Q80X90 · FLNB_MOUSE
- ProteinFilamin-B
- GeneFlnb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2602 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | brush border | |
Cellular Component | cell cortex | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | neuronal cell body | |
Cellular Component | phagocytic vesicle | |
Cellular Component | plasma membrane | |
Cellular Component | stress fiber | |
Cellular Component | Z disc | |
Molecular Function | actin filament binding | |
Molecular Function | identical protein binding | |
Biological Process | actin cytoskeleton organization | |
Biological Process | cellular response to type II interferon | |
Biological Process | epithelial cell morphogenesis | |
Biological Process | keratinocyte development | |
Biological Process | skeletal muscle tissue development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFilamin-B
- Short namesFLN-B
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80X90
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000087299 | 1-2602 | Filamin-B | |||
Sequence: MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMHHKYHQRPTFRQMKLENVSVALEFLDHESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDEGDDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPRKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPKAKLKPGAPLKPKLNPKKARAYGRGIEPTGNMVKQPAKFTVDTISAGQGDVMVFVEDPEGNKEEARVTPDSDKNKTYSVEYLPKVTGLHKVIVLFAGQHISKSPFEVNVDKAQGDASKVTAKGPGLETTGNIANKPTYFDIYTAGAGVGDIGIEVEDPQGKNSVELLVEDRGNQVYRCVYKPVQPGPHVVKVSFAGDAIPKSPFGVQIGEACNPNACRASGRGLQPKGVRIRETADFKVDTKAAGSGELGVTVKGPKGLEELVKQKGFLDGVYSFEYYPSTPGKYSVAVTWGGHHIPKSPFEVQVGPEAGMQKVRAWGPGLHGGIVGRSADFVVESIGSEVGTLGFAIEGPSQAKIEYDDQNDGSCDVKYWPKEPGEYAVHIMCDDEDIKDSPYMAFIHPATGDYNPDLVQAYGPGLEKSGCTINNPAEFIVDPKDAGSAPLKILAQDGEGQPIDIQMKSRMDGTYACSYTPLKAIKHTIAVVWGGVNIPHSPYRVNIGQGSHPQKVKVFGPGVERSGLKANEPTHFTVDCTEAGEGDVSVGIKCDARVLSDDEEDVDFDIIHNANDTFTVKYVPPAPGRYTIKVLFASQEIPASPFRVKVDPSHDASKVKAEGPGLSKAGVENGKPTHFTVHTKGAGKAPLNVQFSSPLPGEAVKDLDIIDNYDYSHTVKYTPTQQGNMQVLVTYGGDPIPKSPFTVGVAAPLDLSKIKINGLENRVEVGKDQEFAIDTNGAGGQGKLDVTILSPSRKVVPCLVAPVAGRECSTAKFIPREEGLFAVDVTYDGHPVPGSPYTVEASLPPDPTKVKAHGPGLEGGLVGKPAEFTIDTKGAGTGGLGLTVEGPCEAKIECSDNGDGTCSVSYLPTKPGEYFVNILFEEVHIPGSPFKADIEMPFDPSKVVASGPGLEHGKVGEPGILCVDCSEAGPGTLGLEAVSDSGAKAEVSIQNNKDGTYAVTYVPLTAGMYTLTMKYGGELVPHFPAWVKVEPAIDTSGIKAFGPGIEGKDVFREATTDFTVDSRPLTQVGGDHIKAQITNPSGASTECFVKDNADGTYQVEYTPFEKGFHVVEVTYDDVPIPNSPFKVAVTEGCQPSRVHAQGPGLKEAFTNKSNVFTVVTRGAGIGGLGITVEGPSESKINCRDNKDGSCSAEYIPFAPGDYDVNITYGGVHIPGSPFRVPSKDVVDPSKVKIAGPGLSSCVRACIPQSFTVDSSKAGLAPLEVRVLGPRGLVEPVNVVDNGDGTHTVTYTPSQEGPYIVSVKYADEEIPRSPFKVKVLPTYDASKVTASGPGLSAYGVPASLPVEFAIDARDAGEGLLAVQITDQEGKPQRATVHDNKDGTYAVTYIPDKTGRYMIGVTYGGDNIPLSPYRIRATQTGDASKCLATGPGIAPTVKTGEEVGFVVDAKTAGKGKVTCVILTPDGTEAEADVIENEDGTYDIFYTAAKPGTYVIYVRFGGVDIPNSPFTVMATDGEVTAMEEAPVNACPPGFRPWVTEEAYVPVSDMNGLGFKPFDLVIPFAVRKGEITGTVHMPSGKKATPEIVDNKDGTVTVRYAPTEVGLHEMHIKYRGSHIPESPLQFYVNYPNSGSVSAYGPGLVYGVANKTATFTIVTEDAGEGGLDLAIEGPSKAEISCIDNKDGTCTVTYLPTLPGDYSILVKYNDKHIPGSPFTAKITDDNRRCSQVKLGSAADFLLDISETDLSTLTASIKAPSGRDEPCLLKRLPNNHIGISFIPREVGEHLVSIKKNGNHVANSPVSIMVVQSEIGDARRAKVYGQGLSEGRTFEMSDFIVDTRDAGYGGISLAVEGPSKVDIQTEDLEDGTCKVSYFPTVPGVYIVSTKFADEHVPGSPFTVKISGEGRVRESITRTSRAPAVATVGSICDLNLKIPEINSSDMSAHVTSPSGHVTEAEIVPMGKNSHCVRFVPQEMGVHTVSVKYRGQHVTGSPFQFTVGPLGEGGAHKVRAGGPGLERGEAGIPAEFSIWTREAGAGGLSIAVEGPSKAEITFDDHKNGSCGVSYIAQEPGNYEVSIKFNDEHIPDSPYLVPVIAPSDDARCLTVLSLQESGLKVNQPASFAIRLNGAKGKIDAKVHSPSGAVEECHVSELEPDKYAVRFIPHENGIHTIDVKFNGSHVVGSPFKVRVGEPGQAGNPALVSAYGAGLETGTTGIQSEFFINTTQAGPGTLSVTIEGPSKVKMDCQEIPEGYKVMYTPMAPGNYLIGVKYGGPNHISRSPFKAKVTGQRLVSPGSANETSSILVESVTRSSTETCYSAIPKSSSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGKQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP | ||||||
Modified residue | 216 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 519 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 681 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 730 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 886 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 932 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 983 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1028 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1307 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1316 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1433 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1505 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1602 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1780 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 2083 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2369 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2465 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2468 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) | ||||
Sequence: K | ||||||
Modified residue | 2478 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2481 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2492 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2518 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 2524 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 2576 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
ISGylation prevents ability to interact with the upstream activators of the JNK cascade and inhibits IFNA-induced JNK signaling.
Ubiquitination by a SCF-like complex containing ASB2 isoform 1 leads to proteasomal degradation which promotes muscle differentiation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in hippocampus, cortex, cerebellar Purkinje cells and granule cell layers.
Developmental stage
Expressed within the ventricular, periventricular and subventricular zones at 12.5 dpc; olfactory epithelium, radial glial fibers, cortical plate and lateral ventricles at 16 dpc; in a lesser degree in lung, renal cortices and alimentary tract.
Gene expression databases
Interaction
Subunit
Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By similarity).
Interacts with MICALL2. Interacts with RFLNA and RFLNB (PubMed:21709252, PubMed:24436304).
Interacts with ASB2 isoform 1; the interaction targets FLNB for proteasomal degradation (PubMed:26343497).
Interacts with MICALL2. Interacts with RFLNA and RFLNB (PubMed:21709252, PubMed:24436304).
