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Entry version 133 (16 Oct 2019)
Sequence version 1 (29 Aug 2001)
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Protein

Acid sphingomyelinase-like phosphodiesterase 3b

Gene

Smpdl3b

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

Lipid-modulating phosphodiesterase. Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity (PubMed:26095358). Acts as a negative regulator of Toll-like receptor signaling (PubMed:26095358, PubMed:27687724). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown (PubMed:26095358, PubMed:27687724). Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (PubMed:27687724).2 Publications

<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+1 PublicationNote: Binds 2 Zn2+ ions per subunit.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 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 bindingi28Zinc 1Combined sources1 Publication1
Metal bindingi30Zinc 1Combined sources1 Publication1
Metal bindingi93Zinc 1Combined sources1 Publication1
Metal bindingi93Zinc 2Combined sources1 Publication1
Metal bindingi134Zinc 2Combined sources1 Publication1
Metal bindingi236Zinc 2Combined sources1 Publication1
Metal bindingi277Zinc 2Combined sources1 Publication1
Metal bindingi279Zinc 1Combined sources1 Publication1

<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 functionGlycosidase, Hydrolase
Biological processImmunity, Inflammatory response, Innate immunity, Lipid degradation, Lipid metabolism
LigandMetal-binding, Zinc

<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:
Acid sphingomyelinase-like phosphodiesterase 3b (EC:3.1.4.-2 Publications)
Short name:
ASM-like phosphodiesterase 3b
<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:Smpdl3b
Synonyms:Asml3b
<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 4

Organism-specific databases

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

More...
MGIi
MGI:1916022 Smpdl3b

<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

Cell membrane, Membrane, Secreted

<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 display higher inflammatory responses in models of TLR-dependent peritonitis. Macrophages show enhanced responsiveness to TLR stimulation and a significant change in membrane fluidity and the global cellular lipid composition.1 Publication

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>Mutagenesisi135H → A: Reduced phosphodiesterase activity. Decreases inhibition of innate immune responses. 2 Publications1
Mutagenesisi140 – 141KN → MA: Reduced phosphodiesterase activity. Decreases inhibition of innate immune responses. 1 Publication2
Mutagenesisi198 – 200YSN → FSA: No effect on enzyme activity and innate immune responses. 1 Publication3
Mutagenesisi307 – 315KTTLPGVVD → SG: Increased phosphodiesterase activity (in vitro). 1 Publication9

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<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_000000233219 – 456Acid sphingomyelinase-like phosphodiesterase 3bAdd BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi34N-linked (GlcNAc...) asparagineCombined sources3 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi45 ↔ 64Combined sources1 Publication
Glycosylationi72N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi164N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi223N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Disulfide bondi405 ↔ 409Combined sources1 Publication
Disulfide bondi415 ↔ 428Combined sources1 Publication

<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

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

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

More...
PaxDbi
P58242

PeptideAtlas

More...
PeptideAtlasi
P58242

PRoteomics IDEntifications database

More...
PRIDEi
P58242

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2104

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P58242

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

More...
PhosphoSitePlusi
P58242

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P58242

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Macrophages and dendritic cells.1 Publication

<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

Strongly up-regulated by TLR stimuli and interferon gamma.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028885 Expressed in 162 organ(s), highest expression level in jejunum

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P58242 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P58242 MM

<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

Interacts with TLR4, TLR7, TLR8 and TLR9.

1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
P58242, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000030709

<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

1456
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
P58242

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

<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 acid sphingomyelinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410ISVB Eukaryota
ENOG410XRWF LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183182

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000294197

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P58242

KEGG Orthology (KO)

More...
KOi
K01128

Identification of Orthologs from Complete Genome Data

More...
OMAi
FRLCLEK

Database of Orthologous Groups

More...
OrthoDBi
1116351at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P58242

TreeFam database of animal gene trees

More...
TreeFami
TF313674

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00842 MPP_ASMase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017064 ASM-like_Pdiesterase_prd
IPR041805 ASMase/PPN1_MPP
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00149 Metallophos, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036767 ASM-like_PDE, 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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P58242-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTLLGWLIFL APWGVAGAQL GRFWHISDLH LDPNYTVSKD PLQVCPSAGS
60 70 80 90 100
QPVLNAGPWG DYLCDSPWAL INSSLYAMKE IEPKPDFILW TGDDTPHVPN
110 120 130 140 150
ESLGEAAVLA IVERLTNLIK EVFPDTKVYA ALGNHDFHPK NQFPAQSNRI
160 170 180 190 200
YNQVAELWRP WLSNESYALF KRGAFYSEKL PGPSRAGRVV VLNTNLYYSN
210 220 230 240 250
NEQTAGMADP GEQFRWLGDV LSNASRDGEM VYVIGHVPPG FFEKTQNKAW
260 270 280 290 300
FRESFNEEYL KVIQKHHRVI AGQFFGHHHT DSFRMFYDNT GAPINVMFLT
310 320 330 340 350
PGVTPWKTTL PGVVDGANNP GIRIFEYDRA TLNLKDLVTY FLNLRQANVQ
360 370 380 390 400
ETPRWEQEYR LTEAYQVPDA SVSSMHTALT RIASEPHILQ RYYVYNSVSY
410 420 430 440 450
NHLTCEDSCR IEHVCAIQHV AFNTYATCLH GLGAKLVPGF LLILTLLPSL

HVLEVL
Length:456
Mass (Da):51,600
Last modified:August 29, 2001 - v1
<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:i11BD6AF4806FD990
GO

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
BC009087 mRNA Translation: AAH09087.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS18733.1

NCBI Reference Sequences

More...
RefSeqi
NP_598649.1, NM_133888.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030709; ENSMUSP00000030709; ENSMUSG00000028885

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100340

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:100340

UCSC genome browser

More...
UCSCi
uc008vbs.1 mouse

<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
BC009087 mRNA Translation: AAH09087.1
CCDSiCCDS18733.1
RefSeqiNP_598649.1, NM_133888.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KARX-ray1.14A19-435[»]
5KASX-ray1.62A19-435[»]
SMRiP58242
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP58242, 1 interactor
STRINGi10090.ENSMUSP00000030709

PTM databases

GlyConnecti2104
iPTMnetiP58242
PhosphoSitePlusiP58242
SwissPalmiP58242

Proteomic databases

PaxDbiP58242
PeptideAtlasiP58242
PRIDEiP58242

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
100340

Genome annotation databases

EnsembliENSMUST00000030709; ENSMUSP00000030709; ENSMUSG00000028885
GeneIDi100340
KEGGimmu:100340
UCSCiuc008vbs.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
27293
MGIiMGI:1916022 Smpdl3b

Phylogenomic databases

eggNOGiENOG410ISVB Eukaryota
ENOG410XRWF LUCA
GeneTreeiENSGT00950000183182
HOGENOMiHOG000294197
InParanoidiP58242
KOiK01128
OMAiFRLCLEK
OrthoDBi1116351at2759
PhylomeDBiP58242
TreeFamiTF313674

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P58242

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028885 Expressed in 162 organ(s), highest expression level in jejunum
ExpressionAtlasiP58242 baseline and differential
GenevisibleiP58242 MM

Family and domain databases

CDDicd00842 MPP_ASMase, 1 hit
Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR017064 ASM-like_Pdiesterase_prd
IPR041805 ASMase/PPN1_MPP
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PIRSFiPIRSF036767 ASM-like_PDE, 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 nameiASM3B_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: P58242
<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: August 29, 2001
Last sequence update: August 29, 2001
Last modified: October 16, 2019
This is version 133 of the entry and version 1 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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