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{{Short description|Protein-coding gene in the species Homo sapiens}}
:''For the ADD2 graphics expansion card system, see [[SDVO]].''
{{for|the ADD2 graphics expansion card system|SDVO}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Beta-adducin''' is a [[protein]] that in humans is encoded by the ''ADD2'' [[gene]].<ref name="pmid1840603">{{cite journal | vauthors = Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V | title = Primary structure and domain organization of human alpha and beta adducin | journal = J Cell Biol | volume = 115 | issue = 3 | pages = 665–75 |date=Nov 1991| pmid = 1840603 | pmc = 2289184 | doi =10.1083/jcb.115.3.665 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADD2 adducin 2 (beta)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=119| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


== Function ==
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Adducin 2 (beta)
| HGNCid = 244
| Symbol = ADD2
| AltSymbols =; ADDB
| OMIM = 102681
| ECnumber =
| Homologene = 1221
| MGIid = 87919
| GeneAtlas_image1 = PBB_GE_ADD2_205268_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0030097 |text = hemopoiesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 119
| Hs_Ensembl = ENSG00000075340
| Hs_RefseqProtein = NP_001608
| Hs_RefseqmRNA = NM_001617
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 70742773
| Hs_GenLoc_end = 70848837
| Hs_Uniprot = P35612
| Mm_EntrezGene = 11519
| Mm_Ensembl = ENSMUSG00000030000
| Mm_RefseqmRNA = NM_013458
| Mm_RefseqProtein = NP_038486
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 86043718
| Mm_GenLoc_end = 86085189
| Mm_Uniprot = Q8C0Y2
}}
}}
'''Adducin 2 (beta)''', also known as '''ADD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADD2 adducin 2 (beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=119| accessdate = }}</ref>


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 [[erythrocyte]]s and at sites of cell-cell contact in epithelial tissues.
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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 comprised 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADD2 adducin 2 (beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=119| accessdate = }}</ref>
}}


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.
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Joshi R, Gilligan DM, Otto E, ''et al.'' |title=Primary structure and domain organization of human alpha and beta adducin. |journal=J. Cell Biol. |volume=115 |issue= 3 |pages= 665-75 |year= 1991 |pmid= 1840603 |doi= }}
*{{cite journal | author=Gilligan DM, Lieman J, Bennett V |title=Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization. |journal=Genomics |volume=28 |issue= 3 |pages= 610-2 |year= 1996 |pmid= 7490111 |doi= 10.1006/geno.1995.1205 }}
*{{cite journal | author=Hughes CA, Bennett V |title=Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. |journal=J. Biol. Chem. |volume=270 |issue= 32 |pages= 18990-6 |year= 1995 |pmid= 7642559 |doi= }}
*{{cite journal | author=Miyazaki M, Kaibuchi K, Shirataki H, ''et al.'' |title=Rabphilin-3A binds to a M(r) 115,000 polypeptide in a phosphatidylserine- and Ca(2+)-dependent manner. |journal=Brain Res. Mol. Brain Res. |volume=28 |issue= 1 |pages= 29-36 |year= 1995 |pmid= 7707875 |doi= }}
*{{cite journal | author=Miyazaki M, Shirataki H, Kohno H, ''et al.'' |title=Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 460-6 |year= 1995 |pmid= 7999065 |doi= 10.1006/bbrc.1994.2688 }}
*{{cite journal | author=White RA, Angeloni SV, Pasztor LM |title=Chromosomal localization of the beta-adducin gene to mouse chromosome 6 and human chromosome 2. |journal=Mamm. Genome |volume=6 |issue= 10 |pages= 741-3 |year= 1996 |pmid= 8563174 |doi= }}
*{{cite journal | author=Tisminetzky S, Devescovi G, Tripodi G, ''et al.'' |title=Genomic organisation and chromosomal localisation of the gene encoding human beta adducin. |journal=Gene |volume=167 |issue= 1-2 |pages= 313-6 |year= 1996 |pmid= 8566798 |doi= }}
*{{cite journal | author=Matsuoka Y, Hughes CA, Bennett V |title=Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25157-66 |year= 1996 |pmid= 8810272 |doi= }}
*{{cite journal | author=Gilligan DM, Lozovatsky L, Silberfein A |title=Organization of the human beta-adducin gene (ADD2). |journal=Genomics |volume=43 |issue= 2 |pages= 141-8 |year= 1997 |pmid= 9244430 |doi= 10.1006/geno.1997.4802 }}
*{{cite journal | author=Matsuoka Y, Li X, Bennett V |title=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. |journal=J. Cell Biol. |volume=142 |issue= 2 |pages= 485-97 |year= 1998 |pmid= 9679146 |doi= }}
*{{cite journal | author=Gilligan DM, Lozovatsky L, Gwynn B, ''et al.'' |title=Targeted disruption of the beta adducin gene (Add2) causes red blood cell spherocytosis in mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 19 |pages= 10717-22 |year= 1999 |pmid= 10485892 |doi= }}
*{{cite journal | author=Shima T, Okumura N, Takao T, ''et al.'' |title=Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42233-40 |year= 2001 |pmid= 11526103 |doi= 10.1074/jbc.M102699200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Citterio L, Tizzoni L, Catalano M, ''et al.'' |title=Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants. |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 2 |pages= 359-67 |year= 2003 |pmid= 12951058 |doi= }}
*{{cite journal | author=Tikhonoff V, Kuznetsova T, Stolarz K, ''et al.'' |title=beta-Adducin polymorphisms, blood pressure, and sodium excretion in three European populations. |journal=Am. J. Hypertens. |volume=16 |issue= 10 |pages= 840-6 |year= 2004 |pmid= 14553963 |doi= }}
*{{cite journal | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{cite journal | author=Ballif BA, Villén J, Beausoleil SA, ''et al.'' |title=Phosphoproteomic analysis of the developing mouse brain. |journal=Mol. Cell Proteomics |volume=3 |issue= 11 |pages= 1093-101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Efendiev R, Krmar RT, Ogimoto G, ''et al.'' |title=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. |journal=Circ. Res. |volume=95 |issue= 11 |pages= 1100-8 |year= 2005 |pmid= 15528469 |doi= 10.1161/01.RES.0000149570.20845.89 }}
*{{cite journal | author=Lanzani C, Citterio L, Jankaricova M, ''et al.'' |title=Role of the adducin family genes in human essential hypertension. |journal=J. Hypertens. |volume=23 |issue= 3 |pages= 543-9 |year= 2005 |pmid= 15716695 |doi= }}
}}
{{refend}}


