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{{Infobox_gene}}
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'''Gamma-adducin''' is a [[protein]] that in humans is encoded by the ''ADD3'' [[gene]].<ref name="pmid8893809">{{cite journal | vauthors = Katagiri T, Ozaki K, Fujiwara T, Shimizu F, Kawai A, Okuno S, Suzuki M, Nakamura Y, Takahashi E, Hirai Y | title = Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin | journal = Cytogenet Cell Genet | volume = 74 | issue = 1–2 | pages = 90–5 |date=Dec 1996| pmid = 8893809 | pmc =  | doi =10.1159/000134389 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADD3 adducin 3 (gamma)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=120| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Adducin 3 (gamma)
| HGNCid = 245
| Symbol = ADD3
| AltSymbols =; ADDL
| OMIM = 601568
| ECnumber =
| Homologene = 40893
| MGIid = 1351615
| GeneAtlas_image1 = PBB_GE_ADD3_201034_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADD3_201753_s_at_tn.png
  | GeneAtlas_image3 = PBB_GE_ADD3_201752_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 120
    | Hs_Ensembl = ENSG00000148700
    | Hs_RefseqProtein = NP_001112
    | Hs_RefseqmRNA = NM_001121
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 111755716
    | Hs_GenLoc_end = 111885313
    | Hs_Uniprot = Q9UEY8
    | Mm_EntrezGene = 27360
    | Mm_Ensembl = ENSMUSG00000025026
    | Mm_RefseqmRNA = NM_013758
    | Mm_RefseqProtein = NP_038786
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 53193853
    | Mm_GenLoc_end = 53300398
    | Mm_Uniprot = Q05C56
  }}
}}
'''Adducin 3 (gamma)''', also known as '''ADD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADD3 adducin 3 (gamma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=120| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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. Alternatively spliced adducin gamma transcripts encoding different isoforms have been described. The functions of the different isoforms are not known.<ref name="entrez">{{cite web | title = Entrez Gene: ADD3 adducin 3 (gamma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=120| accessdate = }}</ref>
| summary_text = [[Adducin]]s 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 [[epithelium|epithelial]] tissues. While adducins alpha and gamma are [[ubiquitous]]ly expressed, the expression of adducin beta is restricted to brain and [[hematopoietic]] tissues. Adducin, originally purified from human [[erythrocyte]]s, was found to be a [[heterodimer]] of adducins alpha and beta. [[Polymorphism (biology)|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 site]]s for [[protein kinase C]], the binding site for [[calmodulin]], and is required for association with [[spectrin]] and [[actin]]. Alternatively [[Protein splicing|spliced]] adducin gamma transcripts encoding different [[isoforms]] have been described. The functions of the different isoforms are not known.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ADD3}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kaiser HW, O'Keefe E, Bennett V |title=Adducin: Ca++-dependent association with sites of cell-cell contact. |journal=J. Cell Biol. |volume=109 |issue= 2 |pages= 557-69 |year= 1989 |pmid= 2503523 |doi=  }}
*{{cite journal  | vauthors=Kaiser HW, O'Keefe E, Bennett V |title=Adducin: Ca++-dependent association with sites of cell-cell contact |journal=J. Cell Biol. |volume=109 |issue= 2 |pages= 557–69 |year= 1989 |pmid= 2503523 |doi=10.1083/jcb.109.2.557  | pmc=2115715 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Katagiri T, Ozaki K, Fujiwara T, ''et al.'' |title=Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin. |journal=Cytogenet. Cell Genet. |volume=74 |issue= 1-2 |pages= 90-5 |year= 1996 |pmid= 8893809 |doi= }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{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  |display-authors=etal}}
*{{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  | vauthors=Citterio L, Azzani T, Duga S, Bianchi G |title=Genomic organization of the human gamma adducin gene |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 1 |pages= 110–4 |year= 2000 |pmid= 10581174 |doi= 10.1006/bbrc.1999.1769 }}
*{{cite journal  | author=Citterio L, Azzani T, Duga S, Bianchi G |title=Genomic organization of the human gamma adducin gene. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 1 |pages= 110-4 |year= 2000 |pmid= 10581174 |doi= 10.1006/bbrc.1999.1769 }}
*{{cite journal  | vauthors=Gilligan DM, Sarid R, Weese J |title=Adducin in platelets: activation-induced phosphorylation by PKC and proteolysis by calpain |journal=Blood |volume=99 |issue= 7 |pages= 2418–26 |year= 2002 |pmid= 11895774 |doi=10.1182/blood.V99.7.2418 }}
*{{cite journal  | author=Gilligan DM, Sarid R, Weese J |title=Adducin in platelets: activation-induced phosphorylation by PKC and proteolysis by calpain. |journal=Blood |volume=99 |issue= 7 |pages= 2418-26 |year= 2002 |pmid= 11895774 |doi=  }}
*{{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 |display-authors=etal}}
*{{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  | 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  | 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  | vauthors=Gocke CB, Yu H, Kang J |title=Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates |journal=J. Biol. Chem. |volume=280 |issue= 6 |pages= 5004–12 |year= 2005 |pmid= 15561718 |doi= 10.1074/jbc.M411718200 }}
*{{cite journal  | author=Gocke CB, Yu H, Kang J |title=Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. |journal=J. Biol. Chem. |volume=280 |issue= 6 |pages= 5004-12 |year= 2005 |pmid= 15561718 |doi= 10.1074/jbc.M411718200 }}
*{{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 |display-authors=etal}}
*{{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=  }}
*{{cite journal  | vauthors=Yenerel MN, Sundell IB, Weese J |title=Expression of adducin genes during erythropoiesis: a novel erythroid promoter for ADD2 |journal=Exp. Hematol. |volume=33 |issue= 7 |pages= 758–66 |year= 2005 |pmid= 15963851 |doi= 10.1016/j.exphem.2005.03.015 |display-authors=etal}}
*{{cite journal  | author=Yenerel MN, Sundell IB, Weese J, ''et al.'' |title=Expression of adducin genes during erythropoiesis: a novel erythroid promoter for ADD2. |journal=Exp. Hematol. |volume=33 |issue= 7 |pages= 758-66 |year= 2005 |pmid= 15963851 |doi= 10.1016/j.exphem.2005.03.015 }}
*{{cite journal  | vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal}}
*{{cite journal  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 17:51, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Gamma-adducin is a protein that in humans is encoded by the ADD3 gene.[1][2]

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. Alternatively spliced adducin gamma transcripts encoding different isoforms have been described. The functions of the different isoforms are not known.[2]

References

  1. Katagiri T, Ozaki K, Fujiwara T, Shimizu F, Kawai A, Okuno S, Suzuki M, Nakamura Y, Takahashi E, Hirai Y (Dec 1996). "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin". Cytogenet Cell Genet. 74 (1–2): 90–5. doi:10.1159/000134389. PMID 8893809.
  2. 2.0 2.1 "Entrez Gene: ADD3 adducin 3 (gamma)".

External links

Further reading