ADD2

Protein-coding gene in the species Homo sapiens
ADD2
Identifiers
AliasesADD2, ADDB, adducin 2
External IDsOMIM: 102681; MGI: 87919; HomoloGene: 1221; GeneCards: ADD2; OMA:ADD2 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for ADD2
Genomic location for ADD2
Band2p13.3Start70,607,618 bp[1]
End70,768,225 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for ADD2
Genomic location for ADD2
Band6 C3- D1|6 37.55 cMStart86,005,663 bp[2]
End86,101,391 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Brodmann area 10

  • middle temporal gyrus

  • Brodmann area 23

  • paraflocculus of cerebellum

  • frontal pole

  • Region I of hippocampus proper

  • postcentral gyrus

  • Brodmann area 46

  • entorhinal cortex

  • superior frontal gyrus
Top expressed in
  • olfactory tubercle

  • Region I of hippocampus proper

  • piriform cortex

  • dentate gyrus

  • facial motor nucleus

  • central gray substance of midbrain

  • dentate gyrus of hippocampal formation granule cell

  • subiculum

  • pontine nuclei

  • visual cortex
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
SpeciesHumanMouse
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 MbChr 6: 86.01 – 86.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000075340 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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

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.


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