Interacts with ASB2 isoform 1; the interaction targets FLNB for proteasomal degradation (PubMed:26343497).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-239 | Actin-binding | ||||
Sequence: MPVTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMHHKYHQRPTFRQMKLENVSVALEFLDHESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPVWEDEGDDDAKKQTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPRKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPK | ||||||
Domain | 16-122 | Calponin-homology (CH) 1 | ||||
Sequence: KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMHHKYHQRPTFRQMKLENVSVALEFLDHESIKLVSIDSKAIVDGNLKLILGLVWTLILHYS | ||||||
Domain | 139-242 | Calponin-homology (CH) 2 | ||||
Sequence: QTPKQRLLGWIQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCPDWESWDPRKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPKAKL | ||||||
Region | 244-267 | Disordered | ||||
Sequence: PGAPLKPKLNPKKARAYGRGIEPT | ||||||
Repeat | 249-347 | Filamin 1 | ||||
Sequence: KPKLNPKKARAYGRGIEPTGNMVKQPAKFTVDTISAGQGDVMVFVEDPEGNKEEARVTPDSDKNKTYSVEYLPKVTGLHKVIVLFAGQHISKSPFEVNV | ||||||
Repeat | 349-446 | Filamin 2 | ||||
Sequence: KAQGDASKVTAKGPGLETTGNIANKPTYFDIYTAGAGVGDIGIEVEDPQGKNSVELLVEDRGNQVYRCVYKPVQPGPHVVKVSFAGDAIPKSPFGVQI | ||||||
Repeat | 447-543 | Filamin 3 | ||||
Sequence: GEACNPNACRASGRGLQPKGVRIRETADFKVDTKAAGSGELGVTVKGPKGLEELVKQKGFLDGVYSFEYYPSTPGKYSVAVTWGGHHIPKSPFEVQV | ||||||
Repeat | 544-636 | Filamin 4 | ||||
Sequence: GPEAGMQKVRAWGPGLHGGIVGRSADFVVESIGSEVGTLGFAIEGPSQAKIEYDDQNDGSCDVKYWPKEPGEYAVHIMCDDEDIKDSPYMAFI | ||||||
Repeat | 640-736 | Filamin 5 | ||||
Sequence: TGDYNPDLVQAYGPGLEKSGCTINNPAEFIVDPKDAGSAPLKILAQDGEGQPIDIQMKSRMDGTYACSYTPLKAIKHTIAVVWGGVNIPHSPYRVNI | ||||||
Repeat | 737-839 | Filamin 6 | ||||
Sequence: GQGSHPQKVKVFGPGVERSGLKANEPTHFTVDCTEAGEGDVSVGIKCDARVLSDDEEDVDFDIIHNANDTFTVKYVPPAPGRYTIKVLFASQEIPASPFRVKV | ||||||
Region | 837-862 | Disordered | ||||
Sequence: VKVDPSHDASKVKAEGPGLSKAGVEN | ||||||
Repeat | 840-938 | Filamin 7 | ||||
Sequence: DPSHDASKVKAEGPGLSKAGVENGKPTHFTVHTKGAGKAPLNVQFSSPLPGEAVKDLDIIDNYDYSHTVKYTPTQQGNMQVLVTYGGDPIPKSPFTVGV | ||||||
Repeat | 939-1034 | Filamin 8 | ||||
Sequence: AAPLDLSKIKINGLENRVEVGKDQEFAIDTNGAGGQGKLDVTILSPSRKVVPCLVAPVAGRECSTAKFIPREEGLFAVDVTYDGHPVPGSPYTVEA | ||||||
Repeat | 1035-1127 | Filamin 9 | ||||
Sequence: SLPPDPTKVKAHGPGLEGGLVGKPAEFTIDTKGAGTGGLGLTVEGPCEAKIECSDNGDGTCSVSYLPTKPGEYFVNILFEEVHIPGSPFKADI | ||||||
Repeat | 1128-1222 | Filamin 10 | ||||
Sequence: EMPFDPSKVVASGPGLEHGKVGEPGILCVDCSEAGPGTLGLEAVSDSGAKAEVSIQNNKDGTYAVTYVPLTAGMYTLTMKYGGELVPHFPAWVKV | ||||||
Repeat | 1223-1322 | Filamin 11 | ||||
Sequence: EPAIDTSGIKAFGPGIEGKDVFREATTDFTVDSRPLTQVGGDHIKAQITNPSGASTECFVKDNADGTYQVEYTPFEKGFHVVEVTYDDVPIPNSPFKVAV | ||||||
Repeat | 1323-1415 | Filamin 12 | ||||
Sequence: TEGCQPSRVHAQGPGLKEAFTNKSNVFTVVTRGAGIGGLGITVEGPSESKINCRDNKDGSCSAEYIPFAPGDYDVNITYGGVHIPGSPFRVPS | ||||||
Repeat | 1416-1511 | Filamin 13 | ||||
