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Protein

Fibulin-5

Gene

FBLN5

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

Functioni

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).By similarity3 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • integrin binding Source: UniProtKB
  • protein C-terminus binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell-matrix adhesion Source: ProtInc
  • elastic fiber assembly Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • protein localization to cell surface Source: BHF-UCL
  • regulation of cell growth Source: Ensembl
  • regulation of removal of superoxide radicals Source: BHF-UCL
  • secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140092-MONOMER.
ReactomeiR-HSA-1566948. Elastic fibre formation.
R-HSA-2129379. Molecules associated with elastic fibres.
SIGNORiQ9UBX5.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibulin-5
Short name:
FIBL-5
Alternative name(s):
Developmental arteries and neural crest EGF-like protein
Short name:
Dance
Urine p50 protein
Short name:
UP50
Gene namesi
Name:FBLN5
Synonyms:DANCE
ORF Names:UNQ184/PRO210
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:3602. FBLN5.

Subcellular locationi

GO - Cellular componenti

  • elastic fiber Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Neuropathy, hereditary, with or without age-related macular degeneration (HNARMD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neuropathy of the Charcot-Marie-Tooth disease group, characterized by distal muscle weakness and atrophy variably affecting the lower and upper limbs. Distal sensory impairement and decreased nerve conduction velocities are present in most but not all patients. Additional variable features are age-related macular degeneration, joint hypermobility, and hyperelastic skin.
See also OMIM:608895
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07628948T → I in HNARMD. 1 PublicationCorresponds to variant rs141200859dbSNPEnsembl.1
Natural variantiVAR_07629090G → S in HNARMD. 1 PublicationCorresponds to variant rs144288844dbSNPEnsembl.1
Natural variantiVAR_072393267G → S in ARMD3, ARCL1A and HNARMD; produces protein misolding; decreases secretion; no effect on homodimerization. 4 PublicationsCorresponds to variant rs149396611dbSNPEnsembl.1
Natural variantiVAR_076291373R → C in HNARMD. 2 Publications1
Cutis laxa, autosomal dominant, 2 (ADCL2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614434
Cutis laxa, autosomal recessive, 1A (ARCL1A)5 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations affecting this gene can modify the phenotype of diseases caused by ELN mutations.1 Publication
Disease descriptionA 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.
See also OMIM:219100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072392217C → R in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization. 4 PublicationsCorresponds to variant rs80338766dbSNPEnsembl.1
Natural variantiVAR_017153227S → P in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development. 6 PublicationsCorresponds to variant rs28939370dbSNPEnsembl.1
Natural variantiVAR_072393267G → S in ARMD3, ARCL1A and HNARMD; produces protein misolding; decreases secretion; no effect on homodimerization. 4 PublicationsCorresponds to variant rs149396611dbSNPEnsembl.1
Macular degeneration, age-related, 3 (ARMD3)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:608895
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01981460V → L in ARMD3; no effect on secretion; no effect on homodimerization. 3 PublicationsCorresponds to variant rs28939371dbSNPEnsembl.1
Natural variantiVAR_01981571R → Q in ARMD3; no effect on secretion; no effect on homodimerization. 3 PublicationsCorresponds to variant rs28939372dbSNPEnsembl.1
Natural variantiVAR_01981687P → S in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs28939373dbSNPEnsembl.1
Natural variantiVAR_072389124Q → P in ARMD3; almost abolishes secretion; no effect on homodimerization. 2 Publications1
Natural variantiVAR_019817169I → T in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding. 4 PublicationsCorresponds to variant rs28939072dbSNPEnsembl.1
Natural variantiVAR_072393267G → S in ARMD3, ARCL1A and HNARMD; produces protein misolding; decreases secretion; no effect on homodimerization. 4 PublicationsCorresponds to variant rs149396611dbSNPEnsembl.1
Natural variantiVAR_019818351R → W in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs28939073dbSNPEnsembl.1
Natural variantiVAR_019819363A → T in ARMD3; no effect on secretion. 2 PublicationsCorresponds to variant rs121434302dbSNPEnsembl.1
Natural variantiVAR_019820412G → E in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs121434303dbSNPEnsembl.1

