User:ProteinBoxBot/PBB Log Ref Test5

Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

Protein Dry Status Log - Date: 21:54, 21 August 2007 (UTC)

Redirected Proteins (10)

CASP3	MMP9	CDKN2A	BRCA1	BCL2
APP	AR	APOE	AKT1	CDKN1A

Protein Status Log - Date: 21:54, 21 August 2007 (UTC)

Skipped: NO BOTS tag (2)

APP

APOE

Skipped: Updates Off (1)

CDKN2A

Skipped: Manual Inspection Required (1)

AR

Updated Existing Page (6)

CASP3	MMP9	BRCA1	BCL2	AKT1
CDKN1A

Condensed Log - Date: 21:54, 21 August 2007 (UTC)

Updated Protein Pages (7)

AKT1	AR	BCL2	BRCA1	CASP3
CDKN1A	MMP9

Skipped Proteins (4)

APOE

APP

AR

CDKN2A

Redirected Proteins (10)

AKT1	APOE	APP	AR	BCL2
BRCA1	CASP3	CDKN1A	CDKN2A	MMP9

Vebose Log - Date: 21:54, 21 August 2007 (UTC)

AKT1

• REDIRECT: Protein Redirected to: AKT1 {August 21, 2007 2:48:16 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:48:18 PM PDT}
• UPDATE SUMMARY: Updating Summary, No Errors. {August 21, 2007 2:48:18 PM PDT}
• UPDATE CITATIONS: Updating Citations, No Errors. {August 21, 2007 2:48:18 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_AKT1 {August 21, 2007 2:48:23 PM PDT}

APOE

• REDIRECT: Protein Redirected to: Apolipoprotein E {August 21, 2007 2:48:32 PM PDT}
• NO BOT: Encounted 'No Bot Edits' flag for this protein. {August 21, 2007 2:48:34 PM PDT}
• NO JOB: Location: User:JonSDSUGrad/Sandbox/TEST9_Apolipoprotein E {August 21, 2007 2:48:34 PM PDT}

