Coronin-1B

<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

<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

• actin filament binding Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "F-actin binding is essential for coronin 1B function in vivo."
    Cai L., Makhov A.M., Bear J.E.
    J. Cell. Sci. 120:1779-1790(2007) [PubMed] [Europe PMC] [Abstract]
• Arp2/3 complex binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
    Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
    J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
  • "Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia."
    Cai L., Makhov A.M., Schafer D.A., Bear J.E.
    Cell 134:828-842(2008) [PubMed] [Europe PMC] [Abstract]
• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
    Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
    J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.

GO - Biological processⁱ

• actin cytoskeleton organization Source: CACAOInferred from direct assayⁱ
  • "Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia."
    Cai L., Makhov A.M., Schafer D.A., Bear J.E.
    Cell 134:828-842(2008) [PubMed] [Europe PMC] [Abstract]
• actin filament branching Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia."
    Cai L., Makhov A.M., Schafer D.A., Bear J.E.
    Cell 134:828-842(2008) [PubMed] [Europe PMC] [Abstract]
• actin filament bundle assembly Source: UniProtKBInferred from direct assayⁱ
  • "F-actin binding is essential for coronin 1B function in vivo."
    Cai L., Makhov A.M., Bear J.E.
    J. Cell. Sci. 120:1779-1790(2007) [PubMed] [Europe PMC] [Abstract]
• actin filament organization 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%2Dgo%2Devidence%2Dcodes#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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cell migration Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
    Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
    J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
• cellular response to platelet-derived growth factor stimulus Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Role of coronin 1B in PDGF-induced migration of vascular smooth muscle cells."
    Williams H.C., San Martin A., Adamo C.M., Seidel-Rogol B., Pounkova L., Datla S.R., Lassegue B., Bear J.E., Griendling K.
    Circ. Res. 111:56-65(2012) [PubMed] [Europe PMC] [Abstract]
• endothelial cell chemotaxis Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B regulates S1P-induced human lung endothelial cell chemotaxis: role of PLD2, protein kinase C and Rac1 signal transduction."
    Usatyuk P.V., Burns M., Mohan V., Pendyala S., He D., Ebenezer D.L., Harijith A., Fu P., Huang L.S., Bear J.E., Garcia J.G., Natarajan V.
    PLoS ONE 8:e63007-e63007(2013) [PubMed] [Europe PMC] [Abstract]
• negative regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge."
    Cai L., Marshall T.W., Uetrecht A.C., Schafer D.A., Bear J.E.
    Cell 128:915-929(2007) [PubMed] [Europe PMC] [Abstract]
  • "Coronin 1B antagonizes cortactin and remodels Arp2/3-containing actin branches in lamellipodia."
    Cai L., Makhov A.M., Schafer D.A., Bear J.E.
    Cell 134:828-842(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of smooth muscle cell chemotaxis Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Role of coronin 1B in PDGF-induced migration of vascular smooth muscle cells."
    Williams H.C., San Martin A., Adamo C.M., Seidel-Rogol B., Pounkova L., Datla S.R., Lassegue B., Bear J.E., Griendling K.
    Circ. Res. 111:56-65(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of lamellipodium morphogenesis Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge."
    Cai L., Marshall T.W., Uetrecht A.C., Schafer D.A., Bear J.E.
    Cell 128:915-929(2007) [PubMed] [Europe PMC] [Abstract]
• protein localization to cell leading edge Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge."
    Cai L., Marshall T.W., Uetrecht A.C., Schafer D.A., Bear J.E.
    Cell 128:915-929(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "Role of coronin 1B in PDGF-induced migration of vascular smooth muscle cells."
    Williams H.C., San Martin A., Adamo C.M., Seidel-Rogol B., Pounkova L., Datla S.R., Lassegue B., Bear J.E., Griendling K.
    Circ. Res. 111:56-65(2012) [PubMed] [Europe PMC] [Abstract]
• ruffle organization Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
    Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
    J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
• wound healing Source: UniProtKBInferred from direct assayⁱ
  • "Coronin 1B regulates S1P-induced human lung endothelial cell chemotaxis: role of PLD2, protein kinase C and Rac1 signal transduction."
    Usatyuk P.V., Burns M., Mohan V., Pendyala S., He D., Ebenezer D.L., Harijith A., Fu P., Huang L.S., Bear J.E., Garcia J.G., Natarajan V.
    PLoS ONE 8:e63007-e63007(2013) [PubMed] [Europe PMC] [Abstract]

<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

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

Mutagenesis

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic 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

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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• actin filament binding Source: UniProtKBInferred from direct assayⁱ
  • "F-actin binding is essential for coronin 1B function in vivo."
    Cai L., Makhov A.M., Bear J.E.
    J. Cell. Sci. 120:1779-1790(2007) [PubMed] [Europe PMC] [Abstract]
• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility."
    Cai L., Holoweckyj N., Schaller M.D., Bear J.E.
    J. Biol. Chem. 280:31913-31923(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INTERACTION WITH ACTR2; ARPC1B AND ARPC2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.

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

3D structure 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

Coiled coil

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

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>Sequence (1+)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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV 
        60         70         80         90        100
IVEASGGGAF LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS 
       110        120        130        140        150
GSEDCTVMVW QIPENGLTSP LTEPVVVLEG HTKRVGIIAW HPTARNVLLS 
       160        170        180        190        200
AGCDNVVLIW NVGTAEELYR LDSLHPDLIY NVSWNHNGSL FCSACKDKSV 
       210        220        230        240        250
RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS RMSERQLALW 
       260        270        280        290        300
DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE 
       310        320        330        340        350
PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM 
       360        370        380        390        400
TVPRKSDLFQ DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK 
       410        420        430        440        450
QRDLKISRRN VLSDSRPAMA PGSSHLGAPA STTTAADATP SGSLARAGEA 
       460        470        480 
GKLEEVMQEL RALRALVKEQ GDRICRLEEQ LGRMENGDA             

Natural variant

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

• 100% Identity
• 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

Polymorphism and mutation 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. SIMILARITY comments
   Index of protein domains and families
2. Human chromosome 11
   Human chromosome 11: entries, gene names and cross-references to MIM
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot