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Protein

Transforming growth factor-beta-induced protein ig-h3

Gene

TGFBI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in cell adhesion (PubMed:8024701). May play a role in cell-collagen interactions (By similarity).By similarity1 Publication

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • extracellular matrix binding Source: Ensembl
  • integrin binding Source: ProtInc

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • cell adhesion Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • cellular protein metabolic process Source: Reactome
  • chondrocyte differentiation Source: Ensembl
  • extracellular matrix organization Source: GO_Central
  • negative regulation of cell adhesion Source: ProtInc
  • response to stimulus Source: UniProtKB-KW
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Sensory transduction, Vision

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120708-MONOMER.
ReactomeiR-HSA-977225. Amyloid fiber formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming growth factor-beta-induced protein ig-h3
Short name:
Beta ig-h3
Alternative name(s):
Kerato-epithelin
RGD-containing collagen-associated protein
Short name:
RGD-CAP
Gene namesi
Name:TGFBI
Synonyms:BIGH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11771. TGFBI.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • plasma membrane Source: Reactome
  • proteinaceous extracellular matrix Source: GO_Central
  • trans-Golgi network Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, epithelial basement membrane (EBMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:121820
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031536509L → R in EBMD. 1 PublicationCorresponds to variant rs121909216dbSNPEnsembl.1
Natural variantiVAR_031546666R → S in EBMD; unknown pathological significance. 1 PublicationCorresponds to variant rs121909217dbSNPEnsembl.1
Corneal dystrophy, Groenouw type 1 (CDGG1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare form of stromal corneal dystrophy characterized by multiple small deposits in the superficial central corneal stroma, and progressive visual impairment.
See also OMIM:121900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012444124R → S in CDGG1; late-onset; mild ocular irritation and reduction in visual acuity. 2 PublicationsCorresponds to variant rs121909210dbSNPEnsembl.1
Natural variantiVAR_005083555R → W in CDGG1; common mutation in Europe and United States; rare in Japan. 7 PublicationsCorresponds to variant rs121909208dbSNPEnsembl.1
Corneal dystrophy, lattice type 1 (CDL1)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:122200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005076124R → C in CDL1. 6 PublicationsCorresponds to variant rs121909210dbSNPEnsembl.1
Natural variantiVAR_031535505V → D in CDL1. 1 Publication1
Natural variantiVAR_012446518L → P in CDL1. 1 Publication1
Natural variantiVAR_018484518L → R in CDL1; severe phenotype; delayed age of onset. 1 Publication1
Natural variantiVAR_005080527L → R in CDL1; late-onset; found also in sporadic cases. 3 Publications1
Natural variantiVAR_018485538T → R in CDL1; delayed age of onset. 1 Publication1
Natural variantiVAR_031539546A → D in CDL1; associated with Q-551. 1 PublicationCorresponds to variant rs267607109dbSNPEnsembl.1
Natural variantiVAR_031540551P → Q in CDL1; associated with D-546. 1 PublicationCorresponds to variant rs267607110dbSNPEnsembl.1
Natural variantiVAR_031541569L → R in CDL1. 1 Publication1
Natural variantiVAR_031543572H → R in CDL1; late-onset. 1 Publication1
Natural variantiVAR_031542572Missing in CDL1; late-onset and unilateral phenotype. 1 Publication1
Natural variantiVAR_018487623G → D in CDL1; delayed age of onset. 1 PublicationCorresponds to variant rs121909215dbSNPEnsembl.1
Natural variantiVAR_018488626H → P in CDL1. 1 Publication1
Natural variantiVAR_012450626H → R in CDL1; delayed age of onset. 4 Publications1
Corneal dystrophy, Thiel-Behnke type (CDTB)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA bilateral disorder of the cornea characterized by progressive honeycomb-like, subepithelial corneal opacities with recurrent erosions.
See also OMIM:602082
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005082555R → Q in CDTB; originally thought to cause CDRB. 4 PublicationsCorresponds to variant rs121909209dbSNPEnsembl.1
Corneal dystrophy, Reis-Bucklers type (CDRB)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:608470
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005078124R → L in CDRB. 5 PublicationsCorresponds to variant rs121909211dbSNPEnsembl.1
Natural variantiVAR_005081540Missing in CDRB. 2 Publications1
Natural variantiVAR_005082555R → Q in CDTB; originally thought to cause CDRB. 4 PublicationsCorresponds to variant rs121909209dbSNPEnsembl.1
Corneal dystrophy, lattice type 3A (CDL3A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:608471
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005079501P → T in CDL3A. 2 PublicationsCorresponds to variant rs121909212dbSNPEnsembl.1
Natural variantiVAR_031538540F → S in CDL3A. 1 PublicationCorresponds to variant rs121909214dbSNPEnsembl.1
Natural variantiVAR_012448546A → T in CDL3A. 1 Publication1
Natural variantiVAR_018486622N → K in CDL3A. 1 Publication1
Corneal dystrophy, Avellino type (CDA)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:607541
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005077124R → H in CDA; most common mutation in Japanese. 6 PublicationsCorresponds to variant rs121909211dbSNPEnsembl.1

