FBLN5
entrez
10516
canonical
uniprot
Q9UBX5
canonical
ensembl
ENSG00000140092
resolver
ensp
ENSP00000267620
resolver
ensp
ENSP00000345008
resolver
ensp
ENSP00000450787
resolver
ensp
ENSP00000451982
resolver
ensp
ENSP00000516493
resolver
ensp
ENSP00000516494
resolver
ensp
ENSP00000565541
resolver
ensp
ENSP00000565542
resolver
enst
ENST00000267620
resolver
enst
ENST00000342058
resolver
enst
ENST00000556154
resolver
enst
ENST00000557570
resolver
enst
ENST00000706677
resolver
enst
ENST00000706679
resolver
enst
ENST00000895482
resolver
enst
ENST00000895483
resolver
genesymbol
FBLN5
resolver
genesymbol_syn
DANCE
resolver
hgnc
HGNC:3602
resolver
uniprot
A0A024R6G3
resolver
uniprot
A0A9L9PXD9
resolver
uniprot
G3V2P8
resolver
uniprot
G3V4U0
resolver
uniprot
G3XA98
resolver
uniprot
O75966
resolver
uniprot
Q6IAL4
resolver
uniprot
Q6UWA3
resolver
uniprot_entry
A0A024R6G3_HUMAN
resolver
uniprot_entry
A0A9L9PXD9_HUMAN
resolver
uniprot_entry
FBLN5_HUMAN
resolver
uniprot_entry
G3V2P8_HUMAN
resolver
uniprot_entry
G3V4U0_HUMAN
resolver
uniprot_entry
G3XA98_HUMAN
resolver
uniprot_sec
O75966
resolver
uniprot_sec
Q6IAL4
resolver
uniprot_sec
Q6UWA3
resolver
amino_acid_sequence
MPGIKRILTVTILALCLPSPGNAQAQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTISRPLICRFGYQMDESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPREIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, demyelinating, type 1H (CMT1H) [MIM:619764]: An autosomal dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. CMT1H is characterized by peripheral sensorimotor neuropathy with onset usually in adulthood. Affected individuals present with foot deformities, upper or lower limb sensory disturbances, and motor deficits, mainly impaired gait. Rare patients may have hyperelastic skin or develop age-related macular degeneration. {ECO:0000269|PubMed:21576112, ECO:0000269|PubMed:23328402}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal dominant, 2 (ADCL2) [MIM:614434]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. {ECO:0000269|PubMed:12618961}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal recessive, 1A (ARCL1A) [MIM:219100]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. Type I autosomal recessive cutis laxa is a specific, life-threatening disorder with organ involvement, lung atelectasis and emphysema, diverticula of the gastrointestinal and genitourinary systems, and vascular anomalies. Associated cranial anomalies, late closure of the fontanel, joint laxity, hip dislocation, and inguinal hernia have been observed but are uncommon. {ECO:0000269|PubMed:12189163, ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:16691202, ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:18185537, ECO:0000269|PubMed:20007835, ECO:0000269|PubMed:20599547}. Note=The disease is caused by variants affecting the gene represented in this entry. Mutations affecting this gene can modify the phenotype of diseases caused by ELN mutations. {ECO:0000269|PubMed:19194475}.; DISEASE: Macular degeneration, age-related, 3 (ARMD3) [MIM:608895]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:15269314, ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:20007835, ECO:0000269|PubMed:20599547}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (PubMed:18185537). Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity). Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823). May act as an adapter that mediates the interaction between FBN1 and ELN (PubMed:17255108). {ECO:0000250|UniProtKB:Q9WVH9, ECO:0000269|PubMed:10428823, ECO:0000269|PubMed:17255108, ECO:0000269|PubMed:18185537}.
uniprot
proteins
mass_dalton
50180
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:15790312, ECO:0000269|PubMed:19617354}.
uniprot
proteins
protein_family
Fibulin family
uniprot
proteins
pubmed
10428823
uniprot
proteins
pubmed
12189163
uniprot
proteins
pubmed
12618961
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15269314
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15790312
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16652333
uniprot
proteins
pubmed
16691202
uniprot
proteins
pubmed
17035250
uniprot
proteins
pubmed
17255108
uniprot
proteins
pubmed
18185537
uniprot
proteins
pubmed
19194475
uniprot
proteins
pubmed
19570982
uniprot
proteins
pubmed
19617354
uniprot
proteins
pubmed
20007835
uniprot
proteins
pubmed
20599547
uniprot
proteins
pubmed
21576112
uniprot
proteins
pubmed
23328402
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:17035250, ECO:0000269|PubMed:20599547}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17035250}. Note=co-localizes with ELN in elastic fibers. {ECO:0000269|PubMed:17035250}.
uniprot
proteins