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{{Infobox_gene}}
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'''AKT-interacting protein''' is a [[protein]] that in humans is encoded by the ''AKTIP'' [[gene]].<ref name="pmid7818539">{{cite journal |vauthors=Fluhmann B, Muff R, Hunziker W, Fischer JA, Born W | title = A human orphan calcitonin receptor-like structure | journal = Biochem Biophys Res Commun | volume = 206 | issue = 1 | pages = 341–7 |date=Feb 1995 | pmid = 7818539 | pmc =  | doi = 10.1006/bbrc.1995.1047 }}</ref><ref name="pmid8626685">{{cite journal |vauthors=Aiyar N, Rand K, Elshourbagy NA, Zeng Z, Adamou JE, Bergsma DJ, Li Y | title = A cDNA encoding the calcitonin gene-related peptide type 1 receptor | journal = J Biol Chem | volume = 271 | issue = 19 | pages = 11325–9 |date=Jun 1996 | pmid = 8626685 | pmc =  | doi =10.1074/jbc.271.19.11325 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKTIP AKT interacting protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64400| accessdate = }}</ref>
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<!-- 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 = AKT interacting protein
| HGNCid = 16710
| Symbol = AKTIP
| AltSymbols =; FT1; FTS
| OMIM = 608483
| ECnumber =
  | Homologene = 7721
| MGIid = 3693832
| GeneAtlas_image1 = PBB_GE_AKTIP_218373_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64400
    | Hs_Ensembl = ENSG00000166971
    | Hs_RefseqProtein = NP_001012398
    | Hs_RefseqmRNA = NM_001012398
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 52082693
    | Hs_GenLoc_end = 52094671
    | Hs_Uniprot = Q9H8T0
    | Mm_EntrezGene = 14339
    | Mm_Ensembl = ENSMUSG00000031667
    | Mm_RefseqmRNA = NM_010241
    | Mm_RefseqProtein = NP_034371
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 94013604
    | Mm_GenLoc_end = 94024570
    | Mm_Uniprot = Q05BP5
  }}
}}
'''AKT interacting protein''', also known as '''AKTIP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AKTIP AKT interacting protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64400| accessdate = }}</ref>


