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0FLNB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFLNB
DescriptionFilamin b (fln-b) (beta-filamin) (actin-binding-like protein) (thyroid autoantigen) (truncated actin-binding protein) (truncated abp) (abp- 280 homolog) (abp-278) (filamin 3) (filamin homolog 1) (fh1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0015629 actin cytoskeleton (TAS)
0005887 integral to plasma membrane (TAS)
0003779 actin binding (NAS)
0030036 actin cytoskeleton organization and biogenesis (TAS)
0007016 cytoskeletal anchoring (TAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The many different actin cross-linking proteins share a common architecture.onsisting of a globular actin-binding domain and an extended rod. Whereas their actin-binding domains consist of two calponin homology domains (see ).heir rods fall into three families.The rod domain of the family including the Dictyostelium discoideum gelation factor (ABP120) and human filamin (ABP280) is constructed from tandem repeats of a 100-residue motif that is glycine and proline rich . The gelation factors rod contains 6 copies of the repeat.hereas filamin has a rod constructed from 24 repeats. The resolution of the 3D structure of rod repeats from the gelation factor has shown that they consist of a beta-sandwich.ormed by two beta-sheets arranged in an immunoglobulin-like fold . Because conserved residues that form the core of the repeats are preserved in filamin.he repeat structure should be common to the members of the gelation factor/filamin family.The head to tail homodimerisation is crucial to the function of the ABP120 and ABP280 proteins. This interaction involves a small portion at the distal end of the rod domains. For the gelation factor it has been shown that the carboxy-terminal repeat 6 dimerises through a double edge-to-edge extension of the beta-sheet and that repeat 5 contributes to dimerisation to some extent .
  IPR001298:Filamin/ABP280 repeat
The calponin homology domain (also known as CH-domain) is a superfamily of actin-binding domains found in both cytoskeletal proteins and signal transduction proteins . It comprises the following groups of actin-binding domains:Actinin-type (including spectrin.imbrin.BP-280) (see ).Calponin-type (see ).A comprehensive review of proteins containing this type of actin-binding domains is given in .The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity . Most proteins have two copies of the CH domain.owever some proteins such as calponin and the human vav proto-oncogene () have only a single copy. The structure of an example CH-domain has recently been solved .
  IPR001715:Calponin-like actin-binding
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR001298:Filamin 
Evalue:-47.0757217407227 
Location:1039-1124IPR001298:Filamin 
Evalue:-41.0861854553223 
Location:1820-1905IPR001298:Filamin 
Evalue:-40.8538703918457 
Location:2192-2277IPR001298:IG_FLMN 
Evalue:-39.301029995664 
Location:1420-1514IPR001298:IG_FLMN 
Evalue:-36.3098039199715 
Location:1613-1707IPR001298:IG_FLMN 
Evalue:-36.0362121726544 
Location:1327-1418IPR001298:IG_FLMN 
Evalue:-35.8538719643218 
Location:353-449IPR001298:Filamin 
Evalue:-35.7212448120117 
Location:253-344IPR001298:Filamin 
Evalue:-35.6197891235352 
Location:2001-2086IPR001298:IG_FLMN 
Evalue:-35.5850266520292 
Location:451-546IPR001298:IG_FLMN 
Evalue:-33.8538719643218 
Location:644-739IPR001298:Filamin 
Evalue:-33.8239097595215 
Location:1516-1605IPR001298:IG_FLMN 
Evalue:-33.568636235841 
Location:1132-1225IPR001298:IG_FLMN 
Evalue:-33.4685210829577 
Location:1227-1325IPR001298:Filamin 
Evalue:-32.0604820251465 
Location:741-836IPR001298:Filamin 
Evalue:-30.0969104766846 
Location:548-633IPR001298:Filamin 
Evalue:-29.7212467193604 
Location:844-935IPR001298:IG_FLMN 
Evalue:-29.1079053973095 
Location:943-1037IPR001298:Filamin 
Evalue:-29.0555171966553 
Location:2511-2598IPR001298:IG_FLMN 
Evalue:-28.7212463990472 
Location:2286-2378IPR001715:CH 
Evalue:-28.6989707946777 
Location:17-122IPR001298:IG_FLMN 
Evalue:-27.0409586076789 
Location:2383-2474IPR001715:CH 
Evalue:-26.0268726348877 
Location:140-242IPR001298:IG_FLMN 
