FBN1
entrez
2200
canonical
uniprot
P35555
canonical
ensembl
ENSG00000166147
resolver
ensp
ENSP00000325527
resolver
enst
ENST00000316623
resolver
genesymbol
FBN1
resolver
genesymbol_syn
FBN
resolver
hgnc
HGNC:3603
resolver
uniprot
B2RUU0
resolver
uniprot
D2JYH6
resolver
uniprot
Q15972
resolver
uniprot
Q75N87
resolver
uniprot_entry
FBN1_HUMAN
resolver
uniprot_sec
B2RUU0
resolver
uniprot_sec
D2JYH6
resolver
uniprot_sec
Q15972
resolver
uniprot_sec
Q75N87
resolver
amino_acid_sequence
MRRGRLLEIALGFTVLLASYTSHGADANLEAGNVKETRASRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQIAPSCGSRSIQHCNIRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVISNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDIDECSTIPGICEGGECTNTVSSYFCKCPPGFYTSPDGTRCIDVRPGYCYTALTNGRCSNQLPQSITKMQCCCDAGRCWSPGVTVAPEMCPIRATEDFNKLCSVPMVIPGRPEYPPPPLGPIPPVLPVPPGFPPGPQIPVPRPPVEYLYPSREPPRVLPVNVTDYCQLVRYLCQNGRCIPTPGSYRCECNKGFQLDLRGECIDVDECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYKRGQCIKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGSDINECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFIYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSSESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSQCCSSLGAAWGSPCTLCQVDPICGKGYSRIKGTQCEDIDECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDIRLETCFLRYEDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPMRNTPEYEELCPRGPGFATKEITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGVCHNTEGSYRCECPPGHQLSPNISACIDINECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDIDECSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKEGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYICDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCEMCPAVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDINECLLEPRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSSGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPYGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILAGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECEEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCVDENECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDNREGYCFTEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFQGTVAFKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTSCIDNNECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHICGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDINECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGNPEPPVSGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASNIEDQSETEANVSLASWDVEKTAIFAFNISHVSNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLH
uniprot
proteins
disease_involvement
DISEASE: Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life. {ECO:0000269|PubMed:10425041, ECO:0000269|PubMed:10441597, ECO:0000269|PubMed:10694921, ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12161601, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:12402346, ECO:0000269|PubMed:1301946, ECO:0000269|PubMed:14695540, ECO:0000269|PubMed:15161917, ECO:0000269|PubMed:15221638, ECO:0000269|PubMed:1569206, ECO:0000269|PubMed:16220557, ECO:0000269|PubMed:16222657, ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:18435798, ECO:0000269|PubMed:1852208, ECO:0000269|PubMed:19533785, ECO:0000269|PubMed:19941982, ECO:0000269|PubMed:20803651, ECO:0000269|PubMed:21542060, ECO:0000269|PubMed:22772377, ECO:0000269|PubMed:7611299, ECO:0000269|PubMed:7738200, ECO:0000269|PubMed:7762551, ECO:0000269|PubMed:7870075, ECO:0000269|PubMed:7951214, ECO:0000269|PubMed:7977366, ECO:0000269|PubMed:8004112, ECO:0000269|PubMed:8040326, ECO:0000269|PubMed:8071963, ECO:0000269|PubMed:8136837, ECO:0000269|PubMed:8281141, ECO:0000269|PubMed:8406497, ECO:0000269|PubMed:8504310, ECO:0000269|PubMed:8863159, ECO:0000269|PubMed:8882780, ECO:0000269|PubMed:9016526, ECO:0000269|PubMed:9254848, ECO:0000269|PubMed:9338581, ECO:0000269|PubMed:9401003, ECO:0000269|PubMed:9452085, ECO:0000269|PubMed:9837823, ECO:0000269|Ref.76}. Note=The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini.; DISEASE: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1) [MIM:129600]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. {ECO:0000269|PubMed:11700157, ECO:0000269|PubMed:11826022, ECO:0000269|PubMed:12203992, ECO:0000269|PubMed:17657824, ECO:0000269|PubMed:8188302}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:12525539}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Overlap