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Q9Y3Z3 (SAMH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Short name=dNTPase
EC=3.1.5.-
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 names
Name:SAMHD1
Synonyms:MOP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.20 Ref.23 Ref.24

Catalytic activity

dNTP + H2O = Deoxynucleoside + triphosphate. Ref.20 Ref.21

Cofactor

Binds 1 zinc ion per subunit. Ref.22

Enzyme regulation

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. Ref.20 Ref.21 Ref.22

Subunit structure

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. Ref.21 Ref.22

Subcellular location

Nucleus Ref.18 Ref.24.

Tissue specificity

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

Induction

By IFNG/IFN-gamma. Up-regulated in TNF treated lung fibroblasts. Ref.1 Ref.12 Ref.20 Ref.21 Ref.22

Post-translational modification

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. Ref.20 Ref.23

Involvement in disease

Aicardi-Goutieres syndrome 5 (AGS5) [MIM:612952]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.24 Ref.25

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

Sequence similarities

Belongs to the SAMHD1 family.

Contains 1 HD domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseAicardi-Goutieres syndrome
Disease mutation
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdATP catabolic process

Inferred from direct assay Ref.22. Source: UniProtKB

dGTP catabolic process

Inferred from direct assay Ref.21. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype Ref.24. Source: UniProtKB

immune response

Non-traceable author statement Ref.1. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

protein homotetramerization

Inferred from direct assay Ref.21. Source: UniProtKB

regulation of innate immune response

Inferred from mutant phenotype Ref.24. Source: UniProtKB

   Cellular_componentintracellular

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay Ref.24. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionRNA binding

Inferred from direct assay PubMed 22461318. Source: UniProtKB

dGTP binding

Inferred from direct assay Ref.22. Source: UniProtKB

dGTPase activity

Inferred from direct assay Ref.21. Source: UniProtKB

nucleic acid binding

Inferred from direct assay PubMed 22461318. Source: UniProtKB

phosphoric diester hydrolase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 21903422PubMed 23414517. Source: IntAct

zinc ion binding

Inferred from direct assay Ref.21. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3Z3-1)

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.
Isoform 2 (identifier: Q9Y3Z3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-136: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y3Z3-3)

Also known as: delta8-9;

The sequence of this isoform differs from the canonical sequence as follows:
     285-354: Missing.
Note: Catalytically inactive.
Isoform 4 (identifier: Q9Y3Z3-4)

Also known as: delta14;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
PRO_0000153732

Regions

Domain45 – 11066SAM
Domain164 – 319156HD
Nucleotide binding137 – 1459dGTP 1
Nucleotide binding352 – 3543dGTP 2
Region309 – 3157Substrate binding
Region370 – 3756Substrate binding

Sites

Active site2331 Probable
Metal binding1671Zinc; via tele nitrogen
Metal binding2061Zinc; via tele nitrogen
Metal binding2071Zinc
Metal binding3111Zinc
Binding site1161dGTP 1
Binding site1191dGTP 2; via amide nitrogen; shared with neighboring subunit
Binding site1491Substrate
Binding site1641Substrate
Binding site2101Substrate
Binding site3151Substrate
Binding site3191Substrate
Binding site3331dGTP 2
Binding site3581dGTP 2
Binding site3661Substrate
Binding site3761dGTP 2; shared with neighboring subunit
Binding site3771dGTP 2; shared with neighboring subunit
Binding site4511dGTP 1; shared with neighboring subunit
Binding site4551dGTP 1; shared with neighboring subunit
Binding site5231dGTP 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.13
Modified residue181Phosphoserine By similarity
Modified residue211Phosphothreonine By similarity
Modified residue5921Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.14 Ref.16

