EMILIN-1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• extracellular matrix constituent conferring elasticity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Self-assembly and supramolecular organization of EMILIN."
    Mongiat M., Mungiguerra G., Bot S., Mucignat M.T., Giacomello E., Doliana R., Colombatti A.
    J Biol Chem 275:25471-25480(2000) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• integrin binding involved in cell-matrix adhesion Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin."
    Verdone G., Doliana R., Corazza A., Colebrooke S.A., Spessotto P., Bot S., Bucciotti F., Capuano A., Silvestri A., Viglino P., Campbell I.D., Colombatti A., Esposito G.
    J Biol Chem 283:18947-18956(2008) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• aortic valve morphogenesis Source: BHF-UCL
• cell adhesion Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "EMILIN, a component of the elastic fiber and a new member of the C1q/tumor necrosis factor superfamily of proteins."
    Doliana R., Mongiat M., Bucciotti F., Giacomello E., Deutzmann R., Volpin D., Bressan G.M., Colombatti A.
    J. Biol. Chem. 274:16773-16781(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• cell adhesion mediated by integrin Source: Ensembl
• cell-matrix adhesion Source: CAFAInferred from mutant phenotypeⁱ
  • "The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin."
    Verdone G., Doliana R., Corazza A., Colebrooke S.A., Spessotto P., Bot S., Bucciotti F., Capuano A., Silvestri A., Viglino P., Campbell I.D., Colombatti A., Esposito G.
    J Biol Chem 283:18947-18956(2008) [PubMed] [Europe PMC] [Abstract]
• cell migration Source: CAFAInferred from mutant phenotypeⁱ
  • "The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin."
    Verdone G., Doliana R., Corazza A., Colebrooke S.A., Spessotto P., Bot S., Bucciotti F., Capuano A., Silvestri A., Viglino P., Campbell I.D., Colombatti A., Esposito G.
    J Biol Chem 283:18947-18956(2008) [PubMed] [Europe PMC] [Abstract]
• elastic fiber assembly Source: BHF-UCL
• negative regulation of angiogenesis Source: BHF-UCL
• negative regulation of cell activation Source: BHF-UCL
• negative regulation of collagen biosynthetic process Source: BHF-UCL
• negative regulation of collagen fibril organization Source: BHF-UCL
• negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
• negative regulation of gene expression Source: BHF-UCL
• negative regulation of macrophage migration Source: BHF-UCL
• negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
• negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
• negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
• positive regulation of angiogenesis Source: Ensembl
• positive regulation of blood coagulation Source: ComplexPortal
• positive regulation of cell-substrate adhesion Source: Ensembl
• positive regulation of defense response to bacterium Source: ComplexPortal <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "EMILINs interact with anthrax protective antigen and inhibit toxin action in vitro."
    Doliana R., Veljkovic V., Prljic J., Veljkovic N., De Lorenzo E., Mongiat M., Ligresti G., Marastoni S., Colombatti A.
    Matrix Biol 27:96-106(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of extracellular matrix assembly Source: BHF-UCL
• positive regulation of gene expression Source: BHF-UCL
• regulation of blood pressure Source: Ensembl
• regulation of cell population proliferation Source: Ensembl

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Self-assembly and supramolecular organization of EMILIN."
    Mongiat M., Mungiguerra G., Bot S., Mucignat M.T., Giacomello E., Doliana R., Colombatti A.
    J Biol Chem 275:25471-25480(2000) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• integrin binding involved in cell-matrix adhesion Source: CAFAInferred from mutant phenotypeⁱ
  • "The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin."
    Verdone G., Doliana R., Corazza A., Colebrooke S.A., Spessotto P., Bot S., Bucciotti F., Capuano A., Silvestri A., Viglino P., Campbell I.D., Colombatti A., Esposito G.
    J Biol Chem 283:18947-18956(2008) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Coiled coil