Keywords - Diseasei

Age-related macular degeneration, Charcot-Marie-Tooth disease, Disease mutation, Neuropathy

Organism-specific databases

DisGeNETi10516.
MalaCardsiFBLN5.
MIMi219100. phenotype.
608895. phenotype.
614434. phenotype.
OpenTargetsiENSG00000140092.
Orphaneti279. Age-related macular degeneration.
90348. Autosomal dominant cutis laxa.
90349. Autosomal recessive cutis laxa type 1.
280598. Hereditary sensorimotor neuropathy with hyperelastic skin.
PharmGKBiPA28015.

Polymorphism and mutation databases

BioMutaiFBLN5.
DMDMi12643876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000757724 – 448Fibulin-5Add BLAST425

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 59PROSITE-ProRule annotation
Disulfide bondi53 ↔ 68PROSITE-ProRule annotation
Disulfide bondi131 ↔ 144PROSITE-ProRule annotation
Disulfide bondi138 ↔ 153PROSITE-ProRule annotation
Disulfide bondi155 ↔ 166PROSITE-ProRule annotation
Disulfide bondi172 ↔ 181PROSITE-ProRule annotation
Disulfide bondi177 ↔ 190PROSITE-ProRule annotation
Disulfide bondi192 ↔ 205PROSITE-ProRule annotation
Disulfide bondi211 ↔ 221PROSITE-ProRule annotation
Disulfide bondi217 ↔ 230PROSITE-ProRule annotation
Disulfide bondi232 ↔ 245PROSITE-ProRule annotation
Disulfide bondi251 ↔ 262PROSITE-ProRule annotation
Disulfide bondi258 ↔ 271PROSITE-ProRule annotation
Disulfide bondi273 ↔ 286PROSITE-ProRule annotation
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi292 ↔ 305PROSITE-ProRule annotation
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi299 ↔ 314PROSITE-ProRule annotation
Disulfide bondi320 ↔ 332PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UBX5.
PeptideAtlasiQ9UBX5.
PRIDEiQ9UBX5.

2D gel databases

REPRODUCTION-2DPAGEIPI00294615.

PTM databases

iPTMnetiQ9UBX5.
PhosphoSitePlusiQ9UBX5.

Expressioni

Tissue specificityi

Expressed in skin fibroblasts (at protein level)(PubMed:17035250). Expressed predominantly in heart, ovary, and colon but also in kidney, pancreas, testis, lung and placenta. Not detectable in brain, liver, thymus, prostate, or peripheral blood leukocytes (PubMed:10428823).2 Publications

Gene expression databases

BgeeiENSG00000140092.
CleanExiHS_FBLN5.
ExpressionAtlasiQ9UBX5. baseline and differential.
GenevisibleiQ9UBX5. HS.

Organism-specific databases

HPAiCAB025843.
HPA000848.
HPA000868.

Interactioni

Subunit structurei

Homodimer (PubMed:20007835). Monomer (PubMed:15790312, PubMed:19617354), homodimerizes in presence of Ca2+ (PubMed:19617354). Interacts with ELN (PubMed:17035250, PubMed:15790312). Interacts (via N-terminus) with the integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (By similarity). Interacts with FBN1 (via N-terminal domain). Forms a ternary complex with ELN and FBN1 (PubMed:17255108).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EFEMP2O959673EBI-947897,EBI-743414
ELNP155023EBI-947897,EBI-1222108
FBN1P355553EBI-947897,EBI-2505934
LOXP283002EBI-947897,EBI-3893481
LTBP2Q147672EBI-947897,EBI-1546118

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • protein C-terminus binding Source: BHF-UCL
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115771. 15 interactors.
DIPiDIP-44301N.
IntActiQ9UBX5. 17 interactors.
MINTiMINT-2868380.
STRINGi9606.ENSP00000345008.

Structurei

3D structure databases

ProteinModelPortaliQ9UBX5.
SMRiQ9UBX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 82EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini127 – 167EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini168 – 206EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini207 – 246EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini247 – 287EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini288 – 333EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST46

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi54 – 56Cell attachment siteSequence analysis3

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 6 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR76. Eukaryota.
ENOG41104WD. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ9UBX5.
KOiK17340.
PhylomeDBiQ9UBX5.
TreeFamiTF317514.

Family and domain databases

InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PfamiPF12662. cEGF. 3 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UBX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGIKRILTV TILALCLPSP GNAQAQCTNG FDLDRQSGQC LDIDECRTIP
60 70 80 90 100
EACRGDMMCV NQNGGYLCIP RTNPVYRGPY SNPYSTPYSG PYPAAAPPLS
110 120 130 140 150
APNYPTISRP LICRFGYQMD ESNQCVDVDE CATDSHQCNP TQICINTEGG
160 170 180 190 200
YTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLNE
210 220 230 240 250
DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE DGVHCSDMDE
260 270 280 290 300
CSFSEFLCQH ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN
310 320 330 340 350
LQQTCYNLQG GFKCIDPIRC EEPYLRISDN RCMCPAENPG CRDQPFTILY
360 370 380 390 400
RDMDVVSGRS VPADIFQMQA TTRYPGAYYI FQIKSGNEGR EFYMRQTGPI
410 420 430 440
SATLVMTRPI KGPREIQLDL EMITVNTVIN FRGSSVIRLR IYVSQYPF
Length:448
Mass (Da):50,180
Last modified:May 1, 2000 - v1
Checksum:i19FCA51FDA328003
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69 – 70IP → HS in AAC62107 (Ref. 3) Curated2
Sequence conflicti147 – 148TE → MK in AAC62107 (Ref. 3) Curated2
Sequence conflicti228F → L in AAQ89257 (PubMed:12975309).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07628948T → I in HNARMD. 1 PublicationCorresponds to variant rs141200859dbSNPEnsembl.1
Natural variantiVAR_01981460V → L in ARMD3; no effect on secretion; no effect on homodimerization. 3 PublicationsCorresponds to variant rs28939371dbSNPEnsembl.1
Natural variantiVAR_01981571R → Q in ARMD3; no effect on secretion; no effect on homodimerization. 3 PublicationsCorresponds to variant rs28939372dbSNPEnsembl.1
Natural variantiVAR_01981687P → S in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs28939373dbSNPEnsembl.1
Natural variantiVAR_07629090G → S in HNARMD. 1 PublicationCorresponds to variant rs144288844dbSNPEnsembl.1
Natural variantiVAR_072389124Q → P in ARMD3; almost abolishes secretion; no effect on homodimerization. 2 Publications1
Natural variantiVAR_072390126V → M Polymorphism; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs61734479dbSNPEnsembl.1
Natural variantiVAR_019817169I → T in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding. 4 PublicationsCorresponds to variant rs28939072dbSNPEnsembl.1
Natural variantiVAR_072391202G → R Polymorphism; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding; no effect on secretion. 3 PublicationsCorresponds to variant rs80338765dbSNPEnsembl.1
Natural variantiVAR_072392217C → R in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization. 4 PublicationsCorresponds to variant rs80338766dbSNPEnsembl.1
Natural variantiVAR_017153227S → P in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development. 6 PublicationsCorresponds to variant rs28939370dbSNPEnsembl.1
Natural variantiVAR_072393267G → S in ARMD3, ARCL1A and HNARMD; produces protein misolding; decreases secretion; no effect on homodimerization. 4 PublicationsCorresponds to variant rs149396611dbSNPEnsembl.1
Natural variantiVAR_072394301L → M Found in a patient with autosomal recessive cutis laxa also carrying a mutation in ELN; unknown pathological significance. 1 PublicationCorresponds to variant rs377360782dbSNPEnsembl.1
Natural variantiVAR_019818351R → W in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs28939073dbSNPEnsembl.1
Natural variantiVAR_019819363A → T in ARMD3; no effect on secretion. 2 PublicationsCorresponds to variant rs121434302dbSNPEnsembl.1
Natural variantiVAR_026986364D → Y.Corresponds to variant rs1802492dbSNPEnsembl.1
Natural variantiVAR_076291373R → C in HNARMD. 2 Publications1
Natural variantiVAR_019820412G → E in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+). 3 PublicationsCorresponds to variant rs121434303dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133490 mRNA. Translation: CAB38568.1.
AF112152 mRNA. Translation: AAD41768.1.
AF093118 mRNA. Translation: AAC62107.1.
AY358898 mRNA. Translation: AAQ89257.1.
CR457140 mRNA. Translation: CAG33421.1.
AK075147 mRNA. Translation: BAG52073.1.
CH471061 Genomic DNA. Translation: EAW81466.1.
BC022280 mRNA. Translation: AAH22280.1.
CCDSiCCDS9898.1.
RefSeqiNP_006320.2. NM_006329.3.
UniGeneiHs.332708.

