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Entry version 175 (16 Oct 2019)
Sequence version 5 (27 Jul 2011)
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Protein

Filamin-A

Gene

Flna

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

Actin binding protein that promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins (By similarity). Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs (PubMed:17172441). Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (PubMed:20713593).By similarity4 Publications

<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 functionActin-binding
Biological processCilium biogenesis/degradation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-114608 Platelet degranulation
R-MMU-430116 GP1b-IX-V activation signalling
R-MMU-446353 Cell-extracellular matrix interactions
R-MMU-5627123 RHO GTPases activate PAKs

<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:
Filamin-A
Short name:
FLN-A
Alternative name(s):
Actin-binding protein 280
Short name:
ABP-280
Alpha-filamin
Endothelial actin-binding protein
Filamin-1
Non-muscle filamin
<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:Flna
Synonyms:Fln, Fln1
<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 X

Organism-specific databases

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

More...
MGIi
MGI:95556 Flna

<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

Cytoplasm, Cytoskeleton

<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

Female heterozygous knockout mice show normal development, but 20% die in the first 3-4 months with many anomalies, including lung edema and emphysema, liver thrombi and necrosis, leukocytosis, and heart dilation. Some females die after birth; only about 50% of expected female heterozygous mice are observed at weaning. Male hemizygous knockout mice die by embryonic day 14.5 dpc with vascular defects; their blood vessels are coarse and dilated and extend aberrant branches and sprouts into somitic tissues. Male hemizygous knockout mice display severe cardiac structural defects involving ventricles, atria, and outflow tracts. Conditional Flna knockout males, in the neural crest, survive until birth but die on the first postnatal day with cyanosis; all males show abnormal cardiac outflow tracts (PubMed:17172441). Female heterozygous knockout mice present a mild thrombocytopenia and conditional Flna knockout males, in platelets display a macrothrombocytopenia (PubMed:20713593).2 Publications

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000872972 – 2647Filamin-AAdd BLAST2646

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 residuei2N-acetylserineBy similarity1
Modified residuei11PhosphoserineBy similarity1
Modified residuei16PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
<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-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei376N6-acetyllysineCombined sources1
Modified residuei508N6-acetyllysineBy similarity1
Modified residuei700N6-acetyllysineCombined sources1
Modified residuei781N6-acetyllysineBy similarity1
Modified residuei837N6-acetyllysineBy similarity1
Modified residuei865N6-acetyllysineCombined sources1
Modified residuei906N6-acetyllysineCombined sources1
Modified residuei968PhosphoserineCombined sources1
Modified residuei1055PhosphoserineBy similarity1
Modified residuei1071N6-acetyllysine; alternateCombined sources1
Modified residuei1071N6-succinyllysine; alternateCombined sources1
Modified residuei1084PhosphoserineBy similarity1
Modified residuei1089PhosphothreonineBy similarity1
Modified residuei1301PhosphoserineBy similarity1
Modified residuei1338PhosphoserineBy similarity1
Modified residuei1372N6-acetyllysineCombined sources1
Modified residuei1459PhosphoserineCombined sources1
Modified residuei1533PhosphoserineBy similarity1
Modified residuei1538N6-acetyllysineCombined sources1
Modified residuei1630PhosphoserineBy similarity1
Modified residuei1734PhosphoserineBy similarity1
Modified residuei1750PhosphothreonineCombined sources1
Modified residuei1835PhosphoserineBy similarity1
Modified residuei1967PhosphoserineBy similarity1
Modified residuei2053PhosphoserineBy similarity1
Modified residuei2128PhosphoserineBy similarity1
Modified residuei2152PhosphoserineCombined sources1
Modified residuei2158PhosphoserineBy similarity1
Modified residuei2163PhosphoserineBy similarity1
Modified residuei2180PhosphoserineCombined sources1
Modified residuei2284PhosphoserineBy similarity1
Modified residuei2327PhosphoserineBy similarity1
Modified residuei2329PhosphoserineCombined sources1
Modified residuei2336PhosphothreonineCombined sources1
Modified residuei2338PhosphoserineBy similarity1
Modified residuei2370PhosphoserineCombined sources1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2510PhosphoserineBy similarity1
Modified residuei2523PhosphoserineCombined sources1
Modified residuei2526PhosphoserineCombined sources1
Modified residuei2569N6-acetyllysine; alternateCombined sources1
Modified residuei2569N6-succinyllysine; alternateCombined sources1
Modified residuei2575N6-acetyllysineCombined sources1
Modified residuei2599PhosphothreonineCombined sources1
Modified residuei2607N6-acetyllysineBy similarity1
Modified residuei2621N6-acetyllysineBy similarity1