connective tissue disease (OCTD) [MIM:604308]: Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable. {ECO:0000269|PubMed:2739055}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness. {ECO:0000269|PubMed:20375004}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal. {ECO:0000269|PubMed:21683322}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: [Asprosin]: Marfanoid-progeroid-lipodystrophy syndrome (MFLS) [MIM:616914]: An autosomal dominant syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome. Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly. Mental and motor development are within normal limits. {ECO:0000269|PubMed:20979188, ECO:0000269|PubMed:21594992, ECO:0000269|PubMed:21594993, ECO:0000269|PubMed:24039054, ECO:0000269|PubMed:24613577, ECO:0000269|PubMed:24665001, ECO:0000269|PubMed:26860060, ECO:0000269|PubMed:27087445}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: [Fibrillin-1]: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:15062093, PubMed:1860873). Fibrillin-1-containing microfibrils provide long-term force bearing structural support (PubMed:27026396). In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin (PubMed:27026396). In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles (PubMed:27026396). Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11 (PubMed:24039232). This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). {ECO:0000250|UniProtKB:Q61554, ECO:0000269|PubMed:11461921, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15062093, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:1860873, ECO:0000269|PubMed:24039232, ECO:0000303|PubMed:27026396}.; FUNCTION: [Asprosin]: Adipokine secreted by white adipose tissue that plays an important regulatory role in the glucose metabolism of liver, muscle and pancreas (PubMed:27087445, PubMed:30853600). Hormone that targets the liver in response to fasting to increase plasma glucose levels (PubMed:27087445). Binds the olfactory receptor OR4M1 at the surface of hepatocytes and promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation (PubMed:27087445, PubMed:31230984). May act as a regulator of adaptive thermogenesis by inhibiting browning and energy consumption, while increasing lipid deposition in white adipose tissue (By similarity). Also acts as an orexigenic hormone that increases appetite: crosses the blood brain barrier and exerts effects on the hypothalamus (By similarity). In the arcuate nucleus of the hypothalamus, asprosin directly activates orexigenic AgRP neurons and indirectly inhibits anorexigenic POMC neurons, resulting in appetite stimulation (By similarity). Activates orexigenic AgRP neurons via binding to the olfactory receptor OR4M1 (By similarity). May also play a role in sperm motility in testis via interaction with OR4M1 receptor (By similarity). {ECO:0000250|UniProtKB:Q61554, ECO:0000269|PubMed:27087445, ECO:0000269|PubMed:30853600, ECO:0000269|PubMed:31230984}.
uniprot
proteins
mass_dalton
312298
uniprot
proteins
mutagenesis
MUTAGEN 1542; /note="G->D: Loss of integrin-mediated cell adhesion."; /evidence="ECO:0000269|PubMed:12807887"; MUTAGEN 2728; /note="R->A: Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus."; /evidence="ECO:0000269|PubMed:9817919"; MUTAGEN 2731; /note="R->K: Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus."; /evidence="ECO:0000269|PubMed:9817919"; MUTAGEN 2732; /note="S->T: Defects in protein processing at the C-terminus."; /evidence="ECO:0000269|PubMed:9817919
uniprot
proteins
post_translational_modification
PTM: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). {ECO:0000269|PubMed:10636927, ECO:0000269|PubMed:24982166, ECO:0000303|PubMed:27026396}.; PTM: [Fibrillin-1]: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. {ECO:0000269|PubMed:9362480}.; PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is necessary for efficient protein secretion. {ECO:0000269|PubMed:34411563}.
