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Entry version 163 (16 Oct 2019)
Sequence version 3 (18 Jul 2018)
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Protein

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene

Samhd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Isoform 1: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (By similarity). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:23972988, PubMed:23872947, PubMed:26667483, PubMed:29379009). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:26667483). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (By similarity). Phosphorylation at Thr-634 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (By similarity). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (By similarity). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (By similarity). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (By similarity). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (PubMed:29669924).By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated and regulated via the combined actions of GTP and dNTPs (dATP, dGTP, dTTP and dCTP): Allosteric site 1 binds GTP, while allosteric site 2 binds dNTP. Allosteric activation promotes the formation of highly active homotetramers. Isoform 1: Phosphorylation at Thr-634 impairs homotetramerization, thereby inhibiting dNTPase activity, leading to reduced ability to restrict infection by viruses.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei148GTPCombined sources1 Publication1
Binding sitei151dNTP; via amide nitrogen; shared with neighboring subunitBy similarity1
Binding sitei181SubstrateBy similarity1
Binding sitei196SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi199Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi238Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi239ZincCombined sources1 Publication1
Binding sitei242SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei265By similarity1
Metal bindingi343ZincCombined sources1 Publication1
Binding sitei347SubstrateBy similarity1
Binding sitei351SubstrateBy similarity1
Binding sitei365dNTPBy similarity1
Binding sitei401dNTPBy similarity1
Binding sitei409SubstrateBy similarity1
Binding sitei419dNTP; shared with neighboring subunitBy similarity1
Binding sitei420dNTP; shared with neighboring subunitCombined sources1 Publication1
Binding sitei494GTP; shared with neighboring subunitCombined sources1 Publication1
Binding sitei498GTP; shared with neighboring subunitBy similarity1
Binding sitei565dNTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi169 – 177GTPCombined sources1 Publication9
Nucleotide bindingi395 – 397dNTPBy similarity3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Hydrolase
Biological processAntiviral defense, DNA damage, DNA repair, DNA replication, Immunity, Innate immunity
LigandGTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8956319 Nucleobase catabolism

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1Curated (EC:3.1.5.-1 Publication)
Short name:
dNTPaseCurated
Alternative name(s):
Interferon-gamma-inducible protein Mg111 Publication
SAM domain and HD domain-containing protein 1Curated
Short name:
mSAMHD11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Samhd1Imported
Synonyms:Mg211 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1927468 Samhd1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice are viable and fertile but show increased cellular dNTP concentrations and impaired ability to restrict retroviral replication in lymphocytes, macrophages and dendritic cells (PubMed:23972988). Mice also diplay interferon (IFN)-beta-dependent transcriptional up-regulation of type I IFN-inducible genes in various cell types indicative of spontaneous IFN production (PubMed:23972988, PubMed:23872947).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi109F → L in LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with C-112 and H-143. 1 Publication1
Mutagenesisi112F → C in LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with L-109 and H-143. 1 Publication1
Mutagenesisi143R → H in LCH mutant; abolishes formation of the tetramer and deoxynucleoside triphosphate (dNTPase) activity; when associated with L-109 and C-112. 1 Publication1
Mutagenesisi634T → A or V: Increased ability to restrict LINE-1 retrotransposon activity. 1 Publication1
Mutagenesisi634T → E: Mimicks phosphorylation state, reduced ability to restrict LINE-1 retrotransposon activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001537331 – 658Deoxynucleoside triphosphate triphosphohydrolase SAMHD1Add BLAST658

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei49PhosphoserineCombined sources1
Modified residuei52PhosphothreonineCombined sources1
Modified residuei55PhosphoserineCombined sources1
Modified residuei56PhosphothreonineCombined sources1
Modified residuei64PhosphoserineBy similarity1
Modified residuei125PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei634PhosphothreonineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Isoform 1: Phosphorylation at Thr-634 by CDK1 acts as a switch to control deoxynucleoside triphosphate (dNTPase)-dependent and -independent functions (PubMed:26667483) (By similarity). Phosphorylation at Thr-634 takes place in cycling cells: it reduces the stability of the homotetramer, impairing the dNTPase activity and subsequent ability to restrict infection by viruses (Probable). It also inhibits ability to suppress LINE-1 retrotransposon activity (PubMed:26667483). In contrast, phosphorylation at Thr-634 promotes DNA end resection at stalled replication forks in response to DNA damage (By similarity).By similarity1 Publication1 Publication
Isoform 2: Not phosphorylated by CDK1 at the C-terminus.Curated

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q60710

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q60710

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q60710

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q60710

PeptideAtlas

More...
PeptideAtlasi
Q60710

PRoteomics IDEntifications database

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PRIDEi
Q60710

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q60710

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q60710

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q60710

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q60710

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q60710

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000027639 Expressed in 267 organ(s), highest expression level in decidua

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q60710 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; in absence of GTP and dNTP (By similarity). Homotetramer; in GTP- and dNTP-bound form (PubMed:29379009).