Keywords - Diseasei

Amyloidosis, Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNETi7045.
MalaCardsiTGFBI.
MIMi121820. phenotype.
121900. phenotype.
122200. phenotype.
602082. phenotype.
607541. phenotype.
608470. phenotype.
608471. phenotype.
OpenTargetsiENSG00000120708.
Orphaneti98962. Granular corneal dystrophy type I.
98963. Granular corneal dystrophy type II.
98964. Lattice corneal dystrophy type I.
98956. Microcystic corneal dystrophy.
98961. Reis-Bucklers corneal dystrophy.
98960. Thiel-Behnke corneal dystrophy.
PharmGKBiPA36484.

Polymorphism and mutation databases

BioMutaiTGFBI.
DMDMi2498193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000000876924 – 683Transforming growth factor-beta-induced protein ig-h3Add BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37PhosphoserineCombined sources1
Disulfide bondi49 ↔ 85PROSITE-ProRule annotation
Disulfide bondi65 ↔ 74PROSITE-ProRule annotation
Disulfide bondi84 ↔ 97PROSITE-ProRule annotation

Post-translational modificationi

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).2 Publications

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Phosphoprotein

Proteomic databases

EPDiQ15582.
MaxQBiQ15582.
PaxDbiQ15582.
PeptideAtlasiQ15582.
PRIDEiQ15582.

PTM databases

iPTMnetiQ15582.
PhosphoSitePlusiQ15582.

Expressioni

Tissue specificityi

Highly expressed in the corneal epithelium (PubMed:8077289). Expressed in heart, placenta, lung, liver, skeletal muscle, kidney and pancreas (PubMed:8077289).1 Publication

Inductioni

By TGF-beta (PubMed:1388724, PubMed:8024701).2 Publications

Gene expression databases

BgeeiENSG00000120708.
CleanExiHS_TGFBI.
ExpressionAtlasiQ15582. baseline and differential.
GenevisibleiQ15582. HS.

Organism-specific databases

HPAiHPA008612.
HPA017019.

Interactioni

Subunit structurei

Binds to type I, II, and IV collagens.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-10236573,EBI-10175124

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • integrin binding Source: ProtInc

Protein-protein interaction databases

BioGridi112903. 2 interactors.
IntActiQ15582. 4 interactors.
MINTiMINT-122359.
STRINGi9606.ENSP00000416330.

Structurei

Secondary structure

1683
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi505 – 509Combined sources5
Beta strandi512 – 515Combined sources4
Helixi516 – 525Combined sources10
Helixi528 – 532Combined sources5
Beta strandi533 – 535Combined sources3
Beta strandi537 – 542Combined sources6
Helixi544 – 549Combined sources6
Helixi552 – 559Combined sources8
Helixi562 – 571Combined sources10
Beta strandi572 – 576Combined sources5
Helixi580 – 583Combined sources4
Beta strandi587 – 591Combined sources5
Beta strandi594 – 602Combined sources9
Beta strandi605 – 610Combined sources6
Beta strandi614 – 620Combined sources7
Beta strandi623 – 630Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3BNMR-A502-634[»]
2LTBNMR-A502-634[»]
2LTCNMR-A502-634[»]
2VXPX-ray2.50A/B502-633[»]
ProteinModelPortaliQ15582.
SMRiQ15582.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15582.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 99EMIPROSITE-ProRule annotationAdd BLAST55
Domaini103 – 236FAS1 1PROSITE-ProRule annotationAdd BLAST134
Domaini240 – 371FAS1 2PROSITE-ProRule annotationAdd BLAST132
Domaini375 – 498FAS1 3PROSITE-ProRule annotationAdd BLAST124
Domaini502 – 632FAS1 4PROSITE-ProRule annotationAdd BLAST131

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi642 – 644Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 1 EMI domain.PROSITE-ProRule annotation
Contains 4 FAS1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1437. Eukaryota.
COG2335. LUCA.
GeneTreeiENSGT00530000063860.
HOVERGENiHBG000715.
InParanoidiQ15582.
KOiK19519.
OMAiVITYECC.
OrthoDBiEOG091G020T.
PhylomeDBiQ15582.
TreeFamiTF316269.

