LAMA3

Summary

LAMA3 (laminin subunit alpha 3, HGNC:6483) is a protein-coding gene on chromosome 18q11.2, encoding Laminin subunit alpha-3 (Q16787). 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.

The protein encoded by this gene belongs to the laminin family of secreted molecules. Laminins are heterotrimeric molecules that consist of alpha, beta, and gamma subunits that assemble through a coiled-coil domain. Laminins are essential for formation and function of the basement membrane and have additional functions in regulating cell migration and mechanical signal transduction. This gene encodes an alpha subunit and is responsive to several epithelial-mesenchymal regulators including keratinocyte growth factor, epidermal growth factor and insulin-like growth factor. Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa and laryngoonychocutaneous syndrome. Alternative splicing and alternative promoter usage result in multiple transcript variants.

Source: NCBI Gene 3909 — RefSeq curated summary.

At a glance

• Gene–disease (curated): junctional epidermolysis bullosa (Definitive, GenCC) — +6 more curated relationships
• Clinical variants (ClinVar): 2,289 total — 126 pathogenic, 134 likely-pathogenic
• Phenotypes (HPO): 98
• Druggable target: yes
• MANE Select transcript: NM_198129

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:6483
Approved symbol	LAMA3
Name	laminin subunit alpha 3
Location	18q11.2
Locus type	gene with protein product
Status	Approved
Aliases	nicein-150kDa, kalinin-165kDa, BM600-150kDa, epiligrin
Ensembl gene	ENSG00000053747
Ensembl biotype	protein_coding
OMIM	600805
Entrez	3909

Gene structure

Transcript identifiers

Ensembl transcripts: 15 — 10 protein_coding, 3 retained_intron, 1 non_stop_decay, 1 protein_coding_CDS_not_defined

ENST00000269217, ENST00000313654, ENST00000399516, ENST00000585600, ENST00000586709, ENST00000586751, ENST00000587184, ENST00000588004, ENST00000588164, ENST00000588770, ENST00000590104, ENST00000591749, ENST00000592442, ENST00000592519, ENST00000649721

RefSeq mRNA: 4 — MANE Select: NM_198129 NM_000227, NM_001127717, NM_001127718, NM_198129

CCDS: CCDS11880, CCDS42419, CCDS45838, CCDS59307

Canonical transcript exons

ENST00000313654 — 75 exons

Exon	Start	End
ENSE00000915302	23750918	23751088
ENSE00000915303	23753721	23753812
ENSE00000948608	23881936	23882045
ENSE00000948613	23876294	23876407
ENSE00000948659	23867834	23867917
ENSE00001109664	23839785	23839929
ENSE00001109665	23814403	23814502
ENSE00001109667	23858689	23858829
ENSE00001109668	23826702	23826799
ENSE00001109669	23763405	23763523
ENSE00001109671	23773497	23773587
ENSE00001109673	23749428	23749546
ENSE00001109674	23815468	23815573
ENSE00001109676	23819841	23819997
ENSE00001109677	23810366	23810503
ENSE00001109679	23815188	23815240
ENSE00001109682	23777557	23777619
ENSE00001109683	23822252	23822375
ENSE00001109685	23816388	23816487
ENSE00001109686	23827314	23827467
ENSE00001109688	23824423	23824565
ENSE00001109689	23845009	23845124
ENSE00001109692	23847464	23847668
ENSE00001109693	23842395	23842521
ENSE00001109695	23713920	23714072
ENSE00001109697	23758396	23758511
ENSE00001109699	23857844	23857988
ENSE00001109701	23747943	23748060
ENSE00001109702	23838781	23838878
ENSE00001109703	23784023	23784157
ENSE00001109704	23775792	23775923
ENSE00001109709	23813057	23813103
ENSE00001109711	23842611	23842750
ENSE00001109767	23894907	23895058
ENSE00001109770	23894298	23894348
ENSE00001136467	23884773	23884853
ENSE00001146014	23871431	23871661
ENSE00001146020	23864785	23864883
ENSE00001179054	23954503	23955066
ENSE00001222103	23836981	23837089
ENSE00001413554	23890011	23890117
ENSE00001426077	23846297	23846508
ENSE00002712166	23861646	23861807
ENSE00002819677	23689453	23689977
ENSE00003463945	23898954	23899065
ENSE00003499000	23899288	23899455
ENSE00003508028	23912711	23912881
ENSE00003516019	23903933	23904087
ENSE00003523652	23946144	23946284
ENSE00003542194	23921452	23921585
ENSE00003547045	23931062	23931201
ENSE00003550360	23949765	23949924
ENSE00003555413	23915289	23915422
ENSE00003557575	23904553	23904694
ENSE00003558318	23932160	23932291
ENSE00003563647	23914698	23914860
ENSE00003566698	23901127	23901323
ENSE00003576290	23943788	23943971
ENSE00003579345	23898738	23898848
ENSE00003587308	23920935	23921054
ENSE00003594674	23928625	23928765
ENSE00003596126	23928123	23928240
ENSE00003603639	23907550	23907666
ENSE00003619747	23907756	23907935
ENSE00003625431	23952990	23953109
ENSE00003625465	23916551	23916695
ENSE00003626876	23903009	23903125
ENSE00003630361	23914410	23914561
ENSE00003638548	23833828	23833988
ENSE00003643714	23951684	23951777
ENSE00003654397	23909153	23909295
ENSE00003670732	23950029	23950159
ENSE00003682989	23905522	23905624
ENSE00003683765	23939223	23939386
ENSE00003690348	23933782	23933935

Expression profiles

Bgee: expression breadth ubiquitous, 239 present calls, max score 94.54.

FANTOM5 (CAGE): breadth broad, TPM avg 28.4891 / max 5394.6643, expressed in 866 samples.

