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Protein

Filamin-A

Gene

FLNA

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

Functioni

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. 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 (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. 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 (By similarity).By similarity1 Publication

Caution

Variant Thr-1764 has been originally associated with periventricular nodular heterotopia. It has been subsequently reported as a benign polymorphism.1 Publication

GO - Molecular functioni

  • actin filament binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • Fc-gamma receptor I complex binding Source: BHF-UCL
  • G-protein coupled receptor binding Source: UniProtKB
  • GTPase binding Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • kinase binding Source: UniProtKB
  • mu-type opioid receptor binding Source: Ensembl
  • potassium channel regulator activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • Rac GTPase binding Source: BHF-UCL
  • Ral GTPase binding Source: BHF-UCL
  • Rho GTPase binding Source: BHF-UCL
  • RNA binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB
  • small GTPase binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • actin crosslink formation Source: BHF-UCL
  • actin cytoskeleton reorganization Source: BHF-UCL
  • adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: BHF-UCL
  • cell junction assembly Source: Reactome
  • cerebral cortex development Source: Ensembl
  • cilium assembly Source: UniProtKB
  • cytoplasmic sequestering of protein Source: BHF-UCL
  • establishment of protein localization Source: BHF-UCL
  • formation of radial glial scaffolds Source: Ensembl
  • mitotic spindle assembly Source: MGI
  • mRNA transcription by RNA polymerase II Source: Ensembl
  • negative regulation of apoptotic process Source: CACAO
  • negative regulation of DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of protein catabolic process Source: BHF-UCL
  • negative regulation of transcription by RNA polymerase I Source: CACAO
  • platelet activation Source: Reactome
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of integrin-mediated signaling pathway Source: CACAO
  • positive regulation of neural precursor cell proliferation Source: Ensembl
  • positive regulation of neuron migration Source: Ensembl
  • positive regulation of potassium ion transmembrane transport Source: BHF-UCL
  • positive regulation of substrate adhesion-dependent cell spreading Source: CACAO
  • protein localization to cell surface Source: BHF-UCL
  • protein localization to plasma membrane Source: BHF-UCL
  • protein stabilization Source: BHF-UCL
  • receptor clustering Source: BHF-UCL
  • regulation of cell migration Source: UniProtKB
  • regulation of membrane repolarization during atrial cardiac muscle cell action potential Source: BHF-UCL
  • regulation of membrane repolarization during cardiac muscle cell action potential Source: BHF-UCL
  • semaphorin-plexin signaling pathway Source: WormBase
  • wound healing, spreading of cells Source: UniProtKB

Keywordsi

Molecular functionActin-binding
Biological processCilium biogenesis/degradation

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-430116 GP1b-IX-V activation signalling
R-HSA-446353 Cell-extracellular matrix interactions
R-HSA-5627123 RHO GTPases activate PAKs
SignaLinkiP21333
SIGNORiP21333

Protein family/group databases

TCDBi8.A.66.1.4 the dystrophin (dystrophin) family

Names & Taxonomyi

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
Gene namesi
Name:FLNA
Synonyms:FLN, FLN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000196924.14
HGNCiHGNC:3754 FLNA
MIMi300017 gene
neXtProtiNX_P21333