Family and domain databases

Gene3Di2.30.180.10. 4 hits.
InterProiIPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR032954. TGFBI.
IPR016666. TGFBI/POSTN.
[Graphical view]
PANTHERiPTHR10900:SF82. PTHR10900:SF82. 2 hits.
PfamiPF02469. Fasciclin. 4 hits.
[Graphical view]
PIRSFiPIRSF016553. BIGH3_OSF2. 1 hit.
SMARTiSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMiSSF82153. SSF82153. 4 hits.
PROSITEiPS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALFVRLLAL ALALALGPAA TLAGPAKSPY QLVLQHSRLR GRQHGPNVCA
60 70 80 90 100
VQKVIGTNRK YFTNCKQWYQ RKICGKSTVI SYECCPGYEK VPGEKGCPAA
110 120 130 140 150
LPLSNLYETL GVVGSTTTQL YTDRTEKLRP EMEGPGSFTI FAPSNEAWAS
160 170 180 190 200
LPAEVLDSLV SNVNIELLNA LRYHMVGRRV LTDELKHGMT LTSMYQNSNI
210 220 230 240 250
QIHHYPNGIV TVNCARLLKA DHHATNGVVH LIDKVISTIT NNIQQIIEIE
260 270 280 290 300
DTFETLRAAV AASGLNTMLE GNGQYTLLAP TNEAFEKIPS ETLNRILGDP
310 320 330 340 350
EALRDLLNNH ILKSAMCAEA IVAGLSVETL EGTTLEVGCS GDMLTINGKA
360 370 380 390 400
IISNKDILAT NGVIHYIDEL LIPDSAKTLF ELAAESDVST AIDLFRQAGL
410 420 430 440 450
GNHLSGSERL TLLAPLNSVF KDGTPPIDAH TRNLLRNHII KDQLASKYLY
460 470 480 490 500
HGQTLETLGG KKLRVFVYRN SLCIENSCIA AHDKRGRYGT LFTMDRVLTP
510 520 530 540 550
PMGTVMDVLK GDNRFSMLVA AIQSAGLTET LNREGVYTVF APTNEAFRAL
560 570 580 590 600
PPRERSRLLG DAKELANILK YHIGDEILVS GGIGALVRLK SLQGDKLEVS
610 620 630 640 650
LKNNVVSVNK EPVAEPDIMA TNGVVHVITN VLQPPANRPQ ERGDELADSA
660 670 680
LEIFKQASAF SRASQRSVRL APVYQKLLER MKH
Length:683
Mass (Da):74,681
Last modified:November 1, 1996 - v1
Checksum:i40FDC8A71EBB3D00
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031531113V → I in granular corneal dystrophy; unclassified form; with centrifuge pattern of opacities. 1 PublicationCorresponds to variant rs757933370dbSNPEnsembl.1
Natural variantiVAR_031532123D → H in granular corneal dystrophy; unclassified form; Hanoi. 1 PublicationCorresponds to variant rs541270955dbSNPEnsembl.1
Natural variantiVAR_005076124R → C in CDL1. 6 PublicationsCorresponds to variant rs121909210dbSNPEnsembl.1
Natural variantiVAR_005077124R → H in CDA; most common mutation in Japanese. 6 PublicationsCorresponds to variant rs121909211dbSNPEnsembl.1
Natural variantiVAR_005078124R → L in CDRB. 5 PublicationsCorresponds to variant rs121909211dbSNPEnsembl.1
Natural variantiVAR_012444124R → S in CDGG1; late-onset; mild ocular irritation and reduction in visual acuity. 2 PublicationsCorresponds to variant rs121909210dbSNPEnsembl.1
Natural variantiVAR_012445125 – 126Missing Associated with Leu-124 in atypical granular dystrophy; French granular variant. 2 Publications2
Natural variantiVAR_014335200I → F.1 PublicationCorresponds to variant rs45455404dbSNPEnsembl.1
Natural variantiVAR_031533269L → F.1 PublicationCorresponds to variant rs199852470dbSNPEnsembl.1
Natural variantiVAR_031534496R → G.Corresponds to variant rs10057190dbSNPEnsembl.1
Natural variantiVAR_005079501P → T in CDL3A. 2 PublicationsCorresponds to variant rs121909212dbSNPEnsembl.1
Natural variantiVAR_031535505V → D in CDL1. 1 Publication1
Natural variantiVAR_031536509L → R in EBMD. 1 PublicationCorresponds to variant rs121909216dbSNPEnsembl.1
