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{{Infobox_gene}}
{{PBB_Controls
'''A-kinase anchor protein 8''' is an [[enzyme]] that, in humans, is encoded by the ''AKAP8'' [[gene]].<ref name="pmid9473338">{{cite journal | vauthors = Eide T, Coghlan V, Orstavik S, Holsve C, Solberg R, Skalhegg BS, Lamb NJ, Langeberg L, Fernandez A, Scott JD, Jahnsen T, Tasken K | title = Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95 | journal = Exp Cell Res | volume = 238 | issue = 2 | pages = 305–16 |date=Mar 1998 | pmid = 9473338 | pmc =  | doi = 10.1006/excr.1997.3855 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKAP8 A kinase (PRKA) anchor protein 8| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10270| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = A kinase (PRKA) anchor protein 8
| HGNCid = 378
| Symbol = AKAP8
| AltSymbols =; AKAP95; DKFZp586B1222
| OMIM = 604692
| ECnumber = 
| Homologene = 4278
| MGIid = 1928488
| GeneAtlas_image1 = PBB_GE_AKAP8_203848_at_tn.png
| GeneAtlas_image2 = PBB_GE_AKAP8_203847_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005351 |text = sugar:hydrogen ion symporter activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051018 |text = protein kinase A binding}}
| Component = {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0001939 |text = female pronucleus}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0007076 |text = mitotic chromosome condensation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10270
    | Hs_Ensembl = ENSG00000105127
    | Hs_RefseqProtein = NP_005849
    | Hs_RefseqmRNA = NM_005858
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 15325341
    | Hs_GenLoc_end = 15351603
    | Hs_Uniprot = O43823
    | Mm_EntrezGene = 56399
    | Mm_Ensembl = ENSMUSG00000024045
    | Mm_RefseqmRNA = NM_019774
    | Mm_RefseqProtein = NP_062748
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 32036865
    | Mm_GenLoc_end = 32050418
    | Mm_Uniprot = Q059U9
  }}
}}
'''A kinase (PRKA) anchor protein 8''', also known as '''AKAP8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AKAP8 A kinase (PRKA) anchor protein 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10270| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of [[protein kinase A]] (PKA) and confining it to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is located in the nucleus during [[interphase]] and is redistributed to distinct locations during [[mitosis]]. This protein has a cell cycle-dependent interaction with the RII subunit of PKA.<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is located in the nucleus during interphase and is distinctly redistributed during mitosis. This protein has a cell cycle-dependent interaction with the RII subunit of PKA.<ref name="entrez">{{cite web | title = Entrez Gene: AKAP8 A kinase (PRKA) anchor protein 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10270| accessdate = }}</ref>
 
}}
AKAP8 has been demonstrated to [[Protein-protein interaction|interact]] with:
* [[Cyclin D3]]<ref name = pmid14641107>{{cite journal | date = Mar 2004 | vauthors = Arsenijevic T, Degraef C, Dumont JE, Roger PP, Pirson I | title = A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95 | journal = Biochem. J. | volume = 378 | issue = Pt 2 | pages = 673–9 | pmid = 14641107 | pmc = 1223988 | doi = 10.1042/BJ20031765}}</ref>
* [[DDX5]],<ref name = pmid11279182>{{cite journal | date = May 2001 | vauthors = Akileswaran L, Taraska JW, Sayer JA, Gettemy JM, Coghlan VM | title = A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase | journal = J. Biol. Chem. | volume = 276 | issue = 20 | pages = 17448–54 | pmid = 11279182 | doi = 10.1074/jbc.M101171200}}</ref>
* [[MCM2]],<ref name = pmid12740381>{{cite journal | date = Jul 2003 | vauthors = Eide T, Taskén KA, Carlson C, Williams G, Jahnsen T, Taskén K, Collas P | title = Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication | journal = J. Biol. Chem. | volume = 278 | issue = 29 | pages = 26750–6 | pmid = 12740381 | doi = 10.1074/jbc.M300765200}}</ref>
* [[MYCBP]],<ref name = pmid12414807>{{cite journal | date = Dec 2002 | vauthors = Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H | title = AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex | journal = J. Biol. Chem. | volume = 277 | issue = 52 | pages = 50885–92 | pmid = 12414807 | doi = 10.1074/jbc.M206387200}}</ref> and
* [[PRKAR2A]].<ref name = pmid9473338 /><ref name = pmid10601332>{{cite journal | date = Dec 1999 | vauthors = Collas P, Le Guellec K, Taskén K | title = The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis | journal = J. Cell Biol. | volume = 147 | issue = 6 | pages = 1167–80 | pmid = 10601332 | pmc = 2168084 | doi = 10.1083/jcb.147.6.1167}}</ref>