<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

Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA.By similarity
Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8BTM8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8BTM8

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

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PaxDbi
Q8BTM8

PeptideAtlas

More...
PeptideAtlasi
Q8BTM8

PRoteomics IDEntifications database

More...
PRIDEi
Q8BTM8

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2316

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8BTM8

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

More...
PhosphoSitePlusi
Q8BTM8

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8BTM8

<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

Widely expressed. Highly expressed in Purkinje cells.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Widely distributed. Expressed at 12.5 dpc in the ventricular and subventricular zones. Highly expressed at 16 dpc in blood vessels, renal cortices, respiratory and alimentary tracts, olfactory epithelium, presumed isles of hematopoiesis within the liver; lower expression in the cerebral cortex and choroid plexus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031328 Expressed in 265 organ(s), highest expression level in aorta tunica media

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q8BTM8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8BTM8 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

Homodimer.

Interacts with FCGR1A, FLNB, FURIN, HSPB7, KCND2, INPPL1, MYOT, MYOZ1, PDLIM2, ARHGAP24, PSEN1, PSEN2 and ECSCR.

Interacts also with various other binding partners in addition to filamentous actin.

Interacts (via N-terminus) with TAF1B.

Interacts (via N-terminus) with MIS18BP1 (via N-terminus) (By similarity).

Interacts with TMEM67 (via C-terminus) and MKS1 (By similarity).

Interacts (via actin-binding domain) with MICALL2 (via calponin-homology (CH) domain).

Interacts with RFLNA and RFLNB (PubMed:24436304, PubMed:21709252).

Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane.

Interacts (via filamin repeats 19 and 21) with DRD3; increased PKA-mediated phosphorylation at Ser-2152.

Interacts (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA at Ser-2152.

Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 (By similarity).

Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA (By similarity).

Interacts with FOXC1 (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Plcg2Q8CIH53EBI-641991,EBI-617954

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
228662, 16 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-118 Glycoprotein Ib-IX-V-Filamin-A complex
CPX-123 Filamin A homodimer

Protein interaction database and analysis system

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IntActi
Q8BTM8, 16 interactors

Molecular INTeraction database

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MINTi
Q8BTM8

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000033699

<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

3D structure databases

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

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SMRi
Q8BTM8

Database of comparative protein structure models

More...
ModBasei
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>Domaini43 – 149Calponin-homology (CH) 1PROSITE-ProRule annotationAdd BLAST107
Domaini166 – 269Calponin-homology (CH) 2PROSITE-ProRule annotationAdd BLAST104
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati276 – 374Filamin 1Add BLAST99
Repeati376 – 474Filamin 2Add BLAST99
Repeati475 – 570Filamin 3Add BLAST96
Repeati571 – 663Filamin 4Add BLAST93
Repeati667 – 763Filamin 5Add BLAST97
Repeati764 – 866Filamin 6Add BLAST103
Repeati867 – 965Filamin 7Add BLAST99
Repeati966 – 1061Filamin 8Add BLAST96
Repeati1062 – 1154Filamin 9Add BLAST93
Repeati1155 – 1249Filamin 10Add BLAST95
Repeati1250 – 1349Filamin 11Add BLAST100
Repeati1350 – 1442Filamin 12Add BLAST93
Repeati1443 – 1539Filamin 13Add BLAST97
Repeati1540 – 1636Filamin 14Add BLAST97
Repeati1641 – 1740Filamin 15Add BLAST100
Repeati1765 – 1860Filamin 16Add BLAST96
Repeati1861 – 1952Filamin 17Add BLAST92
Repeati1953 – 2039Filamin 18Add BLAST87
Repeati2042 – 2134Filamin 19Add BLAST93
Repeati2135 – 2230Filamin 20Add BLAST96
Repeati2233 – 2325Filamin 21Add BLAST93
Repeati2327 – 2420Filamin 22Add BLAST94
Repeati2424 – 2516Filamin 23Add BLAST93
Repeati2552 – 2646Filamin 24Add BLAST95

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>Regioni2 – 274Actin-bindingAdd BLAST273
Regioni1490 – 1607Interaction with furinAdd BLAST118
Regioni1741 – 1778Hinge 1By similarityAdd BLAST38
Regioni2517 – 2647Self-association site, tailBy similarityAdd BLAST131
Regioni2517 – 2553Hinge 2By similarityAdd BLAST37

<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

Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Filamin repeat 20 interacts with filamin repeat 21 masking the ligand binding site on filamin repeat 21, resulting in an autoinhibited conformation. The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1. Filamin repeats 19 and 21 can simultaneously engage ligands.By similarity

<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 filamin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0518 Eukaryota
COG5069 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153588

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8BTM8

Database of Orthologous Groups

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OrthoDBi
660286at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313685

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00014 CH, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.418.10, 2 hits
2.60.40.10, 24 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001589 Actinin_actin-bd_CS
IPR001715 CH-domain
IPR036872 CH_dom_sf
IPR017868 Filamin/ABP280_repeat-like
IPR001298 Filamin/ABP280_rpt
IPR013783 Ig-like_fold
IPR014756 Ig_E-set

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00307 CH, 2 hits
PF00630 Filamin, 23 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00033 CH, 2 hits
SM00557 IG_FLMN, 24 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47576 SSF47576, 1 hit
SSF81296 SSF81296, 24 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00019 ACTININ_1, 1 hit
PS00020 ACTININ_2, 1 hit
PS50021 CH, 2 hits
PS50194 FILAMIN_REPEAT, 24 hits

<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.

<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.

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 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8BTM8-1) [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.

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        10         20         30         40         50
MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT
60 70 80 90 100
RWCNEHLKCV SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR
110 120 130 140 150
QMQLENVSVA LEFLDRESIK LVSIDSKAIV DGNLKLILGL IWTLILHYSI
160 170 180 190 200
SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL PQLPITNFSR DWQSGRALGA
210 220 230 240 250
LVDSCAPGLC PDWDSWDASK PVNNAREAMQ QADDWLGIPQ VITPEEIVDP
260 270 280 290 300
NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK
310 320 330 340 350
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV
360 370 380 390 400
TGTHKVTVLF AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK
410 420 430 440 450
TTYFEIFTAG AGMGEVEVVI QDPTGQKGTV EPQLEARGDS TYRCSYQPTM
460 470 480 490 500
EGVHTVHVTF AGVPIPRSPY TVTVGQACNP AACRAIGRGL QPKGVRVKET
510 520 530 540 550
ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF EYYPTIPGTY
560 570 580 590 600
TVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGI VGKSADFVVE
610 620 630 640 650
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN
660 670 680 690 700
SEDIRLSPFM ADIREAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK
710 720 730 740 750
HAGKAPLRVQ VQDNEGCSVE ATVKDNGNGT YSCSYVPRKP VKHTAMVSWG
760 770 780 790 800
GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA KTGLKAHEPT YFTVDCTEAG
810 820 830 840 850
QGDVSIGIKC APGVVGPTEA DIDFDIIRND NDTFTVKYTP CGAGSYTIMV
860 870 880 890 900
LFADQATPTS PIRVKVEPSH DASKVKAEGP GLNRTGVELG KPTHFTVNAK
910 920 930 940 950
TAGKGKLDVQ FSGLAKGDAV RDVDIIDHHD NTYTVKYIPV QQGPVGVNVT
960 970 980 990 1000
YGGDHIPKSP FSVGVSPSLD LSKIKVSGLG DKVDVGKDQE FTVKSKGAGG
1010 1020 1030 1040 1050
QGKVASKIVS PSGAAVPCKV EPGLGADNSV VRFVPREEGP YEVEVTYDGV
1060 1070 1080 1090 1100
PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG NAGSPARFTI DTKGAGTGGL
1110 1120 1130 1140 1150
GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF ADTHIPGSPF
1160 1170 1180 1190 1200
KAHVAPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE
1210 1220 1230 1240 1250
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE
1260 1270 1280 1290 1300
PAVDTSGVQC YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP
1310 1320 1330 1340 1350
SGNLTDTYVQ DCGDGTYKVE YTPYEEGVHS VDVTYDGSPV PSSPFQVPVT
1360 1370 1380 1390 1400
EGCDPSRVRV HGPGIQSGTT NKPNKFTVET RGAGTGGLGL AVEGPSEAKM
1410 1420 1430 1440 1450
SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV PVHDVTDASK
1460 1470 1480 1490 1500
VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV
1510 1520 1530 1540 1550
DNADGTQTVN YVPSREGSYS ISVLYGEEEV PRSPFKVKVL PTHDASKVKA
1560 1570 1580 1590 1600
SGPGLNTTGV PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH
1610 1620 1630 1640 1650
DGTYTVAYVP DVPGRYTILI KYGGDEIPFS PYRVRAVPTG DASKCTVTVS
1660 1670 1680 1690 1700
IGGHGLGAGI GPTIQIGEET VITVDTKAAG KGKVTCTVCT PDGSEVDVDV
1710 1720 1730 1740 1750
VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA LAGDQPTVQT
1760 1770 1780 1790 1800
PLRSQQLAPQ YNYPQGSQQT WIPERPMVGV NGLDVTSLRP FDLVIPFTIK
1810 1820 1830 1840 1850
KGEITGEVRM PSGKVAQPSI TDNKDGTVTV RYSPSEAGLH EMDIRYDNMH
1860 1870 1880 1890 1900
IPGSPLQFYV DYVNCGHITA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL
1910 1920 1930 1940 1950
AIEGPSKAEI SCTDNQDGTC SVSYLPVLPG DYSILVKYND QHIPGSPFTA
1960 1970 1980 1990 2000
RVTGDDSMRM SHLKVGSAAD IPINISETDL SLLTATVVPP SGREEPCLLK
2010 2020 2030 2040 2050
RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS QSEIGDASRV
2060 2070 2080 2090 2100
RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG
2110 2120 2130 2140 2150
TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA
2160 2170 2180 2190 2200
PSVANIGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI
2210 2220 2230 2240 2250
RFVPAEMGMH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER
2260 2270 2280 2290 2300
AEVGVPAEFG IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ
2310 2320 2330 2340 2350
EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL QESGLKVNQP
2360 2370 2380 2390 2400
ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGIY
2410 2420 2430 2440 2450
LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGSPAEF
2460 2470 2480 2490 2500
IVNTSNAGAG ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK
2510 2520 2530 2540 2550
YGGPYHIGGS PFKAKVTGPR LVSNHSLHET SSVFVDSLTK VATVPQHATS
2560 2570 2580 2590 2600
GPGPADVSKV VAKGLGLSKA YVGQKSNFTV DCSKAGNNML LVGVHGPRTP
2610 2620 2630 2640
CEEILVKHMG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS PYRIMVP
Length:2,647
Mass (Da):281,222
Last modified:July 27, 2011 - v5
<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:i217E3275F8468FEB
GO
Isoform 2 (identifier: Q8BTM8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-249: DSKAIVDGNL...QVITPEEIVD → GEGTGYTGAL...DTHAFHLQQF
     250-2647: Missing.

Note: May be due to an intron retention.
Show »
Length:249
Mass (Da):27,426
Checksum:i5856E9AC74C92E4F
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7FAU9B7FAU9_MOUSE
Filamin, alpha
Flna RP23-436K3.1-002
2,639Annotation 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>
F6XC15F6XC15_MOUSE
Filamin-A
Flna
511Annotation 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>
B7FAV1B7FAV1_MOUSE
Filamin, alpha
Flna RP23-436K3.1-013
2,583Annotation 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>
F6Z2C0F6Z2C0_MOUSE
Filamin-A
Flna
280Annotation 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>
J3JS91J3JS91_MOUSE
Filamin, alpha
Flna RP23-436K3.1-015
277Annotation 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>
F7AVL7F7AVL7_MOUSE
Filamin-A
Flna
74Annotation 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 BAC40787 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAC40837 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BC038478 differs from that shown. Reason: Frameshift.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 conflicti661A → T in BAC40837 (PubMed:16141072).Curated1
Sequence conflicti2127G → D in AAL68447 (PubMed:11807098).Curated1
Sequence conflicti2253V → A in AAH04061 (PubMed:15489334).Curated1
Sequence conflicti2253V → A in BC038478 (PubMed:15489334).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_008779125 – 249DSKAI…EEIVD → GEGTGYTGALSGCGRGRNKF FLSSPLESLLVVFPSCCTQP RLPLGPLAALFFEVLENKRL AWRACEPLRAPARSALLACS QAELTSSVGRAPNAAPEVGQ AQTRLLPLRAAPHPWDTHAF HLQQF in isoform 2. 1 PublicationAdd BLAST125
Alternative sequenceiVSP_008780250 – 2647Missing in isoform 2. 1 PublicationAdd BLAST2398