Natural variantiVAR_012446518L → P in CDL1. 1 Publication1
Natural variantiVAR_018484518L → R in CDL1; severe phenotype; delayed age of onset. 1 Publication1
Natural variantiVAR_005080527L → R in CDL1; late-onset; found also in sporadic cases. 3 Publications1
Natural variantiVAR_018485538T → R in CDL1; delayed age of onset. 1 Publication1
Natural variantiVAR_031537539V → D in lattice corneal dystrophy; unclassified form. 1 Publication1
Natural variantiVAR_031538540F → S in CDL3A. 1 PublicationCorresponds to variant rs121909214dbSNPEnsembl.1
Natural variantiVAR_005081540Missing in CDRB. 2 Publications1
Natural variantiVAR_012447544N → S Found in lattice corneal dystrophy; unclassified form; late-onset. 1 PublicationCorresponds to variant rs777288957dbSNPEnsembl.1
Natural variantiVAR_031539546A → D in CDL1; associated with Q-551. 1 PublicationCorresponds to variant rs267607109dbSNPEnsembl.1
Natural variantiVAR_012448546A → T in CDL3A. 1 Publication1
Natural variantiVAR_031540551P → Q in CDL1; associated with D-546. 1 PublicationCorresponds to variant rs267607110dbSNPEnsembl.1
Natural variantiVAR_005082555R → Q in CDTB; originally thought to cause CDRB. 4 PublicationsCorresponds to variant rs121909209dbSNPEnsembl.1
Natural variantiVAR_005083555R → W in CDGG1; common mutation in Europe and United States; rare in Japan. 7 PublicationsCorresponds to variant rs121909208dbSNPEnsembl.1
Natural variantiVAR_031541569L → R in CDL1. 1 Publication1
Natural variantiVAR_031543572H → R in CDL1; late-onset. 1 Publication1
Natural variantiVAR_031542572Missing in CDL1; late-onset and unilateral phenotype. 1 Publication1
Natural variantiVAR_031544594G → V in lattice corneal dystrophy; unclassified form. 1 Publication1
Natural variantiVAR_012449622N → H in asymmetric lattice corneal dystrophy. 1 Publication1
Natural variantiVAR_018486622N → K in CDL3A. 1 Publication1
Natural variantiVAR_018487623G → D in CDL1; delayed age of onset. 1 PublicationCorresponds to variant rs121909215dbSNPEnsembl.1
Natural variantiVAR_031545624 – 625Missing in lattice corneal dystrophy; unclassified form. 1 Publication2
Natural variantiVAR_018488626H → P in CDL1. 1 Publication1
Natural variantiVAR_012450626H → R in CDL1; delayed age of onset. 4 Publications1
Natural variantiVAR_018489631V → D Found in lattice corneal dystrophy; unclassified form. 1 Publication1
Natural variantiVAR_031546666R → S in EBMD; unknown pathological significance. 1 PublicationCorresponds to variant rs121909217dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77349 mRNA. Translation: AAA61163.1.
AF035626 Genomic DNA. Translation: AAB88695.1.
AF035627 Genomic DNA. Translation: AAB88698.1.
AF035628 Genomic DNA. Translation: AAB88696.1.
AF035629 Genomic DNA. Translation: AAB88697.1.
AY149344 Genomic DNA. Translation: AAN10294.1.
BT009820 mRNA. Translation: AAP88822.1.
AC004503 Genomic DNA. Translation: AAC08449.1.
AC005219 Genomic DNA. Translation: AAC24944.1.
CH471062 Genomic DNA. Translation: EAW62199.1.
CH471062 Genomic DNA. Translation: EAW62200.1.
BC000097 mRNA. Translation: AAH00097.1.
BC004972 mRNA. Translation: AAH04972.1.
CCDSiCCDS47266.1.
PIRiI52996.
RefSeqiNP_000349.1. NM_000358.2.
UniGeneiHs.369397.

