======= LAMB1 =======


== Gene Information ==
  * **<color #00a2e8>Official Symbol</color>**: LAMB1
  * **<color #00a2e8>Official Name</color>**: laminin subunit beta 1
  * **<color #00a2e8>Aliases and Previous Symbols</color>**: N/A
  * **<color #00a2e8>Entrez ID</color>**: [[https://www.ncbi.nlm.nih.gov/gene/?term=3912|3912]]
  * **<color #00a2e8>UniProt</color>**: [[https://www.uniprot.org/uniprot/P07942|P07942]]
  * **<color #00a2e8>Interactions</color>**: [[https://thebiogrid.org/search.php?search=LAMB1&organism=9606|BioGRID]]
  * **<color #00a2e8>PubMed articles</color>**: [[https://www.ncbi.nlm.nih.gov/pubmed/?term=gene%20LAMB1|Open PubMed]]
  * **<color #00a2e8>OMIM</color>**: [[https://omim.org/entry/150240|Open OMIM]]

== Function Summary ==
  * **<color #00a2e8>Entrez Summary</color>**:  Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis. [provided by RefSeq, Aug 2011]. 
  * **<color #00a2e8>UniProt Summary</color>**:  Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. {ECO:0000269|PubMed:23472759}.

<button type='primary' size='sm' modal='Pfam_Domains'>Pfam Domains</button>
<button type='primary' size='sm' modal='GO_terms'>GO Terms</button>


<modal id='Pfam_Domains' size='lg' title='Pfam Domains'>
|Laminin N|
|Laminin EGF|
</modal>

<modal id='GO_terms' size='lg' title='GO Terms'>
|laminin-8 complex|
|laminin-2 complex|
|neuronal-glial interaction involved in cerebral cortex radial glia guided migration|
|laminin-1 complex|
|laminin-10 complex|
|laminin complex|
|basement membrane assembly|
|cerebral cortex radial glia guided migration|
|telencephalon glial cell migration|
|basement membrane organization|
|cerebral cortex radially oriented cell migration|
|glial cell migration|
|endodermal cell differentiation|
|cerebral cortex cell migration|
|endoderm formation|
|substrate adhesion-dependent cell spreading|
|telencephalon cell migration|
|forebrain cell migration|
|endoderm development|
|basement membrane|
|formation of primary germ layer|
|cerebral cortex development|
|odontogenesis|
|integrin binding|
|extracellular matrix structural constituent|
|gastrulation|
|pallium development|
|cell-substrate adhesion|
|positive regulation of epithelial cell proliferation|
|structural molecule activity|
|gliogenesis|
|telencephalon development|
|endoplasmic reticulum lumen|
|regulation of epithelial cell proliferation|
|extracellular matrix organization|
|post-translational protein modification|
|collagen-containing extracellular matrix|
|extracellular structure organization|
|forebrain development|
|positive regulation of cell migration|
|cell-cell adhesion|
|positive regulation of cell motility|
|positive regulation of cellular component movement|
|positive regulation of locomotion|
|cell morphogenesis involved in differentiation|
|embryonic morphogenesis|
|neuron projection development|
|perinuclear region of cytoplasm|
|cell morphogenesis|
|brain development|
|head development|
|neuron development|
|cellular component morphogenesis|
|regulation of cell migration|
|anatomical structure formation involved in morphogenesis|
|regulation of cell motility|
|positive regulation of cell population proliferation|
|cell adhesion|
|biological adhesion|
|animal organ morphogenesis|
|cell migration|
|embryo development|
|central nervous system development|
|regulation of locomotion|
|regulation of cellular component movement|
|neuron differentiation|
|localization of cell|
|cell motility|
|plasma membrane bounded cell projection organization|
|cell projection organization|
|locomotion|
|generation of neurons|
|movement of cell or subcellular component|
|extracellular space|
|regulation of cell population proliferation|
|neurogenesis|
|cell development|
|tissue development|
|extracellular region|
</modal>
\\

 === CRISPR Data ===
<button type='primary' size='small' modal='Compound_Hit'>Compound Hit</button>
<button type='primary' size='small' modal='Most_Correlated_Genes'>Most Correlated Genes in Chemogenomics</button>
<button type='primary' size='small' modal='Essential_Avana'>Tissues where Essential in the Avana Dataset (DepMap 20Q1)</button>

<modal id='Compound_Hit' size='lg' title='Compound Hit'>
^Screen^Score^
|[[:results:exp115|A-366 10μM R03 exp115]]|1.71|
|[[:results:exp216|Erlotinib 10μM R05 exp216]]|1.89|
</modal>

<modal id='Most_Correlated_Genes' size='lg' title='Most Correlated Genes in Chemogenomics'>
^Gene^Correlation^
|[[:human genes:h:hgc6.3|HGC6.3]]|0.435|
</modal>

<modal id='Essential_Avana' size='lg' title='Tissues where Essential in the Avana Dataset (DepMap 20Q1)'>
Global Fraction of Cell Lines Where Essential: 0/739
^Tissue^Fraction Of Cell Lines Where Essential^
|1290807.0|0/1|
|909776.0|0/1|
|bile duct|0/28|
|blood|0/28|
|bone|0/26|
|breast|0/33|
|central nervous system|0/56|
|cervix|0/4|
|colorectal|0/17|
|esophagus|0/13|
|fibroblast|0/1|
|gastric|0/16|
|kidney|0/21|
|liver|0/20|
|lung|0/75|
|lymphocyte|0/16|
|ovary|0/26|
|pancreas|0/24|
|peripheral nervous system|0/16|
|plasma cell|0/15|
|prostate|0/1|
|skin|0/24|
|soft tissue|0/9|
|thyroid|0/2|
|upper aerodigestive|0/22|
|urinary tract|0/29|
|uterus|0/5|
</modal>

== Essentiality in NALM6  ==
    * **<color #00a2e8>Essentiality Rank</color>**: 4335
    * **<color #00a2e8>Expression level (log2 read counts)</color>**: 2.11 
<button type='primary' size='small' modal='Dist_expr'>Expression Distribution</button>
<modal id='Dist_expr' size='lg' title='LAMB1 Expression in NALM6 Cells: 2.11'>
{{:chemogenomics:nalm6 dist.png?nolink |}}
</modal>