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Q08879

- FBLN1_MOUSE

UniProt

Q08879 - FBLN1_MOUSE

Protein

Fibulin-1

Gene

Fbln1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (09 May 2003)
      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.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. peptidase activator activity Source: MGI
    3. protein binding Source: MGI

    GO - Biological processi

    1. embryo implantation Source: Ensembl
    2. extracellular matrix organization Source: MGI
    3. positive regulation of peptidase activity Source: GOC

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_198998. Molecules associated with elastic fibres.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibulin-1
    Short name:
    FIBL-1
    Alternative name(s):
    Basement-membrane protein 90
    Short name:
    BM-90
    Gene namesi
    Name:Fbln1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:95487. Fbln1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 705676Fibulin-1PRO_0000007564Add
    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...)Sequence Analysis
    Disulfide bondi112 ↔ 136By similarity
    Disulfide bondi113 ↔ 143By similarity
    Disulfide bondi126 ↔ 144By similarity
    Disulfide bondi182 ↔ 192By similarity
    Disulfide bondi188 ↔ 201By similarity
    Disulfide bondi203 ↔ 216By similarity
    Disulfide bondi222 ↔ 235By similarity
    Disulfide bondi229 ↔ 244By similarity
    Disulfide bondi250 ↔ 262By similarity
    Disulfide bondi268 ↔ 281By similarity
    Disulfide bondi275 ↔ 290By similarity
    Disulfide bondi296 ↔ 308By similarity
    Disulfide bondi314 ↔ 327By similarity
    Disulfide bondi321 ↔ 336By similarity
    Disulfide bondi343 ↔ 356By similarity
    Disulfide bondi362 ↔ 375By similarity
    Disulfide bondi369 ↔ 384By similarity
    Disulfide bondi386 ↔ 399By similarity
    Disulfide bondi405 ↔ 417By similarity
    Disulfide bondi413 ↔ 426By similarity
    Disulfide bondi428 ↔ 441By similarity
    Disulfide bondi447 ↔ 456By similarity
    Disulfide bondi452 ↔ 465By similarity
    Disulfide bondi467 ↔ 481By similarity
    Disulfide bondi487 ↔ 500By similarity
    Disulfide bondi496 ↔ 509By similarity
    Disulfide bondi511 ↔ 525By similarity
    Disulfide bondi531 ↔ 544By similarity
    Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi538 ↔ 553By similarity
    Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi558 ↔ 579By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ08879.
    PaxDbiQ08879.
    PRIDEiQ08879.

    PTM databases

    PhosphoSiteiQ08879.

    Expressioni

    Tissue specificityi

    Detected in most organs (brain, heart, lung, spleen, liver and kidney). Neurons are the predominant source of production in the brain. Not expressed significantly by astrocytes or microglia.1 Publication

    Developmental stagei

    The differential expression of the fibulin family contributes to the formation of molecularly distinct extracellular matrices already during early developmental stages of a large number of tissues. Increase expression at neonate stage in the brain. Expressed in interdigital regions of the handplate of a 12 dpc embryo and in the lateral perichondrial region. Similar expression persists in the 13 dpc handplate particularly in the perichondrial regions and apical aspects of the developing digits.3 Publications

    Inductioni

    Glucocorticoids suppressed mRNA expression and protein synthesis.

    Gene expression databases

    ArrayExpressiQ08879.
    BgeeiQ08879.
    CleanExiMM_FBLN1.
    GenevestigatoriQ08879.

    Interactioni

    Subunit structurei

    Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and type IV collagen. Interacts also with papillomavirus E6 proteins. Binding analysis demonstrated for isoform C a 100-fold stronger binding to the basement membrane protein NID than for isoform D. Interacts with FBLN7.5 Publications