Genome annotation databases

EnsembliENST00000342058; ENSP00000345008; ENSG00000140092.
GeneIDi10516.
KEGGihsa:10516.
UCSCiuc001xzx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133490 mRNA. Translation: CAB38568.1.
AF112152 mRNA. Translation: AAD41768.1.
AF093118 mRNA. Translation: AAC62107.1.
AY358898 mRNA. Translation: AAQ89257.1.
CR457140 mRNA. Translation: CAG33421.1.
AK075147 mRNA. Translation: BAG52073.1.
CH471061 Genomic DNA. Translation: EAW81466.1.
BC022280 mRNA. Translation: AAH22280.1.
CCDSiCCDS9898.1.
RefSeqiNP_006320.2. NM_006329.3.
UniGeneiHs.332708.

3D structure databases

ProteinModelPortaliQ9UBX5.
SMRiQ9UBX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115771. 15 interactors.
DIPiDIP-44301N.
IntActiQ9UBX5. 17 interactors.
MINTiMINT-2868380.
STRINGi9606.ENSP00000345008.

PTM databases

iPTMnetiQ9UBX5.
PhosphoSitePlusiQ9UBX5.

Polymorphism and mutation databases

BioMutaiFBLN5.
DMDMi12643876.

2D gel databases

REPRODUCTION-2DPAGEIPI00294615.

Proteomic databases

PaxDbiQ9UBX5.
PeptideAtlasiQ9UBX5.
PRIDEiQ9UBX5.

Protocols and materials databases

DNASUi10516.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342058; ENSP00000345008; ENSG00000140092.
GeneIDi10516.
KEGGihsa:10516.
UCSCiuc001xzx.5. human.

Organism-specific databases

CTDi10516.
DisGeNETi10516.
GeneCardsiFBLN5.
GeneReviewsiFBLN5.
HGNCiHGNC:3602. FBLN5.
HPAiCAB025843.
HPA000848.
HPA000868.
MalaCardsiFBLN5.
MIMi219100. phenotype.
604580. gene.
608895. phenotype.
614434. phenotype.
neXtProtiNX_Q9UBX5.
OpenTargetsiENSG00000140092.
Orphaneti279. Age-related macular degeneration.
90348. Autosomal dominant cutis laxa.
90349. Autosomal recessive cutis laxa type 1.
280598. Hereditary sensorimotor neuropathy with hyperelastic skin.
PharmGKBiPA28015.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR76. Eukaryota.
ENOG41104WD. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ9UBX5.
KOiK17340.
PhylomeDBiQ9UBX5.
TreeFamiTF317514.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000140092-MONOMER.
ReactomeiR-HSA-1566948. Elastic fibre formation.
R-HSA-2129379. Molecules associated with elastic fibres.
SIGNORiQ9UBX5.

Miscellaneous databases

GeneWikiiFBLN5.
GenomeRNAii10516.
PROiQ9UBX5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140092.
CleanExiHS_FBLN5.
ExpressionAtlasiQ9UBX5. baseline and differential.
GenevisibleiQ9UBX5. HS.

Family and domain databases

InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PfamiPF12662. cEGF. 3 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBLN5_HUMAN
AccessioniPrimary (citable) accession number: Q9UBX5
Secondary accession number(s): O75966, Q6IAL4, Q6UWA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 162 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. 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.