FANTOM5 promoters (16 alternative TSS)

Promoter ID	TPM avg	Samples expressed
169692	23.6465	251
169691	1.5008	111
169678	1.0584	467
169682	0.8530	370
169677	0.4008	201
169679	0.3233	154
169683	0.2435	124
169680	0.0896	20
208518	0.0732	30
169710	0.0559	25

Top tissues by expression

292 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
right lung	UBERON:0002167	94.54	gold quality
skin of leg	UBERON:0001511	93.94	gold quality
skin of abdomen	UBERON:0001416	93.88	gold quality
periodontal ligament	UBERON:0008266	93.88	gold quality
mucosa of sigmoid colon	UBERON:0004993	93.72	gold quality
colonic mucosa	UBERON:0000317	93.39	gold quality
jejunal mucosa	UBERON:0000399	93.22	gold quality
decidua	UBERON:0002450	93.20	gold quality
sural nerve	UBERON:0015488	92.75	gold quality
zone of skin	UBERON:0000014	92.21	gold quality
upper lobe of left lung	UBERON:0008952	91.61	gold quality
minor salivary gland	UBERON:0001830	91.37	gold quality
hair follicle	UBERON:0002073	90.99	gold quality
upper lobe of lung	UBERON:0008948	90.70	gold quality
body of uterus	UBERON:0009853	90.69	gold quality
ileal mucosa	UBERON:0000331	90.39	gold quality
vagina	UBERON:0000996	90.37	gold quality
mouth mucosa	UBERON:0003729	90.03	gold quality
pancreatic ductal cell	CL:0002079	89.51	silver quality
ectocervix	UBERON:0012249	89.11	gold quality
saliva-secreting gland	UBERON:0001044	89.09	gold quality
right uterine tube	UBERON:0001302	89.09	gold quality
tibial nerve	UBERON:0001323	88.75	gold quality
calcaneal tendon	UBERON:0003701	88.48	gold quality
duodenum	UBERON:0002114	88.18	gold quality
mucosa of transverse colon	UBERON:0004991	88.18	gold quality
lung	UBERON:0002048	88.14	gold quality
olfactory segment of nasal mucosa	UBERON:0005386	87.96	gold quality
left uterine tube	UBERON:0001303	87.77	gold quality
endocervix	UBERON:0000458	87.71	gold quality

Single-cell (SCXA)

Detected in 7 experiment(s), a significant marker in 7.

Experiment	Marker?	Max mean expression
E-ENAD-21	yes	1891.77
E-CURD-7	yes	1843.65
E-MTAB-7249	yes	1222.92
E-MTAB-10855	yes	1110.30
E-GEOD-86618	yes	798.53
E-MTAB-8559	yes	444.74
E-ANND-3	no	0.00

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): EP300, FOSL2, GDNF, KLF4, MSX2, SMAD4, SP1, USF1

miRNA regulators (miRDB)

52 targeting LAMA3, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-3163	100.00	77.23	8605
HSA-MIR-4775	99.98	75.00	6394
HSA-MIR-302C-5P	99.97	72.56	3642
HSA-MIR-3148	99.97	75.06	6478
HSA-MIR-302E	99.96	70.74	2669
HSA-MIR-106A-5P	99.90	73.94	2683
HSA-MIR-302A-3P	99.89	71.23	1777
HSA-MIR-302B-3P	99.89	71.23	1777
HSA-MIR-302C-3P	99.89	71.20	1778
HSA-MIR-302D-3P	99.89	71.25	1777
HSA-MIR-17-5P	99.89	73.83	2665
HSA-MIR-106B-5P	99.88	74.72	2795
HSA-MIR-20A-5P	99.88	74.76	2769
HSA-MIR-20B-5P	99.88	74.01	2621
HSA-MIR-519D-3P	99.88	73.97	2607
HSA-MIR-526B-3P	99.88	74.06	2587
HSA-MIR-93-5P	99.88	73.98	2606
HSA-MIR-3140-3P	99.88	68.47	2069
HSA-MIR-6124	99.87	69.78	3551
HSA-MIR-373-3P	99.84	70.68	1668
HSA-MIR-520E-3P	99.84	70.55	1698
HSA-MIR-372-3P	99.83	70.58	1691
HSA-MIR-520A-3P	99.83	70.59	1687
HSA-MIR-520B-3P	99.83	70.56	1699
HSA-MIR-520C-3P	99.83	70.56	1699
HSA-MIR-520D-3P	99.83	70.78	1676
HSA-MIR-520F-3P	99.82	71.32	1216
HSA-MIR-3681-5P	99.82	66.88	387
HSA-MIR-3617-5P	99.75	69.41	1968
HSA-MIR-641	99.75	69.35	1975

Literature-anchored findings (GeneRIF, showing 40)

• Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V. (PMID:12441389)
• null behavioral phenotype originates in the nervous system and involves a calmodulin function that requires calcium binding to all four sites of the protein (PMID:14668380)
• the direct interaction of melatonin with intact calcium-saturated CaM is calcium-dependent; Molecular dynamics simulations follow the dynamics of melatonin in the binding pocket of CaM (PMID:15498938)
• potential functional role for calmodulin in regulation of the glycolytic pathway (PMID:15527800)
• A mutation to the gene encoding calmodulin deregulates muscle contraction. (PMID:15557269)
• Drosophila CaM is able to fully activate inducible nitric oxide synthase (iNOS); moreover, iNOS activation by CaM, like neuronal NOS, is not dependent on Ca2+ being bound to all four Ca2+-binding sites, but has specific and distinct requirements. (PMID:15896003)
• Calmodulin/CAMTA/Fbxl4 may mediate a long-term feedback regulation of the activity of Ca(2+)-stimulating G protein-coupled receptor, which could prevent cell damage due to extra Ca(2+) influx. (PMID:17110341)
• Thus, Calmodulin and Abelson tyrosine kinase are key signaling molecules working synergistically to transduce both midline attractive and repulsive cues. (PMID:18243630)
• characterized the interdomain motions in the calcium-bound state of calmodulin (Ca(2+)-CaM) using NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations (PMID:24530797)
• Basal body formation in the male testes and the production of functional sperm does not rely on the PLP-CaM interaction, whereas production of functional mechanosensory neurons does. (PMID:25031429)
• Asp-CaM complex has a critical role in centrosome-pole cohesion and centrosome inheritance in neural stem cells (PMID:26620907)
• Calmodulin binds to Drosophila TRP with an unexpected mode. (PMID:33326749)
• Characterization of morphological and cytoskeletal changes in MCF10A breast epithelial cells plated on laminin-5: comparison with breast cancer cell line MCF7. (PMID:11775027)
• Neurite outgrowth promoting sites have been identified on the laminin alpha 3 chain LG4 module. (PMID:12196012)
• In all developing organs investigated, the mRNA of the alpha3 chain of laminin is strictly of epithelial origin and the corresponding protein localised in the underlying basement membrane zones (PMID:12382139)
• These results suggest that the G3 domain of laminin 5 alpha 3 contains two distinct regions that differently regulate cell adhesion and migration. (PMID:12532327)
• laminin alpha 3 LG4 module may play an important role in tissue remodeling by inducing MMP-1 expression during wound healing (PMID:12826666)
• a missense mutation in the adhesion G domain of laminin-5 causes mild junctional epidermolysis bullosa (PMID:12943669)
• results demonstrate that the laminin alpha3 LG4/5 modules within unprocessed laminin-5 permit its cell binding activity through heparan and chondroitin sulfate chains of syndecan-1 (PMID:12947106)
• proteolytic processing of laminin-5 influences its interaction with alpha3beta1 integrin (PMID:14612440)
• LAMA3 promoter methylation is associated with increased breast tumor stage and tumor size (PMID:14695139)
• Characterization of laminin 5B and NH2-terminal proteolytic fragment of its alpha3B chain (PMID:15044476)
• co-cultures of epithelial cells and fibroblasts were studied to analyse the processing of laminin 5 alpha3, beta3, and gamma2 chains (PMID:15149852)
• The G4/5 domain in the alpha3 chain facilitates deposition of precursor laminin 5 into the PBM in epidermal wounds (PMID:15316072)
• Premature termination codon mutations in both alleles of LAMB3 or LAMC2 genes were found in nine of the 11 H junctional epidermolysis bullosa patients (PMID:15373767)
• the LG4-5 domain synergistically enhances integrin signaling as it is released from the precursor LN5 (PMID:15695818)
• the absolute mRNA levels generated from the laminin 5 genes do not determine the translated protein levels of the laminin 5 chains in keratinocytes; the expression of the laminin 5 genes may be controlled by common regulation mechanisms (PMID:15854126)
• The uncoordinated production of chains of ln-5 in allergic asthma could have a bearing on the poor epithelial cell anchorage in these patients. (PMID:16179086)
• Suppression of laminin-5 alpha 3-chain expression in human mammary epithelial cells results in loss of reconstituted extracellular matrix-mediated growth control and apoptosis. (PMID:16219677)
• The hinge region between subdomains G3 and G4 of laminin alpha 3 carries the proteolytic cleavage sites but proteolytic processing plays no role in kerocyte migration. (PMID:16297184)
• tumor cell migration on laminin-5 is inhibited by HYD1, a biologically active integrin-targeting peptide (PMID:16537560)
• Ln-5 is an important regulator of ADPKD cell proliferation and cystogenesis; Ln-5 gamma(2) chain and Ln-5-alpha(6)beta(4) integrin interaction both contribute to these phenotypic changes (PMID:16870608)
• The major contributions of laminin-5 to the resistance of the epidermis against frictional stress but also for basement membrane regeneration and repair of damaged skin are reflected by the phenotype of Herlitz junctional epidermolysis bullosa. (PMID:17000025)
• Laminin-5 may contribute to the development of bone tissues by promoting the proliferation and by suppressing the chondrogenic differentiation of MSCs. (PMID:17071854)
• Laminin-5 alone stimulates global changes in gene/protein expression in mesenchymal stem cells that lead to commitment of these cells to the osteogenic phenotype, and this correlates with extracellular matrix production. (PMID:17137774)
• These results suggest a new possible approach to repairing SCI and, in general, a model which will be useful for other multidisciplinary procedures for complex neurological situations. (PMID:17466943)
• LM-332 is a crucial motility-promoting factor for B-CLL lymphocytes and is a potential constituent favoring the dissemination of B-CLL lymphocytes through vascular basement membranes and possibly lymph node compartments. (PMID:17482449)
• These results suggest that Crk is required for early attachment to laminin, cell motility, and growth of glioblastoma cell line KMG4. (PMID:17825249)
• the alpha3 chain can assemble with only beta3-gamma2 heterodimer to form a heterotrimer via disulfide bonds (PMID:18603785)
• Smad4 mediates transcriptional regulation through three mechanisms: Smad4 binding to a functional SBE site in the LAMA3 promoter, Smad4 binding to AP1 (and Sp1) sites via interaction with AP1 family, and Smad4 impact on transcription of AP1 factors (PMID:18664273)

Cross-species orthologs

4 orthologs

Organism	Symbol	Gene ID
danio_rerio	si:ch211-241e1.3	ENSDARG00000022615
danio_rerio	lama3	ENSDARG00000071462
mus_musculus	Lama3	ENSMUSG00000024421
rattus_norvegicus	Lama3	ENSRNOG00000011300

Paralogs (27): USH2A (ENSG00000042781), LAMC3 (ENSG00000050555), LAMC2 (ENSG00000058085), NTN1 (ENSG00000065320), NTN4 (ENSG00000074527), ATRN (ENSG00000088812), LAMB4 (ENSG00000091128), LAMB1 (ENSG00000091136), LAMA1 (ENSG00000101680), MEGF8 (ENSG00000105429), MEGF9 (ENSG00000106780), ATRNL1 (ENSG00000107518), LAMA4 (ENSG00000112769), LAMA5 (ENSG00000130702), LAMC1 (ENSG00000135862), NTN5 (ENSG00000142233), HSPG2 (ENSG00000142798), TMEFF2 (ENSG00000144339), NTN3 (ENSG00000162068), NTNG1 (ENSG00000162631), EGFLAM (ENSG00000164318), LAMB2 (ENSG00000172037), AGRN (ENSG00000188157), NTNG2 (ENSG00000196358), LAMA2 (ENSG00000196569), LAMB3 (ENSG00000196878), TMEFF1 (ENSG00000241697)

