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0STAB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSTAB1
DescriptionStabilin-1 precursor (feel-1 protein) (ms-1 antigen).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (IDA)
0008367 bacterial binding (IDA)
0005041 low-density lipoprotein receptor activity (IDA)
0005515 protein binding (NAS)
0015035 protein disulfide oxidoreductase activity (NAS)
0005044 scavenger receptor activity (IDA)
0007155 cell adhesion (NAS)
0007267 cell-cell signaling (IDA)
0042742 defense response to bacteria (IDA)
0016525 negative regulation of angiogenesis (IMP)
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 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
Laminins are the major noncollagenous components of basement membranesthat mediate cell adhesion.rowth migration.nd differentiation. They arecomposed of distinct but related alpha.eta and gamma chains. The threechains form a cross-shaped molecule that consist of a long arm and three shortglobular arms. The long arm consist of a coiled coil structure contributed byall three chains and cross-linked by interchain disulphide bonds.Beside different types of globular domains each subunit contains.n its firsthalf.onsecutive repeats of about 60 amino acids in length that include eightconserved cysteines . The tertiary structure .f this domain isremotely similar in its N-terminal to that of the EGF-like module (see ). It is known as a LE or laminin-type EGF-like domain. Thenumber of copies of the LE domain in the different forms of laminins is highlyvariable; from 3 up to 22 copies have been found.A schematic representation of the topology of the four disulphide bonds inthe LE domain is shown below.In mouse laminin gamma-1 chain.he seventh LE domain has been shown to be theonly one that binds with a high affinity to nidogen . The binding-sites arelocated on the surface within the loops C1-C3 and C5-C6 . Longconsecutive arrays of LE domains in laminins form rod-like elements of limitedflexibility .hich determine the spacing in the formation of lamininnetworks of basement membranes .
  IPR002049:EGF-like, laminin
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
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
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
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 growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) .he type-1 insulin-like growth-factor receptor (IGF-1R) .nd the receptor protein-tyrosine kinase Erbb-3 (ErbB3) . The general structure of the growth factor receptor domain is a disulphide-bound fold containing a beta-hairpin with two adjacent disulphides. IGFBPs control the distribution.unction and activity of insulin-like growth factors (IGFs) IGF-I and IGF-II.hich are key regulators of cell proliferation.ifferentiation and transformation. All IGFBPs share a common domain organization.here the highest conservation is found in the N-terminal Cys-rich IGF-binding domain. The N-terminal domain contains 10-12 conserved cysteine residues. IGF-1R is a member of the tyrosine-kinase receptor superfamily that is involved in both normal growth and development and malignant transformation. The Cys-rich domain is flanked by two L-domains.nd together they contribute to hormone binding and ligand specificity.ven though they do not bind ligand directly. The Cys-rich region is composed of eight disulphide-bonded modules.even of which form a rod-shaped domain. ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. The extracellular region of ErbB3 is made up of two Cys-rich domains and two L-domains.rranged alternately. The two L-domains and the first Cys-rich domain are structurally homologous to those found in IGF-1R. The two Cys-rich domains are extended repeats of seven small disulphide-containing modules. A beta-hairpin loop extends from the first Cys-rich domain to contact the C-terminal portion of the second Cys-rich domain.reating a large pore structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009030:Growth factor, receptor
IPR000538:LINK 
Evalue:-51.8239087409443 
Location:2206-2301IPR000782:Fasciclin 
Evalue:-33.3467864990234 
Location:1736-1866IPR000782:FAS1 
Evalue:-25.3767507096021 
Location:1615-1711IPR000782:FAS1 
Evalue:-24.7212463990472 
Location:542-644IPR000782:Fasciclin 
Evalue:-19.7447280883789 
