCardsi GC20M035518.
    GeneReviewsi SAMHD1.
    HGNCi HGNC:15925. SAMHD1.
    HPAi HPA047072.
    MIMi 606754. gene.
    612952. phenotype.
    614415. phenotype.
    neXtProti NX_Q9Y3Z3.
    Orphaneti 51. Aicardi-Goutieres syndrome.
    90280. Chilblain lupus.
    PharmGKBi PA34938.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1078.
    HOVERGENi HBG054208.
    InParanoidi Q9Y3Z3.
    OMAi GNIIEIM.
    OrthoDBi EOG7SJD4J.
    PhylomeDBi Q9Y3Z3.
    TreeFami TF316113.

    Miscellaneous databases

    EvolutionaryTracei Q9Y3Z3.
    GeneWikii SAMHD1.
    GenomeRNAii 25939.
    NextBioi 47504.
    PROi Q9Y3Z3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3Z3.
    Bgeei Q9Y3Z3.
    CleanExi HS_SAMHD1.
    Genevestigatori Q9Y3Z3.

    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. "Identification of human homologue of mouse IFN-gamma induced protein from human dendritic cells."
      Li N., Zhang W., Cao X.
      Immunol. Lett. 74:221-224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
      Tissue: Brain.
    2. "Molecular and biological characterization of a novel monocyte protein, MOP-5."
      Takayama K., Yoshimoto M.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Platelet.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Trachea.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      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.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Dendritic cell-derived interferon-gamma-induced protein mediates tumor necrosis factor-alpha stimulation of human lung fibroblasts."
      Liao W., Bao Z., Cheng C., Mok Y.-K., Wong W.S.
      Proteomics 8:2640-2650(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Cerebral arterial stenoses and stroke: novel features of Aicardi-Goutieres syndrome caused by the Arg164X mutation in SAMHD1 are associated with altered cytokine expression."
      Thiele H., du Moulin M., Barczyk K., George C., Schwindt W., Nurnberg G., Frosch M., Kurlemann G., Roth J., Nurnberg P., Rutsch F.
      Hum. Mutat. 31:E1836-E1850(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AGS5.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Identification and characterization of naturally occurring splice variants of SAMHD1."
      Welbourn S., Miyagi E., White T.E., Diaz-Griffero F., Strebel K.
      Retrovirology 9:86-86(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).
    19. "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)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 23-118.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 120-626, CATALYTIC ACTIVITY, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE, ENZYME REGULATION, UBIQUITINATION, FUNCTION.
    21. "Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase."
      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.
      Nat. Commun. 4:2722-2722(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 109-626 IN COMPLEX WITH ATP; GTP AND ZINC, SUBUNIT, ENZYME REGULATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-137; GLN-142; ARG-145; ARG-333 AND ARG-451.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 113-626 IN COMPLEX WITH GTP AND ZINC, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF GLN-149; 206-HIS-ASP-207; 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, COFACTOR.
    23. "Structural basis of lentiviral subversion of a cellular protein degradation pathway."
      Schwefel D., Groom H.C., Boucherit V.C., Christodoulou E., Walker P.A., Stoye J.P., Bishop K.N., Taylor I.A.
      Nature 505:234-238(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 582-626 IN COMPLEX WITH VPRBP AND SIMIAN IMMUNODEFICIENCY VIRUS PROTEIN VPX, UBIQUITINATION, FUNCTION, MUTAGENESIS OF ARG-609; ARG-617 AND LYS-622.
    24. "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: VARIANTS AGS5 PRO-123; CYS-143; HIS-143; GLN-145; ASN-201; SER-209; VAL-254; SER-369 AND VAL-385, FUNCTION, SUBCELLULAR LOCATION.
    25. Cited for: VARIANTS AGS5 TYR-167 AND HIS-290.
    26. "Autosomal dominant inheritance of a heterozygous mutation in SAMHD1 causing familial chilblain lupus."
      Ravenscroft J.C., Suri M., Rice G.I., Szynkiewicz M., Crow Y.J.
      Am. J. Med. Genet. A 155:235-237(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CHBL2 ASN-201.

    Entry informationi

    Entry nameiSAMH1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3Z3
    Secondary accession number(s): B4E2A5
    , E1P5V2, Q5JXG8, Q8N491, Q9H004, Q9H005, Q9H3U9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3