 <!-- This template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Apolipoprotein E''', also known as '''APOE''', is a human [[gene]].
<!-- This infobox is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_APOE_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b68.
 | PDB = {{PDB2|1b68}}, {{PDB2|1bz4}}, {{PDB2|1ea8}}, {{PDB2|1gs9}}, {{PDB2|1h7i}}, {{PDB2|1le2}}, {{PDB2|1le4}}, {{PDB2|1lpe}}, {{PDB2|1nfn}}, {{PDB2|1nfo}}, {{PDB2|1or2}}, {{PDB2|1or3}}
 | Name = Apolipoprotein E
 | HGNCid = 613
 | Symbol = APOE
 | AltSymbols =; AD2; MGC1571; apoprotein
 | OMIM = 107741
 | ECnumber =  
 | Homologene = 30951
 | MGIid = 88057
 | GeneAtlas_image =  
 <!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
 | DateOfBotUpdate = ~~~~~
 | Function = {{GNF_GO|id=GO:0000302 |text = response to reactive oxygen species}} {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0006707 |text = cholesterol catabolic process}} {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007271 |text = synaptic transmission, cholinergic}} {{GNF_GO|id=GO:0007611 |text = learning and/or memory}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0008034 |text = lipoprotein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0030516 |text = regulation of axon extension}} {{GNF_GO|id=GO:0042157 |text = lipoprotein metabolic process}} {{GNF_GO|id=GO:0042311 |text = vasodilation}} {{GNF_GO|id=GO:0042627 |text = chylomicron}} {{GNF_GO|id=GO:0042632 |text = cholesterol homeostasis}} {{GNF_GO|id=GO:0046907 |text = intracellular transport}} {{GNF_GO|id=GO:0048156 |text = tau protein binding}} {{GNF_GO|id=GO:0048168 |text = regulation of neuronal synaptic plasticity}} {{GNF_GO|id=GO:0050749 |text = apolipoprotein E receptor binding}} {{GNF_GO|id=GO:0051262 |text = protein tetramerization}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 348
    | Hs_Ensembl = ENSG00000130203
    | Hs_RefseqProtein = NP_000032
    | Hs_RefseqmRNA = NM_000041
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 50100879
    | Hs_GenLoc_end = 50104489
    | Hs_Uniprot = P02649
    | Mm_EntrezGene = 11816
    | Mm_Ensembl = ENSMUSG00000002985
    | Mm_RefseqmRNA = NM_009696
    | Mm_RefseqProtein = NP_033826
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 18854795
    | Mm_GenLoc_end = 18857574
    | Mm_Uniprot =  
  }}
}}
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Chylomicron remnants and very low density lipoprotein (VLDL) remnants are rapidly removed from the circulation by receptor-mediated endocytosis in the liver. Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells.  ApoE is essential for the normal catabolism of triglyceride-rich lipoprotein constituents.  The APOE gene is mapped to chromosome 19 in a cluster with APOC1 and APOC2.  Defects in apolipoprotein E result in familial dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III), in which increased plasma cholesterol and triglycerides are the consequence of impaired clearance of chylomicron and VLDL remnants.<ref>{{cite web | title = Entrez Gene: APOE apolipoprotein E| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=348| accessdate = 2007-08-10}}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Mahley RW |title=Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. |journal=Science |volume=240 |issue= 4852 |pages= 622-30 |year= 1988 |pmid= 3283935 |doi=  }}
*{{cite journal  | author=Strittmatter WJ, Roses AD |title=Apolipoprotein E and Alzheimer disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 11 |pages= 4725-7 |year= 1995 |pmid= 7761390 |doi=  }}
*{{cite journal  | author=de Knijff P, van den Maagdenberg AM, Frants RR, Havekes LM |title=Genetic heterogeneity of apolipoprotein E and its influence on plasma lipid and lipoprotein levels. |journal=Hum. Mutat. |volume=4 |issue= 3 |pages= 178-94 |year= 1995 |pmid= 7833947 |doi= 10.1002/humu.1380040303 }}
*{{cite journal  | author=Roses AD, Einstein G, Gilbert J, ''et al.'' |title=Morphological, biochemical, and genetic support for an apolipoprotein E effect on microtubular metabolism. |journal=Ann. N. Y. Acad. Sci. |volume=777 |issue=  |pages= 146-57 |year= 1996 |pmid= 8624078 |doi=  }}
*{{cite journal  | author=Beffert U, Danik M, Krzywkowski P, ''et al.'' |title=The neurobiology of apolipoproteins and their receptors in the CNS and Alzheimer's disease. |journal=Brain Res. Brain Res. Rev. |volume=27 |issue= 2 |pages= 119-42 |year= 1998 |pmid= 9622609 |doi=  }}
*{{cite journal  | author=Mahley RW, Ji ZS |title=Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E. |journal=J. Lipid Res. |volume=40 |issue= 1 |pages= 1-16 |year= 1999 |pmid= 9869645 |doi=  }}
*{{cite journal  | author=Mahley RW, Rall SC |title=Apolipoprotein E: far more than a lipid transport protein. |journal=Annual review of genomics and human genetics |volume=1 |issue=  |pages= 507-37 |year= 2002 |pmid= 11701639 |doi= 10.1146/annurev.genom.1.1.507 }}
*{{cite journal  | author=Parasuraman R, Greenwood PM, Sunderland T |title=The apolipoprotein E gene, attention, and brain function. |journal=Neuropsychology |volume=16 |issue= 2 |pages= 254-74 |year= 2002 |pmid= 11949718 |doi=  }}
*{{cite journal  | author=Bocksch L, Stephens T, Lucas A, Singh B |title=Apolipoprotein E: possible therapeutic target for atherosclerosis. |journal=Current drug targets. Cardiovascular & haematological disorders |volume=1 |issue= 2 |pages= 93-106 |year= 2003 |pmid= 12769659 |doi=  }}
*{{cite journal  | author=Masterman T, Hillert J |title=The telltale scan: APOE epsilon4 in multiple sclerosis. |journal=Lancet neurology |volume=3 |issue= 6 |pages= 331 |year= 2004 |pmid= 15157846 |doi= 10.1016/S1474-4422(04)00763-X }}
*{{cite journal  | author=Ashford JW |title=APOE genotype effects on Alzheimer's disease onset and epidemiology. |journal=J. Mol. Neurosci. |volume=23 |issue= 3 |pages= 157-65 |year= 2004 |pmid= 15181244 |doi=  }}
*{{cite journal  | author=Huang Y, Weisgraber KH, Mucke L, Mahley RW |title=Apolipoprotein E: diversity of cellular origins, structural and biophysical properties, and effects in Alzheimer's disease. |journal=J. Mol. Neurosci. |volume=23 |issue= 3 |pages= 189-204 |year= 2004 |pmid= 15181247 |doi=  }}
*{{cite journal  | author=Itzhaki RF, Dobson CB, Shipley SJ, Wozniak MA |title=The role of viruses and of APOE in dementia. |journal=Ann. N. Y. Acad. Sci. |volume=1019 |issue=  |pages= 15-8 |year= 2004 |pmid= 15246985 |doi= 10.1196/annals.1297.003 }}
}}
{{refend}}
 

