SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y3Z3

- SAMH1_HUMAN

UniProt

Q9Y3Z3 - SAMH1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Gene
SAMHD1, MOP5
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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 nitrogen
Metal bindingi206 – 2061Zinc; via tele nitrogen
Metal bindingi207 – 2071Zinc
Binding sitei210 – 2101Substrate
Active sitei233 – 2331 Inferred
Metal bindingi311 – 3111Zinc
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. RNA binding Source: UniProtKB
  2. dGTP binding Source: UniProtKB
  3. dGTPase activity Source: UniProtKB
  4. nucleic acid binding Source: UniProtKB
  5. phosphoric diester hydrolase activity Source: InterPro
  6. protein binding Source: IntAct
  7. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. dATP catabolic process Source: UniProtKB
  2. dGTP catabolic process Source: UniProtKB
  3. defense response to virus 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 SAMHD1
PRO_0000153732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei18 – 181Phosphoserine By similarity
Modified residuei21 – 211Phosphothreonine By 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.5 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.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi117436. 42 interactions.
DIPiDIP-50704N.
IntActiQ9Y3Z3. 7 interactions.
MINTiMINT-2823520.
STRINGi9606.ENSP00000262878.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9Y3Z3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 11066SAM
Add
BLAST
Domaini164 – 319156HD
Add
BLAST

Region

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

Sequence similaritiesi

Belongs to the SAMHD1 family.
Contains 1 HD domain.

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

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.
VSP_037841Add
BLAST
Alternative sequencei285 – 35470Missing in isoform 3.
VSP_046561Add
BLAST
Alternative sequencei502 – 53635Missing in isoform 4.
VSP_046562Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 3941D → G in AAF32407. 1 Publication
Sequence conflicti394 – 3941D → G in CAB43368. 1 Publication
Sequence conflicti404 – 4041G → E in AAH36450. 1 Publication
Sequence conflicti494 – 4941K → E in AAF32407. 1 Publication
Sequence conflicti494 – 4941K → E in CAB43368. 1 Publication
Sequence conflicti546 – 5461A → V in AAH36450. 1 Publication

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...

Protein-protein interaction databases

BioGridi 117436. 42 interactions.
DIPi DIP-50704N.
IntActi Q9Y3Z3. 7 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

Similar proteinsi