ADD1: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS (v470))
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Alpha-adducin''' is a [[protein]] that in humans is encoded by the ''ADD1'' [[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: ADD1 adducin 1 (alpha)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- 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 1 (alpha)
| HGNCid = 243
| Symbol = ADD1
| AltSymbols =; ADDA; MGC3339; MGC44427
| OMIM = 102680
| ECnumber =
| Homologene = 22758
| MGIid = 87918
| GeneAtlas_image1 = PBB_GE_ADD1_208030_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADD1_214726_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADD1_214736_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{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:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 118
    | Hs_Ensembl = ENSG00000087274
    | Hs_RefseqProtein = NP_001110
    | Hs_RefseqmRNA = NM_001119
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 2815382
    | Hs_GenLoc_end = 2901587
    | Hs_Uniprot = 
    | Mm_EntrezGene = 11518
    | Mm_Ensembl = ENSMUSG00000029106
    | Mm_RefseqmRNA = NM_001024458
    | Mm_RefseqProtein = NP_001019629
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 34890720
    | Mm_GenLoc_end = 34949162
    | Mm_Uniprot = Q8BJT2
  }}
}}
'''Adducin 1 (alpha)''', also known as '''ADD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADD1 adducin 1 (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Adducins are a family of cytoskeleton proteins encoded by three genes (alpha, beta, gamma). Adducin is a heterodimeric protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Alpha- and gamma-adducins are ubiquitously expressed. In contrast, beta-adducin is expressed at high levels in brain and hematopoietic tissues. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing results in multiple variants encoding distinct isoforms; however, not all variants have been fully described.<ref name="entrez">{{cite web | title = Entrez Gene: ADD1 adducin 1 (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| accessdate = }}</ref>
| summary_text = [[Adducin]]s are a family of [[cytoskeleton]] proteins encoded by three genes (alpha, beta, gamma). Adducin is a [[heterodimeric]] protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a [[protease]]-resistant [[N-terminal]] region and a protease-sensitive, [[hydrophilic]] [[C-terminal]] region. Alpha- and gamma-adducins are [[ubiquitous]]ly expressed. In contrast, beta-adducin is expressed at high levels in brain and [[hematopoietic]] tissues. Adducin binds with high affinity to Ca(2+)/[[calmodulin]] and is a [[substrate (biochemistry)|substrate]] for [[protein kinase]]s A and C. Alternative [[Protein splicing|splicing]] results in multiple variants encoding distinct [[isoforms]]; however, not all variants have been fully described. [[Polymorphism (biology)|Polymorphism]] in ADD1 is associated with [[hypertension]].<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ADD1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Mangeat PH |title=Interaction of biological membranes with the cytoskeletal framework of living cells. |journal=Biol. Cell |volume=64 |issue= 3 |pages= 261-81 |year= 1989 |pmid= 2976282 |doi=  }}
*{{cite journal  | author=Mangeat PH |title=Interaction of biological membranes with the cytoskeletal framework of living cells |journal=Biol. Cell |volume=64 |issue= 3 |pages= 261–81 |year= 1989 |pmid= 2976282 |doi=10.1016/0248-4900(88)90001-9 }}
*{{cite journal  | author=Matsuoka Y, Li X, Bennett V |title=Adducin: structure, function and regulation. |journal=Cell. Mol. Life Sci. |volume=57 |issue= 6 |pages= 884-95 |year= 2000 |pmid= 10950304 |doi=  }}
*{{cite journal  | vauthors=Matsuoka Y, Li X, Bennett V |title=Adducin: structure, function and regulation |journal=Cell. Mol. Life Sci. |volume=57 |issue= 6 |pages= 884–95 |year= 2000 |pmid= 10950304 |doi=10.1007/PL00000731 }}
*{{cite journal  | author=Goldberg YP, Lin BY, Andrew SE, ''et al.'' |title=Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease. |journal=Hum. Mol. Genet. |volume=1 |issue= 9 |pages= 669-75 |year= 1993 |pmid= 1284592 |doi=  }}
*{{cite journal  | vauthors=Goldberg YP, Lin BY, Andrew SE |title=Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease |journal=Hum. Mol. Genet. |volume=1 |issue= 9 |pages= 669–75 |year= 1993 |pmid= 1284592 |doi=10.1093/hmg/1.9.669 |display-authors=etal}}
*{{cite journal  | author=Taylor SA, Snell RG, Buckler A, ''et al.'' |title=Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification. |journal=Nat. Genet. |volume=2 |issue= 3 |pages= 223-7 |year= 1994 |pmid= 1345173 |doi= 10.1038/ng1192-223 }}
*{{cite journal  | vauthors=Taylor SA, Snell RG, Buckler A |title=Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification |journal=Nat. Genet. |volume=2 |issue= 3 |pages= 223–7 |year= 1994 |pmid= 1345173 |doi= 10.1038/ng1192-223 |display-authors=etal}}
*{{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  | vauthors=Gardner K, Bennett V |title=Modulation of spectrin-actin assembly by erythrocyte adducin |journal=Nature |volume=328 |issue= 6128 |pages= 359–62 |year= 1987 |pmid= 3600811 |doi= 10.1038/328359a0 }}
*{{cite journal  | author=Gardner K, Bennett V |title=Modulation of spectrin-actin assembly by erythrocyte adducin. |journal=Nature |volume=328 |issue= 6128 |pages= 359-62 |year= 1987 |pmid= 3600811 |doi= 10.1038/328359a0 }}
*{{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 }}