APP

• REDIRECT: Protein Redirected to: Amyloid_precursor_protein {August 21, 2007 2:49:01 PM PDT}
• NO BOT: Encounted 'No Bot Edits' flag for this protein. {August 21, 2007 2:49:03 PM PDT}
• NO JOB: Location: User:JonSDSUGrad/Sandbox/TEST9_Amyloid_precursor_protein {August 21, 2007 2:49:03 PM PDT}

 <!-- This template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
'''Amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease)''', also known as '''APP''', is a human [[gene]].
<!-- This infobox is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_APP_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aap.
 | PDB = {{PDB2|1aap}}, {{PDB2|1amb}}, {{PDB2|1amc}}, {{PDB2|1aml}}, {{PDB2|1ba4}}, {{PDB2|1ba6}}, {{PDB2|1brc}}, {{PDB2|1ca0}}, {{PDB2|1iyt}}, {{PDB2|1mwp}}, {{PDB2|1owt}}, {{PDB2|1rw6}}, {{PDB2|1taw}}, {{PDB2|1tkn}}, {{PDB2|1z0q}}, {{PDB2|1zjd}}, {{PDB2|2beg}}, {{PDB2|2fjz}}, {{PDB2|2fk1}}, {{PDB2|2fk2}}, {{PDB2|2fk3}}, {{PDB2|2fkl}}, {{PDB2|2fma}}, {{PDB2|2g47}}
 | Name = Amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease)
 | HGNCid = 620
 | Symbol = APP
 | AltSymbols =; AAA; ABETA; ABPP; AD1; APPI; CTFgamma; CVAP; PN2
 | OMIM = 104760
 | ECnumber =  
 | Homologene = 56379
 | MGIid = 88059
 | GeneAtlas_image =  
 <!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
 | DateOfBotUpdate = ~~~~~
 | Function = {{GNF_GO|id=GO:0000085 |text = G2 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0001967 |text = suckling behavior}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005905 |text = coated pit}} {{GNF_GO|id=GO:0006378 |text = mRNA polyadenylation}} {{GNF_GO|id=GO:0006878 |text = cellular copper ion homeostasis}} {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0007617 |text = mating behavior}} {{GNF_GO|id=GO:0008088 |text = axon cargo transport}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008344 |text = adult locomotory behavior}} {{GNF_GO|id=GO:0008542 |text = visual learning}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016199 |text = axon midline choice point recognition}} {{GNF_GO|id=GO:0016322 |text = neuron remodeling}} {{GNF_GO|id=GO:0016358 |text = dendrite development}} {{GNF_GO|id=GO:0030198 |text = extracellular matrix organization and biogenesis}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0031410 |text = cytoplasmic vesicle}} {{GNF_GO|id=GO:0031594 |text = neuromuscular junction}} {{GNF_GO|id=GO:0035253 |text = ciliary rootlet}} {{GNF_GO|id=GO:0040014 |text = regulation of body size}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0045177 |text = apical part of cell}} {{GNF_GO|id=GO:0045931 |text = positive regulation of progression through mitotic cell cycle}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}} {{GNF_GO|id=GO:0048669 |text = collateral sprouting in the absence of injury}} {{GNF_GO|id=GO:0050803 |text = regulation of synapse structure and activity}} {{GNF_GO|id=GO:0050885 |text = regulation of balance}} {{GNF_GO|id=GO:0050905 |text = neuromuscular process}} {{GNF_GO|id=GO:0051124 |text = synaptic growth at neuromuscular junction}} {{GNF_GO|id=GO:0051233 |text = spindle midzone}} {{GNF_GO|id=GO:0051563 |text = smooth endoplasmic reticulum calcium ion homeostasis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 351
    | Hs_Ensembl = ENSG00000142192
    | Hs_RefseqProtein = NP_000475
    | Hs_RefseqmRNA = NM_000484
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 26174733
    | Hs_GenLoc_end = 26465003