Sequence: KDVVDPSKVKIAGPGLSSCVRACIPQSFTVDSSKAGLAPLEVRVLGPRGLVEPVNVVDNGDGTHTVTYTPSQEGPYIVSVKYADEEIPRSPFKVKV | ||||||
Repeat | 1512-1608 | Filamin 14 | ||||
Sequence: LPTYDASKVTASGPGLSAYGVPASLPVEFAIDARDAGEGLLAVQITDQEGKPQRATVHDNKDGTYAVTYIPDKTGRYMIGVTYGGDNIPLSPYRIRA | ||||||
Repeat | 1609-1704 | Filamin 15 | ||||
Sequence: TQTGDASKCLATGPGIAPTVKTGEEVGFVVDAKTAGKGKVTCVILTPDGTEAEADVIENEDGTYDIFYTAAKPGTYVIYVRFGGVDIPNSPFTVMA | ||||||
Region | 1705-1728 | Hinge 1 | ||||
Sequence: TDGEVTAMEEAPVNACPPGFRPWV | ||||||
Repeat | 1729-1813 | Filamin 16 | ||||
Sequence: TEEAYVPVSDMNGLGFKPFDLVIPFAVRKGEITGTVHMPSGKKATPEIVDNKDGTVTVRYAPTEVGLHEMHIKYRGSHIPESPLQ | ||||||
Repeat | 1816-1908 | Filamin 17 | ||||
Sequence: VNYPNSGSVSAYGPGLVYGVANKTATFTIVTEDAGEGGLDLAIEGPSKAEISCIDNKDGTCTVTYLPTLPGDYSILVKYNDKHIPGSPFTAKI | ||||||
Repeat | 1919-1994 | Filamin 18 | ||||
Sequence: KLGSAADFLLDISETDLSTLTASIKAPSGRDEPCLLKRLPNNHIGISFIPREVGEHLVSIKKNGNHVANSPVSIMV | ||||||
Repeat | 1997-2089 | Filamin 19 | ||||
Sequence: SEIGDARRAKVYGQGLSEGRTFEMSDFIVDTRDAGYGGISLAVEGPSKVDIQTEDLEDGTCKVSYFPTVPGVYIVSTKFADEHVPGSPFTVKI | ||||||
Repeat | 2091-2185 | Filamin 20 | ||||
Sequence: GEGRVRESITRTSRAPAVATVGSICDLNLKIPEINSSDMSAHVTSPSGHVTEAEIVPMGKNSHCVRFVPQEMGVHTVSVKYRGQHVTGSPFQFTV | ||||||
Repeat | 2188-2280 | Filamin 21 | ||||
Sequence: LGEGGAHKVRAGGPGLERGEAGIPAEFSIWTREAGAGGLSIAVEGPSKAEITFDDHKNGSCGVSYIAQEPGNYEVSIKFNDEHIPDSPYLVPV | ||||||
Repeat | 2282-2375 | Filamin 22 | ||||
Sequence: APSDDARCLTVLSLQESGLKVNQPASFAIRLNGAKGKIDAKVHSPSGAVEECHVSELEPDKYAVRFIPHENGIHTIDVKFNGSHVVGSPFKVRV | ||||||
Repeat | 2379-2471 | Filamin 23 | ||||
Sequence: GQAGNPALVSAYGAGLETGTTGIQSEFFINTTQAGPGTLSVTIEGPSKVKMDCQEIPEGYKVMYTPMAPGNYLIGVKYGGPNHISRSPFKAKV | ||||||
Region | 2472-2506 | Hinge 2 | ||||
Sequence: TGQRLVSPGSANETSSILVESVTRSSTETCYSAIP | ||||||
Region | 2472-2602 | Self-association site, tail | ||||
Sequence: TGQRLVSPGSANETSSILVESVTRSSTETCYSAIPKSSSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGKQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP | ||||||
Repeat | 2507-2601 | Filamin 24 | ||||
Sequence: KSSSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGKQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTV |
Domain
Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. The first hinge region prevents binding to ITGA and ITGB subunits (By similarity).
Sequence similarities
Belongs to the filamin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,602
- Mass (Da)277,825
- Last updated2011-07-27 v3
- Checksum41BA737EC52A89DB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC129222 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC140322 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF353669 EMBL· GenBank· DDBJ | AAL68445.1 EMBL· GenBank· DDBJ | mRNA | ||
AF353672 EMBL· GenBank· DDBJ | AAL68448.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003959 EMBL· GenBank· DDBJ | AAH03959.1 EMBL· GenBank· DDBJ | mRNA | ||
BC048835 EMBL· GenBank· DDBJ | AAH48835.1 EMBL· GenBank· DDBJ | mRNA |