SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0SPTB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSPTBN1
DescriptionSpectrin beta chain, brain 1 (spectrin, non-erythroid beta chain 1) (beta-ii spectrin) (fodrin beta chain).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008091 spectrin (TAS)
0003779 actin binding (TAS)
0005200 structural constituent of cytoskeleton (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/214607036.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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:
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
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
The pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
Spectrin repeats are found in several proteins involved incytoskeletal structure. These include spectrin.lpha-actininand dystrophin. The spectrin repeat forms athree helix bundle. The second helix is interrupted by prolinein some sequences. The repeats are defined by a characteristictryptophan (W) residue at position 17 in helix A and a leucine(L) at 2 residues from the carboxyl end of helix C.
  IPR002017:Spectrin repeat
Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane; it associates with band 4.1 and actin to form the cytoskeletal super-structure. The native spectrin molecule is a tetramer comprising two anti-parallel heterodimers joined head to head.uch that the C terminus of the alpha-subunit and the N terminus of the beta-subunit are included within the same molecule.Spectrin is similar to alpha-actinin and dystrophin.nd contains a pleckstrin homology (PH) domain. The exact function of the PH domain is unknown.ut evidence suggests that it contains an electrostatically-polarised pocket that facilitates binding of a ligand (e.g.. peptide). The PH domain contains a number of hydrophobic residues that form a hydrophobic core responsible for protein stability. The spectrin PH domain .hich has the familiar 7-stranded anti-parallel up and down beta-barrel capped by a C-terminal amphiphilic alpha helical cap .ontains insertions that confer 2 additional turns of alpha-helix in the loop between strands 3 and 4. The C-terminal helix is packed into a gorge between strands 1 and 2.nd lies parallel to strand 7 .
  IPR001605:Spectrin/pleckstrin-like
IPR001715:CH 
Evalue:-38.7212448120117 
Location:174-278IPR002017:Spectrin 
Evalue:-38.3872146606445 
Location:638-742IPR011993:PH_type 
Evalue:-36.6197891235352 
Location:2200-2305IPR001715:CH 
Evalue:-33.5376014709473 
Location:55-158IPR002017:Spectrin 
Evalue:-33.1135101318359 
Location:744-847IPR002017:Spectrin 
Evalue:-31.408935546875 
Location:528-636IPR002017:Spectrin 
Evalue:-31.236572265625 
Location:1698-1803IPR002017:Spectrin 
Evalue:-30.7958793640137 
Location:849-953IPR002017:Spectrin 
Evalue:-30.1307678222656 
Location:422-526IPR002017:Spectrin 
Evalue:-29.8538722991943 
Location:1592-1696IPR002017:Spectrin 
Evalue:-29.6575775146484 
Location:1485-1590IPR002017:Spectrin 
Evalue:-26.2757244110107 
Location:955-1060IPR002017:Spectrin 
Evalue:-25.8860569000244 
Location:1805-1909IPR002017:Spectrin 
Evalue:-25.4685211181641 
Location:1275-1378IPR002017:Spectrin 
Evalue:-24.075719833374 
Location:1911-2015IPR002017:SPEC 
Evalue:-23.7447274948967 
Location:1065-1166IPR002017:SPEC 
Evalue:-23.4814860601221 
Location:1172-1272IPR002017:Spectrin 
Evalue:-23.4685211181641 
Location:1380-1483IPR002017:Spectrin 
Evalue:-16.0132274627686 
Location:2017-2077IPR002017:Spectrin 
Evalue:-16 
Location:302-412
SequencesProtein: SPTB2_HUMAN (2364 aa)
mRNA: NM_003128
Local Annotation
Synapse Ontology
A dendritic spine is a mushroom-shaped bud that protrudes from a dendrite and forms one half of a synapse, especially in synapses of the cortex. The dendrites of cortical neurons typically are densely covered with such spines, which enable single cells to receive input from thousands of others.
sdb:0134 dendritic spine  (Evidence:keywords)
cytoskeleton filaments is one kind of structural components to maintain synapse morphology and bear the related function which is connected with the synaptic morphology.
sdb:0280 cytoskeletal filaments  (Evidence:keywords)
actin exists in two states within the cell: as polymerized two-stranded helical filaments (F-actin) or as monomers (Gactin), which provide the building blocks for filament assembly.
sdb:0283 G-actin  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 66 residues, 54607010-54607207Exon2: 52 residues, 54679732-54679884Exon3: 60 residues, 54692801-54692975Exon4: 32 residues, 54696847-54696939Exon5: 29 residues, 54698248-54698329Exon6: 40 residues, 54698718-54698834Exon7: 39 residues, 54702040-54702153Exon8: 64 residues, 54702940-54703128Exon9: 41 residues, 54704119-54704237Exon10: 55 residues, 54705444-54705603Exon11: 103 residues, 54706572-54706875Exon12: 53 residues, 54708737-54708891Exon13: 292 residues, 54709573-54710444Exon14: 48 residues, 54710532-54710670Exon15: 254 residues, 54711495-54712252Exon16: 69 residues, 54713206-54713409Exon17: 32 residues, 54718353-54718444Exon18: 51 residues, 54723623-54723770Exon19: 90 residues, 54724963-54725227Exon20: 77 residues, 54725869-54726094Exon21: 32 residues, 54726568-54726658Exon22: 96 residues, 54726834-54727116Exon23: 45 residues, 54727771-54727902Exon24: 70 residues, 54729626-54729831Exon25: 127 residues, 54730255-54730630Exon26: 83 residues, 54734249-54734494Exon27: 48 residues, 54735710-54735849Exon28: 30 residues, 54736554-54736639Exon29: 67 residues, 54738490-54738687Exon30: 39 residues, 54739794-54739907Exon31: 23 residues, 54740576-54740640Exon32: 81 residues, 54745093-54745332Exon33: 60 residues, 54746555-54746729Exon34: 16 residues, 54748244-54748287Exon35: 127 residues, 54748991-54749366Exon36: 2 residues, -Jump to SPTB2_HUMAN  
Tune and view alternative isoforms