Natural variations

Alternative sequence113 – 13624Missing in isoform 2.
VSP_037841
Alternative sequence285 – 35470Missing in isoform 3.
VSP_046561
Alternative sequence502 – 53635Missing in isoform 4.
VSP_046562
Natural variant1231H → P in AGS5. Ref.24
VAR_058481
Natural variant1431R → C in AGS5. Ref.24
VAR_058482
Natural variant1431R → H in AGS5. Ref.24
VAR_058483
Natural variant1451R → Q in AGS5. Ref.24
VAR_058484
Natural variant1671H → Y in AGS5. Ref.25
VAR_070633
Natural variant2011I → N in AGS5 and CHBL2. Ref.24 Ref.26
VAR_058485
Natural variant2091G → S in AGS5. Ref.24
VAR_058486
Natural variant2541M → V in AGS5. Ref.24
VAR_058487
Natural variant2901R → H in AGS5. Ref.25
VAR_070634
Natural variant3691L → S in AGS5. Ref.24
VAR_058488
Natural variant3851M → V in AGS5. Ref.24
VAR_058489

Experimental info

Mutagenesis1371D → A: Impairs homotetramerization and nearly abolishes enzyme activity. Ref.21
Mutagenesis1421Q → E: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-145. Ref.21
Mutagenesis1451R → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-145. Ref.21
Mutagenesis1491Q → A: Abolishes enzyme activity; when associated with A-319. Ref.22
Mutagenesis206 – 2072HD → RN: Abolishes zinc binding and enzyme activity.
Mutagenesis3121K → A: Abolishes enzyme activity; when associated with A-315 and A-366.
Mutagenesis3151Y → A: Abolishes enzyme activity; when associated with A-312 and A-366.
Mutagenesis3191D → A: Abolishes enzyme activity; when associated with A-149. Ref.22
Mutagenesis3301D → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-358. Ref.22
Mutagenesis3331R → E: Decreases enzyme activity. Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-451. Ref.21 Ref.22
Mutagenesis3521R → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-376 and A-377. Ref.22
Mutagenesis3581N → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-330. Ref.22
Mutagenesis3611D → R: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-364. Ref.22
Mutagenesis3641H → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with R-361. Ref.22
Mutagenesis3661R → A: Abolishes enzyme activity; when associated with A-312 and A-315. Ref.22
Mutagenesis3701H → A: Abolishes enzyme activity; when associated with G-374. Ref.22
Mutagenesis3741Y → G: Abolishes enzyme activity; when associated with A-370. Ref.22
Mutagenesis3761H → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-377.
Mutagenesis3771K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-376.
Mutagenesis4511R → E: Impairs homotetramerization and abolishes enzyme activity. Ref.21
Mutagenesis5341K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and D-540. Ref.22
Mutagenesis5371V → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-534 and D-540. Ref.22
Mutagenesis5401L → D: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and A-534. Ref.22
Mutagenesis6091R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. Ref.23
Mutagenesis6171R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. Ref.23
Mutagenesis6221K → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. Ref.23
Sequence conflict3941D → G in AAF32407. Ref.1
Sequence conflict3941D → G in CAB43368. Ref.3
Sequence conflict4041G → E in AAH36450. Ref.7
Sequence conflict4941K → E in AAF32407. Ref.1
Sequence conflict4941K → E in CAB43368. Ref.3
Sequence conflict5461A → V in AAH36450. Ref.7

Secondary structure

............................................................................................................. 626
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 13, 2002. Version 2.
Checksum: 559CB6BB029E6558

FASTA62672,201
        10         20         30         40         50         60 
MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV CSFLRRGGFE 

        70         80         90        100        110        120 
EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL LSYIQRLVQI HVDTMKVIND 

       130        140        150        160        170        180 
PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH 

       190        200        210        220        230        240 
ALGEKQPELQ ISERDVLCVQ IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM 

       250        260        270        280        290        300 
FEHLINSNGI KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI 

       310        320        330        340        350        360 
VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC ARDKEVGNLY 

       370        380        390        400        410        420 
DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT GAGGKKYRIS TAIDDMEAYT 

       430        440        450        460        470        480 
KLTDNIFLEI LYSTDPKLKD AREILKQIEY RNLFKYVGET QPTGQIKIKR EDYESLPKEV 

       490        500        510        520        530        540 
ASAKPKVLLD VKLKAEDFIV DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL 

       550        560        570        580        590        600 
LPEKFAEQLI RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND 

       610        620 
STSVQNPTRL REASKSRVQL FKDDPM 

« Hide

Isoform 2 [UniParc].

