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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).By similarity2 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

ReactomeiREACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

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
ProteomesiUP000005640 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

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171C → R in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization. 4 Publications
VAR_072392
Natural varianti227 – 2271S → P in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development. 6 Publications
Corresponds to variant rs28939370 [ dbSNP | Ensembl ].
VAR_017153
Natural varianti267 – 2671G → S in ARMD3 and ARCL1A; produces protein misolding; decreases secretion; no effect on homodimerization. 3 Publications
VAR_072393
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601V → L in ARMD3; no effect on secretion; no effect on homodimerization. 3 Publications
Corresponds to variant rs28939371 [ dbSNP | Ensembl ].
VAR_019814
Natural varianti71 – 711R → Q in ARMD3; no effect on secretion; no effect on homodimerization. 3 Publications
Corresponds to variant rs28939372 [ dbSNP | Ensembl ].
VAR_019815
Natural varianti87 – 871P → S in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
Corresponds to variant rs28939373 [ dbSNP | Ensembl ].
VAR_019816
Natural varianti124 – 1241Q → P in ARMD3; almost abolishes secretion; no effect on homodimerization. 2 Publications
VAR_072389
Natural varianti169 – 1691I → T in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding. 4 Publications
Corresponds to variant rs28939072 [ dbSNP | Ensembl ].
VAR_019817
Natural varianti267 – 2671G → S in ARMD3 and ARCL1A; produces protein misolding; decreases secretion; no effect on homodimerization. 3 Publications
VAR_072393
Natural varianti351 – 3511R → W in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
Corresponds to variant rs28939073 [ dbSNP | Ensembl ].
VAR_019818
Natural varianti363 – 3631A → T in ARMD3; no effect on secretion. 2 Publications
VAR_019819
Natural varianti412 – 4121G → E in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
VAR_019820

Keywords - Diseasei

Age-related macular degeneration, Disease mutation

Organism-specific databases

MIMi219100. phenotype.
608895. phenotype.
614434. phenotype.
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 448425Fibulin-5PRO_0000007577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi292 ↔ 305PROSITE-ProRule annotation
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi299 ↔ 314PROSITE-ProRule annotation
Disulfide bondi320 ↔ 332PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UBX5.
PeptideAtlasiQ9UBX5.
PRIDEiQ9UBX5.

2D gel databases

REPRODUCTION-2DPAGEIPI00294615.

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

BgeeiQ9UBX5.
CleanExiHS_FBLN5.
ExpressionAtlasiQ9UBX5. baseline and differential.
GenevisibleiQ9UBX5. HS.

Organism-specific databases

HPAiCAB025843.
HPA000848.
HPA000868.

Interactioni

Subunit structurei

Homodimer (PubMed:20007835). Monomer, homodimerizes in presence of Ca2+ (PubMed:19617354). Interacts with ELN (PubMed:17035250). Interacts (via N-terminus) with the integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (By similarity).By similarity3 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

Protein-protein interaction databases

BioGridi115771. 10 interactions.
IntActiQ9UBX5. 17 interactions.
MINTiMINT-2868380.
STRINGi9606.ENSP00000345008.

Structurei

3D structure databases

ProteinModelPortaliQ9UBX5.
SMRiQ9UBX5. Positions 42-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 8241EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini127 – 16741EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini168 – 20639EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini207 – 24640EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini247 – 28741EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini288 – 33346EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 563Cell attachment siteSequence Analysis

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

eggNOGiNOG309650.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ9UBX5.
KOiK17340.
PhylomeDBiQ9UBX5.
TreeFamiTF317514.

Family and domain databases

InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00179. EGF_CA. 4 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 702IP → HS in AAC62107 (Ref. 3) Curated
Sequence conflicti147 – 1482TE → MK in AAC62107 (Ref. 3) Curated
Sequence conflicti228 – 2281F → L in AAQ89257 (PubMed:12975309).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601V → L in ARMD3; no effect on secretion; no effect on homodimerization. 3 Publications
Corresponds to variant rs28939371 [ dbSNP | Ensembl ].
VAR_019814
Natural varianti71 – 711R → Q in ARMD3; no effect on secretion; no effect on homodimerization. 3 Publications
Corresponds to variant rs28939372 [ dbSNP | Ensembl ].
VAR_019815
Natural varianti87 – 871P → S in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
Corresponds to variant rs28939373 [ dbSNP | Ensembl ].
VAR_019816
Natural varianti124 – 1241Q → P in ARMD3; almost abolishes secretion; no effect on homodimerization. 2 Publications
VAR_072389
Natural varianti126 – 1261V → M Polymorphism; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 2 Publications
VAR_072390
Natural varianti169 – 1691I → T in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding. 4 Publications
Corresponds to variant rs28939072 [ dbSNP | Ensembl ].
VAR_019817
Natural varianti202 – 2021G → R Polymorphism; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding; no effect on secretion. 3 Publications
VAR_072391
Natural varianti217 – 2171C → R in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization. 4 Publications
VAR_072392
Natural varianti227 – 2271S → P in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development. 6 Publications
Corresponds to variant rs28939370 [ dbSNP | Ensembl ].
VAR_017153
Natural varianti267 – 2671G → S in ARMD3 and ARCL1A; produces protein misolding; decreases secretion; no effect on homodimerization. 3 Publications
VAR_072393
Natural varianti301 – 3011L → M Found in a patient with autosomal recessive cutis laxa also carrying a mutation in ELN; unknown pathological significance. 1 Publication
VAR_072394
Natural varianti351 – 3511R → W in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
Corresponds to variant rs28939073 [ dbSNP | Ensembl ].
VAR_019818
Natural varianti363 – 3631A → T in ARMD3; no effect on secretion. 2 Publications
VAR_019819
Natural varianti364 – 3641D → Y.
Corresponds to variant rs1802492 [ dbSNP | Ensembl ].
VAR_026986
Natural varianti412 – 4121G → E in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+). 3 Publications
VAR_019820

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.4. 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. Positions 42-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115771. 10 interactions.
IntActiQ9UBX5. 17 interactions.
MINTiMINT-2868380.
STRINGi9606.ENSP00000345008.

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.4. human.

Organism-specific databases

CTDi10516.
GeneCardsiGC14M092335.
GeneReviewsiFBLN5.
HGNCiHGNC:3602. FBLN5.
HPAiCAB025843.
HPA000848.
HPA000868.
MIMi219100. phenotype.
604580. gene.
608895. phenotype.
614434. phenotype.
neXtProtiNX_Q9UBX5.
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

eggNOGiNOG309650.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ9UBX5.
KOiK17340.
PhylomeDBiQ9UBX5.
TreeFamiTF317514.

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

GeneWikiiFBLN5.
GenomeRNAii10516.
NextBioi39880.
PROiQ9UBX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBX5.
CleanExiHS_FBLN5.
ExpressionAtlasiQ9UBX5. baseline and differential.
GenevisibleiQ9UBX5. HS.

Family and domain databases

InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00179. EGF_CA. 4 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...

