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P23142

- FBLN1_HUMAN

UniProt

P23142 - FBLN1_HUMAN

Protein

Fibulin-1

Gene

FBLN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    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

    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: UniProt
    5. proteinaceous extracellular matrix Source: ProtInc

    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.
    Orphaneti295197. 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

    ArrayExpressiP23142.
    BgeeiP23142.
    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. 30 interactions.
    IntActiP23142. 26 interactions.
    MINTiMINT-5005948.

    Structurei

    3D structure databases

    ProteinModelPortaliP23142.
    SMRiP23142. Positions 184-591.
    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.
    HOGENOMiHOG000007079.
    HOVERGENiHBG051559.
    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

    MERAAPSRRV PLPLLLLGGL ALLAAGVDAD VLLEACCADG HRMATHQKDC    50
    SLPYATESKE CRMVQEQCCH SQLEELHCAT GISLANEQDR CATPHGDNAS 100
    LEATFVKRCC HCCLLGRAAQ AQGQSCEYSL MVGYQCGQVF QACCVKSQET 150
    GDLDVGGLQE TDKIIEVEEE QEDPYLNDRC RGGGPCKQQC RDTGDEVVCS 200
    CFVGYQLLSD GVSCEDVNEC ITGSHSCRLG ESCINTVGSF RCQRDSSCGT 250
    GYELTEDNSC KDIDECESGI HNCLPDFICQ NTLGSFRCRP KLQCKSGFIQ 300
    DALGNCIDIN ECLSISAPCP IGHTCINTEG SYTCQKNVPN CGRGYHLNEE 350
    GTRCVDVDEC APPAEPCGKG HRCVNSPGSF RCECKTGYYF DGISRMCVDV 400
    NECQRYPGRL CGHKCENTLG SYLCSCSVGF RLSVDGRSCE DINECSSSPC 450
    SQECANVYGS YQCYCRRGYQ LSDVDGVTCE DIDECALPTG GHICSYRCIN 500
    IPGSFQCSCP SSGYRLAPNG RNCQDIDECV TGIHNCSINE TCFNIQGGFR 550
    CLAFECPENY RRSAATLQQE KTDTVRCIKS CRPNDVTCVF DPVHTISHTV 600
    ISLPTFREFT RPEEIIFLRA ITPPHPASQA NIIFDITEGN LRDSFDIIKR 650
    YMDGMTVGVV RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE 700
    YWF 703
    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 184-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108486. 30 interactions.
    IntActi P23142. 26 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 295197. Synpolydactyly type 2.
    PharmGKBi PA28013.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000007079.
    HOVERGENi HBG051559.
    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

    ArrayExpressi P23142.
    Bgeei P23142.
    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

    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 1, 2014
    This is version 180 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