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0SPTA1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSPTA1
DescriptionSpectrin alpha chain, erythrocyte (erythroid alpha-spectrin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008091 spectrin (TAS)
0051015 actin filament binding (TAS)
0005515 protein binding (IPI)
0005200 structural constituent of cytoskeleton (TAS)
0007015 actin filament organization (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:
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
Phagocytes form the first line of defence against invasion by micro-organisms. Engulfing of bacteria by neutrophils is accompanied by theconsumption of large amounts of oxygen - a so-called respiratory burst.Defects in phagocytosis involving the lack of a respiratory burst giverise to chronic granulomatous disease (CGD).n which patients are pre-disposed to infection.ften from otherwise non-pathogenic bacteria .Regulation of the respiratory burst takes place at the phagocytic vacuole.The process is mediated by NADPH oxidase.hich transports electrons acrossthe plasma membrane to form superoxide (an oxygen molecule with an extraelectron that is toxic to normal cells) in the vacuole interior. Theelectrons are carried across the membrane by a short electron transportchain in the form of an unusual flavocytochrome b .To conserve NADPH and avoid the toxic effects of superoxide.he oxidase remains inactive until it receives an appropriate stimulus. Activationinvolves the participation of a number of cytosolic proteins.ome of which attach to the flavocytochrome. P47phox.67phox and p40phox arespecialised components of phagocytic cells.ll of which contain SH3domains .y means of which they attach to proline-rich regions of otherproteins. Upon activation.47phox and p67phox are phosphorylated and.ith p40phox.ranslocate to the region of the plasma membrane formingthe phagocytic vacuole.here they associates with hydrophilic regionsof the flavocytochrome .
  IPR000108:Neutrophil cytosol factor 2
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1.... and 12; these residues are denoted by X...Y.X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand).
  IPR002048:Calcium-binding EF-hand
This domain consists of a duplication of two EF-hand units.here each unit is composed of two helices connected by a twelve-residue calcium-binding loop. The calcium ion in the EF-hand loop is coordinated in a pentagonal bipyramidal configuration. Many calcium-binding proteins contain an EF-hand type calcium-binding domain . These include: calbindin D9K.100 proteins such as calcyclin.olcalcin phl p 7 (a calcium-binding pollen allergen).steonectin.arvalbumin.almodulin family of proteins (troponin C.altractin.dc4p.yosin essential chain.alcineurin.ecoverin.eurocalcin).lasmodial-specific CaII-binding protein Cbp40.enta-EF-Hand proteins (sorcin.rancalcin.alpain).s well as multidomain proteins such as phosphoinositide-specific phospholipase C.ystrophin.b1 and alpha-actinin. The fold consists of four helices and an open array of two hairpins.
  IPR011992:EF-Hand type
Spectrin is an elongated protein that belongs to a family of related molecules (including dystrophin and alpha-actinin) that contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments . The protein is an alpha-beta heterodimer in which the alpha and beta monomers associate in an anti-parallel fashion . Assembly involves initial contact of complementary nucleation sites on each subunit.ia four tandem repeat regions . Following nucleation.he remainder of the subunits associate rapidly along their full lengths to form a dimer by super-coiling around each other.orming a rope-like.lexible rod . Assembly terminates if either polypeptide is interrupted by protease cleavage. Heterozygotic mutations involving either nucleation site are predicted to affect allele incorporation into the mature membrane skeleton . The structure of a repeat unit of alpha-spectrin has been determined to 1.8A resolution by means of X-ray crystallography . This was shown to comprise an anti-parallel three-helix bundle separated by two loops.hich folds into a left-handed coiled coil . At the interface between tandem repeats.ydrophobic interactions may constrain intersegment flexibility. The interaction between alpha- and beta-subunits is mediated by the association of two helices at the C-terminus of the beta-chain and a single helix from the N-terminus of the alpha-chain. Mutations that affect these critical helix side-chain interactions disrupt spectrin associations that sustain the integrity of erythrocyte membranes giving rise to haemolytic anaemias . These haemolytic syndromes include hereditary elliptocytosis.ts aggravated form hereditary pyropoikilocytosis and hereditary spherocytosis .
