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Protein

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene

SAMHD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Zn2+1 PublicationNote: 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)DescriptionActionsGraphical viewLength
Binding sitei116dGTP 11
Binding sitei119dGTP 2; via amide nitrogen; shared with neighboring subunit1
Binding sitei149Substrate1
Binding sitei164Substrate1
Metal bindingi167Zinc; via tele nitrogen2 Publications1
Metal bindingi206Zinc; via tele nitrogen2 Publications1
Metal bindingi207Zinc2 Publications1
Binding sitei210Substrate1
Active sitei2331 Publication1
Metal bindingi311Zinc2 Publications1
Binding sitei315Substrate1
Binding sitei319Substrate1
Binding sitei333dGTP 21
Binding sitei358dGTP 21
Binding sitei366Substrate1
Binding sitei376dGTP 2; shared with neighboring subunit1
Binding sitei377dGTP 2; shared with neighboring subunit1
Binding sitei451dGTP 1; shared with neighboring subunit1
Binding sitei455dGTP 1; shared with neighboring subunit1
Binding sitei523dGTP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi137 – 145dGTP 19
Nucleotide bindingi352 – 354dGTP 23

GO - Molecular functioni

  • dGTPase activity Source: UniProtKB
  • dGTP binding Source: UniProtKB
  • nucleic acid binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • dATP catabolic process Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • dGTP catabolic process Source: UniProtKB
  • immune response Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • regulation of innate immune response Source: UniProtKB
  • type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101347-MONOMER.
ReactomeiR-HSA-909733. Interferon alpha/beta signaling.
SIGNORiQ9Y3Z3.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15925. SAMHD1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Aicardi-Goutieres syndrome 5 (AGS5)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612952
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058481123H → P in AGS5. 1 PublicationCorresponds to variant rs121434520dbSNPEnsembl.1
Natural variantiVAR_058482143R → C in AGS5. 1 PublicationCorresponds to variant rs387906948dbSNPEnsembl.1
Natural variantiVAR_058483143R → H in AGS5. 1 PublicationCorresponds to variant rs369035155dbSNPEnsembl.1
Natural variantiVAR_058484145R → Q in AGS5. 1 PublicationCorresponds to variant rs515726145dbSNPEnsembl.1
Natural variantiVAR_070633167H → Y in AGS5. 1 Publication1
Natural variantiVAR_058485201I → N in AGS5 and CHBL2. 2 PublicationsCorresponds to variant rs138603088dbSNPEnsembl.1
Natural variantiVAR_058486209G → S in AGS5. 1 PublicationCorresponds to variant rs121434516dbSNPEnsembl.1
Natural variantiVAR_058487254M → V in AGS5. 1 PublicationCorresponds to variant rs121434521dbSNPEnsembl.1
Natural variantiVAR_070634290R → H in AGS5. 1 PublicationCorresponds to variant rs559553527dbSNPEnsembl.1
Natural variantiVAR_058488369L → S in AGS5. 1 PublicationCorresponds to variant rs515726139dbSNPEnsembl.1
Natural variantiVAR_058489385M → V in AGS5. 1 PublicationCorresponds to variant rs515726140dbSNPEnsembl.1
Chilblain lupus 2 (CHBL2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614415
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058485201I → N in AGS5 and CHBL2. 2 PublicationsCorresponds to variant rs138603088dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137D → A: Impairs homotetramerization and nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi142Q → E: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-145. 1 Publication1
Mutagenesisi145R → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-145. 1 Publication1
Mutagenesisi149Q → A: Abolishes enzyme activity; when associated with A-319. 1 Publication1
Mutagenesisi206 – 207HD → RN: Abolishes zinc binding and enzyme activity. 1 Publication2
Mutagenesisi312K → A: Abolishes enzyme activity; when associated with A-315 and A-366. 1
Mutagenesisi315Y → A: Abolishes enzyme activity; when associated with A-312 and A-366. 1
Mutagenesisi319D → A: Abolishes enzyme activity; when associated with A-149. 1 Publication1
Mutagenesisi330D → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-358. 1 Publication1
Mutagenesisi333R → E: Decreases enzyme activity. Impairs homotetramerization and nearly abolishes enzyme activity; when associated with E-451. 2 Publications1
Mutagenesisi352R → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-376 and A-377. 1 Publication1
Mutagenesisi358N → A: Impairs homotetramerization and reduces enzyme activity; when associated with A-330. 1 Publication1
Mutagenesisi361D → R: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with K-364. 1 Publication1
Mutagenesisi364H → K: Impairs homotetramerization and nearly abolishes enzyme activity; when associated with R-361. 1 Publication1
Mutagenesisi366R → A: Abolishes enzyme activity; when associated with A-312 and A-315. 1 Publication1
Mutagenesisi370H → A: Abolishes enzyme activity; when associated with G-374. 1 Publication1
Mutagenesisi374Y → G: Abolishes enzyme activity; when associated with A-370. 1 Publication1
Mutagenesisi376H → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-377. 1
Mutagenesisi377K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-352 and A-376. 1
Mutagenesisi451R → E: Impairs homotetramerization and abolishes enzyme activity. 1 Publication1
Mutagenesisi534K → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and D-540. 1 Publication1
Mutagenesisi537V → A: Impairs homotetramerization and abolishes enzyme activity; when associated with A-534 and D-540. 1 Publication1
Mutagenesisi540L → D: Impairs homotetramerization and abolishes enzyme activity; when associated with A-537 and A-534. 1 Publication1
Mutagenesisi609R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication1
Mutagenesisi617R → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication1
Mutagenesisi622K → A or E: Abolishes proteasomal degradation triggered by the viral accessory protein vpx. 1 Publication1

