Actin, aortic smooth muscle

<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

• ATP binding Source: UniProtKB-KW
• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J. Neurosci. 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• glomerular mesangial cell development Source: RGDInferred from sequence orthologyⁱ
  • "Development of glomerular endothelial cells, podocytes and mesangial cells in the human fetus and infant."
    Takano K., Kawasaki Y., Imaizumi T., Matsuura H., Nozawa R., Tannji M., Suyama K., Isome M., Suzuki H., Hosoya M.
    Tohoku J. Exp. Med. 212:81-90(2007) [PubMed] [Europe PMC] [Abstract]
• mesenchyme migration Source: AgBase
• muscle contraction Source: RGD <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
  • "Transcriptional regulation of a contractile gene by mechanical forces applied through integrins in osteoblasts."
    Wang J., Su M., Fan J., Seth A., McCulloch C.A.
    J. Biol. Chem. 277:22889-22895(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ERK1 and ERK2 cascade Source: RGD <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
  • "Smooth muscle alpha actin (Acta2) and myofibroblast function during hepatic wound healing."
    Rockey D.C., Weymouth N., Shi Z.
    PLoS ONE 8:e77166-e77166(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: AgBase
• positive regulation of hepatic stellate cell activation Source: RGDInferred from mutant phenotypeⁱ
  • "Smooth muscle alpha actin (Acta2) and myofibroblast function during hepatic wound healing."
    Rockey D.C., Weymouth N., Shi Z.
    PLoS ONE 8:e77166-e77166(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of hepatic stellate cell contraction Source: RGDInferred from mutant phenotypeⁱ
  • "Smooth muscle alpha actin (Acta2) and myofibroblast function during hepatic wound healing."
    Rockey D.C., Weymouth N., Shi Z.
    PLoS ONE 8:e77166-e77166(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of hepatic stellate cell migration Source: RGDInferred from mutant phenotypeⁱ
  • "Smooth muscle alpha actin (Acta2) and myofibroblast function during hepatic wound healing."
    Rockey D.C., Weymouth N., Shi Z.
    PLoS ONE 8:e77166-e77166(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of blood pressure Source: RGDInferred from sequence orthologyⁱ
  • "Impaired vascular contractility and blood pressure homeostasis in the smooth muscle alpha-actin null mouse."
    Schildmeyer L.A., Braun R., Taffet G., Debiasi M., Burns A.E., Bradley A., Schwartz R.J.
    FASEB J. 14:2213-2220(2000) [PubMed] [Europe PMC] [Abstract]
• regulation of wound healing Source: RGDInferred from mutant phenotypeⁱ
  • "Smooth muscle alpha actin (Acta2) and myofibroblast function during hepatic wound healing."
    Rockey D.C., Weymouth N., Shi Z.
    PLoS ONE 8:e77166-e77166(2013) [PubMed] [Europe PMC] [Abstract]
• response to virus Source: RGDInferred from sequence orthologyⁱ
  • "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
• vascular smooth muscle contraction Source: RGDInferred from sequence orthologyⁱ
  • "Impaired vascular contractility and blood pressure homeostasis in the smooth muscle alpha-actin null mouse."
    Schildmeyer L.A., Braun R., Taffet G., Debiasi M., Burns A.E., Bradley A., Schwartz R.J.
    FASEB J. 14:2213-2220(2000) [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 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 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

GO - Molecular functionⁱ

• protein kinase binding Source: RGDInferred from sequence orthologyⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J. Neurosci. 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction 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

<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

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.

<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 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG 
        60         70         80         90        100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP 
       110        120        130        140        150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 
       160        170        180        190        200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 
       210        220        230        240        250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 
       260        270        280        290        300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 
       310        320        330        340        350
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 
       360        370 
LSTFQQMWIS KQEYDEAGPS IVHRKCF                          

Sequence databases

Genome annotation databases

<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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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