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.<ref name="entrez" />
{{protein-stub}}

== Interactions ==

ADD2 has been shown to [[Protein-protein interaction|interact]] with [[FYN]].<ref name="pmid11526103">{{cite journal | vauthors = Shima T, Okumura N, Takao T, Satomi Y, Yagi T, Okada M, Nagai K | title = Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin | journal = J. Biol. Chem. | volume = 276 | issue = 45 | pages = 42233–40 | date = November 2001 |pmid = 11526103 | doi = 10.1074/jbc.M102699200 | doi-access = free }}</ref>

== References ==
{{Reflist}}

==External links==
* {{UCSC gene info|ADD2}}

== Further reading ==
{{Refbegin | 2}}
*{{cite journal | vauthors=Gilligan DM, Lieman J, Bennett V |title=Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization |journal=Genomics |volume=28 |issue= 3 |pages= 610–2 |year= 1996 |pmid= 7490111 |doi= 10.1006/geno.1995.1205 |doi-access= free }}
*{{cite journal | vauthors=Hughes CA, Bennett V |title=Adducin: a physical model with implications for function in assembly of spectrin-actin complexes |journal=J. Biol. Chem. |volume=270 |issue= 32 |pages= 18990–6 |year= 1995 |pmid= 7642559 |doi=10.1074/jbc.270.32.18990 |doi-access=free }}
*{{cite journal | vauthors=Miyazaki M, Kaibuchi K, Shirataki H |title=Rabphilin-3A binds to a M(r) 115,000 polypeptide in a phosphatidylserine- and Ca(2+)-dependent manner |journal=Brain Res. Mol. Brain Res. |volume=28 |issue= 1 |pages= 29–36 |year= 1995 |pmid= 7707875 |doi=10.1016/0169-328X(94)00180-M |display-authors=etal}}
*{{cite journal | vauthors=Miyazaki M, Shirataki H, Kohno H |title=Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 460–6 |year= 1995 |pmid= 7999065 |doi= 10.1006/bbrc.1994.2688 |display-authors=etal}}
*{{cite journal | vauthors=White RA, Angeloni SV, Pasztor LM |title=Chromosomal localization of the beta-adducin gene to mouse chromosome 6 and human chromosome 2 |journal=Mamm. Genome |volume=6 |issue= 10 |pages= 741–3 |year= 1996 |pmid= 8563174 |doi=10.1007/BF00354298 |s2cid=23628451 }}
*{{cite journal | vauthors=Tisminetzky S, Devescovi G, Tripodi G |title=Genomic organisation and chromosomal localisation of the gene encoding human beta adducin |journal=Gene |volume=167 |issue= 1–2 |pages= 313–6 |year= 1996 |pmid= 8566798 |doi=10.1016/0378-1119(95)00591-9 |display-authors=etal}}
*{{cite journal | vauthors=Matsuoka Y, Hughes CA, Bennett V |title=Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25157–66 |year= 1996 |pmid= 8810272 |doi=10.1074/jbc.271.41.25157 |doi-access=free }}
*{{cite journal | vauthors=Gilligan DM, Lozovatsky L, Silberfein A |title=Organization of the human beta-adducin gene (ADD2) |journal=Genomics |volume=43 |issue= 2 |pages= 141–8 |year= 1997 |pmid= 9244430 |doi= 10.1006/geno.1997.4802 |doi-access= free }}
*{{cite journal | vauthors=Matsuoka Y, Li X, Bennett V |title=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 |journal=J. Cell Biol. |volume=142 |issue= 2 |pages= 485–97 |year= 1998 |pmid= 9679146 |doi=10.1083/jcb.142.2.485 | pmc=2133059 }}
