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0STAB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSTAB2
DescriptionStabilin-2 precursor (feel-2 protein) (fasciclin egf-like laminin-type egf-like and link domain-containing scavenger receptor-1) (fas1 egf- like and x-link domain containing adhesion molecule 2) (hyaluronan receptor for endocytosis) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009897 external side of plasma membrane (ISS)
0005887 integral to plasma membrane (IDA)
0008368 Gram-negative bacterial binding (IDA)
0005540 hyaluronic acid binding (ISS)
0005041 low-density lipoprotein receptor activity (IDA)
0005515 protein binding (NAS)
0015035 protein disulfide oxidoreductase activity (NAS)
0005044 scavenger receptor activity (IDA)
0001525 angiogenesis (NAS)
0007155 cell adhesion (NAS)
0042742 defense response to bacteria (IDA)
0006898 receptor mediated endocytosis (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 link domain is a hyaluronan(HA)-binding region found in proteins of vertebrates that are involved in the assembly of extracellular matrix.ell adhesion.nd migration. The structure has been shown to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core similar to that of C-typelectin. This domain contains four conserved cysteines involved in two disulphide bonds. The link domain has also been termed HABM (HA binding module) and PTR (proteoglycan tandem repeat). Proteins with such a domain include the proteoglycans aggrecan.revican.eurocan and versican.hich are expressed in the CNS; the cartilage link protein (LP). proteoglycan that together with HA and aggrecan forms multimolecular aggregates; Tumor necrosis factor-inducible protein TSG-6.hich may be involved in cell-cell and cell-matrix interactions during inflammation and tumorgenesis; and CD44 antigen.he main cell surface receptor for HA.
  IPR000538:Link
The FAS1 or BIgH3 domain is an extracellular module of about 140 amino acidresidues. It has been suggested that the FAS1 domain represents an ancientcell adhesion domain common to plants and animals ; related FAS1 domainsare also found in bacteria . Most FAS1 domain containing proteins are GPIanchored and contain two or four copies of the domain. FAS1 domains of BIgH3protein mediate cell adhesion throught an interaction with alpha3/beta1integrin. A short motif (EPDIM).ocated on the C-teminal side of the fourthdomain.s essential for the binding to integrin .The crystal structure of two FAS1 domains (FAS1 3-4) of a fas1 protein havebeen solved . Each domain consists of seven-stranded wedgeand at least five alpha helices. Two well-ordered N-acetylglucosamine moitiesattached to a conserved asparagine are located in the interface region betweenthe two FAS1 domains.Some of the proteins containing a FAS1 domain are listed below: Drosophila fasciclin I (fas1) protein. A cell adhesion molecule involved in axon guidance. It is attached to the membrane by a GPI-anchor (4 copies). Human TGF-beta induced Ig-H3 (BIgH3) protein. Mutation in its FAS1 domains result in corneal distrophy.ue to the deposition of insoluble protein aggregates (4 copies). Arabidopsis fasciclin-like arabinogalactan proteins (2 copies). Volvox major cell adhesion protein (2 copies). Bacterial immunogenic protein MPT70 (1 copy). Human extracellular matrix protein periostin (4 copies). Mammalian stabilin protein (7 copies).
  IPR000782:Beta-Ig-H3/fasciclin
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Allicin is a thiosulphinate that gives rise to dithiines.llyl sulphides and ajoenes.he three groups of active compounds in Allium species. Allicin is synthesised from sulphoxide cysteine derivatives by alliinase.hose C-S lyase activity cleaves C(beta)-S(gamma) bonds. It is thought that this enzyme forms part of a primitive plant defence system .