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Periventricular nodular heterotopia 1 (PVNH1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.
See also OMIM:300049
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02273439A → G in PVNH1. 1 PublicationCorresponds to variant dbSNP:rs137853313EnsemblClinVar.1
Natural variantiVAR_01569982E → V in PVNH1. 1 PublicationCorresponds to variant dbSNP:rs28935169EnsemblClinVar.1
Natural variantiVAR_031305102M → V in PVNH1. 1 Publication1
Natural variantiVAR_031306128A → V in PVNH1. 1 PublicationCorresponds to variant dbSNP:rs137853315EnsemblClinVar.1
Natural variantiVAR_031307149S → F in PVNH1. 1 Publication1
Natural variantiVAR_012834656L → F in PVNH1. 1 PublicationCorresponds to variant dbSNP:rs137853311EnsemblClinVar.1
Otopalatodigital syndrome 1 (OPD1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionX-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.
See also OMIM:311300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015714172L → F in OPD1. 1 Publication1
Natural variantiVAR_015716196R → W in OPD1. 1 PublicationCorresponds to variant dbSNP:rs137853317EnsemblClinVar.1
Natural variantiVAR_031308203D → Y in OPD1. 1 PublicationCorresponds to variant dbSNP:rs137853314EnsemblClinVar.1
Natural variantiVAR_015700207P → L in OPD1. 2 PublicationsCorresponds to variant dbSNP:rs28935469EnsemblClinVar.1
Natural variantiVAR_076501267A → T in OPD1; unknown pathological significance. 1 Publication1
Natural variantiVAR_076502804V → D in OPD1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0765062391R → H in OPD1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs727503930Ensembl.1
Otopalatodigital syndrome 2 (OPD2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCongenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects.
See also OMIM:304120
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015713170Q → P in OPD2. 1 PublicationCorresponds to variant dbSNP:rs863223628Ensembl.1
Natural variantiVAR_076500187N → S in OPD2; unknown pathological significance. 1 Publication1
Natural variantiVAR_015715196R → G in OPD2. 2 Publications1
Natural variantiVAR_015717200A → S in OPD2. 1 Publication1
Natural variantiVAR_058720210C → F in OPD2. 1 PublicationCorresponds to variant dbSNP:rs137853318EnsemblClinVar.1
Natural variantiVAR_015701254E → K in OPD2. 1 PublicationCorresponds to variant dbSNP:rs28935470EnsemblClinVar.1
Natural variantiVAR_015718273A → P in OPD2. 1 Publication1
Natural variantiVAR_015719555T → K in OPD2. 1 PublicationCorresponds to variant dbSNP:rs782611953Ensembl.1
Natural variantiVAR_0157231645C → F in OPD2. 1 Publication1
Frontometaphyseal dysplasia 1 (FMD1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked disease characterized by generalized skeletal dysplasia, deafness, and urogenital defects.
See also OMIM:305620
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0765031142D → V in FMD1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0157021159D → A in FMD1; does not inhibit interaction with MIS18BP1. 2 PublicationsCorresponds to variant dbSNP:rs28935471EnsemblClinVar.1
Natural variantiVAR_0157211186S → L in FMD1. 3 PublicationsCorresponds to variant dbSNP:rs137853312EnsemblClinVar.1
Natural variantiVAR_0157221620Missing in FMD1. 1 Publication1
Natural variantiVAR_0313121728G → C in FMD1. 1 PublicationCorresponds to variant dbSNP:rs137853316EnsemblClinVar.1
Natural variantiVAR_0765051840H → R in FMD1; unknown pathological significance. 1 Publication1
Melnick-Needles syndrome (MNS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSevere congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.
See also OMIM:309350
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0765041163V → L in MNS; unknown pathological significance. 1 Publication1
Natural variantiVAR_0157201184D → E in MNS. 1 PublicationCorresponds to variant dbSNP:rs80338837EnsemblClinVar.1
Natural variantiVAR_0157031188A → T in MNS; does not inhibit interaction with MIS18BP1. 3 PublicationsCorresponds to variant dbSNP:rs28935472EnsemblClinVar.1
Natural variantiVAR_0157041199S → L in MNS; does not inhibit interaction with MIS18BP1. 2 PublicationsCorresponds to variant dbSNP:rs28935473EnsemblClinVar.1
Intestinal pseudoobstruction, neuronal, chronic idiopathic, X-linked (IPOX)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.
See also OMIM:300048
FG syndrome 2 (FGS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionFG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
See also OMIM:300321
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0587211291P → L in FGS2. 1 PublicationCorresponds to variant dbSNP:rs137853319EnsemblClinVar.1
Terminal osseous dysplasia (TOD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.
See also OMIM:300244
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0641591724 – 1739Missing in TOD. 1 PublicationAdd BLAST16
Cardiac valvular dysplasia X-linked (CVDX)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.
See also OMIM:314400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064156288G → R in CVDX. 1 PublicationCorresponds to variant dbSNP:rs267606816EnsemblClinVar.1
Natural variantiVAR_064157637P → Q in CVDX. 1 PublicationCorresponds to variant dbSNP:rs267606815EnsemblClinVar.1
Natural variantiVAR_064158711V → D in CVDX. 1 PublicationCorresponds to variant dbSNP:rs267606817EnsemblClinVar.1
Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abnormally enlarged (PubMed:21960593).1 Publication
Congenital short bowel syndrome, X-linked (CSBSX)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by a shortened small intestine, and malabsorption. The mean length of the small intestine in affected individuals is approximately 50 cm, compared with a normal length at birth of 190-280 cm. It is associated with significant mortality and morbidity. Infants usually present with failure to thrive, recurrent vomiting, and diarrhea.
See also OMIM:300048

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42K → R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-43 and R-135. 1 Publication1
Mutagenesisi43K → R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-135. 1 Publication1
Mutagenesisi135K → R: Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-43. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