Protein

Protein identifiers

Laminin subunit alpha-3 — Q16787 (reviewed: Q16787)

Alternative names: Epiligrin 170 kDa subunit, Epiligrin subunit alpha, Kalinin subunit alpha, Laminin-5 subunit alpha, Laminin-6 subunit alpha, Laminin-7 subunit alpha, Nicein subunit alpha

All UniProt accessions (11): A0A075B783, A0A0A0MSA0, A0A0A0MTS5, A0A0A6YYF2, A0A3B3ITG1, Q16787, K7EIP4, K7EMU9, K7EPP3, K7EQ42, K7ERM0

UniProt curated annotations — full annotation on UniProt →

Function. 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. Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes.

Subunit / interactions. Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).

Subcellular location. Secreted. Extracellular space. Extracellular matrix. Basement membrane.

Tissue specificity. Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.

Disease relevance. Epidermolysis bullosa, junctional 2A, intermediate (JEB2A) [MIM:619783] A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2A is an autosomal recessive, intermediate form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. In intermediate forms of junctional epidermolysis bullosa, blistering does not lead to the formation of chronic granulation tissue and does not affect the lifespan of affected individuals. Nail dystrophy and dental enamel defects are present. Scarring or non-scarring alopecia and diffuse hair loss may occur. The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa, junctional 2B, severe (JEB2B) [MIM:619784] A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2B is an autosomal recessive form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. It belongs to the severe spectrum of junctional epidermolysis bullosa (previously known as generalized severe or Herlitz type), characterized by onset of blistering over large regions of the body at birth or in early infancy. Blistering also affects the mucous membranes, such as the moist lining of the mouth and digestive tract, which can make it difficult to eat and digest food. The extensive blistering leads to scarring and the formation of red, bumpy patches called granulation tissue. Other complications can include fusion of the fingers and toes, abnormalities of the fingernails and toenails, joint deformities, dental enamel defects, and alopecia. Severe, junctional forms are associated with death in the first 6 to 24 months of life. The disease is caused by variants affecting the gene represented in this entry. Epidermolysis bullosa, junctional 2C, laryngoonychocutaneous (JEB2C) [MIM:245660] A form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma. JEB2C is an autosomal recessive, severe form in which blistering lesions occur between the epidermis and the dermis at the lamina lucida level of the basement membrane zone. JEB2C manifestations appear in early infancy and include hoarse cry, skin ulceration, nail dystrophy with recurrent loss of toenails and fingernails, and conjunctival scarring. Some patients have amelogenesis imperfecta. Death in childhood is common. The disease is caused by variants affecting the gene represented in this entry.

Domain organisation. The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. Domain G is globular.

Induction. Laminin-5 is up-regulated in wound sites of human skin.

Isoforms (4)

UniProt ID	Names	Canonical?
Q16787-2	2, B	yes
Q16787-1	1, A
Q16787-3	3
Q16787-4	4

RefSeq proteins (4): NP_000218, NP_001121189, NP_001121190, NP_937762* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000034	Laminin_IV	Domain
IPR000742	EGF	Domain
IPR001791	Laminin_G	Domain
IPR002049	LE_dom	Domain
IPR008211	Laminin_N	Domain
IPR009254	Laminin_aI	Domain
IPR010307	Laminin_dom_II	Domain
IPR013320	ConA-like_dom_sf	Homologous_superfamily
IPR050440	Laminin/Netrin_ECM	Family
IPR056863	LMN_ATRN_NET-like_EGF	Domain

Pfam: PF00052, PF00053, PF00055, PF02210, PF06008, PF06009, PF24973

UniProt features (118 total): disulfide bond 60, domain 22, sequence variant 8, sequence conflict 7, splice variant 5, region of interest 5, glycosylation site 5, coiled-coil region 3, signal peptide 1, chain 1, short sequence motif 1

Structure

Experimental structures (PDB)

0 structures.

Predicted structure (AlphaFold)

No AlphaFold model available for Q16787 — AlphaFold DB does not currently provide models for proteins above ~3000 aa.

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Disulfide bonds (60): 299–308, 301–319, 321–330, 333–353, 356–365, 358–390, 393–402, 405–423, 426–436, 428–443, 445–454, 457–467, 491–503, 493–509, 511–520, 523–533, 536–548, 538–555, 557–566, 569–586 …

Glycosylation sites (5): 142, 242, 2365, 2502, 2584

Function

Pathways and Gene Ontology

Reactome pathways

19 pathways

ID	Pathway
R-HSA-1474228	Degradation of the extracellular matrix
R-HSA-2022090	Assembly of collagen fibrils and other multimeric structures
R-HSA-2214320	Anchoring fibril formation
R-HSA-3000157	Laminin interactions
R-HSA-3000171	Non-integrin membrane-ECM interactions
R-HSA-3000178	ECM proteoglycans
R-HSA-446107	Type I hemidesmosome assembly
R-HSA-8874081	MET activates PTK2 signaling
R-HSA-9638630	Attachment of bacteria to epithelial cells
R-HSA-9913351	Formation of the dystrophin-glycoprotein complex (DGC)
R-HSA-9925563	Developmental Lineage of Pancreatic Ductal Cells
R-HSA-1474244	Extracellular matrix organization
R-HSA-1474290	Collagen formation
R-HSA-1500931	Cell-Cell communication
R-HSA-162582	Signal Transduction
R-HSA-446728	Cell junction organization
R-HSA-6806834	Signaling by MET
R-HSA-8875878	MET promotes cell motility
R-HSA-9006934	Signaling by Receptor Tyrosine Kinases

