TGFBI
entrez
7045
canonical
uniprot
Q15582
canonical
ensembl
ENSG00000120708
resolver
ensp
ENSP00000416330
resolver
enst
ENST00000442011
resolver
genesymbol
TGFBI
resolver
genesymbol_syn
BIGH3
resolver
hgnc
HGNC:11771
resolver
uniprot
A0A0S2Z4Q2
resolver
uniprot
D3DQB1
resolver
uniprot
O14471
resolver
uniprot
O14472
resolver
uniprot
O14476
resolver
uniprot
O43216
resolver
uniprot
O43217
resolver
uniprot
O43218
resolver
uniprot
O43219
resolver
uniprot
Q53XM1
resolver
uniprot_entry
A0A0S2Z4Q2_HUMAN
resolver
uniprot_entry
BGH3_HUMAN
resolver
uniprot_sec
D3DQB1
resolver
uniprot_sec
O14471
resolver
uniprot_sec
O14472
resolver
uniprot_sec
O14476
resolver
uniprot_sec
O43216
resolver
uniprot_sec
O43217
resolver
uniprot_sec
O43218
resolver
uniprot_sec
O43219
resolver
uniprot_sec
Q53XM1
resolver
amino_acid_sequence
MALFVRLLALALALALGPAATLAGPAKSPYQLVLQHSRLRGRQHGPNVCAVQKVIGTNRKYFTNCKQWYQRKICGKSTVISYECCPGYEKVPGEKGCPAALPLSNLYETLGVVGSTTTQLYTDRTEKLRPEMEGPGSFTIFAPSNEAWASLPAEVLDSLVSNVNIELLNALRYHMVGRRVLTDELKHGMTLTSMYQNSNIQIHHYPNGIVTVNCARLLKADHHATNGVVHLIDKVISTITNNIQQIIEIEDTFETLRAAVAASGLNTMLEGNGQYTLLAPTNEAFEKIPSETLNRILGDPEALRDLLNNHILKSAMCAEAIVAGLSVETLEGTTLEVGCSGDMLTINGKAIISNKDILATNGVIHYIDELLIPDSAKTLFELAAESDVSTAIDLFRQAGLGNHLSGSERLTLLAPLNSVFKDGTPPIDAHTRNLLRNHIIKDQLASKYLYHGQTLETLGGKKLRVFVYRNSLCIENSCIAAHDKRGRYGTLFTMDRVLTPPMGTVMDVLKGDNRFSMLVAAIQSAGLTETLNREGVYTVFAPTNEAFRALPPRERSRLLGDAKELANILKYHIGDEILVSGGIGALVRLKSLQGDKLEVSLKNNVVSVNKEPVAEPDIMATNGVVHVITNVLQPPANRPQERGDELADSALEIFKQASAFSRASQRSVRLAPVYQKLLERMKH
uniprot
proteins
disease_involvement
DISEASE: Corneal dystrophy, epithelial basement membrane (EBMD) [MIM:121820]: A bilateral anterior corneal dystrophy characterized by grayish epithelial fingerprint lines, geographic map-like lines, and dots (or microcysts) on slit-lamp examination. Pathologic studies show abnormal, redundant basement membrane and intraepithelial lacunae filled with cellular debris. {ECO:0000269|PubMed:16652336}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Groenouw type 1 (CDGG1) [MIM:121900]: A rare form of stromal corneal dystrophy characterized by multiple small deposits in the superficial central corneal stroma, and progressive visual impairment. {ECO:0000269|PubMed:15623763}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, lattice type 1 (CDL1) [MIM:122200]: A form of lattice corneal dystrophy, a class of inherited stromal amyloidoses characterized by pathognomonic branching lattice figures in the cornea. CDL1 is characterized by progressive visual impairment, and the presence of delicate, double-contoured, interdigitating, elongated deposits that form a reticular pattern in the corneal stroma. Systemic amyloidosis is absent. Recurrent corneal ulceration sometimes occurs. {ECO:0000269|PubMed:10837380, ECO:0000269|PubMed:11413411, ECO:0000269|PubMed:14597039, ECO:0000269|PubMed:15531312, ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:15838722, ECO:0000269|PubMed:16541014, ECO:0000269|PubMed:17013691, ECO:0000269|PubMed:9799082}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Thiel-Behnke type (CDTB) [MIM:602082]: A bilateral disorder of the cornea characterized by progressive honeycomb-like, subepithelial corneal opacities with recurrent erosions. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Reis-Bucklers type (CDRB) [MIM:608470]: A bilateral disorder of the cornea characterized by intermittent attacks of ocular irritation, recurrent painful corneal erosions starting in childhood, corneal opacities in a geographic pattern at the level of the Bowman layer, and a progressive decrease of visual acuity. The lesions are primarily in Bowman membrane with secondary involvement of the epithelium and superficial part of the stroma. Bowman membrane is almost completely replaced by pathologic materials including disoriented collagen fibrils. {ECO:0000269|PubMed:10660331, ECO:0000269|PubMed:15623763, ECO:0000269|PubMed:9780098}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, lattice type 3A (CDL3A) [MIM:608471]: A form of lattice corneal dystrophy, a class of inherited stromal amyloidoses characterized by pathognomonic branching lattice figures in the cornea. CDL3A is characterized by decreased visual acuity, and the presence of thick, ropy branching lattice lines and accumulations of amyloid deposits in the corneal stroma. Systemic amyloidosis is absent. CDL3A clinically resembles to lattice corneal dystrophy type 3, but differs in that its age of onset is 70 to 90 years. It has an autosomal dominant inheritance pattern. {ECO:0000269|PubMed:15790870, ECO:0000269|PubMed:9497262}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Corneal dystrophy, Avellino type (CDA) [MIM:607541]: A corneal disease resulting in reduced visual acuity and characterized by gray, crumb-like granular deposits in the anterior third of the stroma in each corneal button. Fusiform amyloid deposits, histochemically and morphologically identical to those of lattice corneal dystrophy, are found in the deeper stroma. Additional features include recurrent corneal erosions, and glare and decreased night vision. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Plays a role in cell adhesion (PubMed:8024701). May play a role in cell-collagen interactions (By similarity). {ECO:0000250|UniProtKB:O11780, ECO:0000269|PubMed:8024701}.
uniprot
proteins
mass_dalton
74681
uniprot
proteins
post_translational_modification
PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated; gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation; these residues may be required for binding to calcium (PubMed:18450759). According to a more recent report, does not contain vitamin K-dependent gamma-carboxyglutamate residues (PubMed:26273833). {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.; PTM: The EMI domain contains 2 expected intradomain disulfide bridges (Cys-49-Cys85 and Cys-84-Cys-97) and one unusual interdomain disulfide bridge to the second FAS1 domain (Cys-74-Cys-339). This arrangement violates the predicted disulfide bridge pattern of an EMI domain. {ECO:0000305|PubMed:27609313}.
uniprot
proteins
pubmed
10328397
uniprot
proteins
pubmed
10425035
uniprot
proteins
pubmed
10660331
uniprot
proteins
pubmed
10837380
uniprot
proteins
pubmed
10865320
uniprot
proteins
pubmed
11024425
uniprot
proteins
pubmed
11297504
uniprot
proteins
pubmed
11413411
uniprot
proteins
pubmed
11501939
uniprot
proteins
pubmed
11923233
uniprot
proteins
pubmed
12782158
uniprot
proteins
pubmed
1388724
uniprot
proteins
pubmed
14597039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15531312
uniprot
proteins
pubmed
15623763
uniprot
proteins
pubmed
15790870
uniprot
proteins
pubmed
15838722
uniprot
proteins
pubmed
16541014
uniprot
proteins
pubmed
16636649
uniprot
proteins
pubmed
16652336
uniprot
proteins
pubmed
17013691
uniprot
proteins
pubmed
18450759
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26273833
uniprot
proteins
pubmed
27609313
uniprot
proteins
pubmed
8024701
uniprot
proteins
pubmed
8077289
uniprot
proteins
pubmed
9054935
uniprot
proteins
pubmed
9463327
uniprot
proteins
pubmed
9497262
uniprot
proteins
pubmed
9780098
uniprot
proteins
pubmed
9799082
uniprot
proteins
sequence_length
683
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833, ECO:0000269|PubMed:8024701}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8077289}. Note=May be associated both with microfibrils and with the cell surface (PubMed:8077289). {ECO:0000269|PubMed:8077289}.
uniprot
proteins