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The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegans and laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3).
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.
16776 Ensembl ENSG00000130702 ENSMUSG00000015647 UniProt O15230 Q61001 RefSeq (mRNA) NM_005560 NM_001081171 RefSeq (protein) NP_005551 NP_001074640 Location (UCSC) Chr 20: 62.31 – 62.37 Mb Chr 2: 179.82 – 179.87 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene. Function Components of the extracellular ...
The nuclear lamina consists of two components, lamins and nuclear lamin-associated membrane proteins. The lamins are type V intermediate filaments which can be categorized as either A-type (lamin A, C) or B-type (lamin B 1, B 2) according to homology of their DNA sequences, biochemical properties and cellular localization during the cell cycle.
16773 Ensembl ENSG00000196569 ENSMUSG00000019899 UniProt P24043 Q60675 RefSeq (mRNA) NM_000426 NM_001079823 NM_008481 RefSeq (protein) NP_000417 NP_001073291 NP_032507 Location (UCSC) Chr 6: 128.88 – 129.52 Mb Chr 10: 26.86 – 27.5 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene. Function Laminin, an ...
Confocal microscopic analysis of a dermal fibroblast in primary culture from a control (a and b) and the subject with HGPS (c and d). Labelling was performed with anti-lamin A/C antibodies. Note the presence of irregularly shaped nuclear envelopes in many of the subject's fibroblasts