MSigDB gene sets: 468 (showing top): GSE18804_SPLEEN_MACROPHAGE_VS_TUMORAL_MACROPHAGE_DN, AP1_01, XU_GH1_AUTOCRINE_TARGETS_UP, GOBP_FORMATION_OF_PRIMARY_GERM_LAYER, JAEGER_METASTASIS_DN, LI_PROSTATE_CANCER_EPIGENETIC, SCHLESINGER_METHYLATED_DE_NOVO_IN_CANCER, NAGASHIMA_NRG1_SIGNALING_UP, HATADA_METHYLATED_IN_LUNG_CANCER_DN, CHANG_IMMORTALIZED_BY_HPV31_DN, GOBP_CELL_CELL_ADHESION, CAIRO_HEPATOBLASTOMA_CLASSES_DN, GOBP_HEMIDESMOSOME_ASSEMBLY, GOBP_CELL_JUNCTION_ORGANIZATION, AP1_Q4_01

GO Biological Process (9): epidermis development (GO:0008544), regulation of cell adhesion (GO:0030155), regulation of cell migration (GO:0030334), hemidesmosome assembly (GO:0031581), endodermal cell differentiation (GO:0035987), regulation of embryonic development (GO:0045995), cell-cell adhesion (GO:0098609), cell adhesion (GO:0007155), anatomical structure morphogenesis (GO:0009653)

GO Molecular Function (3): signaling receptor binding (GO:0005102), structural molecule activity (GO:0005198), extracellular matrix structural constituent (GO:0005201)

GO Cellular Component (10): extracellular region (GO:0005576), basement membrane (GO:0005604), laminin-121 trimer (GO:0005608), laminin-332 trimer (GO:0005610), endoplasmic reticulum (GO:0005783), adherens junction (GO:0005912), hemidesmosome (GO:0030056), extracellular matrix (GO:0031012), extracellular exosome (GO:0070062), membrane (GO:0016020)

Reactome top-level categories

Rollup of top-12 pathways:

Category	Pathways
Extracellular matrix organization	5
Collagen formation	1
Assembly of collagen fibrils and other multimeric structures	1
Cell junction organization	1
MET promotes cell motility	1
Biofilm formation	1
Non-integrin membrane-ECM interactions	1
Developmental Cell Lineages of the Exocrine Pancreas	1
Cell-Cell communication	1
Signaling by Receptor Tyrosine Kinases	1
Signaling by MET	1
Signal Transduction	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cell adhesion	2
extracellular matrix	2
cellular anatomical structure	2
laminin trimer	2
tissue development	1
regulation of cellular process	1
cell migration	1
regulation of cell motility	1
cell-substrate junction assembly	1
endoderm formation	1
cell differentiation	1
embryo development	1
regulation of multicellular organismal development	1
cellular process	1
developmental process	1
anatomical structure development	1
protein binding	1
molecular_function	1
structural molecule activity	1
cytoplasm	1
endomembrane system	1
intracellular membrane-bounded organelle	1
cell-cell junction	1
cell-substrate junction	1
external encapsulating structure	1
extracellular vesicle	1

Protein interactions and networks

STRING

2066 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
LAMA3	LAMB3	Q13751	985
LAMA3	LAMC2	Q13753	982
LAMA3	COL17A1	Q9UMD9	936
LAMA3	ITGB4	P16144	830
LAMA3	ITGA6	P23229	785
LAMA3	ITGA3	P26006	736
LAMA3	DST	Q03001	675
LAMA3	COL7A1	Q02388	647
LAMA3	TLL2	Q9Y6L7	639
LAMA3	COL4A1	P02462	637
LAMA3	COL4A2	P08572	636
LAMA3	ITGA5	P08648	613
LAMA3	LAMB1	P07942	612
LAMA3	NID1	P14543	611
LAMA3	COL6A1	P12109	573

IntAct

57 interactions, top by confidence:

A	B	Type	Score
CFTR	ESYT2	psi-mi:“MI:0914”(association)	0.710
SPINK4	PLXNA2	psi-mi:“MI:0914”(association)	0.530
DEFA1	MANBA	psi-mi:“MI:0914”(association)	0.530
SCGB1D4	EGFR	psi-mi:“MI:0914”(association)	0.530
FBXO2	TMEM131L	psi-mi:“MI:0914”(association)	0.530
OS9	AGRN	psi-mi:“MI:0914”(association)	0.530
CFTR	CNOT1	psi-mi:“MI:0914”(association)	0.480
LAMA3	SDC1	psi-mi:“MI:0915”(physical association)	0.400
SIRT1	KPNA3	psi-mi:“MI:0915”(physical association)	0.400
LAMA3	KDM3A	psi-mi:“MI:0915”(physical association)	0.400
	VWA8	psi-mi:“MI:0914”(association)	0.350
SCGB2A2	GXYLT2	psi-mi:“MI:0914”(association)	0.350
TSHR	POTEF	psi-mi:“MI:0914”(association)	0.350
CD44	TCAF2	psi-mi:“MI:0914”(association)	0.350
PTPRK	MANBA	psi-mi:“MI:0914”(association)	0.350
TAZ	MANBA	psi-mi:“MI:0914”(association)	0.350
SLAMF1	RTCA	psi-mi:“MI:0914”(association)	0.350
GML	CLSTN1	psi-mi:“MI:0914”(association)	0.350
HRAS	RPL7	psi-mi:“MI:0914”(association)	0.350
CFTR	MYH7B	psi-mi:“MI:0914”(association)	0.350
ATG16L1	ESYT2	psi-mi:“MI:0914”(association)	0.350
OS9	GXYLT2	psi-mi:“MI:0914”(association)	0.350
CDH23	GTPBP10	psi-mi:“MI:0914”(association)	0.350

BioGRID (72): LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), PLG (Reconstituted Complex), PLAT (Reconstituted Complex), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS), LAMA3 (Affinity Capture-MS)