Keywords - Diseasei

Aicardi-Goutieres syndrome, Disease mutation

Organism-specific databases

DisGeNETi25939.
MalaCardsiSAMHD1.
MIMi612952. phenotype.
614415. phenotype.
OpenTargetsiENSG00000101347.
Orphaneti51. Aicardi-Goutieres syndrome.
90280. Chilblain lupus.
PharmGKBiPA34938.

Polymorphism and mutation databases

BioMutaiSAMHD1.
DMDMi22257047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001537321 – 626Deoxynucleoside triphosphate triphosphohydrolase SAMHD1Add BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei18PhosphoserineBy similarity1
Modified residuei21PhosphothreonineBy similarity1
Modified residuei25PhosphothreonineBy similarity1
Modified residuei33PhosphoserineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei592PhosphothreonineCombined sources1

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

EPDiQ9Y3Z3.
PaxDbiQ9Y3Z3.
PeptideAtlasiQ9Y3Z3.
PRIDEiQ9Y3Z3.

PTM databases

iPTMnetiQ9Y3Z3.
PhosphoSitePlusiQ9Y3Z3.

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

BgeeiENSG00000101347.
CleanExiHS_SAMHD1.
GenevisibleiQ9Y3Z3. HS.

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. 69 interactors.
DIPiDIP-50704N.
IntActiQ9Y3Z3. 26 interactors.
MINTiMINT-2823520.
STRINGi9606.ENSP00000262878.