    Protein-protein interaction databases

    BioGridi199605. 1 interaction.
    IntActiQ08879. 1 interaction.
    MINTiMINT-245863.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08879.
    SMRiQ08879. Positions 186-528.
    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
    Domaini178 – 21740EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini218 – 26346EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 30946EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini310 – 35748EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini358 – 40043EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 44242EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini443 – 48240EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini483 – 52644EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini527 – 58054EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni358 – 44285Self-association and FN1-bindingBy similarityAdd
    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.
    GeneTreeiENSGT00750000117498.
    HOGENOMiHOG000007079.
    HOVERGENiHBG051559.
    InParanoidiQ08879.
    KOiK17307.
    OMAiNDEACVR.
    OrthoDBiEOG7P5T0C.
    PhylomeDBiQ08879.
    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. 3 hits.
    PF07645. EGF_CA. 4 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. 4 hits.
    PROSITEiPS01177. ANAPHYLATOXIN_1. 3 hits.
    PS01178. ANAPHYLATOXIN_2. 3 hits.
    PS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 3 hits.
    PS50026. EGF_3. 4 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: Q08879-1) [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

    MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC    50
    SLPYTSESKE CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS 100
    LETIFIKRCC HCCMLGKASL ARDQTCEPIV MISYQCGLVF RACCVKAREN 150
    SDFVQGNGAD LQDPAKIPDE EDQEDPYLND RCRGGGPCKQ QCRDTGDEVI 200
    CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG SFRCQRDSSC 250
    GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF 300
    IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN 350
    EEGTRCVDVD ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV 400
    DINECQRYPG RLCGHKCENT PGSFHCSCSA GFRLSVDGRS CEDVNECLNS 450
    PCSQECANVY GSYQCYCRRG YQLSDVDGVT CEDIDECALP TGGHICSYRC 500
    INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI NETCFNIQGS 550
    FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH 600
    TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII 650
    KRYEDGMTVG VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV 700
    SEYWF 705
    Length:705
    Mass (Da):78,033
    Last modified:May 9, 2003 - v2
    Checksum:i76C527A12E97D0E1
    GO
    Isoform A (identifier: Q08879-3)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform B (identifier: Q08879-4)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform C (identifier: Q08879-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-705: FRQEKTDTVR...VHIFVSEYWF → RCERLPCHEN...KLFIFVSAEL

    Show »
    Length:685
    Mass (Da):75,284
    Checksum:iEF0D77D7F66B73B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301D → N AA sequence (PubMed:2249686)Curated
    Sequence conflicti40 – 401G → P in CAA50207. (PubMed:8354280)Curated
    Sequence conflicti363 – 3631S → A in CAA50207. (PubMed:8354280)Curated
    Sequence conflicti385 – 3851E → K in BAC39669. (PubMed:16141072)Curated
    Sequence conflicti553 – 5531C → Q AA sequence (PubMed:2249686)Curated
    Sequence conflicti558 – 5581C → Q AA sequence (PubMed:2249686)Curated
    Isoform C (identifier: Q08879-2)
    Sequence conflicti571 – 5711E → A in CAA50206. (PubMed:8354280)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei569 – 705137FRQEK…SEYWF → RCERLPCHENQECPRLPLRI TYYHLSFPTNIQVPAVVFRM GPSSAVPGDSMQLAITAGNE EGFFTTRKVSHHSGVVALTK PIPEPRDLLLTVKMDLYRHG TVSSFVAKLFIFVSAEL in isoform C. 3 PublicationsVSP_001386Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70854 mRNA. Translation: CAA50207.1.
    X70853 mRNA. Translation: CAA50206.1.
    AK086451 mRNA. Translation: BAC39669.1.
    AK035388 mRNA. Translation: BAC29054.1.
    BC007140 mRNA. Translation: AAH07140.1.
    AY040588 Genomic DNA. Translation: AAK82944.1.
    CCDSiCCDS27719.1. [Q08879-1]
    PIRiS34968.
    S78040.
    RefSeqiNP_034310.2. NM_010180.2. [Q08879-1]
    XP_006520500.1. XM_006520437.1. [Q08879-2]
    UniGeneiMm.297992.