ESM2 similar proteins: A0JP86, A1A5Y0, A4D0S4, G5ECE3, O15230, P11046, P15215, P15800, P16144, P18563, P18564, P19137, P24043, P25391, P26010, P26011, P55268, P58459, P97607, Q13751, Q13753, Q16787, Q1EHB3, Q1RPR6, Q2KIT5, Q2QI47, Q5RB89, Q60438, Q60675, Q61001, Q61087, Q61092, Q61292, Q61789, Q68SA9, Q6AYF4, Q75N90, Q863C4, Q8BG22, Q8HZI9

Diamond homologs: A0JP86, A2ASQ1, G5ECE3, O00468, O00634, O09118, O15230, O75445, O75882, O95631, P02468, P11047, P15215, P19137, P24043, P25304, P25391, P31696, P34710, P97927, Q00174, Q01635, Q13751, Q13753, Q16363, Q16787, Q18823, Q19981, Q1LVF0, Q24567, Q24568, Q27262, Q2HXW4, Q2QI47, Q5RB89, Q5VV63, Q60675, Q61001, Q61087, Q61092

SIGNOR signaling

2 interactions.

A	Effect	B	Mechanism
GDNF	“up-regulates quantity by expression”	LAMA3	“transcriptional regulation”
LAMA3	“form complex”	Laminin-5	binding

Disease & clinical

Clinical variants and AI predictions

ClinVar

2289 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	126
Likely pathogenic	134
Uncertain significance	626
Likely benign	1111
Benign	144

Top pathogenic / likely-pathogenic (30)

Variant ID	HGVS	Classification
1047960	NM_198129.4(LAMA3):c.6319-1G>T	Pathogenic
1047961	NM_198129.4(LAMA3):c.6348_6352delinsCTGGCAAGA (p.Glu2117fs)	Pathogenic
1047962	NM_198129.4(LAMA3):c.9856G>T (p.Ala3286Ser)	Pathogenic
1068548	NM_198129.4(LAMA3):c.6469G>T (p.Glu2157Ter)	Pathogenic
1069997	NM_198129.4(LAMA3):c.5622_5635del (p.Leu1874fs)	Pathogenic
1070832	NM_198129.4(LAMA3):c.8145T>A (p.Tyr2715Ter)	Pathogenic
1070853	NC_000018.9:g.(?21478692)(21479039_?)del	Pathogenic
1071930	NM_198129.4(LAMA3):c.6100A>T (p.Lys2034Ter)	Pathogenic
1071950	NM_198129.4(LAMA3):c.9887G>A (p.Trp3296Ter)	Pathogenic
1072339	NM_198129.4(LAMA3):c.5394T>A (p.Cys1798Ter)	Pathogenic
1072501	NM_198129.4(LAMA3):c.6847_6854del (p.Ala2283fs)	Pathogenic
1074803	NC_000018.9:g.(?21484507)(21485598_?)del	Pathogenic
1075696	NM_198129.4(LAMA3):c.5568dup (p.Leu1857fs)	Pathogenic
1252054	NM_198129.4(LAMA3):c.8302C>T (p.Arg2768Ter)	Pathogenic
1321416	NM_198129.4(LAMA3):c.7204C>T (p.Arg2402Ter)	Pathogenic
1323177	NM_198129.4(LAMA3):c.5000_5003del (p.Gly1667fs)	Pathogenic
1323178	NM_198129.4(LAMA3):c.8087_8090delinsTGC (p.Asn2696fs)	Pathogenic
1350464	NM_198129.4(LAMA3):c.9617T>G (p.Leu3206Ter)	Pathogenic
1361060	NM_198129.4(LAMA3):c.9893C>A (p.Ser3298Ter)	Pathogenic
1369957	NM_198129.4(LAMA3):c.8755A>T (p.Lys2919Ter)	Pathogenic
1371125	NM_198129.4(LAMA3):c.7738del (p.Thr2580fs)	Pathogenic
1379401	NM_198129.4(LAMA3):c.5137G>T (p.Glu1713Ter)	Pathogenic
1400822	NM_198129.4(LAMA3):c.9236dup (p.Arg3081fs)	Pathogenic
1404615	NM_198129.4(LAMA3):c.5728C>T (p.Gln1910Ter)	Pathogenic
1412135	NM_198129.4(LAMA3):c.5992G>T (p.Glu1998Ter)	Pathogenic
1412583	NM_198129.4(LAMA3):c.6778G>T (p.Glu2260Ter)	Pathogenic
1417958	NM_198129.4(LAMA3):c.8284del (p.Glu2762fs)	Pathogenic
1422229	NM_198129.4(LAMA3):c.8911C>T (p.Gln2971Ter)	Pathogenic
1422425	NM_198129.4(LAMA3):c.6199C>T (p.Gln2067Ter)	Pathogenic
1441309	NM_198129.4(LAMA3):c.5119C>T (p.Gln1707Ter)	Pathogenic

SpliceAI

11506 predictions. Top by Δscore:

Variant	Effect	Δscore
18:23713916:TCAG:T	acceptor_loss	1.0000
18:23713917:CAGG:C	acceptor_loss	1.0000
18:23713918:A:AG	acceptor_gain	1.0000
18:23713918:AG:A	acceptor_gain	1.0000
18:23713919:G:GT	acceptor_gain	1.0000
18:23713919:GG:G	acceptor_gain	1.0000
18:23713919:GGGCC:G	acceptor_gain	1.0000
18:23714070:CAGGT:C	donor_loss	1.0000
18:23714071:AGGTG:A	donor_loss	1.0000
18:23714073:GTG:G	donor_loss	1.0000
18:23714074:T:G	donor_loss	1.0000
18:23747937:TATCA:T	acceptor_loss	1.0000
18:23747938:ATCAG:A	acceptor_loss	1.0000
18:23747939:TCAG:T	acceptor_loss	1.0000
18:23747940:CAGC:C	acceptor_loss	1.0000
18:23747941:A:AG	acceptor_gain	1.0000
18:23747941:AGC:A	acceptor_loss	1.0000
18:23747942:G:A	acceptor_loss	1.0000
18:23747942:G:GA	acceptor_gain	1.0000
18:23748056:TGCTC:T	donor_gain	1.0000
18:23748057:GCTC:G	donor_gain	1.0000
18:23748057:GCTCG:G	donor_gain	1.0000
18:23748058:CTC:C	donor_gain	1.0000
18:23748059:TC:T	donor_gain	1.0000
18:23748060:CG:C	donor_loss	1.0000
18:23748061:G:GG	donor_gain	1.0000
18:23748061:GT:G	donor_loss	1.0000
18:23748062:TAAG:T	donor_loss	1.0000
18:23748063:A:AT	donor_loss	1.0000
18:23748064:AGT:A	donor_loss	1.0000