Interacts with MRE11; leading to stimulate the exonuclease activity of MRE11 (By similarity).

Interacts with RBBP8/CtIP (By similarity).

Interacts with RBBP8/CtIP.

Interacts (via its C-terminus) with CD81.

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
207791, 11 interactors

Protein interaction database and analysis system

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IntActi
Q60710, 3 interactors

Molecular INTeraction database

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MINTi
Q60710

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000059717

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1658
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q60710

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini77 – 142SAMPROSITE-ProRule annotationAdd BLAST66
Domaini196 – 348HDPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni341 – 347Substrate bindingBy similarity7
Regioni413 – 418Substrate bindingBy similarity6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

In mouse, the SAM domain is required for deoxynucleoside triphosphate (dNTPase) activity and ability to restrict infection by viruses. It acts by capping allosteric sites.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SAMHD1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2681 Eukaryota
COG1078 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000013867

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000264286

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q60710

KEGG Orthology (KO)

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KOi
K22544

Database of Orthologous Groups

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OrthoDBi
835545at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q60710

TreeFam database of animal gene trees

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TreeFami
TF316113

Family and domain databases

Conserved Domains Database

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CDDi
cd00077 HDc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.150.50, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003607 HD/PDEase_dom
IPR006674 HD_domain
IPR001660 SAM
IPR013761 SAM/pointed_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01966 HD, 1 hit
PF07647 SAM_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00471 HDc, 1 hit
SM00454 SAM, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47769 SSF47769, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51831 HD, 1 hit
PS50105 SAM_DOMAIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q60710-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MDSLLGCGVS AAAREPVPRY LTSQPRVSEV AMQSAPLEQP AKRPRCDGSP
60 70 80 90 100
RTPPSTPPAT ANLSADDDFQ NTDLRTWEPE DVCSFLENRG FREKKVLDIF
110 120 130 140 150
RDNKIAGSFL PFLDEDRLED LGVSSLEERK KMIECIQQLS QSRIDLMKVF
160 170 180 190 200
NDPIHGHIEF HPLLIRIIDT PQFQRLRYIK QLGGGYYVFP GASHNRFEHS
210 220 230 240 250
LGVGYLAGCL VRALAEKQPE LQISERDILC VQIAGLCHDL GHGPFSHMFD
260 270 280 290 300
GRFIPRARPE KKWKHEQGSI EMFEHLVNSN ELKLVMKNYG LVPEEDITFI
310 320 330 340 350
KEQIMGPPIT PVKDSLWPYK GRPATKSFLY EIVSNKRNGI DVDKWDYFAR
360 370 380 390 400
DCHHLGIQNN FDYKRFIKFA RICEVEYKVK EDKTYIRKVK HICSREKEVG
410 420 430 440 450
NLYDMFHTRN CLHRRAYQHK ISNLIDIMIT DAFLKADPYV EITGTAGKKF
460 470 480 490 500
RISTAIDDME AFTKLTDNIF LEVLHSTDPQ LSEAQSILRN IECRNLYKYL
510 520 530 540 550
GETQPKREKI RKEEYERLPQ EVAKAKPEKA PDVELKAEDF IVDVINVDYG
560 570 580 590 600
MEDKNPIDRV HFYCKSNSKQ AVRINKEQVS QLLPEKFAEQ LIRVYCKKKD
610 620 630 640 650
GKSLDAAGKH FVQWCALRDF TKPQDGDIIA PLITPLKWNN KTSSCLQEVS

KVKTCLKF
Length:658
Mass (Da):75,893
Last modified:July 18, 2018 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8ED07CE9EB6239D6
GO
Isoform 2 (identifier: Q60710-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     625-658: DGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLKF → QCGAGEMAEDPDSIPSTQQPHAAHNQL