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<!-- 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 = The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKB's regulatory sites. Alternative splicing results in two transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: AKTIP AKT interacting protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64400| accessdate = }}</ref>
| summary_text = The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKB's regulatory sites. Alternative splicing results in two transcript variants encoding the same protein.<ref name="entrez"/>
}}
}}
==Interactions==
AKTIP has been shown to [[Protein-protein interaction|interact]] with [[AKT1]].<ref name=pmid14749367>{{cite journal |last=Remy |first=Ingrid |author2=Michnick Stephen W |date=Feb 2004 |title=Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt |journal=Mol. Cell. Biol. |volume=24 |issue=4 |pages=1493–504 |publisher= |location = United States| issn = 0270-7306| pmid = 14749367 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1128/MCB.24.4.1493-1504.2004 |pmc=344167 }}</ref>
== Molecular genetics ==
The association between the AKTIP gene variants in a sample of 273 [[Bipolar Disorder|bipolar]] patients using 3 [[single-nucleotide polymorphism]]s has been investigated. No association between [[suicide|suicidal behavior]] and AKTIP variants nor any interaction between AKTIP and [[AKT1]] polymorphisms was observed.<ref name="pmid20132317">{{cite journal |vauthors=Magno LA, Miranda DM, Neves FS, Pimenta GJ, Mello MP, De Marco LA, Correa H, Romano-Silva MA | title = Association between AKT1 but not AKTIP genetic variants and increased risk for suicidal behavior in bipolar patients | journal = Genes Brain Behav | volume = 9| issue = 4| pages = 411–8|date=January 2010 | pmid = 20132317 | doi = 10.1111/j.1601-183X.2010.00571.x | url = | issn = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|AKTIP}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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=Aiyar N, Rand K, Elshourbagy NA, ''et al.'' |title=A cDNA encoding the calcitonin gene-related peptide type 1 receptor. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11325-9 |year= 1996 |pmid= 8626685 |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=Lesche R, Peetz A, van der Hoeven F, Rüther U |title=Ft1, a novel gene related to ubiquitin-conjugating enzymes, is deleted in the Fused toes mouse mutation |journal=Mamm. Genome |volume=8 |issue= 12 |pages= 879–83 |year= 1998 |pmid= 9383278 |doi=10.1007/s003359900604 }}
*{{cite journal  | author=Lesche R, Peetz A, van der Hoeven F, Rüther U |title=Ft1, a novel gene related to ubiquitin-conjugating enzymes, is deleted in the Fused toes mouse mutation. |journal=Mamm. Genome |volume=8 |issue= 12 |pages= 879-83 |year= 1998 |pmid= 9383278 |doi=  }}
*{{cite journal  |vauthors=Lesche R, Rüther U |title=Close linkage of p130 and Ft1 is conserved among mammals |journal=Mamm. Genome |volume=9 |issue= 3 |pages= 253–5 |year= 1998 |pmid= 9501314 |doi=10.1007/s003359900737 }}
*{{cite journal  | author=Lesche R, Rüther U |title=Close linkage of p130 and Ft1 is conserved among mammals. |journal=Mamm. Genome |volume=9 |issue= 3 |pages= 253-5 |year= 1998 |pmid= 9501314 |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|bibcode=2002PNAS...9916899M }}
*{{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=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Remy I, Michnick SW |title=Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt |journal=Mol. Cell. Biol. |volume=24 |issue= 4 |pages= 1493–504 |year= 2004 |pmid= 14749367 |doi=10.1128/MCB.24.4.1493-1504.2004  | pmc=344167 }}
*{{cite journal  | author=Remy I, Michnick SW |title=Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt. |journal=Mol. Cell. Biol. |volume=24 |issue= 4 |pages= 1493-504 |year= 2004 |pmid= 14749367 |doi=  }}
*{{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=Stelzl U, Worm U, Lalowski M |title=A human protein-protein interaction network: a resource for annotating the proteome |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 |display-authors=etal}}
*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal  |vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal|bibcode=2005Natur.437.1173R }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  |vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein-protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 09:18, 10 January 2019

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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

AKT-interacting protein is a protein that in humans is encoded by the AKTIP gene.[1][2][3]

The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKB's regulatory sites. Alternative splicing results in two transcript variants encoding the same protein.[3]

Interactions

AKTIP has been shown to interact with AKT1.[4]

Molecular genetics

The association between the AKTIP gene variants in a sample of 273 bipolar patients using 3 single-nucleotide polymorphisms has been investigated. No association between suicidal behavior and AKTIP variants nor any interaction between AKTIP and AKT1 polymorphisms was observed.[5]

References

  1. ↑ Fluhmann B, Muff R, Hunziker W, Fischer JA, Born W (Feb 1995). "A human orphan calcitonin receptor-like structure". Biochem Biophys Res Commun. 206 (1): 341–7. doi:10.1006/bbrc.1995.1047. PMID 7818539.
  2. ↑ Aiyar N, Rand K, Elshourbagy NA, Zeng Z, Adamou JE, Bergsma DJ, Li Y (Jun 1996). "A cDNA encoding the calcitonin gene-related peptide type 1 receptor". J Biol Chem. 271 (19): 11325–9. doi:10.1074/jbc.271.19.11325. PMID 8626685.
  3. ↑ 3.0 3.1 "Entrez Gene: AKTIP AKT interacting protein".
  4. ↑ Remy, Ingrid; Michnick Stephen W (Feb 2004). "Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt". Mol. Cell. Biol. United States. 24 (4): 1493–504. doi:10.1128/MCB.24.4.1493-1504.2004. ISSN 0270-7306. PMC 344167. PMID 14749367.
  5. ↑ Magno LA, Miranda DM, Neves FS, Pimenta GJ, Mello MP, De Marco LA, Correa H, Romano-Silva MA (January 2010). "Association between AKT1 but not AKTIP genetic variants and increased risk for suicidal behavior in bipolar patients". Genes Brain Behav. 9 (4): 411–8. doi:10.1111/j.1601-183X.2010.00571.x. PMID 20132317.

External links

Further reading



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