AlphaMissense

21889 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
18:23909264:T:C	L2376P	0.998
18:23909275:G:C	A2380P	0.998
18:23861664:T:A	W1481R	0.996
18:23861664:T:C	W1481R	0.996
18:23928151:G:C	G2736R	0.996
18:23928154:T:A	C2737S	0.996
18:23928155:G:C	C2737S	0.996
18:23928223:T:C	C2760R	0.996
18:23714006:G:C	W127C	0.995
18:23714006:G:T	W127C	0.995
18:23714010:A:C	S129R	0.995
18:23714012:C:A	S129R	0.995
18:23714012:C:G	S129R	0.995
18:23928154:T:C	C2737R	0.995
18:23928223:T:A	C2760S	0.995
18:23928224:G:C	C2760S	0.995
18:23689927:T:A	C82S	0.994
18:23689928:G:C	C82S	0.994
18:23689929:C:G	C82W	0.994
18:23713929:T:A	C102S	0.994
18:23713930:G:C	C102S	0.994
18:23714004:T:A	W127R	0.994
18:23714004:T:C	W127R	0.994
18:23915361:A:C	S2573R	0.994
18:23915363:C:A	S2573R	0.994
18:23915363:C:G	S2573R	0.994
18:23916580:T:G	F2603C	0.994
18:23920951:T:C	L2647P	0.994
18:23921558:G:A	G2717E	0.994
18:23928152:G:A	G2736D	0.994

dbSNP variants (sampled 300 via entrez): RS1000004758 (18:23925781 G>T), RS1000008419 (18:23846639 T>C), RS1000009756 (18:23809926 T>C), RS1000011371 (18:23744686 G>A), RS1000013857 (18:23853186 AAAAT>A,AAAATAAAT), RS1000024389 (18:23837372 G>C,T), RS1000025785 (18:23698276 G>A,C), RS1000030198 (18:23840560 A>T), RS1000054308 (18:23937609 G>T), RS1000055444 (18:23729888 C>T), RS1000058071 (18:23695159 A>G), RS1000067236 (18:23701369 T>C), RS1000071294 (18:23906581 A>G), RS1000102051 (18:23906025 A>G), RS1000108879 (18:23795837 A>T)

Disease associations

OMIM: gene MIM:600805 | disease phenotypes: MIM:226650, MIM:226700, MIM:245660, MIM:619783, MIM:619784, MIM:178500

GenCC curated gene-disease

Disease	Classification	Inheritance
laryngo-onycho-cutaneous syndrome	Definitive	Autosomal recessive
junctional epidermolysis bullosa	Definitive	Autosomal recessive
junctional epidermolysis bullosa, non-Herlitz type	Strong	Autosomal recessive
junctional epidermolysis bullosa Herlitz type	Strong	Autosomal recessive
epidermolysis bullosa, junctional 2A, intermediate	Strong	Autosomal recessive
epidermolysis bullosa, junctional 2B, severe	Strong	Autosomal recessive
generalized junctional epidermolysis bullosa non-Herlitz type	Supportive	Autosomal recessive

Mondo (8): junctional epidermolysis bullosa, non-Herlitz type (MONDO:0009180), junctional epidermolysis bullosa (MONDO:0017612), junctional epidermolysis bullosa Herlitz type (MONDO:0009182), laryngo-onycho-cutaneous syndrome (MONDO:0009513), epidermolysis bullosa, junctional 2A, intermediate (MONDO:0030746), epidermolysis bullosa, junctional 2B, severe (MONDO:0030747), interstitial lung disease 2 (MONDO:0800497), generalized junctional epidermolysis bullosa non-Herlitz type (MONDO:0019307)

Orphanet (9): Localized junctional epidermolysis bullosa (Orphanet:251393), Intermediate generalized junctional epidermolysis bullosa (Orphanet:79402), Junctional epidermolysis bullosa inversa (Orphanet:79405), OBSOLETE: Junctional epidermolysis bullosa, non-Herlitz type (Orphanet:89840), Junctional epidermolysis bullosa (Orphanet:305), Laryngo-onycho-cutaneous syndrome (Orphanet:2407), Severe generalized junctional epidermolysis bullosa (Orphanet:79404), Idiopathic pulmonary fibrosis (Orphanet:2032), Acute interstitial pneumonia (Orphanet:79126)

HPO phenotypes

98 total (30 of 98 shown, HPO-id order):

HPO	Term
HP:0000003	Multicystic kidney dysplasia
HP:0000007	Autosomal recessive inheritance
HP:0000010	Recurrent urinary tract infections
HP:0000014	Abnormality of the bladder
HP:0000016	Urinary retention
HP:0000070	Ureterocele
HP:0000072	Hydroureter
HP:0000081	Duplicated collecting system
HP:0000107	Renal cyst
HP:0000126	Hydronephrosis
HP:0000421	Epistaxis
HP:0000481	Abnormal cornea morphology
HP:0000505	Visual impairment
HP:0000670	Carious teeth
HP:0000684	Delayed eruption of teeth
HP:0000691	Microdontia
HP:0000705	Amelogenesis imperfecta
HP:0000939	Osteoporosis
HP:0000969	Edema
HP:0000982	Palmoplantar keratoderma
HP:0000999	Pyoderma
HP:0001000	Abnormality of skin pigmentation
HP:0001030	Fragile skin
HP:0001056	Milia
HP:0001057	Aplasia cutis congenita
HP:0001075	Atrophic scars
HP:0001159	Syndactyly
HP:0001211	Abnormal fingertip morphology
HP:0001250	Seizure
HP:0001508	Failure to thrive