Structurei

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 44Combined sources3
Helixi46 – 57Combined sources12
Helixi62 – 70Combined sources9
Turni75 – 80Combined sources6
Helixi83 – 88Combined sources6
Helixi94 – 108Combined sources15
Turni109 – 112Combined sources4
Beta strandi116 – 120Combined sources5
Turni121 – 123Combined sources3
Beta strandi124 – 128Combined sources5
Helixi130 – 136Combined sources7
Helixi139 – 142Combined sources4
Helixi143 – 146Combined sources4
Beta strandi147 – 150Combined sources4
Helixi151 – 155Combined sources5
Helixi164 – 185Combined sources22
Helixi187 – 189Combined sources3
Helixi193 – 205Combined sources13
Turni206 – 209Combined sources4
Turni212 – 214Combined sources3
Helixi215 – 219Combined sources5
Helixi221 – 225Combined sources5
Beta strandi226 – 229Combined sources4
Helixi233 – 247Combined sources15
Helixi250 – 256Combined sources7
Helixi261 – 273Combined sources13
Beta strandi288 – 290Combined sources3
Helixi292 – 299Combined sources8
Beta strandi300 – 302Combined sources3
Turni304 – 306Combined sources3
Helixi310 – 323Combined sources14
Helixi331 – 336Combined sources6
Beta strandi338 – 343Combined sources6
Beta strandi346 – 352Combined sources7
Helixi353 – 355Combined sources3
Helixi356 – 372Combined sources17
Turni373 – 375Combined sources3
Helixi377 – 393Combined sources17
Turni394 – 396Combined sources3
Helixi402 – 404Combined sources3
Turni409 – 411Combined sources3
Helixi412 – 414Combined sources3
Helixi416 – 419Combined sources4
Helixi425 – 432Combined sources8
Helixi436 – 438Combined sources3
Helixi439 – 449Combined sources11
Beta strandi455 – 460Combined sources6
Beta strandi463 – 465Combined sources3
Helixi470 – 475Combined sources6
Helixi476 – 482Combined sources7
Helixi495 – 497Combined sources3
Beta strandi498 – 509Combined sources12
Helixi514 – 517Combined sources4
Beta strandi519 – 522Combined sources4
Beta strandi525 – 530Combined sources6
Helixi534 – 536Combined sources3
Beta strandi539 – 541Combined sources3
Beta strandi545 – 555Combined sources11
Helixi559 – 576Combined sources18
Helixi584 – 587Combined sources4
Turni589 – 591Combined sources3
Helixi592 – 594Combined sources3
Turni596 – 598Combined sources3
Helixi611 – 613Combined sources3
Helixi617 – 622Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Q7HX-ray2.59A/B/C/D109-626[»]
4QFXX-ray2.20A/B/C/D113-626[»]
4QFYX-ray2.10A/B/C/D113-626[»]
4QFZX-ray2.30A/B/C/D113-626[»]
4QG0X-ray2.30A/B/C/D113-626[»]
4QG1X-ray2.20A/B/C/D113-626[»]
4QG2X-ray2.25A/B/C/D113-626[»]
4QG4X-ray2.10A/B/C/D113-626[»]
4RXOX-ray2.60A/B/C/D109-626[»]
4RXPX-ray2.10A/B109-626[»]
4RXQX-ray2.10A/B109-626[»]
4RXRX-ray2.12A/B109-626[»]
4RXSX-ray2.20A/B109-626[»]
4TNPX-ray2.00A/B/C/D113-626[»]
4TNQX-ray2.55A/B/C/D113-626[»]
4TNRX-ray2.75A/B/C/D113-626[»]
4TNXX-ray2.31A/B/C/D113-626[»]
4TNYX-ray2.60A/B/C/D113-626[»]
4TNZX-ray2.38A/B/C/D113-626[»]
4TO0X-ray2.30A/B/C/D113-626[»]
4TO1X-ray2.55A/B/C/D113-626[»]
4TO2X-ray2.27A/B/C/D113-626[»]
4TO3X-ray2.20A/B/C/D113-626[»]
4TO4X-ray2.10A/B/C/D113-626[»]
4TO5X-ray2.80A/B/C/D113-626[»]
4TO6X-ray2.33A/B/C/D113-626[»]
4ZWEX-ray2.81A/B/C/D113-626[»]
4ZWGX-ray2.30A/B/C/D113-626[»]
5AO0X-ray3.73A/B41-583[»]
5AO1X-ray2.54A/B/C/D115-583[»]
5AO2X-ray2.97A/B/C/D115-583[»]
5AO3X-ray3.00A/B/C/D115-626[»]
5AO4X-ray3.70A/B/C/D115-626[»]
ProteinModelPortaliQ9Y3Z3.
SMRiQ9Y3Z3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3Z3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 110SAMPROSITE-ProRule annotationAdd BLAST66
Domaini164 – 319HDAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni309 – 315Substrate binding7
Regioni370 – 375Substrate binding6

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

eggNOGiKOG2681. Eukaryota.
COG1078. LUCA.
GeneTreeiENSGT00390000013867.
HOVERGENiHBG054208.
InParanoidiQ9Y3Z3.
OMAiTQRDILC.
OrthoDBiEOG091G060J.
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.
[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. AlignAdd to basket

