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P23142

- FBLN1_HUMAN

UniProt

P23142 - FBLN1_HUMAN

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Protein

Fibulin-1

Gene

FBLN1

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

Functioni

Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP.3 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: ProtInc
  3. peptidase activator activity Source: Ensembl

GO - Biological processi

  1. embryo implantation Source: Ensembl
  2. extracellular matrix organization Source: Reactome
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibulin-1
Short name:
FIBL-1
Gene namesi
Name:FBLN1
ORF Names:PP213
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:3600. FBLN1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FBLN1 is found in a complex type of synpolydactyly referred to as 3/3-prime/4 synpolydactyly associated with metacarpal and metatarsal synostoses. Reciprocal translocation t(12;22)(p11.2;q13.3) with RASSF8. Fibroblasts derived from a patient with synpolydactyly displayed alterations in the level of isoform D splice variant incorporated into the ECM and secreted into the conditioned culture medium. By contrast, the expression of isoform C was not perturbed in the patients fibroblasts. Furthermore, no aberrant polypeptides were detected in extracts of cultured patients fibroblasts. The translocation t(12;22) may result in haploinsufficiency of the isoform D splice variant, which could lead to the observed limb malformation.
Elevated expression and altered processing of FBLN1 protein is associated with human breast cancer.

Organism-specific databases

MIMi608180. phenotype.
Orphaneti404451. FBLN1-related developmental delay-central nervous system anomaly-syndactyly syndrome.
295197. Synpolydactyly type 2.
PharmGKBiPA28013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 703674Fibulin-1PRO_0000007563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 61By similarity
Disulfide bondi37 ↔ 68By similarity
Disulfide bondi50 ↔ 69By similarity
Disulfide bondi78 ↔ 109By similarity
Disulfide bondi91 ↔ 110By similarity
Glycosylationi98 – 981N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi112 ↔ 136By similarity
Disulfide bondi113 ↔ 143By similarity
Disulfide bondi126 ↔ 144By similarity
Disulfide bondi180 ↔ 190By similarity
Disulfide bondi186 ↔ 199By similarity
Disulfide bondi201 ↔ 214By similarity
Disulfide bondi220 ↔ 233By similarity
Disulfide bondi227 ↔ 242By similarity
Disulfide bondi248 ↔ 260By similarity
Disulfide bondi266 ↔ 279By similarity
Disulfide bondi273 ↔ 288By similarity
Disulfide bondi294 ↔ 306By similarity
Disulfide bondi312 ↔ 325By similarity
Disulfide bondi319 ↔ 334By similarity
Disulfide bondi341 ↔ 354By similarity
Disulfide bondi360 ↔ 373By similarity
Disulfide bondi367 ↔ 382By similarity
Disulfide bondi384 ↔ 397By similarity
Disulfide bondi403 ↔ 415By similarity
Disulfide bondi411 ↔ 424By similarity
Disulfide bondi426 ↔ 439By similarity
Disulfide bondi445 ↔ 454By similarity
Disulfide bondi450 ↔ 463By similarity
Disulfide bondi465 ↔ 479By similarity
Disulfide bondi485 ↔ 498By similarity
Disulfide bondi494 ↔ 507By similarity
Disulfide bondi509 ↔ 523By similarity
Disulfide bondi529 ↔ 542By similarity
Glycosylationi535 – 5351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi536 ↔ 551By similarity
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi556 ↔ 577By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP23142.
PaxDbiP23142.
PRIDEiP23142.

PTM databases

PhosphoSiteiP23142.

Expressioni

Tissue specificityi

Isoform A and isoform B are only expressed in placenta. Isoform C and isoform D are expressed in a variety of tissues and cultured cells.1 Publication

Developmental stagei

Widely expressed during embryonic development. Prominent in the matrix of the leptomeningeal anlage, in basement membranes of the neuroepithelium and the perineurium of peripheral nerves. In embryos of gestational week (gw) 4, staining was observed in the early mesenchymal bone anlagen. In gw 6.5 and 8, all perichondrial structures showed expression but the chondrocytes themselves showed no staining. In gw 10, expression is prominent in the interterritorial matrix surrounding the hypertrophic chondrocytes.1 Publication

Inductioni

Expression increased by estrogen in ovarian cancer cells.3 Publications

Gene expression databases

BgeeiP23142.
ExpressionAtlasiP23142. baseline and differential.
GenevestigatoriP23142.