DisGeNETi2316
GeneReviewsiFLNA
MalaCardsiFLNA
MIMi300048 phenotype
300049 phenotype
300244 phenotype
300321 phenotype
304120 phenotype
305620 phenotype
309350 phenotype
311300 phenotype
314400 phenotype
OpenTargetsiENSG00000196924
Orphaneti2301 Congenital short bowel syndrome
1864 Congenital valvular dysplasia
82004 Ehlers-Danlos syndrome with periventricular heterotopia
323 FG syndrome
1826 Frontometaphyseal dysplasia
99811 Neuronal intestinal pseudoobstruction
2484 Osteodysplasty, Melnick-Needles type
90650 Otopalatodigital syndrome type 1
90652 Otopalatodigital syndrome type 2
98892 Periventricular nodular heterotopia
88630 Terminal osseous dysplasia - pigmentary defects
PharmGKBiPA28172

Polymorphism and mutation databases

BioMutaiFLNA
DMDMi116241365

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000872962 – 2647Filamin-AAdd BLAST2646

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei11PhosphoserineCombined sources1
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei376N6-acetyllysineBy similarity1
Modified residuei508N6-acetyllysineCombined sources1
Modified residuei700N6-acetyllysineCombined sources1
Modified residuei781N6-acetyllysineCombined sources1
Modified residuei837N6-acetyllysineCombined sources1
Modified residuei865N6-acetyllysineBy similarity1
Modified residuei906N6-acetyllysineBy similarity1
Modified residuei968PhosphoserineBy similarity1
Modified residuei1055PhosphoserineCombined sources1
Modified residuei1071N6-acetyllysine; alternateBy similarity1
Modified residuei1071N6-succinyllysine; alternateBy similarity1
Modified residuei1081PhosphoserineCombined sources1
Modified residuei1084PhosphoserineCombined sources1
Modified residuei1089PhosphothreonineCombined sources1
Modified residuei1301PhosphoserineCombined sources1
Modified residuei1338PhosphoserineCombined sources1
Modified residuei1372N6-acetyllysineBy similarity1
Modified residuei1459PhosphoserineCombined sources1
Modified residuei1533PhosphoserineCombined sources1
Modified residuei1538N6-acetyllysineBy similarity1
Modified residuei1630PhosphoserineCombined sources1
Modified residuei1734PhosphoserineCombined sources1
Modified residuei1835PhosphoserineCombined sources1
Modified residuei1967PhosphoserineCombined sources1
Modified residuei2053PhosphoserineCombined sources1
Modified residuei2128PhosphoserineCombined sources1
Modified residuei2152PhosphoserineCombined sources2 Publications1
Modified residuei2158PhosphoserineCombined sources1
Modified residuei2163PhosphoserineCombined sources1
Modified residuei2180PhosphoserineBy similarity1
Modified residuei2284PhosphoserineCombined sources1
Modified residuei2327PhosphoserineCombined sources1
Modified residuei2329PhosphoserineBy similarity1
Modified residuei2336PhosphothreonineCombined sources1 Publication1
Modified residuei2338PhosphoserineCombined sources1
Modified residuei2370PhosphoserineBy similarity1
Modified residuei2414PhosphoserineCombined sources1
Modified residuei2510PhosphoserineCombined sources1
Modified residuei2523PhosphoserineBy similarity1
Modified residuei2526PhosphoserineBy similarity1
Modified residuei2569N6-acetyllysine; alternateBy similarity1
Modified residuei2569N6-succinyllysine; alternateBy similarity1
Modified residuei2575N6-acetyllysineBy similarity1
Modified residuei2599PhosphothreonineBy similarity1
Modified residuei2607N6-acetyllysineCombined sources1
Modified residuei2621N6-acetyllysineCombined sources1

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.1 Publication
Phosphorylation extent changes in response to cell activation.
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 (PubMed:24052262). Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome (PubMed:26766444).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1761 – 1762Cleavage; by calpain2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP21333
MaxQBiP21333
PaxDbiP21333
PeptideAtlasiP21333
PRIDEiP21333

2D gel databases

OGPiP21333

PTM databases

CarbonylDBiP21333
iPTMnetiP21333
PhosphoSitePlusiP21333
SwissPalmiP21333

Miscellaneous databases

PMAP-CutDBP21333

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000196924
CleanExiHS_FLNA
ExpressionAtlasiP21333 baseline and differential
GenevisibleiP21333 HS