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Lester LB, Scott JD |title=Anchoring and scaffold proteins for kinases and phosphatases. |journal=Recent Prog. Horm. Res. |volume=52 |issue=  |pages= 409–29; discussion 429–30 |year= 1997 |pmid= 9238861 |doi=  }}
| citations =
*{{cite journal  | vauthors=Michel JJ, Scott JD |title=AKAP mediated signal transduction. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=42 |issue=  |pages= 235–57 |year= 2002 |pmid= 11807172 |doi= 10.1146/annurev.pharmtox.42.083101.135801 }}
*{{cite journal  | author=Lester LB, Scott JD |title=Anchoring and scaffold proteins for kinases and phosphatases. |journal=Recent Prog. Horm. Res. |volume=52 |issue=  |pages= 409-29; discussion 429-30 |year= 1997 |pmid= 9238861 |doi=  }}
*{{cite journal  | vauthors=Collas P, Le Guellec K, Taskén K |title=The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1167–80 |year= 2000 |pmid= 10601332 |doi=10.1083/jcb.147.6.1167  | pmc=2168084 }}
*{{cite journal  | author=Michel JJ, Scott JD |title=AKAP mediated signal transduction. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=42 |issue=  |pages= 235-57 |year= 2002 |pmid= 11807172 |doi= 10.1146/annurev.pharmtox.42.083101.135801 }}
*{{cite journal  | vauthors=Steen RL, Cubizolles F, Le Guellec K, Collas P |title=A kinase-anchoring protein (AKAP)95 recruits human chromosome-associated protein (hCAP)-D2/Eg7 for chromosome condensation in mitotic extract. |journal=J. Cell Biol. |volume=149 |issue= 3 |pages= 531–6 |year= 2000 |pmid= 10791967 |doi=10.1083/jcb.149.3.531  | pmc=2174845 }}
*{{cite journal  | author=Eide T, Coghlan V, Orstavik S, ''et al.'' |title=Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95. |journal=Exp. Cell Res. |volume=238 |issue= 2 |pages= 305-16 |year= 1998 |pmid= 9473338 |doi= 10.1006/excr.1997.3855 }}
*{{cite journal  | vauthors=Akileswaran L, Taraska JW, Sayer JA |title=A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17448–54 |year= 2001 |pmid= 11279182 |doi= 10.1074/jbc.M101171200 |display-authors=etal}}
*{{cite journal  | author=Collas P, Le Guellec K, Taskén K |title=The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1167-80 |year= 2000 |pmid= 10601332 |doi=  }}
*{{cite journal  | vauthors=Eide T, Carlson C, Taskén KA |title=Distinct but overlapping domains of AKAP95 are implicated in chromosome condensation and condensin targeting. |journal=EMBO Rep. |volume=3 |issue= 5 |pages= 426–32 |year= 2002 |pmid= 11964380 |doi= 10.1093/embo-reports/kvf089 | pmc=1084102 |display-authors=etal}}
*{{cite journal  | author=Steen RL, Cubizolles F, Le Guellec K, Collas P |title=A kinase-anchoring protein (AKAP)95 recruits human chromosome-associated protein (hCAP)-D2/Eg7 for chromosome condensation in mitotic extract. |journal=J. Cell Biol. |volume=149 |issue= 3 |pages= 531-6 |year= 2000 |pmid= 10791967 |doi=  }}
*{{cite journal  | vauthors=Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H |title=AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50885–92 |year= 2003 |pmid= 12414807 |doi= 10.1074/jbc.M206387200 }}
*{{cite journal  | author=Akileswaran L, Taraska JW, Sayer JA, ''et al.'' |title=A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17448-54 |year= 2001 |pmid= 11279182 |doi= 10.1074/jbc.M101171200 }}
*{{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=Eide T, Carlson C, Taskén KA, ''et al.'' |title=Distinct but overlapping domains of AKAP95 are implicated in chromosome condensation and condensin targeting. |journal=EMBO Rep. |volume=3 |issue= 5 |pages= 426-32 |year= 2002 |pmid= 11964380 |doi= 10.1093/embo-reports/kvf089 }}
*{{cite journal  | vauthors=Eide T, Taskén KA, Carlson C |title=Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26750–6 |year= 2003 |pmid= 12740381 |doi= 10.1074/jbc.M300765200 |display-authors=etal}}
*{{cite journal  | author=Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H |title=AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50885-92 |year= 2003 |pmid= 12414807 |doi= 10.1074/jbc.M206387200 }}
*{{cite journal  | vauthors=Arsenijevic T, Degraef C, Dumont JE |title=A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95. |journal=Biochem. J. |volume=378 |issue= Pt 2 |pages= 673–9 |year= 2004 |pmid= 14641107 |doi= 10.1042/BJ20031765 | pmc=1223988 |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=Bouwmeester T, Bauch A, Ruffner H |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 |display-authors=etal}}
*{{cite journal  | author=Eide T, Taskén KA, Carlson C, ''et al.'' |title=Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26750-6 |year= 2003 |pmid= 12740381 |doi= 10.1074/jbc.M300765200 }}
*{{cite journal  | vauthors=Grimwood J, Gordon LA, Olsen A |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 |display-authors=etal}}
*{{cite journal  | author=Arsenijevic T, Degraef C, Dumont JE, ''et al.'' |title=A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95. |journal=Biochem. J. |volume=378 |issue= Pt 2 |pages= 673-9 |year= 2004 |pmid= 14641107 |doi= 10.1042/BJ20031765 }}
*{{cite journal  | vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 |display-authors=etal}}
*{{cite journal  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  | vauthors=Kamada S, Kikkawa U, Tsujimoto Y, Hunter T |title=A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association. |journal=Mol. Cell. Biol. |volume=25 |issue= 21 |pages= 9469–77 |year= 2005 |pmid= 16227597 |doi= 10.1128/MCB.25.21.9469-9477.2005 | pmc=1265837 }}
*{{cite journal  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal  | vauthors=Beausoleil SA, Villén J, Gerber SA |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 |display-authors=etal}}
*{{cite journal  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{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=Kamada S, Kikkawa U, Tsujimoto Y, Hunter T |title=A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association. |journal=Mol. Cell. Biol. |volume=25 |issue= 21 |pages= 9469-77 |year= 2005 |pmid= 16227597 |doi= 10.1128/MCB.25.21.9469-9477.2005 }}
{{Refend}}
*{{cite journal  | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
 