  IPR006947:EGF-like, alliinase
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.This entry contains EGF domains found in a variety of extracellular and membrane proteins
  IPR013111:EGF, extracellular
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
IPR000538:LINK 
Evalue:-31.602059991328 
Location:2196-2291IPR000782:FAS1 
Evalue:-27.5528419686578 
Location:1631-1727IPR000782:FAS1 
Evalue:-22.698970004336 
Location:1778-1884IPR000782:FAS1 
Evalue:-16.7695510786217 
Location:2356-2449IPR000782:FAS1 
Evalue:-14.8538719643218 
Location:554-655IPR000782:FAS1 
Evalue:-14.602059991328 
Location:1030-1130IPR000782:FAS1 
Evalue:-12.7447274948967 
Location:1173-1268IPR000782:FAS1 
Evalue:-9.20065945054642 
Location:406-508IPR006210:EGF 
Evalue:-2.38721614328026 
Location:870-909IPR006210:EGF 
Evalue:-2.20065945054642 
Location:240-276IPR006210:EGF 
Evalue:-2.03151705144606 
Location:2126-2165IPR006210:EGF 
Evalue:-0.853871964321762 
Location:325-362IPR006210:EGF 
Evalue:-0.619788758288394 
Location:198-236IPR006210:EGF 
Evalue:-0.130768280269024 
Location:829-866IPR000742:EGF_3 
Evalue:0 
Location:910-952IPR000742:EGF_3 
Evalue:0 
Location:1513-1554IPR000742:EGF_3 
Evalue:0 
Location:1471-1512IPR000742:EGF_3 
Evalue:0 
Location:736-776IPR000742:EGF_3 
Evalue:0 
Location:108-148IPR000742:EGF_3 
Evalue:0 
Location:2082-2122IPR000742:EGF_3 
Evalue:0 
Location:1958-1998IPR000742:EGF_3 
Evalue:0 
Location:953-992IPR000742:EGF_3 
Evalue:0 
Location:1555-1594IPR000742:EGF_3 
Evalue:0 
Location:1346-1384IPR000742:EGF_3 
Evalue:0 
Location:1432-1470IPR000742:EGF_3 
Evalue:0 
Location:156-193IPR000742:EGF_3 
Evalue:0 
Location:2005-2042IPR000742:EGF_3 
Evalue:0 
Location:1391-1428IPR000742:EGF_3 
Evalue:0 
Location:2047-2081IPR013032:EGF_2 
Evalue:0 
Location:2297-2310IPR002049:EGF_LAM_2 
Evalue:0 
Location:0-0
SequencesProtein: STAB2_HUMAN (2551 aa)
mRNA: NM_017564
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (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: 90 residues, 102505198-102505465Exon2: 46 residues, 102508804-102508938Exon3: 40 residues, 102512302-102512418Exon4: 30 residues, 102538375-102538461Exon5: 25 residues, 102539949-102540019Exon6: 34 residues, 102549505-102549601Exon7: 44 residues, 102555018-102555144Exon8: 67 residues, 102555923-102556120Exon9: 46 residues, 102558030-102558164Exon10: 46 residues, 102566597-102566731Exon11: 29 residues, 102568403-102568486Exon12: 52 residues, 102570463-102570613Exon13: 50 residues, 102572462-102572606Exon14: 21 residues, 102573158-102573215Exon15: 44 residues, 102573363-102573489Exon16: 20 residues, 102578238-102578292Exon17: 29 residues, 102578590-102578671Exon18: 53 residues, 102580753-102580906Exon19: 23 residues, 102584198-102584261Exon20: 31 residues, 102586550-102586637Exon21: 31 residues, 102587448-102587535Exon22: 39 residues, 102588603-102588715Exon23: 62 residues, 102591814-102591995Exon24: 33 residues, 102593835-102593929Exon25: 55 residues, 102595360-102595519Exon26: 34 residues, 102601112-102601208Exon27: 34 residues, 102602896-102602992Exon28: 18 residues, 102606075-102606123Exon29: 47 residues, 102607753-102607890Exon30: 40 residues, 102608331-102608446Exon31: 28 residues, 102610719-102610797Exon32: 35 residues, 102613457-102613556Exon33: 38 residues, 102613644-102613752Exon34: 46 residues, 102617003-102617135Exon35: 45 residues, 102621055-102621184Exon36: 21 residues, 102622465-102622522Exon37: 34 residues, 102623539-102623635Exon38: 67 residues, 102624699-102624895Exon39: 34 residues, 102626348-102626444Exon40: 17 residues, 102629378-102629424Exon41: 27 residues, 102630274-102630351Exon42: 44 residues, 102631550-102631676Exon43: 26 residues, 102633722-102633796Exon44: 26 residues, 102635677-102635749Exon45: 42 residues, 102642882-102643002Exon46: 18 residues, 102644023-102644071Exon47: 30 residues, 102645174-102645258Exon48: 51 residues, 102646756-102646903Exon49: 49 residues, 102648023-102648164Exon50: 22 residues, 102649483-102649543Exon51: 61 residues, 102650913-102651090Exon52: 32 residues, 102653398-102653488Exon53: 51 residues, 102655541-102655688Exon54: 21 residues, 102657319-102657376Exon55: 44 residues, 102658537-102658664Exon56: 52 residues, 102660312-102660462Exon57: 37 residues, 102663080-102663185Exon58: 38 residues, 102664504-102664612Exon59: 66 residues, 102666870-102667064Exon60: 49 residues, 102668486-102668628Exon61: 46 residues, 102671127-102671261Exon62: 57 residues, 102673209-102673375Exon63: 37 residues, 102673519-102673626Exon64: 42 residues, 102676077-102676197Exon65: 49 residues, 102677040-102677181Exon66: 39 residues, 102679207-102679318Exon67: 45 residues, 102680181-102680310Exon68: 41 residues, 102681399-102681516Exon69: 147 residues, 102684193-102684630Exon70: 2 residues, -Jump to STAB2_HUMAN  
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