ADD2

For the ADD2 graphics expansion card system, see SDVO.

ADD2
Identifiers
Aliases	ADD2 , ADDB, adducin 2
External IDs	OMIM: 102681 MGI: 87919 HomoloGene: 1221 GeneCards: ADD2
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2p13.3 Start 70,607,618 bp [1] End 70,768,225 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6 C3- D1|6 37.55 cM Start 86,005,663 bp [2] End 86,101,391 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 10 middle temporal gyrus Brodmann area 23 frontal pole Region I of hippocampus proper postcentral gyrus Brodmann area 46 entorhinal cortex superior frontal gyrus orbitofrontal cortex Top expressed in olfactory tubercle Region I of hippocampus proper piriform cortex dentate gyrus facial motor nucleus subiculum pontine nuclei visual cortex primary motor cortex nucleus accumbens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function spectrin binding protein homodimerization activity structural molecule activity calmodulin binding actin filament binding protein heterodimerization activity actin binding protein kinase binding Cellular component F-actin capping protein complex cytoplasm cytosol membrane plasma membrane cytoskeleton postsynaptic density cytoplasmic vesicle plasma membrane raft Biological process barbed-end actin filament capping actin filament bundle assembly transmembrane transport positive regulation of protein binding actin cytoskeleton organization leukocyte migration leukocyte tethering or rolling protein-containing complex assembly hemopoiesis synapse assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 119 11519 Ensembl ENSG00000075340 ENSMUSG00000030000 UniProt P35612 Q9QYB8 RefSeq (mRNA) NM_001185054 NM_001185055 NM_001617 NM_017482 NM_017483 NM_017484 NM_017485 NM_017486 NM_017487 NM_017488 NM_001271857 NM_001271858 NM_001271859 NM_001271860 NM_001271861 NM_013458 RefSeq (protein) NP_001171983 NP_001171984 NP_001608 NP_059516 NP_059522 NP_001258786 NP_001258787 NP_001258788 NP_001258789 NP_001258790 NP_038486 Location (UCSC) Chr 2: 70.61 – 70.77 Mb Chr 6: 86.01 – 86.1 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Beta-adducin is a protein that in humans is encoded by the ADD2 gene. ^{[5] [6]}

Function

Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta, and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues.

While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is composed of two distinct domains.

The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Various adducin beta mRNAs, alternatively spliced at 3' end and/or internally spliced and encoding different isoforms, have been described. The functions of all the different isoforms are not known. ^[6]

Interactions

ADD2 has been shown to interact with FYN. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000075340 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030000 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V (Nov 1991). "Primary structure and domain organization of human alpha and beta adducin". J Cell Biol. 115 (3): 665–75. doi:10.1083/jcb.115.3.665. PMC   2289184 . PMID   1840603.
6. "Entrez Gene: ADD2 adducin 2 (beta)".
7. Shima T, Okumura N, Takao T, Satomi Y, Yagi T, Okada M, Nagai K (November 2001). "Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin". J. Biol. Chem. 276 (45): 42233–40. doi: 10.1074/jbc.M102699200 . PMID   11526103.

External links

• Human ADD2 genome location and ADD2 gene details page in the UCSC Genome Browser .

Further reading

• Gilligan DM, Lieman J, Bennett V (1996). "Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization". Genomics. 28 (3): 610–2. doi: 10.1006/geno.1995.1205 . PMID   7490111.
• Hughes CA, Bennett V (1995). "Adducin: a physical model with implications for function in assembly of spectrin-actin complexes". J. Biol. Chem. 270 (32): 18990–6. doi: 10.1074/jbc.270.32.18990 . PMID   7642559.
• Miyazaki M, Kaibuchi K, Shirataki H, et al. (1995). "Rabphilin-3A binds to a M(r) 115,000 polypeptide in a phosphatidylserine- and Ca(2+)-dependent manner". Brain Res. Mol. Brain Res. 28 (1): 29–36. doi:10.1016/0169-328X(94)00180-M. PMID   7707875.
• Miyazaki M, Shirataki H, Kohno H, et al. (1995). "Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine". Biochem. Biophys. Res. Commun. 205 (1): 460–6. doi:10.1006/bbrc.1994.2688. PMID   7999065.
• White RA, Angeloni SV, Pasztor LM (1996). "Chromosomal localization of the beta-adducin gene to mouse chromosome 6 and human chromosome 2". Mamm. Genome. 6 (10): 741–3. doi:10.1007/BF00354298. PMID   8563174. S2CID   23628451.
• Tisminetzky S, Devescovi G, Tripodi G, et al. (1996). "Genomic organisation and chromosomal localisation of the gene encoding human beta adducin". Gene. 167 (1–2): 313–6. doi:10.1016/0378-1119(95)00591-9. PMID   8566798.
• Matsuoka Y, Hughes CA, Bennett V (1996). "Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C". J. Biol. Chem. 271 (41): 25157–66. doi: 10.1074/jbc.271.41.25157 . PMID   8810272.
• Gilligan DM, Lozovatsky L, Silberfein A (1997). "Organization of the human beta-adducin gene (ADD2)". Genomics. 43 (2): 141–8. doi: 10.1006/geno.1997.4802 . PMID   9244430.
• Matsuoka Y, Li X, Bennett V (1998). "Adducin Is an In Vivo Substrate for Protein Kinase C: Phosphorylation in the MARCKS-related Domain Inhibits Activity in Promoting Spectrin–Actin Complexes and Occurs in Many Cells, Including Dendritic Spines of Neurons". J. Cell Biol. 142 (2): 485–97. doi:10.1083/jcb.142.2.485. PMC   2133059 . PMID   9679146.
• Gilligan DM, Lozovatsky L, Gwynn B, et al. (1999). "Targeted disruption of the β adducin gene (Add2) causes red blood cell spherocytosis in mice". Proc. Natl. Acad. Sci. U.S.A. 96 (19): 10717–22. Bibcode:1999PNAS...9610717G. doi: 10.1073/pnas.96.19.10717 . PMC   17949 . PMID   10485892.
• Shima T, Okumura N, Takao T, et al. (2001). "Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin". J. Biol. Chem. 276 (45): 42233–40. doi: 10.1074/jbc.M102699200 . PMID   11526103.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Citterio L, Tizzoni L, Catalano M, et al. (2003). "Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants". Biochem. Biophys. Res. Commun. 309 (2): 359–67. doi:10.1016/j.bbrc.2003.08.011. PMID   12951058.
• Tikhonoff V, Kuznetsova T, Stolarz K, et al. (2004). "beta-Adducin polymorphisms, blood pressure, and sodium excretion in three European populations". Am. J. Hypertens. 16 (10): 840–6. doi: 10.1016/S0895-7061(03)00975-0 . PMID   14553963.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID   15146197. S2CID   27764390.
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi: 10.1074/mcp.M400085-MCP200 . PMID   15345747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Efendiev R, Krmar RT, Ogimoto G, et al. (2005). "Hypertension-linked mutation in the adducin alpha-subunit leads to higher AP2-mu2 phosphorylation and impaired Na+,K+-ATPase trafficking in response to GPCR signals and intracellular sodium". Circ. Res. 95 (11): 1100–8. doi: 10.1161/01.RES.0000149570.20845.89 . PMID   15528469.
• Lanzani C, Citterio L, Jankaricova M, et al. (2005). "Role of the adducin family genes in human essential hypertension". J. Hypertens. 23 (3): 543–9. doi:10.1097/01.hjh.0000160210.48479.78. PMID   15716695. S2CID   37253591.