Organism-specific databases

HPAiCAB004393.
HPA001612.
HPA001613.

Interactioni

Subunit structurei

Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LAMA2, NID, ACAN, CSPG2 and type IV collagen. Interacts also with APP, NOV, FGB and HPV type 16, HPV type 18, HPV type 31 and BPV type 1 E6 proteins. Interacts with FBLN7 (By similarity).By similarity

Protein-protein interaction databases

BioGridi108486. 42 interactions.
IntActiP23142. 28 interactions.
MINTiMINT-5005948.

Structurei

3D structure databases

ProteinModelPortaliP23142.
SMRiP23142. Positions 159-593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 7641Anaphylatoxin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 11135Anaphylatoxin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 14433Anaphylatoxin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini176 – 21540EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini216 – 26146EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini262 – 30746EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini308 – 35548EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini356 – 39843EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini399 – 44042EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini441 – 48040EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini481 – 52444EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini525 – 57854EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 44085Self-association and FN1-binding; calcium is necessary for homotypic binding, but not for heterotypic bindingAdd
BLAST

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 3 anaphylatoxin-like domains.PROSITE-ProRule annotation
Contains 9 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000007079.
HOVERGENiHBG051559.
InParanoidiP23142.
KOiK17307.
PhylomeDBiP23142.
TreeFamiTF317514.

Family and domain databases

InterProiIPR000020. Anaphylatoxin/fibulin.
IPR026823. 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.
IPR017048. Fibulin-1.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 5 hits.
[Graphical view]
PIRSFiPIRSF036313. Fibulin-1. 1 hit.
SMARTiSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
PROSITEiPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform D (identifier: P23142-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERAAPSRRV PLPLLLLGGL ALLAAGVDAD VLLEACCADG HRMATHQKDC
60 70 80 90 100
SLPYATESKE CRMVQEQCCH SQLEELHCAT GISLANEQDR CATPHGDNAS
110 120 130 140 150
LEATFVKRCC HCCLLGRAAQ AQGQSCEYSL MVGYQCGQVF QACCVKSQET
160 170 180 190 200
GDLDVGGLQE TDKIIEVEEE QEDPYLNDRC RGGGPCKQQC RDTGDEVVCS
210 220 230 240 250
CFVGYQLLSD GVSCEDVNEC ITGSHSCRLG ESCINTVGSF RCQRDSSCGT
260 270 280 290 300
GYELTEDNSC KDIDECESGI HNCLPDFICQ NTLGSFRCRP KLQCKSGFIQ
310 320 330 340 350
DALGNCIDIN ECLSISAPCP IGHTCINTEG SYTCQKNVPN CGRGYHLNEE
360 370 380 390 400
GTRCVDVDEC APPAEPCGKG HRCVNSPGSF RCECKTGYYF DGISRMCVDV
410 420 430 440 450
NECQRYPGRL CGHKCENTLG SYLCSCSVGF RLSVDGRSCE DINECSSSPC
460 470 480 490 500
SQECANVYGS YQCYCRRGYQ LSDVDGVTCE DIDECALPTG GHICSYRCIN
510 520 530 540 550
IPGSFQCSCP SSGYRLAPNG RNCQDIDECV TGIHNCSINE TCFNIQGGFR
560 570 580 590 600
CLAFECPENY RRSAATLQQE KTDTVRCIKS CRPNDVTCVF DPVHTISHTV
610 620 630 640 650
ISLPTFREFT RPEEIIFLRA ITPPHPASQA NIIFDITEGN LRDSFDIIKR
660 670 680 690 700
YMDGMTVGVV RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE

YWF
Length:703
Mass (Da):77,214
Last modified:November 25, 2008 - v4
Checksum:i302F7ED2DF34CA71
GO
Isoform A (identifier: P23142-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: Missing.