Checksum: 1C1BEBBF78784F57
Show »

FASTA60269,444
Isoform 3 (delta8-9) [UniParc].

Checksum: D9C169FB9758B462
Show »

FASTA55663,676
Isoform 4 (delta14) [UniParc].

Checksum: E31590B50311FD5F
Show »

FASTA59168,122

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase."
Goldstone D.C., Ennis-Adeniran V., Hedden J.J., Groom H.C., Rice G.I., Christodoulou E., Walker P.A., Kelly G., Haire L.F., Yap M.W., de Carvalho L.P., Stoye J.P., Crow Y.J., Taylor I.A., Webb M.
Nature 480:379-382(2011) [PubMed] [Europe PMC] [Abstract]
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]"Mechanism of allosteric activation of SAMHD1 by dGTP."
Ji X., Wu Y., Yan J., Mehrens J., Yang H., DeLucia M., Hao C., Gronenborn A.M., Skowronski J., Ahn J., Xiong Y.
Nat. Struct. Mol. Biol. 20:1304-1309(2013) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-Goutieres syndrome."
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K., Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H., Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C., Ikonomidou C., Thomas K., Proud V. expand/collapse author list , Niemann F., Wieczorek D., Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P., Lee-Kirsch M.A.
Arthritis Rheum. 62:1469-1477(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13288.1. [Q9Y3Z3-1]
PIRT08686.
RefSeqNP_056289.2. NM_015474.3. [Q9Y3Z3-1]
XP_005260441.1. XM_005260384.1. [Q9Y3Z3-4]
UniGeneHs.580681.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9Y3Z3.
SMRQ9Y3Z3. Positions 24-599.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117436. 41 interactions.
DIPDIP-50704N.
IntActQ9Y3Z3. 6 interactions.
MINTMINT-2823520.
STRING9606.ENSP00000262878.

PTM databases

PhosphoSiteQ9Y3Z3.

Polymorphism databases

DMDM22257047.

Proteomic databases

MaxQBQ9Y3Z3.
PaxDbQ9Y3Z3.
PeptideAtlasQ9Y3Z3.
PRIDEQ9Y3Z3.

Protocols and materials databases

DNASU25939.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262878; ENSP00000262878; ENSG00000101347. [Q9Y3Z3-1]
GeneID25939.
KEGGhsa:25939.
UCSCuc002xgh.2. human. [Q9Y3Z3-1]

Organism-specific databases

CTD25939.
GeneCardsGC20M035518.
GeneReviewsSAMHD1.
HGNCHGNC:15925. SAMHD1.
HPAHPA047072.
MIM606754. gene.
612952. phenotype.
614415. phenotype.
neXtProtNX_Q9Y3Z3.
Orphanet51. Aicardi-Goutieres syndrome.
90280. Chilblain lupus.
PharmGKBPA34938.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1078.
HOVERGENHBG054208.
InParanoidQ9Y3Z3.
OMAGNIIEIM.
OrthoDBEOG7SJD4J.
PhylomeDBQ9Y3Z3.
TreeFamTF316113.

Gene expression databases

ArrayExpressQ9Y3Z3.
BgeeQ9Y3Z3.
CleanExHS_SAMHD1.
GenevestigatorQ9Y3Z3.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.10.3210.10. 2 hits.
InterProIPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
PfamPF01966. HD. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y3Z3.
GeneWikiSAMHD1.
GenomeRNAi25939.
NextBio47504.
PROQ9Y3Z3.
SOURCESearch...

Entry information

Entry nameSAMH1_HUMAN
AccessionPrimary (citable) accession number: Q9Y3Z3
Secondary accession number(s): B4E2A5 expand/collapse secondary AC list , E1P5V2, Q5JXG8, Q8N491, Q9H004, Q9H005, Q9H3U9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: August 13, 2002
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM