alpha actinin assay simus

Channel: eganResearch   |   2014/02/14
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RESULTS [40 .. 90]
From Wikipedia, the free encyclopedia
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Actinin, alpha 2

PDB rendering based on 1h8b.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ACTN2 ; CMD1AA
External IDs OMIM102573 MGI109192 HomoloGene31016 GeneCards: ACTN2 Gene
RNA expression pattern
PBB GE ACTN2 203862 s at tn.png
PBB GE ACTN2 203861 s at tn.png
PBB GE ACTN2 203863 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 88 11472
Ensembl ENSG00000077522 ENSMUSG00000052374
UniProt P35609 Q9JI91
RefSeq (mRNA) NM_001103 NM_033268
RefSeq (protein) NP_001094 NP_150371
Location (UCSC) Chr 1:
236.85 – 236.93 Mb
Chr 13:
12.27 – 12.34 Mb
PubMed search [1] [2]

Actinin, alpha 2, also known as ACTN2, is a protein which in humans is encoded by the ACTN2 gene.[1]

Function[edit]

Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. Studies have also implicated alpha actinin in the binding of cardiac ion channels, Kv1.5 in particular.[2] This gene encodes a muscle-specific, alpha actinin isoform that is expressed in both skeletal and cardiac muscles. Transcript variants resulting from the use of multiple poly_A sites have been observed.[1]

Interactions[edit]

Actinin, alpha 2 has been shown to interact with KCNA5,[2][3] DLG1,[2] DISC1,[4] MYOZ1,[5] GRIN2B,[6] ADAM12,[7] ACTN3[8] and MYPN.[9]

References[edit]

  1. ^ a b "Entrez Gene: ACTN2 actinin, alpha 2". 
  2. ^ a b c Eldstrom, Jodene; Choi Woo Sung; Steele David F; Fedida David (Jul 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. (Netherlands) 547 (1-3): 205–11. doi:10.1016/S0014-5793(03)00668-9. ISSN 0014-5793. PMID 12860415. 
  3. ^ Maruoka, N D; Steele D F; Au B P; Dan P; Zhang X; Moore E D; Fedida D (May 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Lett. (NETHERLANDS) 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. ISSN 0014-5793. PMID 10812072. 
  4. ^ Morris, Jill A; Kandpal Geeta; Ma Lei; Austin Christopher P (Jul 2003). "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation". Hum. Mol. Genet. (England) 12 (13): 1591–608. doi:10.1093/hmg/ddg162. ISSN 0964-6906. PMID 12812986. 
  5. ^ Faulkner, G; Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojic' S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G (Dec 2000). "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle". J. Biol. Chem. (UNITED STATES) 275 (52): 41234–42. doi:10.1074/jbc.M007493200. ISSN 0021-9258. PMID 10984498. 
  6. ^ Wyszynski, M; Lin J; Rao A; Nigh E; Beggs A H; Craig A M; Sheng M (Jan 1997). "Competitive binding of alpha-actinin and calmodulin to the NMDA receptor". Nature (ENGLAND) 385 (6615): 439–42. doi:10.1038/385439a0. ISSN 0028-0836. PMID 9009191. 
  7. ^ Galliano, M F; Huet C; Frygelius J; Polgren A; Wewer U M; Engvall E (May 2000). "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion". J. Biol. Chem. (UNITED STATES) 275 (18): 13933–9. doi:10.1074/jbc.275.18.13933. ISSN 0021-9258. PMID 10788519. 
  8. ^ Chan, Y; Tong H Q; Beggs A H; Kunkel L M (Jul 1998). "Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo". Biochem. Biophys. Res. Commun. (UNITED STATES) 248 (1): 134–9. doi:10.1006/bbrc.1998.8920. ISSN 0006-291X. PMID 9675099. 
  9. ^ Bang, M L; Mudry R E, McElhinny A S, Trombitás K, Geach A J, Yamasaki R, Sorimachi H, Granzier H, Gregorio C C, Labeit S (Apr 2001). "Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies". J. Cell Biol. (United States) 153 (2): 413–27. doi:10.1083/jcb.153.2.413. ISSN 0021-9525. PMC 2169455. PMID 11309420. 

Further reading[edit]

External links[edit]



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