Show »
Length:566
Mass (Da):61,552
Checksum:i2F8AAA8886D2A1C0
GO
Isoform B (identifier: P23142-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: LQQEKTDTVR...VHIFVSEYWF → QKSKKGRQNTPAGSSKEDCRVLPWKQGLEDTHLDA

Show »
Length:601
Mass (Da):65,443
Checksum:i2203FEF959DB3925
GO
Isoform C (identifier: P23142-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: LQQEKTDTVR...VHIFVSEYWF → RCERLPCHEN...KLFIFVSAEL

Show »
Length:683
Mass (Da):74,434
Checksum:iB6B9ED49F590F612
GO

Sequence cautioni

The sequence AAG17241.1 differs from that shown. Reason: Frameshift at positions 116, 619 and 639.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131P → Q in AAH22497. (PubMed:15489334)Curated
Sequence conflicti36 – 361C → S AA sequence (PubMed:2527614)Curated
Sequence conflicti41 – 422HR → SH AA sequence (PubMed:2527614)Curated
Sequence conflicti521 – 5211R → S in AAH22497. (PubMed:15489334)Curated
Sequence conflicti548 – 5481G → A in CAA37770. (PubMed:2269669)Curated
Sequence conflicti548 – 5481G → A in CAA37771. (PubMed:2269669)Curated
Sequence conflicti548 – 5481G → A in CAA37772. (PubMed:2269669)Curated
Sequence conflicti548 – 5481G → A in AAB17099. (PubMed:9106159)Curated
Sequence conflicti548 – 5481G → A in AAK37822. (PubMed:10318851)Curated
Isoform C (identifier: P23142-4)
Sequence conflicti650 – 6501E → K in AAG17241. (PubMed:15498874)Curated
Sequence conflicti662 – 6621L → F in AAG17241. (PubMed:15498874)Curated
Sequence conflicti680 – 6823SAE → FAK in AAG17241. (PubMed:15498874)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411Q → R.5 Publications
Corresponds to variant rs136730 [ dbSNP | Ensembl ].
VAR_015650
Natural varianti509 – 5091C → S.
Corresponds to variant rs1802787 [ dbSNP | Ensembl ].
VAR_055720
Natural varianti695 – 6951H → R.1 Publication
Corresponds to variant rs13268 [ dbSNP | Ensembl ].
VAR_055721

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei567 – 703137Missing in isoform A. 1 PublicationVSP_001383Add
BLAST
Alternative sequencei567 – 703137LQQEK…SEYWF → QKSKKGRQNTPAGSSKEDCR VLPWKQGLEDTHLDA in isoform B. 1 PublicationVSP_001384Add
BLAST
Alternative sequencei567 – 703137LQQEK…SEYWF → RCERLPCHENRECSKLPLRI TYYHLSFPTNIQAPAVVFRM GPSSAVPGDSMQLAITGGNE EGFFTTRKVSPHSGVVALTK PVPEPRDLLLTVKMDLSRHG TVSSFVAKLFIFVSAEL in isoform C. 3 PublicationsVSP_001385Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53741 mRNA. Translation: CAA37770.1.
X53742 mRNA. Translation: CAA37771.1.
X53743 mRNA. Translation: CAA37772.1.
U01244 mRNA. Translation: AAB17099.1.
AF126110 mRNA. Translation: AAK37822.1.
AF217999 mRNA. Translation: AAG17241.1. Frameshift.
AL021391 Genomic DNA. No translation available.
Z95331 Genomic DNA. No translation available.
Z98047 Genomic DNA. No translation available.
BC022497 mRNA. Translation: AAH22497.1.
AY040589 Genomic DNA. Translation: AAK82945.1.
CCDSiCCDS14067.1. [P23142-1]
CCDS14068.1. [P23142-3]
CCDS14069.1. [P23142-4]
CCDS43028.1. [P23142-2]
PIRiC36346.
RefSeqiNP_001987.2. NM_001996.3.
NP_006476.2. NM_006485.3.
NP_006477.2. NM_006486.2.
NP_006478.2. NM_006487.2.
UniGeneiHs.24601.