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK044856 mRNA Translation: BAC32121.1
AK089195 mRNA Translation: BAC40787.1 Different initiation.
AK089311 mRNA Translation: BAC40837.2 Different initiation.
AL807376 Genomic DNA Translation: CAT00728.1
BC004061 mRNA Translation: AAH04061.1
BC038478 mRNA No translation available.
BC054432 mRNA Translation: AAH54432.1
AF034129 mRNA Translation: AAC02062.1
AF353668 mRNA Translation: AAL68444.1
AF353671 mRNA Translation: AAL68447.1

NCBI Reference Sequences

More...
RefSeqi
XP_006527974.1, XM_006527911.3 [Q8BTM8-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328 [Q8BTM8-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
192176

UCSC genome browser

More...
UCSCi
uc009tnz.1 mouse [Q8BTM8-1]

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
AK044856 mRNA Translation: BAC32121.1
AK089195 mRNA Translation: BAC40787.1 Different initiation.
AK089311 mRNA Translation: BAC40837.2 Different initiation.
AL807376 Genomic DNA Translation: CAT00728.1
BC004061 mRNA Translation: AAH04061.1
BC038478 mRNA No translation available.
BC054432 mRNA Translation: AAH54432.1
AF034129 mRNA Translation: AAC02062.1
AF353668 mRNA Translation: AAL68444.1
AF353671 mRNA Translation: AAL68447.1
RefSeqiXP_006527974.1, XM_006527911.3 [Q8BTM8-1]

3D structure databases

SMRiQ8BTM8
ModBaseiSearch...

Protein-protein interaction databases

BioGridi228662, 16 interactors
ComplexPortaliCPX-118 Glycoprotein Ib-IX-V-Filamin-A complex
CPX-123 Filamin A homodimer
IntActiQ8BTM8, 16 interactors
MINTiQ8BTM8
STRINGi10090.ENSMUSP00000033699

PTM databases

GlyConnecti2316
iPTMnetiQ8BTM8
PhosphoSitePlusiQ8BTM8
SwissPalmiQ8BTM8

Proteomic databases

EPDiQ8BTM8
jPOSTiQ8BTM8
PaxDbiQ8BTM8
PeptideAtlasiQ8BTM8
PRIDEiQ8BTM8

Genome annotation databases

EnsembliENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328 [Q8BTM8-1]
GeneIDi192176
UCSCiuc009tnz.1 mouse [Q8BTM8-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2316
MGIiMGI:95556 Flna

Phylogenomic databases

eggNOGiKOG0518 Eukaryota
COG5069 LUCA
GeneTreeiENSGT00940000153588
InParanoidiQ8BTM8
OrthoDBi660286at2759
TreeFamiTF313685

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-430116 GP1b-IX-V activation signalling
R-MMU-446353 Cell-extracellular matrix interactions
R-MMU-5627123 RHO GTPases activate PAKs

Miscellaneous databases

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

More...
ChiTaRSi
Flna mouse

Protein Ontology

More...
PROi
PR:Q8BTM8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031328 Expressed in 265 organ(s), highest expression level in aorta tunica media
ExpressionAtlasiQ8BTM8 baseline and differential
GenevisibleiQ8BTM8 MM

Family and domain databases

CDDicd00014 CH, 2 hits
Gene3Di1.10.418.10, 2 hits
2.60.40.10, 24 hits
InterProiView protein in InterPro
IPR001589 Actinin_actin-bd_CS
IPR001715 CH-domain
IPR036872 CH_dom_sf
IPR017868 Filamin/ABP280_repeat-like
IPR001298 Filamin/ABP280_rpt
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PfamiView protein in Pfam
PF00307 CH, 2 hits
PF00630 Filamin, 23 hits
SMARTiView protein in SMART
SM00033 CH, 2 hits
SM00557 IG_FLMN, 24 hits
SUPFAMiSSF47576 SSF47576, 1 hit
SSF81296 SSF81296, 24 hits
PROSITEiView protein in PROSITE
PS00019 ACTININ_1, 1 hit
PS00020 ACTININ_2, 1 hit
PS50021 CH, 2 hits
PS50194 FILAMIN_REPEAT, 24 hits

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 nameiFLNA_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: Q8BTM8
Secondary accession number(s): B7FAV0
, O54934, Q7TQI1, Q8BLK1, Q8BTN7, Q8VHX5, Q8VHX8, Q99KQ2
<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 7, 2003
Last sequence update: July 27, 2011
Last modified: October 16, 2019
This is version 175 of the entry and version 5 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

Complete proteome, Reference proteome

Documents

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