    Genome annotation databases

    EnsembliENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369. [Q08879-1]
    ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369. [Q08879-2]
    GeneIDi14114.
    KEGGimmu:14114.
    UCSCiuc007xdb.2. mouse. [Q08879-2]
    uc011zxk.1. mouse. [Q08879-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70854 mRNA. Translation: CAA50207.1 .
    X70853 mRNA. Translation: CAA50206.1 .
    AK086451 mRNA. Translation: BAC39669.1 .
    AK035388 mRNA. Translation: BAC29054.1 .
    BC007140 mRNA. Translation: AAH07140.1 .
    AY040588 Genomic DNA. Translation: AAK82944.1 .
    CCDSi CCDS27719.1. [Q08879-1 ]
    PIRi S34968.
    S78040.
    RefSeqi NP_034310.2. NM_010180.2. [Q08879-1 ]
    XP_006520500.1. XM_006520437.1. [Q08879-2 ]
    UniGenei Mm.297992.

    3D structure databases

    ProteinModelPortali Q08879.
    SMRi Q08879. Positions 186-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199605. 1 interaction.
    IntActi Q08879. 1 interaction.
    MINTi MINT-245863.

    PTM databases

    PhosphoSitei Q08879.

    Proteomic databases

    MaxQBi Q08879.
    PaxDbi Q08879.
    PRIDEi Q08879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000057410 ; ENSMUSP00000054583 ; ENSMUSG00000006369 . [Q08879-1 ]
    ENSMUST00000109432 ; ENSMUSP00000105058 ; ENSMUSG00000006369 . [Q08879-2 ]
    GeneIDi 14114.
    KEGGi mmu:14114.
    UCSCi uc007xdb.2. mouse. [Q08879-2 ]
    uc011zxk.1. mouse. [Q08879-1 ]

    Organism-specific databases

    CTDi 2192.
    MGIi MGI:95487. Fbln1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00750000117498.
    HOGENOMi HOG000007079.
    HOVERGENi HBG051559.
    InParanoidi Q08879.
    KOi K17307.
    OMAi NDEACVR.
    OrthoDBi EOG7P5T0C.
    PhylomeDBi Q08879.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_198998. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi FBLN1. mouse.
    NextBioi 285170.
    PROi Q08879.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08879.
    Bgeei Q08879.
    CleanExi MM_FBLN1.
    Genevestigatori Q08879.

    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. 3 hits.
    PF07645. EGF_CA. 4 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. 4 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. 4 hits.
    PS01187. EGF_CA. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands."
      Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.
      Eur. J. Biochem. 215:733-740(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), LIGANDS INTERACTION.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
      Strain: C57BL/6J.
      Tissue: Head and Urinary bladder.
    3. "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).
      Tissue: Mammary tumor.
    4. "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.
    5. "Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum."
      Kluge M., Mann K., Dziadek M., Timpl R.
      Eur. J. Biochem. 193:651-659(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439; 469-476; 553-563 AND 574-581.
    6. "Structural characterization of two variants of fibulin-1 that differ in nidogen affinity."
      Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L., Timpl R.
      J. Mol. Biol. 245:241-250(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF NID AFFINITY.
    7. "Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo."
      Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.
      Dev. Dyn. 205:348-364(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules."
      Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.
      J. Mol. Biol. 272:226-236(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NID-BINDING SITE.
      Strain: 129/Sv.
    9. "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins."
      Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.
      EMBO J. 18:863-870(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAMA2.
    10. "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican."
      Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.
      J. Biol. Chem. 274:20444-20449(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACAN AND CSPG2.
    11. "Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies."
      Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.
      Eur. J. Biochem. 268:5119-5128(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NID.
    12. "Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma."
      Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.
      Eur. J. Haematol. 67:176-184(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOWN-REGULATION BY GLUCOCORTICOIDS.
    13. "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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    14. "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 E6, INHIBITION OF E6-MEDIATED TRANSFORMATION.
    15. "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: DEVELOPMENTAL STAGE.
    16. "TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding."
      de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W., Fukumoto S., Yamada Y.
      J. Biol. Chem. 282:30878-30888(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBLN7.

    Entry informationi

    Entry nameiFBLN1_MOUSE
    AccessioniPrimary (citable) accession number: Q08879
    Secondary accession number(s): Q08878
    , Q8C3B1, Q91ZC9, Q922K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: May 9, 2003
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3