Genome annotation databases

EnsembliENST00000262722; ENSP00000262722; ENSG00000077942. [P23142-4]
ENST00000327858; ENSP00000331544; ENSG00000077942. [P23142-1]
ENST00000340923; ENSP00000342212; ENSG00000077942. [P23142-2]
ENST00000442170; ENSP00000393812; ENSG00000077942. [P23142-3]
GeneIDi2192.
KEGGihsa:2192.
UCSCiuc003bgg.1. human. [P23142-1]
uc003bgh.3. human. [P23142-4]

Polymorphism databases

DMDMi215274249.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53741 mRNA. Translation: CAA37770.1 .
X53742 mRNA. Translation: CAA37771.1 .
X53743 mRNA. Translation: CAA37772.1 .
U01244 mRNA. Translation: AAB17099.1 .
AF126110 mRNA. Translation: AAK37822.1 .
AF217999 mRNA. Translation: AAG17241.1 . Frameshift.
AL021391 Genomic DNA. No translation available.
Z95331 Genomic DNA. No translation available.
Z98047 Genomic DNA. No translation available.
BC022497 mRNA. Translation: AAH22497.1 .
AY040589 Genomic DNA. Translation: AAK82945.1 .
CCDSi CCDS14067.1. [P23142-1 ]
CCDS14068.1. [P23142-3 ]
CCDS14069.1. [P23142-4 ]
CCDS43028.1. [P23142-2 ]
PIRi C36346.
RefSeqi NP_001987.2. NM_001996.3.
NP_006476.2. NM_006485.3.
NP_006477.2. NM_006486.2.
NP_006478.2. NM_006487.2.
UniGenei Hs.24601.

3D structure databases

ProteinModelPortali P23142.
SMRi P23142. Positions 159-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108486. 42 interactions.
IntActi P23142. 28 interactions.
MINTi MINT-5005948.

PTM databases

PhosphoSitei P23142.

Polymorphism databases

DMDMi 215274249.

Proteomic databases

MaxQBi P23142.
PaxDbi P23142.
PRIDEi P23142.

Protocols and materials databases

DNASUi 2192.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262722 ; ENSP00000262722 ; ENSG00000077942 . [P23142-4 ]
ENST00000327858 ; ENSP00000331544 ; ENSG00000077942 . [P23142-1 ]
ENST00000340923 ; ENSP00000342212 ; ENSG00000077942 . [P23142-2 ]
ENST00000442170 ; ENSP00000393812 ; ENSG00000077942 . [P23142-3 ]
GeneIDi 2192.
KEGGi hsa:2192.
UCSCi uc003bgg.1. human. [P23142-1 ]
uc003bgh.3. human. [P23142-4 ]

Organism-specific databases

CTDi 2192.
GeneCardsi GC22P045898.
HGNCi HGNC:3600. FBLN1.
HPAi CAB004393.
HPA001612.
HPA001613.
MIMi 135820. gene.
608180. phenotype.
neXtProti NX_P23142.
Orphaneti 404451. FBLN1-related developmental delay-central nervous system anomaly-syndactyly syndrome.
295197. Synpolydactyly type 2.
PharmGKBi PA28013.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118806.
HOGENOMi HOG000007079.
HOVERGENi HBG051559.
InParanoidi P23142.
KOi K17307.
PhylomeDBi P23142.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi FBLN1. human.
GeneWikii FBLN1.
GenomeRNAii 2192.
NextBioi 35466434.
PROi P23142.
SOURCEi Search...

Gene expression databases

Bgeei P23142.
ExpressionAtlasi P23142. baseline and differential.
Genevestigatori P23142.