    | Hs_Uniprot = P05067
    | Mm_EntrezGene = 11820
    | Mm_Ensembl = ENSMUSG00000022892
    | Mm_RefseqmRNA = NM_007471
    | Mm_RefseqProtein = NP_031497
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 84837873
    | Mm_GenLoc_end = 85057149
    | Mm_Uniprot =  
  }}
}}
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: APP amyloid beta (A4) precursor protein (peptidase nexin-II, Alzheimer disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=351| accessdate = 2007-08-10}}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Beyreuther K, Pollwein P, Multhaup G, ''et al.'' |title=Regulation and expression of the Alzheimer's beta/A4 amyloid protein precursor in health, disease, and Down's syndrome. |journal=Ann. N. Y. Acad. Sci. |volume=695 |issue=  |pages= 91-102 |year= 1993 |pmid= 8239320 |doi=  }}
*{{cite journal  | author=Janciauskiene S, Wright HT |title=Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of Alzheimer's disease. |journal=Bioessays |volume=20 |issue= 12 |pages= 1039-46 |year= 1999 |pmid= 10048303 |doi= 10.1002/(SICI)1521-1878(199812)20:12<1039::AID-BIES10>3.0.CO;2-Z }}
*{{cite journal  | author=Kontush A |title=Alzheimer's amyloid-beta as a preventive antioxidant for brain lipoproteins. |journal=Cell. Mol. Neurobiol. |volume=21 |issue= 4 |pages= 299-315 |year= 2002 |pmid= 11775062 |doi=  }}
*{{cite journal  | author=Blennow K, Vanmechelen E, Hampel H |title=CSF total tau, Abeta42 and phosphorylated tau protein as biomarkers for Alzheimer's disease. |journal=Mol. Neurobiol. |volume=24 |issue= 1-3 |pages= 87-97 |year= 2002 |pmid= 11831556 |doi=  }}
*{{cite journal  | author=Yanagisawa K |title=[Pathological implications of GM1 ganglioside-bound amyloid beta-protein in Alzheimer's disease] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 344-50 |year= 2002 |pmid= 11915325 |doi=  }}
*{{cite journal  | author=Matsuzaki K |title=[Interactions between amyloid beta--protein and gangliosides] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 351-6 |year= 2002 |pmid= 11915326 |doi=  }}
*{{cite journal  | author=Bush AI, Tanzi RE |title=The galvanization of beta-amyloid in Alzheimer's disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 11 |pages= 7317-9 |year= 2002 |pmid= 12032279 |doi= 10.1073/pnas.122249699 }}
*{{cite journal  | author=Doré S |title=Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease. |journal=Free Radic. Biol. Med. |volume=32 |issue= 12 |pages= 1276-82 |year= 2002 |pmid= 12057765 |doi=  }}
*{{cite journal  | author=Straub JE, Guevara J, Huo S, Lee JP |title=Long time dynamic simulations: exploring the folding pathways of an Alzheimer's amyloid Abeta-peptide. |journal=Acc. Chem. Res. |volume=35 |issue= 6 |pages= 473-81 |year= 2003 |pmid= 12069633 |doi=  }}
*{{cite journal  | author=Annaert W, De Strooper B |title=A cell biological perspective on Alzheimer's disease. |journal=Annu. Rev. Cell Dev. Biol. |volume=18 |issue=  |pages= 25-51 |year= 2003 |pmid= 12142279 |doi= 10.1146/annurev.cellbio.18.020402.142302 }}
*{{cite journal  | author=Koo EH |title=The beta-amyloid precursor protein (APP) and Alzheimer's disease: does the tail wag the dog? |journal=Traffic |volume=3 |issue= 11 |pages= 763-70 |year= 2003 |pmid= 12383342 |doi=  }}
*{{cite journal  | author=Van Nostrand WE, Melchor JP, Romanov G, ''et al.'' |title=Pathogenic effects of cerebral amyloid angiopathy mutations in the amyloid beta-protein precursor. |journal=Ann. N. Y. Acad. Sci. |volume=977 |issue=  |pages= 258-65 |year= 2003 |pmid= 12480759 |doi=  }}