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Length:651
Mass (Da):74,935
Checksum:i691307229BD269DA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6TVP2F6TVP2_MOUSE
Deoxynucleoside triphosphate tripho...
Samhd1
631Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PYG9E9PYG9_MOUSE
Deoxynucleoside triphosphate tripho...
Samhd1
582Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E0CXZ5E0CXZ5_MOUSE
Deoxynucleoside triphosphate tripho...
Samhd1
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA66219 differs from that shown. Reason: Frameshift.Curated
The sequence AAA66219 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAH12721 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAH67198 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAC35801 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAE30313 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAE31954 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti371R → L in BAE31954 (PubMed:16141072).Curated1
Sequence conflicti371R → L in BAE30313 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_059661625 – 658DGDII…TCLKF → QCGAGEMAEDPDSIPSTQQP HAAHNQL in isoform 2. Add BLAST34

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U15635 mRNA Translation: AAA66219.1 Sequence problems.
AK054490 mRNA Translation: BAC35801.1 Different initiation.
AK151335 mRNA Translation: BAE30313.1 Different initiation.
AK153390 mRNA Translation: BAE31954.1 Different initiation.
AL669828 Genomic DNA No translation available.
BC012721 mRNA Translation: AAH12721.1 Different initiation.
BC067198 mRNA Translation: AAH67198.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
I49127

NCBI Reference Sequences

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RefSeqi
NP_001132992.1, NM_001139520.1
NP_061339.3, NM_018851.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000057725; ENSMUSP00000059717; ENSMUSG00000027639 [Q60710-1]
ENSMUST00000088523; ENSMUSP00000085880; ENSMUSG00000027639 [Q60710-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
56045

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:56045

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15635 mRNA Translation: AAA66219.1 Sequence problems.
AK054490 mRNA Translation: BAC35801.1 Different initiation.
AK151335 mRNA Translation: BAE30313.1 Different initiation.
AK153390 mRNA Translation: BAE31954.1 Different initiation.
AL669828 Genomic DNA No translation available.
BC012721 mRNA Translation: AAH12721.1 Different initiation.
BC067198 mRNA Translation: AAH67198.1 Different initiation.
PIRiI49127
RefSeqiNP_001132992.1, NM_001139520.1
NP_061339.3, NM_018851.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6BRGX-ray3.50A/B/C/D1-658[»]
6BRHX-ray3.40A/B1-658[»]
6BRKX-ray3.50A1-658[»]
SMRiQ60710
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi207791, 11 interactors
IntActiQ60710, 3 interactors
MINTiQ60710
STRINGi10090.ENSMUSP00000059717

PTM databases

CarbonylDBiQ60710
iPTMnetiQ60710
PhosphoSitePlusiQ60710
SwissPalmiQ60710

Proteomic databases

EPDiQ60710
jPOSTiQ60710
MaxQBiQ60710
PaxDbiQ60710
PeptideAtlasiQ60710
PRIDEiQ60710

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
56045

Genome annotation databases

EnsembliENSMUST00000057725; ENSMUSP00000059717; ENSMUSG00000027639 [Q60710-1]
ENSMUST00000088523; ENSMUSP00000085880; ENSMUSG00000027639 [Q60710-2]
GeneIDi56045
KEGGimmu:56045

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
25939
MGIiMGI:1927468 Samhd1

Phylogenomic databases

eggNOGiKOG2681 Eukaryota
COG1078 LUCA
GeneTreeiENSGT00390000013867
HOGENOMiHOG000264286
InParanoidiQ60710
KOiK22544
OrthoDBi835545at2759
PhylomeDBiQ60710
TreeFamiTF316113

Enzyme and pathway databases

ReactomeiR-MMU-8956319 Nucleobase catabolism

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Samhd1 mouse
PMAP-CutDBiQ60710

Protein Ontology

More...
PROi
PR:Q60710

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000027639 Expressed in 267 organ(s), highest expression level in decidua
ExpressionAtlasiQ60710 baseline and differential

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.150.50, 1 hit
InterProiView protein in InterPro
IPR003607 HD/PDEase_dom
IPR006674 HD_domain
IPR001660 SAM
IPR013761 SAM/pointed_sf
PfamiView protein in Pfam
PF01966 HD, 1 hit
PF07647 SAM_2, 1 hit
SMARTiView protein in SMART
SM00471 HDc, 1 hit
SM00454 SAM, 1 hit
SUPFAMiSSF47769 SSF47769, 1 hit
PROSITEiView protein in PROSITE
PS51831 HD, 1 hit
PS50105 SAM_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSAMH1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q60710
Secondary accession number(s): E9Q0K6
, F8WJE0, Q3U5X2, Q543A4, Q91VK8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 18, 2018
Last modified: October 16, 2019
This is version 163 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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