Compositional bias

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAPRTLWSCY LCCLLTAAAG AASYPPRGFS LYTGSSGALS PGGPQAQIAP 
        60         70         80         90        100
RPASRHRNWC AYVVTRTVSC VLEDGVETYV KYQPCAWGQP QCPQSIMYRR 
       110        120        130        140        150
FLRPRYRVAY KTVTDMEWRC CQGYGGDDCA ESPAPALGPA SSTPRPLARP 
       160        170        180        190        200
ARPNLSGSSA GSPLSGLGGE GPGESEKVQQ LEEQVQSLTK ELQGLRGVLQ 
       210        220        230        240        250
GLSGRLAEDV QRAVETAFNG RQQPADAAAR PGVHETLNEI QHQLQLLDTR 
       260        270        280        290        300
VSTHDQELGH LNNHHGGSSS SGGSRAPAPA SAPPGPSEEL LRQLEQRLQE 
       310        320        330        340        350
SCSVCLAGLD GFRRQQQEDR ERLRAMEKLL ASVEERQRHL AGLAVGRRPP 
       360        370        380        390        400
QECCSPELGR RLAELERRLD VVAGSVTVLS GRRGTELGGA AGQGGHPPGY 
       410        420        430        440        450
TSLASRLSRL EDRFNSTLGP SEEQEESWPG APGGLSHWLP AARGRLEQLG 
       460        470        480        490        500
GLLANVSGEL GGRLDLLEEQ VAGAMQACGQ LCSGAPGEQD SQVSEILSAL 
       510        520        530        540        550
ERRVLDSEGQ LRLVGSGLHT VEAAGEARQA TLEGLQEVVG RLQDRVDAQD 
       560        570        580        590        600
ETAAEFTLRL NLTAARLGQL EGLLQAHGDE GCGACGGVQE ELGRLRDGVE 
       610        620        630        640        650
RCSCPLLPPR GPGAGPGVGG PSRGPLDGFS VFGGSSGSAL QALQGELSEV 
       660        670        680        690        700
ILSFSSLNDS LNELQTTVEG QGADLADLGA TKDRIISEIN RLQQEATEHA 
       710        720        730        740        750
TESEERFRGL EEGQAQAGQC PSLEGRLGRL EGVCERLDTV AGGLQGLREG 
       760        770        780        790        800
LSRHVAGLWA GLRETNTTSQ MQAALLEKLV GGQAGLGRRL GALNSSLQLL 
       810        820        830        840        850
EDRLHQLSLK DLTGPAGEAG PPGPPGLQGP PGPAGPPGSP GKDGQEGPIG 
       860        870        880        890        900
PPGPQGEQGV EGAPAAPVPQ VAFSAALSLP RSEPGTVPFD RVLLNDGGYY 
       910        920        930        940        950
DPETGVFTAP LAGRYLLSAV LTGHRHEKVE AVLSRSNQGV ARVDSGGYEP 
       960        970        980        990       1000
EGLENKPVAE SQPSPGTLGV FSLILPLQAG DTVCVDLVMG QLAHSEEPLT 
      1010 
IFSGALLYGD PELEHA                                      

        10         20         30         40         50
MADLGATKDR IISEINRLQQ EATEHATESE ERFRGLEEGQ AQAGQCPSLE 
        60         70         80         90        100
GRLGRLEGVC ERLDTVAGGL QGLREGLSRH VAGLWAGLRE TNTTSQMQAA 
       110        120        130        140        150
LLEKLVGGQA GLGRRLGALN SSLQLLEDRL HQLSLKDLTG EGTKGPAGEA 
       160        170        180        190        200
GPPGPPGLQG PPGPAGPPGS PGKDGQEGPI GPPGPQGEQG VEGAPAAPVP 
       210        220        230        240        250
QVAFSAALSL PRSEPGTVPF DRVLLNDGGY YDPETGVFTA PLAGRYLLSA 
       260        270        280        290        300
VLTGHRHEKV EAVLSRSNQG VARVDSGGYE PEGLENKPVA ESQPSPGTLG 
       310        320        330        340 
VFSLILPLQA GDTVCVDLVM GQLAHSEEPL TIFSGALLYG DPELEHA    

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 2
   Human chromosome 2: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references