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

        10         20         30         40         50
MQRADSEQPS KRPRCDDSPR TPSNTPSAEA DWSPGLELHP DYKTWGPEQV
60 70 80 90 100
CSFLRRGGFE EPVLLKNIRE NEITGALLPC LDESRFENLG VSSLGERKKL
110 120 130 140 150
LSYIQRLVQI HVDTMKVIND PIHGHIELHP LLVRIIDTPQ FQRLRYIKQL
160 170 180 190 200
GGGYYVFPGA SHNRFEHSLG VGYLAGCLVH ALGEKQPELQ ISERDVLCVQ
210 220 230 240 250
IAGLCHDLGH GPFSHMFDGR FIPLARPEVK WTHEQGSVMM FEHLINSNGI
260 270 280 290 300
KPVMEQYGLI PEEDICFIKE QIVGPLESPV EDSLWPYKGR PENKSFLYEI
310 320 330 340 350
VSNKRNGIDV DKWDYFARDC HHLGIQNNFD YKRFIKFARV CEVDNELRIC
360 370 380 390 400
ARDKEVGNLY DMFHTRNSLH RRAYQHKVGN IIDTMITDAF LKADDYIEIT
410 420 430 440 450
GAGGKKYRIS TAIDDMEAYT KLTDNIFLEI LYSTDPKLKD AREILKQIEY
460 470 480 490 500
RNLFKYVGET QPTGQIKIKR EDYESLPKEV ASAKPKVLLD VKLKAEDFIV
510 520 530 540 550
DVINMDYGMQ EKNPIDHVSF YCKTAPNRAI RITKNQVSQL LPEKFAEQLI
560 570 580 590 600
RVYCKKVDRK SLYAARQYFV QWCADRNFTK PQDGDVIAPL ITPQKKEWND
610 620
STSVQNPTRL REASKSRVQL FKDDPM
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)DescriptionActionsGraphical viewLength
Sequence conflicti394D → G in AAF32407 (PubMed:11064105).Curated1
Sequence conflicti394D → G in CAB43368 (PubMed:11230166).Curated1
Sequence conflicti404G → E in AAH36450 (PubMed:15489334).Curated1
Sequence conflicti494K → E in AAF32407 (PubMed:11064105).Curated1
Sequence conflicti494K → E in CAB43368 (PubMed:11230166).Curated1
Sequence conflicti546A → V in AAH36450 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058481123H → P in AGS5. 1 PublicationCorresponds to variant rs121434520dbSNPEnsembl.1
Natural variantiVAR_058482143R → C in AGS5. 1 PublicationCorresponds to variant rs387906948dbSNPEnsembl.1
Natural variantiVAR_058483143R → H in AGS5. 1 PublicationCorresponds to variant rs369035155dbSNPEnsembl.1
Natural variantiVAR_058484145R → Q in AGS5. 1 PublicationCorresponds to variant rs515726145dbSNPEnsembl.1
Natural variantiVAR_070633167H → Y in AGS5. 1 Publication1
Natural variantiVAR_058485201I → N in AGS5 and CHBL2. 2 PublicationsCorresponds to variant rs138603088dbSNPEnsembl.1
Natural variantiVAR_058486209G → S in AGS5. 1 PublicationCorresponds to variant rs121434516dbSNPEnsembl.1
Natural variantiVAR_058487254M → V in AGS5. 1 PublicationCorresponds to variant rs121434521dbSNPEnsembl.1
Natural variantiVAR_070634290R → H in AGS5. 1 PublicationCorresponds to variant rs559553527dbSNPEnsembl.1
Natural variantiVAR_058488369L → S in AGS5. 1 PublicationCorresponds to variant rs515726139dbSNPEnsembl.1
Natural variantiVAR_058489385M → V in AGS5. 1 PublicationCorresponds to variant rs515726140dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_037841113 – 136Missing in isoform 2. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_046561285 – 354Missing in isoform 3. CuratedAdd BLAST70
Alternative sequenceiVSP_046562502 – 536Missing in isoform 4. CuratedAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005260384.3. [Q9Y3Z3-4]
UniGeneiHs.580681.