*{{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 }}
==External links==
}}
* {{UCSC genome browser|AKAP8}}
{{refend}}
* {{UCSC gene details|AKAP8}}
 
 
{{Gene-19-stub}}


{{protein-stub}}
[[Category:A-kinase-anchoring proteins]]
{{WikiDoc Sources}}

Latest revision as of 17:55, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

A-kinase anchor protein 8 is an enzyme that, in humans, is encoded by the AKAP8 gene.[1][2]

Function

The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining it to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is located in the nucleus during interphase and is redistributed to distinct locations during mitosis. This protein has a cell cycle-dependent interaction with the RII subunit of PKA.[2]

Interactions

AKAP8 has been demonstrated to interact with:

References

  1. ↑ 1.0 1.1 Eide T, Coghlan V, Orstavik S, Holsve C, Solberg R, Skalhegg BS, Lamb NJ, Langeberg L, Fernandez A, Scott JD, Jahnsen T, Tasken K (Mar 1998). "Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95". Exp Cell Res. 238 (2): 305–16. doi:10.1006/excr.1997.3855. PMID 9473338.
  2. ↑ 2.0 2.1 "Entrez Gene: AKAP8 A kinase (PRKA) anchor protein 8".
  3. ↑ Arsenijevic T, Degraef C, Dumont JE, Roger PP, Pirson I (Mar 2004). "A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95". Biochem. J. 378 (Pt 2): 673–9. doi:10.1042/BJ20031765. PMC 1223988. PMID 14641107.
  4. ↑ Akileswaran L, Taraska JW, Sayer JA, Gettemy JM, Coghlan VM (May 2001). "A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase". J. Biol. Chem. 276 (20): 17448–54. doi:10.1074/jbc.M101171200. PMID 11279182.
  5. ↑ Eide T, Taskén KA, Carlson C, Williams G, Jahnsen T, Taskén K, Collas P (Jul 2003). "Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication". J. Biol. Chem. 278 (29): 26750–6. doi:10.1074/jbc.M300765200. PMID 12740381.
  6. ↑ Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H (Dec 2002). "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex". J. Biol. Chem. 277 (52): 50885–92. doi:10.1074/jbc.M206387200. PMID 12414807.
  7. ↑ Collas P, Le Guellec K, Taskén K (Dec 1999). "The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis". J. Cell Biol. 147 (6): 1167–80. doi:10.1083/jcb.147.6.1167. PMC 2168084. PMID 10601332.

Further reading

External links


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