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0LAMB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionLaminin beta-2 chain precursor (s-laminin) (laminin b1s chain).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005605 basal lamina (TAS)
0005198 structural molecule activity (NAS)

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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:
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Laminin is thought to mediate the attachment.igration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components . Each laminin is a heterotrimer assembled from alpha.eta and gamma chain subunits.ecreted and incorporated into cell-associated extracellular matrices . Basement membrane assembly is a cooperative process in which laminins polymerize through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains. Netrins may also associate with this network through heterotypic LN domain interactions . This leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes.s highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the alpha 2 laminin chain . The laminin N-terminal domain is found in all laminin and netrin subunits except laminin alpha 3A.lpha 4 and gamma 2.
  IPR008211:Laminin, N-terminal
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
Proteins containing a galactose-binding domain-like fold can be found in several different protein families.n both eukaryotes and prokaryotes. The common function of these domains is to bind to specific ligands.uch as cell-surface-attached carbohydrate substrates for galactose oxidase and sialidase .hospholipids on the outer side of the mammalian cell membrane for coagulation factor Va .embrane-anchored ephrin for the Eph family of receptor tyrosine kinases .nd a complex of broken single-stranded DNA and DNA polymerase beta for XRCC1 . The structure of the galactose-binding domain-like members consists of a beta-sandwich.n which the strands making up the sheets exhibit a jellyroll fold. There is a high degree of similarity in the beta-sandwich and in the loops between different family members.espite an often low level of sequence similarity.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008979:Galactose-binding like
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 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
SequencesProtein: LAMB2_HUMAN (1798 aa)
mRNA: NM_002292
Local Annotation
Synapse Ontology
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 83 residues, 49133551-49133799Exon2: 55 residues, 49133869-49134029Exon3: 61 residues, 49134120-49134297Exon4: 49 residues, 49134380-49134522Exon5: 71 residues, 49134599-49134807Exon6: 118 residues, 49135140-49135489Exon7: 82 residues, 49135568-49135810Exon8: 63 residues, 49135883-49136068Exon9: 126 residues, 49136164-49136537Exon10: 34 residues, 49136626-49136723Exon11: 74 residues, 49136831-49137049Exon12: 77 residues, 49137137-49137362Exon13: 56 residues, 49137442-49137606Exon14: 79 residues, 49137689-49137921Exon15: 50 residues, 49138183-49138327Exon16: 66 residues, 49138403-49138596Exon17: 46 residues, 49138801-49138934Exon18: 44 residues, 49140894-49141022Exon19: 55 residues, 49141097-49141256Exon20: 46 residues, 49141456-49141589Exon21: 28 residues, 49141681-49141761Exon22: 39 residues, 49142040-49142153Exon23: 62 residues, 49142275-49142455Exon24: 65 residues, 49142667-49142856Exon25: 42 residues, 49143176-49143297Exon26: 69 residues, 49143386-49143589Exon27: 23 residues, 49143815-49143879Exon28: 65 residues, 49143971-49144160Exon29: 26 residues, 49144552-49144626Exon30: 47 residues, 49144706-49144842Exon31: 59 residues, 49144927-49145100Exon32: 127 residues, 49145228-49145603Exon33: 2 residues, -Jump to LAMB2_HUMAN  
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Loci Cluster (Details)Loci: 4601 48530128-48569231 ~-39K 25651(PFKFB4)(-)Loci: 4602 48611435-48622102 ~-11K 25656(UQCRC1)(-)Loci: 4603 48637834-48684985 ~-47K 25658(CELSR3)(-)Loci: 4604 48686283-48698338 ~-12K 25669(NCKIPSD)(-)Loci: 4605 48762098-48860265 ~-98K 25672(-)Loci: 4606 49133551-49145603 ~-12K 25699(LAMB2)(-)Loci: 4607 49429215-49435016 ~-6K 25713(AMT)(-)Loci: 3354 49566925-49683976 ~-117K 25718(BSN)(+)Loci: 4608 49921309-49942261 ~-21K 25739(-)Loci: 4609 50330243-50333903 ~-4K 25774(HYAL2)(-)Loci: 4600 48420266-48441746 ~-21K 25634(PLXNB1)(-)Link out to UCSC