  IPR013315:Spectrin alpha chain
IPR002017:Spectrin 
Evalue:-37.1870880126953 
Location:1712-1816IPR002017:Spectrin 
Evalue:-33.7958793640137 
Location:793-897IPR002017:Spectrin 
Evalue:-33.5376014709473 
Location:476-580IPR002017:Spectrin 
Evalue:-33.0757217407227 
Location:264-368IPR002017:Spectrin 
Evalue:-32.9586067199707 
Location:158-262IPR002017:Spectrin 
Evalue:-32.9208183288574 
Location:687-791IPR002017:Spectrin 
Evalue:-31.9208183288574 
Location:582-685IPR002017:Spectrin 
Evalue:-31.2006587982178 
Location:370-474IPR002017:Spectrin 
Evalue:-30.5376014709473 
Location:1183-1287IPR002017:Spectrin 
Evalue:-29.2518119812012 
Location:1289-1393IPR002017:Spectrin 
Evalue:-28.9586067199707 
Location:1818-1925IPR002017:Spectrin 
Evalue:-27.3872165679932 
Location:1606-1710IPR002017:Spectrin 
Evalue:-26.7958793640137 
Location:53-156IPR002017:Spectrin 
Evalue:-25.6989707946777 
Location:1395-1498IPR002017:Spectrin 
Evalue:-25.4814853668213 
Location:1927-2032IPR002017:SPEC 
Evalue:-24.8860566476932 
Location:1503-1603IPR002017:Spectrin 
Evalue:-23.2757244110107 
Location:2042-2146IPR002017:Spectrin 
Evalue:-21.6777801513672 
Location:1082-1181IPR001452:SH3_1 
Evalue:-20.2291488647461 
Location:980-1034IPR002017:Spectrin 
Evalue:-14.0915145874023 
Location:899-969IPR002017:Spectrin 
Evalue:-12.5228786468506 
Location:2156-2257IPR002017:Spectrin 
Evalue:-6.92081880569458 
Location:19-51IPR002048:efhand 
Evalue:-1.69896996021271 
Location:2274-2302IPR011992:EF-Hand_type 
Evalue:0 
Location:2345-2418
SequencesProtein: SPTA1_HUMAN (2418 aa)
mRNA: M61877
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)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 229 residues, 156847119-156847803Exon2: 50 residues, 156849230-156849375Exon3: 51 residues, 156850134-156850281Exon4: 20 residues, 156850666-156850720Exon5: 64 residues, 156851629-156851817Exon6: 19 residues, 156853950-156854002Exon7: 8 residues, 156854452-156854470Exon8: 39 residues, 156855635-156855748Exon9: 101 residues, 156856583-156856880Exon10: 72 residues, 156859396-156859606Exon11: 27 residues, 156862559-156862636Exon12: 58 residues, 156863252-156863421Exon13: 35 residues, 156864038-156864137Exon14: 46 residues, 156870956-156871089Exon15: 42 residues, 156872326-156872448Exon16: 42 residues, 156873054-156873175Exon17: 71 residues, 156874446-156874655Exon18: 37 residues, 156875995-156876100Exon19: 48 residues, 156876283-156876421Exon20: 46 residues, 156878824-156878956Exon21: 56 residues, 156879227-156879390Exon22: 36 residues, 156879735-156879839Exon23: 50 residues, 156880666-156880810Exon24: 68 residues, 156881601-156881799Exon25: 35 residues, 156881908-156882008Exon26: 62 residues, 156883952-156884134Exon27: 50 residues, 156884922-156885067Exon28: 32 residues, 156886269-156886361Exon29: 36 residues, 156887780-156887882Exon30: 64 residues, 156888880-156889067Exon31: 52 residues, 156889687-156889839Exon32: 48 residues, 156891024-156891162Exon33: 33 residues, 156892977-156893070Exon34: 74 residues, 156893890-156894108Exon35: 43 residues, 156897700-156897823Exon36: 83 residues, 156899115-156899359Exon37: 62 residues, 156902729-156902911Exon38: 70 residues, 156904271-156904476Exon39: 54 residues, 156905821-156905977Exon40: 28 residues, 156906122-156906200Exon41: 39 residues, 156907756-156907867Exon42: 48 residues, 156908472-156908610Exon43: 36 residues, 156910742-156910844Exon44: 47 residues, 156910953-156911089Exon45: 53 residues, 156912554-156912709Exon46: 50 residues, 156914103-156914248Exon47: 46 residues, 156914814-156914948Exon48: 51 residues, 156916996-156917143Exon49: 49 residues, 156917940-156918081Exon50: 44 residues, 156919784-156919910Exon51: 82 residues, 156921521-156921761Exon52: 70 residues, 156922907-156923112Exon53: 2 residues, -Jump to SPTA1_HUMAN  
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