Evalue:-8.63827216398241 
Location:1730-1819IPR001298:IG_FLMN 
Evalue:-8.52287874528034 
Location:2101-2188IPR001298:IG_FLMN 
Evalue:-8.4089353929735 
Location:1912-1997
SequencesProtein: FLNB_HUMAN (2602 aa)
mRNA: AB191258 NM_001457
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK04437
  Level 3 annotation:
    filamin
  Level 2 annotation:
    MAPK signaling pathway
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 146 residues, 57969188-57969623Exon2: 85 residues, 58037812-58038061Exon3: 34 residues, 58039483-58039581Exon4: 51 residues, 58042395-58042543Exon5: 41 residues, 58055602-58055721Exon6: 28 residues, 58056907-58056985Exon7: 56 residues, 58058581-58058744Exon8: 68 residues, 58059477-58059675Exon9: 48 residues, 58062969-58063107Exon10: 44 residues, 58064725-58064852Exon11: 47 residues, 58065846-58065983Exon12: 66 residues, 58067446-58067640Exon13: 40 residues, 58069224-58069338Exon14: 50 residues, 58069945-58070089Exon15: 43 residues, 58070342-58070466Exon16: 55 residues, 58070776-58070937Exon17: 32 residues, 58072557-58072648Exon18: 58 residues, 58072915-58073085Exon19: 41 residues, 58079638-58079756Exon20: 89 residues, 58082007-58082270Exon21: 201 residues, 58083859-58084457Exon22: 60 residues, 58085098-58085272Exon23: 56 residues, 58086347-58086510Exon24: 55 residues, 58087368-58087529Exon25: 58 residues, 58091507-58091675Exon26: 43 residues, 58093574-58093698Exon27: 54 residues, 58095382-58095539Exon28: 65 residues, 58096745-58096935Exon29: 84 residues, 58099048-58099296Exon30: 15 residues, 58102624-58102663Exon31: 36 residues, 58103416-58103519Exon32: 49 residues, 58104239-58104380Exon33: 45 residues, 58106687-58106816Exon34: 60 residues, 58107586-58107760Exon35: 55 residues, 58108972-58109131Exon36: 70 residues, 58109415-58109619Exon37: 53 residues, 58110616-58110769Exon38: 43 residues, 58110871-58110994Exon39: 91 residues, 58114141-58114408Exon40: 48 residues, 58115557-58115695Exon41: 40 residues, 58116726-58116842Exon42: 46 residues, 58120320-58120453Exon43: 61 residues, 58123920-58124097Exon44: 75 residues, 58129206-58129425Exon45: 70 residues, 58130356-58130560Exon46: 560 residues, 58131341-58133015Exon47: 2 residues, -Jump to FLNB_HUMANExon1: 142 residues, 57969200-57969623Exon2: 85 residues, 58037812-58038061Exon3: 34 residues, 58039483-58039581Exon4: 51 residues, 58042395-58042543Exon5: 41 residues, 58055602-58055721Exon6: 28 residues, 58056907-58056985Exon7: 56 residues, 58058581-58058744Exon8: 68 residues, 58059477-58059675Exon9: 48 residues, 58062969-58063107Exon10: 44 residues, 58064725-58064852Exon11: 47 residues, 58065846-58065983Exon12: 66 residues, 58067446-58067640Exon13: 40 residues, 58069224-58069338Exon14: 50 residues, 58069945-58070089Exon15: 43 residues, 58070342-58070466Exon16: 55 residues, 58070776-58070937Exon17: 32 residues, 58072557-58072648Exon18: 58 residues, 58072915-58073085Exon19: 41 residues, 58079638-58079756Exon20: 89 residues, 58082007-58082270Exon21: 201 residues, 58083859-58084457Exon22: 60 residues, 58085098-58085272Exon23: 56 residues, 58086347-58086510Exon24: 55 residues, 58087368-58087529Exon25: 58 residues, 58091507-58091675Exon26: 43 residues, 58093574-58093698Exon27: 54 residues, 58095382-58095539Exon28: 65 residues, 58096745-58096935Exon29: 84 residues, 58099048-58099296Exon30: 26 residues, 58102624-58102696Exon31: 36 residues, 58103416-58103519Exon32: 49 residues, 58104239-58104380Exon33: 45 residues, 58106687-58106816Exon34: 60 residues, 58107586-58107760Exon35: 55 residues, 58108972-58109131Exon36: 70 residues, 58109415-58109619Exon37: 53 residues, 58110616-58110769Exon38: 43 residues, 58110871-58110994Exon39: 91 residues, 58114141-58114408Exon40: 48 residues, 58115557-58115695Exon41: 40 residues, 58116726-58116842Exon42: 46 residues, 58120320-58120453Exon43: 61 residues, 58123920-58124097Exon44: 75 residues, 58129206-58129425Exon45: 70 residues, 58130356-58130560Exon46: 560 residues, 58131341-58133015Exon47: 2 residues, -Jump to FLNB_HUMAN  
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Loci Cluster (Details)Loci: 4613 58388397-58394594 ~-6K 25949(PDHB)(-)Loci: 3362 57969188-58133015 ~-164K 25933(FLNB)(+)Link out to UCSC