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Q12805

- FBLN3_HUMAN

UniProt

Q12805 - FBLN3_HUMAN

Protein

EGF-containing fibulin-like extracellular matrix protein 1

Gene

EFEMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.3 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. epidermal growth factor-activated receptor activity Source: UniProtKB
    3. epidermal growth factor receptor binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: UniProtKB
    2. extracellular matrix organization Source: Reactome
    3. negative regulation of chondrocyte differentiation Source: UniProtKB
    4. peptidyl-tyrosine phosphorylation Source: UniProtKB
    5. regulation of transcription, DNA-templated Source: UniProtKB
    6. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Growth factor

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_150331. Molecules associated with elastic fibres.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EGF-containing fibulin-like extracellular matrix protein 1
    Alternative name(s):
    Extracellular protein S1-5
    Fibrillin-like protein
    Fibulin-3
    Short name:
    FIBL-3
    Gene namesi
    Name:EFEMP1
    Synonyms:FBLN3, FBNL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:3218. EFEMP1.

    Subcellular locationi

    Secretedextracellular space By similarity. Secretedextracellular spaceextracellular matrix By similarity
    Note: Localizes to the lamina propria underneath the olfactory epithelium.By similarity

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]: Autosomal dominant disease characterized by yellow-white deposits known as drusen that accumulate beneath the retinal pigment epithelium.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti345 – 3451R → W in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates. 2 Publications
    VAR_009513

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi126600. phenotype.
    Orphaneti75376. Familial drusen.
    PharmGKBiPA27652.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 493476EGF-containing fibulin-like extracellular matrix protein 1PRO_0000007570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi177 ↔ 190PROSITE-ProRule annotation
    Disulfide bondi184 ↔ 199PROSITE-ProRule annotation
    Disulfide bondi201 ↔ 212PROSITE-ProRule annotation
    Disulfide bondi218 ↔ 228PROSITE-ProRule annotation
    Disulfide bondi224 ↔ 237PROSITE-ProRule annotation
    Disulfide bondi239 ↔ 252PROSITE-ProRule annotation
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi258 ↔ 268PROSITE-ProRule annotation
    Disulfide bondi264 ↔ 277PROSITE-ProRule annotation
    Disulfide bondi279 ↔ 292PROSITE-ProRule annotation
    Disulfide bondi298 ↔ 309PROSITE-ProRule annotation
    Disulfide bondi305 ↔ 318PROSITE-ProRule annotation
    Disulfide bondi320 ↔ 332PROSITE-ProRule annotation
    Disulfide bondi338 ↔ 350PROSITE-ProRule annotation
    Disulfide bondi344 ↔ 359PROSITE-ProRule annotation
    Disulfide bondi365 ↔ 377PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ12805.
    PaxDbiQ12805.
    PRIDEiQ12805.

    PTM databases

    PhosphoSiteiQ12805.

    Expressioni

    Tissue specificityi

    In the eye, associated with photoreceptor outer and inner segment regions, the nerve fiber layer, outer nuclear layer and inner and outer plexiform layers of the retina.2 Publications

    Gene expression databases

    ArrayExpressiQ12805.
    BgeeiQ12805.
    CleanExiHS_EFEMP1.
    GenevestigatoriQ12805.

    Organism-specific databases

    HPAiCAB016368.

    Interactioni

    Subunit structurei

    Interacts with ECM1. Interacts with TIMP3.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-536772,EBI-6863748From a different organism.
    ARAFP103983EBI-536772,EBI-365961
    ATN1P542593EBI-536772,EBI-945980

    Protein-protein interaction databases

    BioGridi108496. 15 interactions.
    IntActiQ12805. 23 interactions.
    MINTiMINT-1466511.
    STRINGi9606.ENSP00000347596.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12805.
    SMRiQ12805. Positions 44-78, 172-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 7146EGF-like 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 21341EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini214 – 25340EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 29340EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 33340EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini334 – 37845EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni259 – 493235Mediates interaction with TIMP3Add
    BLAST

    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

    eggNOGiNOG250502.
    HOGENOMiHOG000234337.
    HOVERGENiHBG051560.
    InParanoidiQ12805.
    KOiK18262.
    OMAiVQTGRNN.
    OrthoDBiEOG7W9RTF.
    PhylomeDBiQ12805.
    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. 2 hits.
    PF07645. EGF_CA. 3 hits.
    [Graphical view]
    SMARTiSM00179. EGF_CA. 4 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 6 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q12805-1) [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

    MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI    50
    VPDACKGGMK CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG 100
    VVAASSMATS GVLPGGGFVA SAAAVAGPEM QTGRNNFVIR RNPADPQRIP 150
    SNPSHRIQCA AGYEQSEHNV CQDIDECTAG THNCRADQVC INLRGSFACQ 200
    CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS PGFQLAANNY 250
    TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT 300
    SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC 350
    WNYHGGFRCY PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI 400
    RSDRSVPSDI FQIQATTIYA NTINTFRIKS GNENGEFYLR QTSPVSAMLV 450
    LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS VLRLTIIVGP FSF 493
    Length:493
    Mass (Da):54,641
    Last modified:December 1, 2000 - v2
    Checksum:i128CA5ED140DF414
    GO
    Isoform 2 (identifier: Q12805-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: Missing.

    Show »
    Length:485
    Mass (Da):53,722
    Checksum:iCF3DF7CCD89C58AC
    GO
    Isoform 3 (identifier: Q12805-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-58: Missing.

    Show »
    Length:492
    Mass (Da):54,583
    Checksum:iFD09CF260582EA63
    GO
    Isoform 4 (identifier: Q12805-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-106: Missing.

    Show »
    Length:492
    Mass (Da):54,553
    Checksum:iEF7B59437CAA3C67
    GO
    Isoform 5 (identifier: Q12805-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: Missing.
         214-293: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:355
    Mass (Da):39,195
    Checksum:i3E9B55D15D9331EE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti220 – 2201I → F.1 Publication
    VAR_009512
    Natural varianti345 – 3451R → W in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates. 2 Publications
    VAR_009513

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858Missing in isoform 5. 1 PublicationVSP_054372Add
    BLAST
    Alternative sequencei1 – 88Missing in isoform 2. CuratedVSP_001392
    Alternative sequencei58 – 581Missing in isoform 3. CuratedVSP_001393
    Alternative sequencei106 – 1061Missing in isoform 4. CuratedVSP_001394
    Alternative sequencei214 – 29380Missing in isoform 5. 1 PublicationVSP_054373Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03877 mRNA. Translation: AAA65590.1.
    AY004330
    , AY004321, AY004322, AY004325, AY004324, AY004323, AY004326, AY004328, AY004329, AY004327 Genomic DNA. Translation: AAK11491.1.
    AK290599 mRNA. Translation: BAF83288.1.
    AK301402 mRNA. Translation: BAG62937.1.
    AC010895 Genomic DNA. No translation available.
    AC096549 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00080.1.
    CH471053 Genomic DNA. Translation: EAX00081.1.
    CH471053 Genomic DNA. Translation: EAX00082.1.
    BC014410 mRNA. Translation: AAH14410.1.
    BC098561 mRNA. Translation: AAH98561.1.
    CCDSiCCDS1857.1. [Q12805-1]
    PIRiI38449.
    RefSeqiNP_001034437.1. NM_001039348.2. [Q12805-1]
    NP_001034438.1. NM_001039349.2. [Q12805-1]
    UniGeneiHs.732348.
    Hs.76224.

    Genome annotation databases

    EnsembliENST00000355426; ENSP00000347596; ENSG00000115380. [Q12805-1]
    ENST00000394555; ENSP00000378058; ENSG00000115380. [Q12805-1]
    GeneIDi2202.
    KEGGihsa:2202.
    UCSCiuc002rzi.3. human. [Q12805-1]

    Polymorphism databases

    DMDMi9973182.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the EFEMP1 gene

    Retina International's Scientific Newsletter

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03877 mRNA. Translation: AAA65590.1 .
    AY004330
    , AY004321 , AY004322 , AY004325 , AY004324 , AY004323 , AY004326 , AY004328 , AY004329 , AY004327 Genomic DNA. Translation: AAK11491.1 .
    AK290599 mRNA. Translation: BAF83288.1 .
    AK301402 mRNA. Translation: BAG62937.1 .
    AC010895 Genomic DNA. No translation available.
    AC096549 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00080.1 .
    CH471053 Genomic DNA. Translation: EAX00081.1 .
    CH471053 Genomic DNA. Translation: EAX00082.1 .
    BC014410 mRNA. Translation: AAH14410.1 .
    BC098561 mRNA. Translation: AAH98561.1 .
    CCDSi CCDS1857.1. [Q12805-1 ]
    PIRi I38449.
    RefSeqi NP_001034437.1. NM_001039348.2. [Q12805-1 ]
    NP_001034438.1. NM_001039349.2. [Q12805-1 ]
    UniGenei Hs.732348.
    Hs.76224.