uniprot
proteins
protein_family
Fibrillin family
uniprot
proteins
pubmed
10425041
uniprot
proteins
pubmed
10441597
uniprot
proteins
pubmed
10633129
uniprot
proteins
pubmed
10636927
uniprot
proteins
pubmed
10694921
uniprot
proteins
pubmed
11461921
uniprot
proteins
pubmed
11700157
uniprot
proteins
pubmed
11826022
uniprot
proteins
pubmed
12161601
uniprot
proteins
pubmed
12203987
uniprot
proteins
pubmed
12203992
uniprot
proteins
pubmed
12402346
uniprot
proteins
pubmed
12511552
uniprot
proteins
pubmed
12525539
uniprot
proteins
pubmed
12807887
uniprot
proteins
pubmed
1301946
uniprot
proteins
pubmed
14695540
uniprot
proteins
pubmed
15062093
uniprot
proteins
pubmed
15131124
uniprot
proteins
pubmed
15161917
uniprot
proteins
pubmed
15165854
uniprot
proteins
pubmed
15221638
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1569206
uniprot
proteins
pubmed
15790312
uniprot
proteins
pubmed
16220557
uniprot
proteins
pubmed
16222657
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
17158881
uniprot
proteins
pubmed
17255108
uniprot
proteins
pubmed
17293099
uniprot
proteins
pubmed
17657824
uniprot
proteins
pubmed
18339631
uniprot
proteins
pubmed
18435798
uniprot
proteins
pubmed
1852206
uniprot
proteins
pubmed
1852207
uniprot
proteins
pubmed
1852208
uniprot
proteins
pubmed
1860873
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19293843
uniprot
proteins
pubmed
19349279
uniprot
proteins
pubmed
19446531
uniprot
proteins
pubmed
19533785
uniprot
proteins
pubmed
19570982
uniprot
proteins
pubmed
19941982
uniprot
proteins
pubmed
20375004
uniprot
proteins
pubmed
20547088
uniprot
proteins
pubmed
20803651
uniprot
proteins
pubmed
20979188
uniprot
proteins
pubmed
21034599
uniprot
proteins
pubmed
21402694
uniprot
proteins
pubmed
21542060
uniprot
proteins
pubmed
21594992
uniprot
proteins
pubmed
21594993
uniprot
proteins
pubmed
21683322
uniprot
proteins
pubmed
22772377
uniprot
proteins
pubmed
23010571
uniprot
proteins
pubmed
24035709
uniprot
proteins
pubmed
24039054
uniprot
proteins
pubmed
24039232
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24613577
uniprot
proteins
pubmed
24665001
uniprot
proteins
pubmed
24982166
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
26601954
uniprot
proteins
pubmed
26860060
uniprot
proteins
pubmed
27026396
uniprot
proteins
pubmed
27087445
uniprot
proteins
pubmed
2739055
uniprot
proteins
pubmed
29104036
uniprot
proteins
pubmed
30853600
uniprot
proteins
pubmed
31230984
uniprot
proteins
pubmed
31775140
uniprot
proteins
pubmed
33904407
uniprot
proteins
pubmed
34411563
uniprot
proteins
pubmed
7611299
uniprot
proteins
pubmed
7691719
uniprot
proteins
pubmed
7738200
uniprot
proteins
pubmed
7762551
uniprot
proteins
pubmed
7870075
uniprot
proteins
pubmed
7911051
uniprot
proteins
pubmed
7951214
uniprot
proteins
pubmed
7977366
uniprot
proteins
pubmed
8004112
uniprot
proteins
pubmed
8040326
uniprot
proteins
pubmed
8071963
uniprot
proteins
pubmed
8136837
uniprot
proteins
pubmed
8188302
uniprot
proteins
pubmed
8281141
uniprot
proteins
pubmed
8364578
uniprot
proteins
pubmed
8406497
uniprot
proteins
pubmed
8430317
uniprot
proteins
pubmed
8504310
uniprot
proteins
pubmed
8568869
uniprot
proteins
pubmed
8594563
uniprot
proteins
pubmed
8653794
uniprot
proteins
pubmed
8863159
uniprot
proteins
pubmed
8882780
uniprot
proteins
pubmed
8988160
uniprot
proteins
pubmed
9016526
uniprot
proteins
pubmed
9150726
uniprot
proteins
pubmed
9254848
uniprot
proteins
pubmed
9338581
uniprot
proteins
pubmed
9338588
uniprot
proteins
pubmed
9362480
uniprot
proteins
pubmed
9401003
uniprot
proteins
pubmed
9452085
uniprot
proteins
pubmed
9817919
uniprot
proteins
pubmed
9837823
uniprot
proteins
sequence_length
2871
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24982166, ECO:0000269|PubMed:34411563}. Note=Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). {ECO:0000269|PubMed:24982166}.; SUBCELLULAR LOCATION: [Fibrillin-1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11461921, ECO:0000269|PubMed:24982166}.; SUBCELLULAR LOCATION: [Asprosin]: Secreted {ECO:0000269|PubMed:27087445}. Note=Secreted by white adipose tissue and circulates in the plasma. {ECO:0000269|PubMed:27087445}.
uniprot
proteins