Family and domain databases

InterProi IPR000020. Anaphylatoxin/fibulin.
IPR026823. 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.
IPR017048. Fibulin-1.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view ]
Pfami PF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 5 hits.
[Graphical view ]
PIRSFi PIRSF036313. Fibulin-1. 1 hit.
SMARTi SM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 2 hits.
PROSITEi PS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure."
    Argraves W.S., Tran H., Burgess W.H., Dickerson K.
    J. Cell Biol. 111:3155-3164(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), VARIANT ARG-141.
  2. "Human fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin gene family."
    Tran H., Mattei M.-G., Godyna S., Argraves W.S.
    Matrix Biol. 15:479-493(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), TISSUE SPECIFICITY, VARIANT ARG-141, INTERACTION WITH FN1 AND FGB.
  3. "Translational control of specific genes during differentiation of HL-60 cells."
    Krichevsky A.M., Metzer E., Rosen H.
    J. Biol. Chem. 274:14295-14305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), VARIANTS ARG-141 AND ARG-695.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), VARIANT ARG-141.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM C), VARIANT ARG-141.
    Tissue: Brain.
  7. "Structural and functional characterization of the human and mouse fibulin-1 gene promoters: role of Sp1 and Sp3."
    Castoldi M., Chu M.-L.
    Biochem. J. 362:41-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
  8. "Fibulin, a novel protein that interacts with the fibronectin receptor beta subunit cytoplasmic domain."
    Argraves W.S., Dickerson K., Burgess W.H., Ruoslahti E.
    Cell 58:623-629(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-44.
  9. "Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin."
    Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K., Argraves W.S.
    J. Biol. Chem. 267:20120-20125(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH FN1.
  10. "The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study."
    Roark E.F., Keene D.R., Haudenschild C.C., Godyna S., Little C.D., Argraves W.S.
    J. Histochem. Cytochem. 43:401-411(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  11. "The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis."
    Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C., Argraves W.S.
    J. Biol. Chem. 270:19458-19464(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGB.
  12. "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo."
    Miosge N., Gotz W., Sasaki T., Chu M.-L., Timpl R., Herken R.
    Histochem. J. 28:109-116(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  13. "Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells."
    Clinton G.M., Rougeot C., Derancourt J., Roger P., Defrenne A., Godyna S., Argraves W.S., Rochefort H.
    Proc. Natl. Acad. Sci. U.S.A. 93:316-320(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains."
    Tran H., VanDusen W.J., Argraves W.S.
    J. Biol. Chem. 272:22600-22606(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING, SELF-ASSOCIATION, FN1-BINDING SITES.
  15. "Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines."
    Qing J., Maher V.M., Tran H., Argraves W.S., Dunstan R.W., McCormick J.J.
    Oncogene 15:2159-2168(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN TUMOR FORMATION AND INVASION.
  16. "Increased immunostaining of fibulin-1, an estrogen-regulated protein in the stroma of human ovarian epithelial tumors."
    Roger P., Pujol P., Lucas A., Baldet P., Rochefort H.
    Am. J. Pathol. 153:1579-1588(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  17. "Estradiol and fibulin-1 inhibit motility of human ovarian- and breast-cancer cells induced by fibronectin."
    Hayashido Y., Lucas A., Rougeot C., Godyna S., Argraves W.S., Rochefort H.
    Int. J. Cancer 75:654-658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN TUMOR FORMATION AND INVASION.
  18. "The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling."
    Perbal B., Martinerie C., Sainson R., Werner M., He B., Roizman B.
    Proc. Natl. Acad. Sci. U.S.A. 96:869-874(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOV.
  19. "Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility."
    Twal W.O., Czirok A., Hegedus B., Knaak C., Chintalapudi M.R., Okagawa H., Sugi Y., Argraves W.S.
    J. Cell Sci. 114:4587-4598(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN CELL ADHESION AND MOTILITY.
  20. "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function."
    Ohsawa I., Takamura C., Kohsaka S.
    J. Neurochem. 76:1411-1420(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APP.
  21. "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1."
    Du M., Fan X., Hong E., Chen J.J.
    Biochem. Biophys. Res. Commun. 296:962-969(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIGH-RISK HUMAN PAPILLOMAVIRUSES E6 PROTEIN, INHIBITION OF E6-MEDIATED TRANSFORMATION.
  22. "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly."
    Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S., De Smet L., Fryns J.-P., Van De Ven W.J.M.
    J. Med. Genet. 39:98-104(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION.
  23. "Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells."
    Moll F., Katsaros D., Lazennec G., Hellio N., Roger P., Giacalone P.-L., Chalbos D., Maudelonde T., Rochefort H., Pujol P.
    Oncogene 21:1097-1107(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  24. "Elevated expression and altered processing of fibulin-1 protein in human breast cancer."
    Greene L.M., Twal W.O., Duffy M.J., McDermott E.W., Hill A.D., O'Higgins N.J., McCann A.H., Dervan P.A., Argraves W.S., Gallagher W.M.
    Br. J. Cancer 88:871-878(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH BREAST CANCER.
  25. Cited for: GLYCOSYLATION AT ASN-98.

Entry informationi

Entry nameiFBLN1_HUMAN
AccessioniPrimary (citable) accession number: P23142
Secondary accession number(s): B0QY42
, B1AHL4, P23143, P23144, P37888, Q5TIC4, Q8TBH8, Q9HBQ5, Q9UC21, Q9UGR4, Q9UH41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 25, 2008
Last modified: October 29, 2014
This is version 181 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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