Genome annotation databases

EnsembliENST00000262878; ENSP00000262878; ENSG00000101347. [Q9Y3Z3-1]
GeneIDi25939.
KEGGihsa:25939.
UCSCiuc002xgh.3. human. [Q9Y3Z3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005260384.3. [Q9Y3Z3-4]
UniGeneiHs.580681.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Q7HX-ray2.59A/B/C/D109-626[»]
4QFXX-ray2.20A/B/C/D113-626[»]
4QFYX-ray2.10A/B/C/D113-626[»]
4QFZX-ray2.30A/B/C/D113-626[»]
4QG0X-ray2.30A/B/C/D113-626[»]
4QG1X-ray2.20A/B/C/D113-626[»]
4QG2X-ray2.25A/B/C/D113-626[»]
4QG4X-ray2.10A/B/C/D113-626[»]
4RXOX-ray2.60A/B/C/D109-626[»]
4RXPX-ray2.10A/B109-626[»]
4RXQX-ray2.10A/B109-626[»]
4RXRX-ray2.12A/B109-626[»]
4RXSX-ray2.20A/B109-626[»]
4TNPX-ray2.00A/B/C/D113-626[»]
4TNQX-ray2.55A/B/C/D113-626[»]
4TNRX-ray2.75A/B/C/D113-626[»]
4TNXX-ray2.31A/B/C/D113-626[»]
4TNYX-ray2.60A/B/C/D113-626[»]
4TNZX-ray2.38A/B/C/D113-626[»]
4TO0X-ray2.30A/B/C/D113-626[»]
4TO1X-ray2.55A/B/C/D113-626[»]
4TO2X-ray2.27A/B/C/D113-626[»]
4TO3X-ray2.20A/B/C/D113-626[»]
4TO4X-ray2.10A/B/C/D113-626[»]
4TO5X-ray2.80A/B/C/D113-626[»]
4TO6X-ray2.33A/B/C/D113-626[»]
4ZWEX-ray2.81A/B/C/D113-626[»]
4ZWGX-ray2.30A/B/C/D113-626[»]
5AO0X-ray3.73A/B41-583[»]
5AO1X-ray2.54A/B/C/D115-583[»]
5AO2X-ray2.97A/B/C/D115-583[»]
5AO3X-ray3.00A/B/C/D115-626[»]
5AO4X-ray3.70A/B/C/D115-626[»]
ProteinModelPortaliQ9Y3Z3.
SMRiQ9Y3Z3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117436. 69 interactors.
DIPiDIP-50704N.
IntActiQ9Y3Z3. 26 interactors.
MINTiMINT-2823520.
STRINGi9606.ENSP00000262878.

PTM databases

iPTMnetiQ9Y3Z3.
PhosphoSitePlusiQ9Y3Z3.

Polymorphism and mutation databases

BioMutaiSAMHD1.
DMDMi22257047.

Proteomic databases

EPDiQ9Y3Z3.
PaxDbiQ9Y3Z3.
PeptideAtlasiQ9Y3Z3.
PRIDEiQ9Y3Z3.

Protocols and materials databases

DNASUi25939.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262878; ENSP00000262878; ENSG00000101347. [Q9Y3Z3-1]
GeneIDi25939.
KEGGihsa:25939.
UCSCiuc002xgh.3. human. [Q9Y3Z3-1]

Organism-specific databases

CTDi25939.
DisGeNETi25939.
GeneCardsiSAMHD1.
GeneReviewsiSAMHD1.
HGNCiHGNC:15925. SAMHD1.
HPAiHPA047072.
MalaCardsiSAMHD1.
MIMi606754. gene.
612952. phenotype.
614415. phenotype.
neXtProtiNX_Q9Y3Z3.
OpenTargetsiENSG00000101347.
Orphaneti51. Aicardi-Goutieres syndrome.
90280. Chilblain lupus.
PharmGKBiPA34938.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2681. Eukaryota.
COG1078. LUCA.
GeneTreeiENSGT00390000013867.
HOVERGENiHBG054208.
InParanoidiQ9Y3Z3.
OMAiTQRDILC.
OrthoDBiEOG091G060J.
PhylomeDBiQ9Y3Z3.
TreeFamiTF316113.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101347-MONOMER.
ReactomeiR-HSA-909733. Interferon alpha/beta signaling.
SIGNORiQ9Y3Z3.

Miscellaneous databases

EvolutionaryTraceiQ9Y3Z3.
GeneWikiiSAMHD1.
GenomeRNAii25939.
PROiQ9Y3Z3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101347.
CleanExiHS_SAMHD1.
GenevisibleiQ9Y3Z3. HS.

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.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.