Organism-specific databases

HPAiCAB000356
HPA000368
HPA001016
HPA001115
HPA002925

Interactioni

Subunit structurei

Homodimer. Interacts with PDLIM2 (By similarity). Interacts with RFLNA and RFLNB (By similarity). Interacts with FCGR1A, FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-terminus). Interacts (via N-terminus) with TAF1B. Interacts with TMEM67 (via C-terminus) and MKS1. Interacts (via actin-binding domain) with MICALL2 (via CH domain). Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane (PubMed:20713593). 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 (PubMed:26460884). Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 (PubMed:19828450, PubMed:21524097, PubMed:25666618). Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA (PubMed:16291724). Interacts with FOXC1 (PubMed:15684392).By similarity19 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • Fc-gamma receptor I complex binding Source: BHF-UCL
  • G-protein coupled receptor binding Source: UniProtKB
  • GTPase binding Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • kinase binding Source: UniProtKB
  • mu-type opioid receptor binding Source: Ensembl
  • protein homodimerization activity Source: BHF-UCL
  • Rac GTPase binding Source: BHF-UCL
  • Ral GTPase binding Source: BHF-UCL
  • Rho GTPase binding Source: BHF-UCL
  • small GTPase binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108605, 290 interactors
CORUMiP21333
DIPiDIP-1136N
IntActiP21333, 234 interactors
MINTiP21333
STRINGi9606.ENSP00000358866