*{{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  | vauthors=Lin B, Nasir J, McDonald H |title=Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms |journal=Genomics |volume=25 |issue= 1 |pages= 93–9 |year= 1995 |pmid= 7774961 |doi=10.1016/0888-7543(95)80113-Z  |display-authors=etal}}
*{{cite journal  | author=Lin B, Nasir J, McDonald H, ''et al.'' |title=Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms. |journal=Genomics |volume=25 |issue= 1 |pages= 93-9 |year= 1995 |pmid= 7774961 |doi= }}
*{{cite journal  | vauthors=Nasir J, Lin B, Bucan M |title=The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3 |journal=Genomics |volume=22 |issue= 1 |pages= 198–201 |year= 1994 |pmid= 7959767 |doi= 10.1006/geno.1994.1361 |display-authors=etal}}
*{{cite journal  | author=Nasir J, Lin B, Bucan M, ''et al.'' |title=The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3. |journal=Genomics |volume=22 |issue= 1 |pages= 198-201 |year= 1994 |pmid= 7959767 |doi= 10.1006/geno.1994.1361 }}
*{{cite journal  | vauthors=Kuhlman PA, Hughes CA, Bennett V, Fowler VM |title=A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 7986–91 |year= 1996 |pmid= 8626479 |doi= 10.1074/jbc.271.14.7986}}
*{{cite journal  | author=Kuhlman PA, Hughes CA, Bennett V, Fowler VM |title=A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 7986-91 |year= 1996 |pmid= 8626479 |doi=  }}
*{{cite journal  | vauthors=Li X, Bennett V |title=Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15695–702 |year= 1996 |pmid= 8663089 |doi=10.1074/jbc.271.26.15695 }}
*{{cite journal  | author=Li X, Bennett V |title=Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15695-702 |year= 1996 |pmid= 8663089 |doi=  }}
*{{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 }}
*{{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  | vauthors=Hadano S, Ishida Y, Tomiyasu H |title=Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus |journal=DNA Res. |volume=3 |issue= 4 |pages= 239–55 |year= 1997 |pmid= 8946164 |doi=10.1093/dnares/3.4.239 |display-authors=etal}}
*{{cite journal  | author=Hadano S, Ishida Y, Tomiyasu H, ''et al.'' |title=Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus. |journal=DNA Res. |volume=3 |issue= 4 |pages= 239-55 |year= 1997 |pmid= 8946164 |doi=  }}
*{{cite journal  | vauthors=Cusi D, Barlassina C, Azzani T |title=Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension |journal=Lancet |volume=349 |issue= 9062 |pages= 1353–7 |year= 1997 |pmid= 9149697 |doi=10.1016/S0140-6736(97)01029-5 |display-authors=etal}}
*{{cite journal  | author=Cusi D, Barlassina C, Azzani T, ''et al.'' |title=Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension. |journal=Lancet |volume=349 |issue= 9062 |pages= 1353-7 |year= 1997 |pmid= 9149697 |doi= }}
*{{cite journal  | vauthors=Kamitani A, Wong ZY, Fraser R |title=Human alpha-adducin gene, blood pressure, and sodium metabolism |journal=Hypertension |volume=32 |issue= 1 |pages= 138–43 |year= 1998 |pmid= 9674650 |doi=10.1161/01.HYP.32.1.138  |display-authors=etal}}
*{{cite journal  | author=Kamitani A, Wong ZY, Fraser R, ''et al.'' |title=Human alpha-adducin gene, blood pressure, and sodium metabolism. |journal=Hypertension |volume=32 |issue= 1 |pages= 138-43 |year= 1998 |pmid= 9674650 |doi=  }}
*{{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  | 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  | vauthors=Fukata Y, Oshiro N, Kinoshita N |title=Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 347–61 |year= 1999 |pmid= 10209029 |doi=10.1083/jcb.145.2.347  | pmc=2133101 |display-authors=etal}}
*{{cite journal  | author=Fukata Y, Oshiro N, Kinoshita N, ''et al.'' |title=Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility. |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 347-61 |year= 1999 |pmid= 10209029 |doi= }}
*{{cite journal  | vauthors=Halushka MK, Fan JB, Bentley K |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239–47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 |display-authors=etal}}
*{{cite journal  | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal  | vauthors=Ferrandi M, Salardi S, Tripodi G |title=Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension |journal=Am. J. Physiol. |volume=277 |issue= 4 Pt 2 |pages= H1338–49 |year= 1999 |pmid= 10516168 |doi=  |display-authors=etal}}
*{{cite journal | author=Ferrandi M, Salardi S, Tripodi G, ''et al.'' |title=Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension. |journal=Am. J. Physiol. |volume=277 |issue= 4 Pt 2 |pages= H1338-49 |year= 1999 |pmid= 10516168 |doi=  }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{WikiDoc Sources}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
 
{{gene-4-stub}}

Latest revision as of 01:41, 27 October 2017

VALUE_ERROR (nil)
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

Alpha-adducin is a protein that in humans is encoded by the ADD1 gene.[1][2]

Adducins are a family of cytoskeleton proteins encoded by three genes (alpha, beta, gamma). Adducin is a heterodimeric protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Alpha- and gamma-adducins are ubiquitously expressed. In contrast, beta-adducin is expressed at high levels in brain and hematopoietic tissues. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing results in multiple variants encoding distinct isoforms; however, not all variants have been fully described. Polymorphism in ADD1 is associated with hypertension.[2]

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: ADD1 adducin 1 (alpha)".

External links

Further reading