    3D structure databases

    ProteinModelPortali Q12805.
    SMRi Q12805. Positions 44-78, 172-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108496. 15 interactions.
    IntActi Q12805. 23 interactions.
    MINTi MINT-1466511.
    STRINGi 9606.ENSP00000347596.

    PTM databases

    PhosphoSitei Q12805.

    Polymorphism databases

    DMDMi 9973182.

    Proteomic databases

    MaxQBi Q12805.
    PaxDbi Q12805.
    PRIDEi Q12805.

    Protocols and materials databases

    DNASUi 2202.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355426 ; ENSP00000347596 ; ENSG00000115380 . [Q12805-1 ]
    ENST00000394555 ; ENSP00000378058 ; ENSG00000115380 . [Q12805-1 ]
    GeneIDi 2202.
    KEGGi hsa:2202.
    UCSCi uc002rzi.3. human. [Q12805-1 ]

    Organism-specific databases

    CTDi 2202.
    GeneCardsi GC02M056093.
    HGNCi HGNC:3218. EFEMP1.
    HPAi CAB016368.
    MIMi 126600. phenotype.
    601548. gene.
    neXtProti NX_Q12805.
    Orphaneti 75376. Familial drusen.
    PharmGKBi PA27652.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250502.
    HOGENOMi HOG000234337.
    HOVERGENi HBG051560.
    InParanoidi Q12805.
    KOi K18262.
    OMAi VQTGRNN.
    OrthoDBi EOG7W9RTF.
    PhylomeDBi Q12805.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi EFEMP1. human.
    GeneWikii EFEMP1.
    GenomeRNAii 2202.
    NextBioi 35475649.
    PROi Q12805.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12805.
    Bgeei Q12805.
    CleanExi HS_EFEMP1.
    Genevestigatori Q12805.

    Family and domain databases

    InterProi 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.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view ]
    Pfami PF12662. cEGF. 2 hits.
    PF07645. EGF_CA. 3 hits.
    [Graphical view ]
    SMARTi SM00179. EGF_CA. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis."
      Lecka-Czernik B., Lumpkin C.K. Jr., Goldstein S.
      Mol. Cell. Biol. 15:120-128(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE ALTERNATIVE SPLICING.
      Tissue: Skin.
    2. "Structure and chromosomal assignment of the human S1-5 gene (FBNL) that is highly homologous to fibrillin."
      Ikegawa S., Toda T., Okui K., Nakamura Y.
      Genomics 35:590-592(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4."
      Giltay R., Timpl R., Kostka G.
      Matrix Biol. 18:469-480(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
      Tissue: Synovium.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Lung.
    9. "Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration."
      Marmorstein L.Y., Munier F.L., Arsenijevic Y., Schorderet D.F., McLaughlin P.J., Chung D., Traboulsi E., Marmorstein A.D.
      Proc. Natl. Acad. Sci. U.S.A. 99:13067-13072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT DHRD TRP-345.
    10. "Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations."
      Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B.
      J. Biol. Chem. 279:30469-30473(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIMP3.
    11. "EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells."
      Camaj P., Seeliger H., Ischenko I., Krebs S., Blum H., De Toni E.N., Faktorova D., Jauch K.W., Bruns C.J.
      Biol. Chem. 390:1293-1302(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EGFR ACTIVATION.
    12. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
      Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
      Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECM1.
    13. "Fibulin-3 is uniquely upregulated in malignant gliomas and promotes tumor cell motility and invasion."
      Hu B., Thirtamara-Rajamani K.K., Sim H., Viapiano M.S.
      Mol. Cancer Res. 7:1756-1770(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    15. Cited for: VARIANT DHRD TRP-345, VARIANT PHE-220.
    16. "Dominant radial drusen and Arg345Trp EFEMP1 mutation."
      Matsumoto M., Traboulsi E.I.
      Am. J. Ophthalmol. 131:810-812(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DHRD TRP-345.
    17. "The R345W mutation in EFEMP1 is pathogenic and causes AMD-like deposits in mice."
      Fu L., Garland D., Yang Z., Shukla D., Rajendran A., Pearson E., Stone E.M., Zhang K., Pierce E.A.
      Hum. Mol. Genet. 16:2411-2422(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT DHRD TRP-345.

    Entry informationi

    Entry nameiFBLN3_HUMAN
    AccessioniPrimary (citable) accession number: Q12805
    Secondary accession number(s): A8K3I4
    , B4DW75, D6W5D2, Q541U7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 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

    Miscellaneous

    Up-regulated in malignant gliomas. May increase glioma cell adhesiveness and invasive properties.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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