Structurei

Secondary structure

12647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 43Combined sources4
Helixi44 – 57Combined sources14
Helixi58 – 60Combined sources3
Turni67 – 73Combined sources7
Helixi75 – 85Combined sources11
Helixi100 – 116Combined sources17
Helixi126 – 130Combined sources5
Helixi134 – 149Combined sources16
Beta strandi157 – 159Combined sources3
Helixi168 – 179Combined sources12
Beta strandi181 – 183Combined sources3
Helixi190 – 192Combined sources3
Beta strandi193 – 195Combined sources3
Helixi196 – 205Combined sources10
Helixi213 – 215Combined sources3
Helixi221 – 236Combined sources16
Helixi244 – 247Combined sources4
Helixi254 – 261Combined sources8
Helixi263 – 266Combined sources4
Helixi480 – 482Combined sources3
Beta strandi484 – 487Combined sources4
Helixi488 – 490Combined sources3
Beta strandi501 – 506Combined sources6
Beta strandi515 – 521Combined sources7
Beta strandi529 – 534Combined sources6
Beta strandi537 – 542Combined sources6
Beta strandi548 – 556Combined sources9
Beta strandi565 – 571Combined sources7
Beta strandi579 – 583Combined sources5
Helixi584 – 586Combined sources3
Beta strandi588 – 590Combined sources3
Beta strandi595 – 604Combined sources10
Beta strandi609 – 617Combined sources9
Beta strandi620 – 625Combined sources6
Beta strandi627 – 636Combined sources10
Beta strandi639 – 649Combined sources11
Beta strandi658 – 664Combined sources7
Helixi672 – 674Combined sources3
Beta strandi676 – 679Combined sources4
Helixi680 – 682Combined sources3
Beta strandi683 – 685Combined sources3
Beta strandi693 – 698Combined sources6
Beta strandi707 – 712Combined sources6
Beta strandi714 – 716Combined sources3
Beta strandi721 – 725Combined sources5
Beta strandi727 – 735Combined sources9
Beta strandi739 – 749Combined sources11
Beta strandi758 – 762Combined sources5
Helixi1160 – 1162Combined sources3
Beta strandi1164 – 1167Combined sources4
Helixi1168 – 1170Combined sources3
Beta strandi1172 – 1174Combined sources3
Beta strandi1179 – 1184Combined sources6
Beta strandi1193 – 1198Combined sources6
Beta strandi1206 – 1211Combined sources6
Beta strandi1213 – 1222Combined sources10
Beta strandi1225 – 1235Combined sources11
Beta strandi1244 – 1250Combined sources7
Turni1785 – 1787Combined sources3
Beta strandi1791 – 1796Combined sources6
Beta strandi1804 – 1809Combined sources6
Beta strandi1819 – 1822Combined sources4
Beta strandi1824 – 1832Combined sources9
Beta strandi1838 – 1846Combined sources9
Beta strandi1855 – 1860Combined sources6
Beta strandi1865 – 1867Combined sources3
Beta strandi1869 – 1872Combined sources4
Helixi1873 – 1875Combined sources3
Beta strandi1877 – 1879Combined sources3
Beta strandi1884 – 1889Combined sources6
Turni1891 – 1893Combined sources3
Beta strandi1895 – 1906Combined sources12
Beta strandi1909 – 1914Combined sources6
Beta strandi1916 – 1925Combined sources10
Beta strandi1930 – 1938Combined sources9
Beta strandi1947 – 1953Combined sources7
Beta strandi1959 – 1967Combined sources9
Beta strandi1980 – 1988Combined sources9
Beta strandi1998 – 2001Combined sources4
Beta strandi2007 – 2010Combined sources4
Beta strandi2014 – 2025Combined sources12
Beta strandi2034 – 2039Combined sources6
Helixi2041 – 2043Combined sources3
Helixi2047 – 2049Combined sources3
Beta strandi2051 – 2054Combined sources4
Helixi2055 – 2057Combined sources3
Beta strandi2059 – 2061Combined sources3
Beta strandi2066 – 2071Combined sources6
Beta strandi2075 – 2077Combined sources3
Beta strandi2080 – 2088Combined sources9
Beta strandi2091 – 2096Combined sources6
Beta strandi2100 – 2107Combined sources8
Beta strandi2112 – 2120Combined sources9
Beta strandi2129 – 2136Combined sources8
Beta strandi2139 – 2148Combined sources10
Beta strandi2161 – 2165Combined sources5
Helixi2171 – 2173Combined sources3
Beta strandi2174 – 2179Combined sources6
Beta strandi2185 – 2187Combined sources3
Beta strandi2189 – 2192Combined sources4
Beta strandi2194 – 2201Combined sources8
Beta strandi2208 – 2216Combined sources9
Beta strandi2225 – 2229Combined sources5
Beta strandi2234 – 2236Combined sources3
Helixi2238 – 2240Combined sources3
Beta strandi2242 – 2245Combined sources4
Helixi2246 – 2248Combined sources3
Beta strandi2257 – 2262Combined sources6
Helixi2264 – 2266Combined sources3
Beta strandi2271 – 2279Combined sources9
Beta strandi2282 – 2287Combined sources6
Beta strandi2293 – 2298Combined sources6
Beta strandi2303 – 2311Combined sources9
Beta strandi2320 – 2326Combined sources7
Turni2429 – 2431Combined sources3
Beta strandi2433 – 2436Combined sources4
Helixi2437 – 2439Combined sources3
Beta strandi2441 – 2443Combined sources3
Beta strandi2448 – 2453Combined sources6
Turni2455 – 2457Combined sources3
Beta strandi2462 – 2470Combined sources9
Beta strandi2472 – 2479Combined sources8
Beta strandi2482 – 2489Combined sources8
Beta strandi2491 – 2506Combined sources16
Beta strandi2511 – 2518Combined sources8
Beta strandi2561 – 2564Combined sources4
Helixi2565 – 2567Combined sources3
Beta strandi2576 – 2581Combined sources6
Beta strandi2590 – 2595Combined sources6
Beta strandi2597 – 2599Combined sources3
Beta strandi2602 – 2610Combined sources9
Beta strandi2613 – 2619Combined sources7
Beta strandi2624 – 2632Combined sources9
Beta strandi2641 – 2646Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AAVNMR-A1863-1956[»]
2BP3X-ray2.32A/B1863-1956[»]
2BRQX-ray2.10A/B2236-2329[»]
2J3SX-ray2.50A/B2045-2329[»]
2JF1X-ray2.20A2236-2329[»]
2K3TNMR-A2427-2522[»]
2K7PNMR-A1772-1956[»]
2K7QNMR-A1954-2141[»]
2MTPNMR-A2236-2330[»]
2W0PX-ray1.90A/B2236-2329[»]
2WFNX-ray3.20A/B1-278[»]
3CNKX-ray1.65A/B2559-2647[»]
3HOCX-ray2.30A/B2-269[»]
3HOPX-ray2.30A/B2-269[»]
3HORX-ray2.70A/B2-269[»]
3ISWX-ray2.80A/B2236-2329[»]
3RGHX-ray2.44A/B1158-1252[»]
4M9PX-ray1.72A478-766[»]
4P3WX-ray2.00A/B/C/D/E/F2152-2329[»]
ProteinModelPortaliP21333
SMRiP21333
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21333

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 149Calponin-homology (CH) 1PROSITE-ProRule annotationAdd BLAST107
Domaini166 – 269Calponin-homology (CH) 2PROSITE-ProRule annotationAdd BLAST104
Repeati276 – 374Filamin 1Add BLAST99
Repeati376 – 474Filamin 2Add BLAST99
Repeati475 – 570Filamin 3Add BLAST96
Repeati571 – 663Filamin 4Add BLAST93
Repeati667 – 763Filamin 5Add BLAST97