GWAS associations

0 associations (top):

MeSH disease descriptors (2)

Descriptor	Name	Tree numbers
D016109	Epidermolysis Bullosa, Junctional	C16.131.831.493.170; C16.320.850.275.170; C17.800.804.493.170; C17.800.827.275.170; C17.800.865.410.170
C537032	Laryngo onycho cutaneous syndrome (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL2364187 (PROTEIN COMPLEX GROUP)

PharmGKB: 1 entry (VIP=true, CPIC=false)

CTD chemical–gene interactions

82 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Estradiol	affects expression, affects cotreatment, increases expression, decreases expression	5
sodium arsenite	affects expression, affects methylation, increases expression	3
Zoledronic Acid	increases expression	3
Air Pollutants	affects cotreatment, decreases expression, increases abundance, increases oxidation, increases expression	3
Tetrachlorodibenzodioxin	affects cotreatment, increases expression, decreases expression	3
bisphenol A	increases methylation, increases expression, affects cotreatment	2
chloropicrin	affects expression, decreases expression	2
Benzo(a)pyrene	increases expression, affects methylation, decreases methylation	2
Cisplatin	decreases expression, increases expression	2
Formaldehyde	decreases expression, increases expression	2
Tobacco Smoke Pollution	affects expression, increases expression	2
Tretinoin	decreases expression, increases expression	2
Cyclosporine	decreases expression, affects expression	2
Aflatoxin B1	increases expression, increases methylation	2
Cadmium Chloride	affects expression, decreases expression	2
Particulate Matter	increases expression, affects cotreatment, increases abundance	2
4-oxoretinoic acid	decreases expression	1
chloroacetaldehyde	affects expression	1
alpha-pinene	decreases expression, increases oxidation, increases abundance, affects cotreatment	1
pyrogallol 1,3-dimethyl ether	affects localization, affects cotreatment, increases expression, decreases expression	1
2,4,5,2’,4’,5’-hexachlorobiphenyl	increases expression	1
beta-lapachone	increases expression	1
butyraldehyde	decreases expression	1
benzo(e)pyrene	affects methylation, increases methylation	1
cupric chloride	increases expression	1
phenanthrene	increases expression	1
lysophosphatidic acid	increases expression	1
benazol P	affects expression	1
methacrylaldehyde	increases oxidation, increases abundance, affects cotreatment, decreases expression	1
brequinar	increases expression	1

Cellosaurus cell lines

2 cell lines: 1 cancer cell line, 1 transformed cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_B1VH	Abcam HeLa LAMA3 KO	Cancer cell line	Female
CVCL_D9I7	Ubigene HEK293 LAMA3 KO	Transformed cell line	Female

Clinical trials (associated diseases)

17 trials via MONDO — disease-level, not drug-specific.

Trial	Phase	Status	Title
NCT00587223	PHASE3	TERMINATED	Safety and Efficacy of Apligraf in Nonhealing Wounds of Subjects With Junctional or Dystrophic Epidermolysis Bullosa (EB)
NCT06917690	PHASE3	RECRUITING	A Study to Learn About the Safety and Efficacy of the Drug Oleogel-S10 in Japanese Patients With Epidermolysis Bullosa
NCT03578029	PHASE2	TERMINATED	Evaluation of the Safety and Efficacy Study of RGN-137 Topical Gel for Junctional and Dystrophic Epidermolysis Bullosa
NCT04908215	PHASE2	COMPLETED	INM-755 (Cannabinol) Cream for Treatment of Epidermolysis Bullosa
NCT06594393	PHASE2	RECRUITING	A Phase 2 Study of TCP-25 Gel in Patients With Epidermolysis Bullosa, STEP-study
NCT03472287	PHASE1	COMPLETED	To Evaluate the Pharmacokinetic of Diacerein and Rhein After Maximum Use in Patients With Epidermolysis Bullosa (EB)
NCT06713434	PHASE1	ACTIVE_NOT_RECRUITING	Pilot Study of ELK-003 Eye Drops for Treating Ocular Manifestations of Epidermolysis Bullosa
NCT04727268	Not specified	UNKNOWN	Genotype-phenotype Correlation in Junctional Epidermolysis Bullosa
NCT03490331	PHASE1/PHASE2	TERMINATED	Clinical Trial to Assess Safety and Efficacy of Autologous Cultured Epidermal Grafts Containing Epidermal Stem Cells Genetically Modified in Patients With JEB (HOLOGENE17)
NCT03526159	PHASE1/PHASE2	RECRUITING	Gentamicin for Junctional Epidermolysis Bullosa
NCT04140786	PHASE1/PHASE2	UNKNOWN	Optimizing IV Gentamicin in JEB
NCT03269474	Not specified	UNKNOWN	Computational Drug Repurposing for All EBS Cases
NCT05033574	Not specified	UNKNOWN	The State of Sexual Development in Children With Inherited Epidermolysis Bullosa
NCT06007235	Not specified	UNKNOWN	CACIPLIQ20 in Wound Healing in Subjects With Epidermolysis Bullosa
NCT06423573	Not specified	RECRUITING	A Study to Assess the Incidence of Skin Cancers in Patients With Epidermolysis Bullosa Receiving Filsuvez
NCT06372353	Not specified	COMPLETED	The Effect Of Baduanjin Exercises In Patients With Idiopathic Pulmonary Fibrosis
NCT06644144	Not specified	RECRUITING	P4O2 ILD Extension