*{{cite journal | vauthors=Gilligan DM, Lozovatsky L, Gwynn B |title=Targeted disruption of the β adducin gene (Add2) causes red blood cell spherocytosis in mice |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 19 |pages= 10717–22 |year= 1999 |pmid= 10485892 |doi=10.1073/pnas.96.19.10717 | pmc=17949 |bibcode=1999PNAS...9610717G |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Shima T, Okumura N, Takao T |title=Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42233–40 |year= 2001 |pmid= 11526103 |doi= 10.1074/jbc.M102699200 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Citterio L, Tizzoni L, Catalano M |title=Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 2 |pages= 359–67 |year= 2003 |pmid= 12951058 |doi=10.1016/j.bbrc.2003.08.011 |display-authors=etal}}
*{{cite journal | vauthors=Tikhonoff V, Kuznetsova T, Stolarz K |title=beta-Adducin polymorphisms, blood pressure, and sodium excretion in three European populations |journal=Am. J. Hypertens. |volume=16 |issue= 10 |pages= 840–6 |year= 2004 |pmid= 14553963 |doi=10.1016/S0895-7061(03)00975-0 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Brandenberger R, Wei H, Zhang S |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |s2cid=27764390 |display-authors=etal}}
*{{cite journal | vauthors=Ballif BA, Villén J, Beausoleil SA |title=Phosphoproteomic analysis of the developing mouse brain |journal=Mol. Cell. Proteomics |volume=3 |issue= 11 |pages= 1093–101 |year= 2005 |pmid= 15345747 |doi= 10.1074/mcp.M400085-MCP200 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal | vauthors=Efendiev R, Krmar RT, Ogimoto G |title=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 |journal=Circ. Res. |volume=95 |issue= 11 |pages= 1100–8 |year= 2005 |pmid= 15528469 |doi= 10.1161/01.RES.0000149570.20845.89 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Lanzani C, Citterio L, Jankaricova M |title=Role of the adducin family genes in human essential hypertension |journal=J. Hypertens. |volume=23 |issue= 3 |pages= 543–9 |year= 2005 |pmid= 15716695 |doi=10.1097/01.hjh.0000160210.48479.78 |s2cid=37253591 |display-authors=etal}}
{{Refend}}


{{Gene-2-stub}}

Latest revision as of 17:52, 20 November 2023

For the ADD2 graphics expansion card system, see SDVO.
ADD2
Identifiers
AliasesADD2, ADDB, adducin 2
External IDsOMIM: 102681; MGI: 87919; HomoloGene: 1221; GeneCards: ADD2; OMA:ADD2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

119

11519

Ensembl

ENSG00000075340

ENSMUSG00000030000

UniProt

P35612

Q9QYB8

RefSeq (mRNA)
RefSeq (protein)

NP_001171983
NP_001171984
NP_001608
NP_059516
NP_059522

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

[edit]

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

[edit]

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

References

[edit]
  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.
[edit]

Further reading

[edit]


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