Genome annotation databases

EnsembliENST00000442011; ENSP00000416330; ENSG00000120708.
GeneIDi7045.
KEGGihsa:7045.
UCSCiuc003lbf.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77349 mRNA. Translation: AAA61163.1.
AF035626 Genomic DNA. Translation: AAB88695.1.
AF035627 Genomic DNA. Translation: AAB88698.1.
AF035628 Genomic DNA. Translation: AAB88696.1.
AF035629 Genomic DNA. Translation: AAB88697.1.
AY149344 Genomic DNA. Translation: AAN10294.1.
BT009820 mRNA. Translation: AAP88822.1.
AC004503 Genomic DNA. Translation: AAC08449.1.
AC005219 Genomic DNA. Translation: AAC24944.1.
CH471062 Genomic DNA. Translation: EAW62199.1.
CH471062 Genomic DNA. Translation: EAW62200.1.
BC000097 mRNA. Translation: AAH00097.1.
BC004972 mRNA. Translation: AAH04972.1.
CCDSiCCDS47266.1.
PIRiI52996.
RefSeqiNP_000349.1. NM_000358.2.
UniGeneiHs.369397.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3BNMR-A502-634[»]
2LTBNMR-A502-634[»]
2LTCNMR-A502-634[»]
2VXPX-ray2.50A/B502-633[»]
ProteinModelPortaliQ15582.
SMRiQ15582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112903. 2 interactors.
IntActiQ15582. 4 interactors.
MINTiMINT-122359.
STRINGi9606.ENSP00000416330.

PTM databases

iPTMnetiQ15582.
PhosphoSitePlusiQ15582.

Polymorphism and mutation databases

BioMutaiTGFBI.
DMDMi2498193.

Proteomic databases

EPDiQ15582.
MaxQBiQ15582.
PaxDbiQ15582.
PeptideAtlasiQ15582.
PRIDEiQ15582.

Protocols and materials databases

DNASUi7045.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000442011; ENSP00000416330; ENSG00000120708.
GeneIDi7045.
KEGGihsa:7045.
UCSCiuc003lbf.5. human.

Organism-specific databases

CTDi7045.
DisGeNETi7045.
GeneCardsiTGFBI.
HGNCiHGNC:11771. TGFBI.
HPAiHPA008612.
HPA017019.
MalaCardsiTGFBI.
MIMi121820. phenotype.
121900. phenotype.
122200. phenotype.
601692. gene.
602082. phenotype.
607541. phenotype.
608470. phenotype.
608471. phenotype.
neXtProtiNX_Q15582.
OpenTargetsiENSG00000120708.
Orphaneti98962. Granular corneal dystrophy type I.
98963. Granular corneal dystrophy type II.
98964. Lattice corneal dystrophy type I.
98956. Microcystic corneal dystrophy.
98961. Reis-Bucklers corneal dystrophy.
98960. Thiel-Behnke corneal dystrophy.
PharmGKBiPA36484.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1437. Eukaryota.
COG2335. LUCA.
GeneTreeiENSGT00530000063860.
HOVERGENiHBG000715.
InParanoidiQ15582.
KOiK19519.
OMAiVITYECC.
OrthoDBiEOG091G020T.
PhylomeDBiQ15582.
TreeFamiTF316269.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120708-MONOMER.
ReactomeiR-HSA-977225. Amyloid fiber formation.

Miscellaneous databases

ChiTaRSiTGFBI. human.
EvolutionaryTraceiQ15582.
GeneWikiiTGFBI.
GenomeRNAii7045.
PROiQ15582.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120708.
CleanExiHS_TGFBI.
ExpressionAtlasiQ15582. baseline and differential.
GenevisibleiQ15582. HS.

Family and domain databases

Gene3Di2.30.180.10. 4 hits.
InterProiIPR011489. EMI_domain.
IPR000782. FAS1_domain.
IPR032954. TGFBI.
IPR016666. TGFBI/POSTN.
[Graphical view]
PANTHERiPTHR10900:SF82. PTHR10900:SF82. 2 hits.
PfamiPF02469. Fasciclin. 4 hits.
[Graphical view]
PIRSFiPIRSF016553. BIGH3_OSF2. 1 hit.
SMARTiSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMiSSF82153. SSF82153. 4 hits.
PROSITEiPS51041. EMI. 1 hit.
PS50213. FAS1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBGH3_HUMAN
AccessioniPrimary (citable) accession number: Q15582
Secondary accession number(s): D3DQB1
, O14471, O14472, O14476, O43216, O43217, O43218, O43219, Q53XM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 179 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.