Location:1000-1120IPR000782:FAS1 
Evalue:-10.5528419686578 
Location:2367-2462IPR002049:Laminin_EGF 
Evalue:-5.08092212677002 
Location:1992-2021IPR006209:EGF 
Evalue:-4.95860719680786 
Location:865-902IPR006209:EGF 
Evalue:-2.79588007926941 
Location:2136-2173IPR013111:EGF_2 
Evalue:-2.65757727622986 
Location:112-147IPR000782:Fasciclin 
Evalue:-2.60206007957458 
Location:1140-1255IPR006209:EGF 
Evalue:-2.25963735580444 
Location:2095-2130IPR006209:EGF 
Evalue:-2.25181198120117 
Location:1501-1538IPR006209:EGF 
Evalue:-2.11350917816162 
Location:236-270IPR006209:EGF 
Evalue:-2.0915150642395 
Location:951-987IPR006210:EGF 
Evalue:-1.95860731484177 
Location:1458-1496IPR006210:EGF 
Evalue:-0.455931955649724 
Location:1331-1368IPR006210:EGF 
Evalue:-0.0757207139381184 
Location:1378-1412IPR000782:FAS1 
Evalue:0 
Location:356-494IPR009030:Grow_fac_recept 
Evalue:0 
Location:706-769IPR000742:EGF_3 
Evalue:0 
Location:1540-1582IPR000742:EGF_3 
Evalue:0 
Location:904-946IPR000742:EGF_3 
Evalue:0 
Location:818-858IPR000742:EGF_3 
Evalue:0 
Location:1416-1454IPR000742:EGF_3 
Evalue:0 
Location:156-193IPR000742:EGF_3 
Evalue:0 
Location:2056-2090IPR000742:EGF_3 
Evalue:0 
Location:195-229IPR013032:EGF_2 
Evalue:0 
Location:2307-2321IPR013032:EGF_2 
Evalue:0 
Location:2039-2050IPR002049:EGF_LAM_2 
Evalue:0 
Location:0-0
SequencesProtein: STAB1_HUMAN (2570 aa)
mRNA: NM_015136
Local Annotation
Synapse Ontology
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 51 residues, 52504395-52504547Exon2: 47 residues, 52510221-52510358Exon3: 40 residues, 52510693-52510809Exon4: 30 residues, 52511061-52511147Exon5: 25 residues, 52511214-52511284Exon6: 34 residues, 52511687-52511783Exon7: 39 residues, 52512054-52512165Exon8: 67 residues, 52512399-52512596Exon9: 45 residues, 52512827-52512958Exon10: 44 residues, 52513083-52513211Exon11: 31 residues, 52513516-52513605Exon12: 48 residues, 52513794-52513932Exon13: 49 residues, 52514058-52514199Exon14: 23 residues, 52514374-52514437Exon15: 40 residues, 52514723-52514837Exon16: 20 residues, 52514938-52514992Exon17: 29 residues, 52515225-52515306Exon18: 55 residues, 52515747-52515906Exon19: 23 residues, 52516668-52516731Exon20: 34 residues, 52516986-52517082Exon21: 31 residues, 52517328-52517415Exon22: 39 residues, 52518265-52518377Exon23: 64 residues, 52518925-52519112Exon24: 33 residues, 52519197-52519291Exon25: 55 residues, 52519404-52519563Exon26: 34 residues, 52520705-52520801Exon27: 34 residues, 52521396-52521492Exon28: 18 residues, 52521651-52521699Exon29: 45 residues, 52521883-52522014Exon30: 39 residues, 52522185-52522297Exon31: 28 residues, 52522772-52522850Exon32: 35 residues, 52522938-52523037Exon33: 35 residues, 52523170-52523269Exon34: 46 residues, 52523420-52523552Exon35: 45 residues, 52523756-52523885Exon36: 21 residues, 52524044-52524101Exon37: 30 residues, 52524478-52524562Exon38: 67 residues, 52525098-52525294Exon39: 34 residues, 52525411-52525507Exon40: 17 residues, 52525597-52525643Exon41: 27 residues, 52525747-52525824Exon42: 44 residues, 52526039-52526165Exon43: 26 residues, 52526375-52526449Exon44: 27 residues, 52526605-52526680Exon45: 43 residues, 52526936-52527059Exon46: 18 residues, 52527367-52527415Exon47: 28 residues, 52527591-52527669Exon48: 51 residues, 52527778-52527925Exon49: 49 residues, 52528319-52528460Exon50: 22 residues, 52528560-52528620Exon51: 61 residues, 52528999-52529176Exon52: 31 residues, 52529259-52529346Exon53: 52 residues, 52529455-52529605Exon54: 21 residues, 52529697-52529754Exon55: 69 residues, 52529859-52530061Exon56: 52 residues, 52530416-52530566Exon57: 37 residues, 52530651-52530756Exon58: 38 residues, 52530899-52531007Exon59: 66 residues, 52531092-52531286Exon60: 50 residues, 52531385-52531530Exon61: 46 residues, 52531610-52531744Exon62: 57 residues, 52531830-52531996Exon63: 38 residues, 52532080-52532190Exon64: 42 residues, 52532277-52532397Exon65: 52 residues, 52532482-52532632Exon66: 37 residues, 52532707-52532812Exon67: 51 residues, 52532926-52533073Exon68: 40 residues, 52533155-52533269Exon69: 66 residues, 52533355-52533549Exon70: 2 residues, -Jump to STAB1_HUMAN  
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Loci Cluster (Details)Loci: 4610 52848937-52906587 ~-58K 25881(-)Loci: 3358 53170262-53201771 ~-32K 25886(PRKCD)(+)Loci: 3357 52504395-52533549 ~-29K 25852(STAB1)(+)Link out to UCSC