Publicationsi

« Hide 'large scale' publications
  1. Kostka G.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Melanoma.
  2. "DANCE, a novel secreted RGD protein expressed in developing, atherosclerotic, and balloon-injured arteries."
    Nakamura T., Ruiz-Lozano P., Lindner V., Yabe D., Taniwaki M., Furukawa Y., Kobuke K., Tashiro K., Lu Z., Andon N.L., Schaub R., Matsumori A., Sasayama S., Chien K.R., Honjo T.
    J. Biol. Chem. 274:22476-22483(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. Zemel R., Sholto O., Shaul Y.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Urine.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  9. Cited for: SUBUNIT, GLYCOSYLATION.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa."
    Loeys B., van Maldergem L., Mortier G., Coucke P., Gerniers S., Naeyaert J.-M., de Paepe A.
    Hum. Mol. Genet. 11:2113-2118(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1A PRO-227.
  12. "Genetic heterogeneity of cutis laxa: a heterozygous tandem duplication within the fibulin-5 (FBLN5) gene."
    Markova D., Zou Y., Ringpfeil F., Sasaki T., Kostka G., Timpl R., Uitto J., Chu M.-L.
    Am. J. Hum. Genet. 72:998-1004(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ADCL2.
  13. Cited for: VARIANTS ARMD3 LEU-60; GLN-71; SER-87; THR-169; TRP-351; THR-363 AND GLU-412.
  14. "Fibulin-5 mutations: mechanisms of impaired elastic fiber formation in recessive cutis laxa."
    Hu Q., Loeys B.L., Coucke P.J., De Paepe A., Mecham R.P., Choi J., Davis E.C., Urban Z.
    Hum. Mol. Genet. 15:3379-3386(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARCL1A ARG-217 AND PRO-227, CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND PRO-227, FUNCTION, INTERACTION WITH ELN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. "Reduced secretion of fibulin 5 in age-related macular degeneration and cutis laxa."
    Lotery A.J., Baas D., Ridley C., Jones R.P., Klaver C.C., Stone E., Nakamura T., Luff A., Griffiths H., Wang T., Bergen A.A., Trump D.
    Hum. Mutat. 27:568-574(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351; THR-363 AND GLU-412, CHARACTERIZATION OF VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351; THR-363 AND GLU-412, VARIANTS ARCL1A ARG-217 AND PRO-227, CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND PRO-227, VARIANTS MET-126 AND ARG-202, SUBCELLULAR LOCATION.
  16. "Homozygous missense mutation in fibulin-5 in an Iranian autosomal recessive cutis laxa pedigree and associated haplotype."
    Elahi E., Kalhor R., Banihosseini S.S., Torabi N., Pour-Jafari H., Houshmand M., Amini S.S.H., Ramezani A., Loeys B.
    J. Invest. Dermatol. 126:1506-1509(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1A PRO-227.
  17. "A p.C217R mutation in fibulin-5 from cutis laxa patients is associated with incomplete extracellular matrix formation in a skin equivalent model."
    Claus S., Fischer J., Megarbane H., Megarbane A., Jobard F., Debret R., Peyrol S., Saker S., Devillers M., Sommer P., Damour O.
    J. Invest. Dermatol. 128:1442-1450(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARCL1A ARG-217, CHARACTERIZATION OF VARIANT ARCL1A ARG-217, FUNCTION.
  18. "An autosomal-recessive form of cutis laxa is due to homozygous elastin mutations, and the phenotype may be modified by a heterozygous fibulin 5 polymorphism."
    Megarbane H., Florence J., Sass J.O., Schwonbeck S., Foglio M., de Cid R., Cure S., Saker S., Megarbane A., Fischer J.
    J. Invest. Dermatol. 129:1650-1655(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MET-301.
  19. "Structural effects of fibulin 5 missense mutations associated with age-related macular degeneration and cutis laxa."
    Jones R.P., Ridley C., Jowitt T.A., Wang M.C., Howard M., Bobola N., Wang T., Bishop P.N., Kielty C.M., Baldock C., Lotery A.J., Trump D.
    Invest. Ophthalmol. Vis. Sci. 51:2356-2362(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS MET-126 AND ARG-202, CHARACTERIZATION OF VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351 AND GLU-412, CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND PRO-227, SUBUNIT.
  20. "Biophysical characterisation of fibulin-5 proteins associated with disease."
    Schneider R., Jensen S.A., Whiteman P., McCullagh J.S., Redfield C., Handford P.A.
    J. Mol. Biol. 401:605-617(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS ARCL1A PRO-227 AND SER-267, CHARACTERIZATION OF VARIANT ARMD3 THR-169, CHARACTERIZATION OF VARIANT ARG-202, SUBCELLULAR LOCATION.

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: June 24, 2015
This is version 150 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

External Data

Dasty 3

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 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.