*{{cite journal  | author=Ling Y, Morgan K, Kalsheker N |title=Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer's disease. |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 11 |pages= 1505-35 |year= 2004 |pmid= 12824062 |doi=  }}
*{{cite journal  | author=Kerr ML, Small DH |title=Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: function, regulation of proteolysis, and implications for drug development. |journal=J. Neurosci. Res. |volume=80 |issue= 2 |pages= 151-9 |year= 2005 |pmid= 15672415 |doi= 10.1002/jnr.20408 }}
*{{cite journal  | author=Maynard CJ, Bush AI, Masters CL, ''et al.'' |title=Metals and amyloid-beta in Alzheimer's disease. |journal=International journal of experimental pathology |volume=86 |issue= 3 |pages= 147-59 |year= 2005 |pmid= 15910549 |doi= 10.1111/j.0959-9673.2005.00434.x }}
*{{cite journal  | author=Tickler AK, Wade JD, Separovic F |title=The role of Abeta peptides in Alzheimer's disease. |journal=Protein Pept. Lett. |volume=12 |issue= 6 |pages= 513-9 |year= 2005 |pmid= 16101387 |doi=  }}
*{{cite journal  | author=Reinhard C, Hébert SS, De Strooper B |title=The amyloid-beta precursor protein: integrating structure with biological function. |journal=EMBO J. |volume=24 |issue= 23 |pages= 3996-4006 |year= 2006 |pmid= 16252002 |doi= 10.1038/sj.emboj.7600860 }}
*{{cite journal  | author=Watson D, Castaño E, Kokjohn TA, ''et al.'' |title=Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease. |journal=Neurol. Res. |volume=27 |issue= 8 |pages= 869-81 |year= 2006 |pmid= 16354549 |doi= 10.1179/016164105X49436 }}
*{{cite journal  | author=Calinisan V, Gravem D, Chen RP, ''et al.'' |title=New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. |journal=Front. Biosci. |volume=11 |issue=  |pages= 1646-66 |year= 2006 |pmid= 16368544 |doi=  }}
*{{cite journal  | author=Vetrivel KS, Thinakaran G |title=Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments. |journal=Neurology |volume=66 |issue= 2 Suppl 1 |pages= S69-73 |year= 2006 |pmid= 16432149 |doi= 10.1212/01.wnl.0000192107.17175.39 }}
*{{cite journal  | author=Gallo C, Orlassino R, Vineis C |title=[Recurrent intraparenchimal haemorrhages in a patient with cerebral amyloidotic angiopathy: description of one autopsy case] |journal=Pathologica |volume=98 |issue= 1 |pages= 44-7 |year= 2006 |pmid= 16789686 |doi=  }}
*{{cite journal  | author=Coulson EJ |title=Does the p75 neurotrophin receptor mediate Abeta-induced toxicity in Alzheimer's disease? |journal=J. Neurochem. |volume=98 |issue= 3 |pages= 654-60 |year= 2006 |pmid= 16893414 |doi= 10.1111/j.1471-4159.2006.03905.x }}
*{{cite journal  | author=Menéndez-González M, Pérez-Pinera P, Martínez-Rivera M, ''et al.'' |title=APP processing and the APP-KPI domain involvement in the amyloid cascade. |journal=Neuro-degenerative diseases |volume=2 |issue= 6 |pages= 277-83 |year= 2006 |pmid= 16909010 |doi= 10.1159/000092315 }}
*{{cite journal  | author=Neve RL, McPhie DL |title=Dysfunction of amyloid precursor protein signaling in neurons leads to DNA synthesis and apoptosis. |journal=Biochim. Biophys. Acta |volume=1772 |issue= 4 |pages= 430-7 |year= 2007 |pmid= 17113271 |doi= 10.1016/j.bbadis.2006.10.008 }}
*{{cite journal  | author=Chen X, Stern D, Yan SD |title=Mitochondrial dysfunction and Alzheimer's disease. |journal=Current Alzheimer research |volume=3 |issue= 5 |pages= 515-20 |year= 2007 |pmid= 17168650 |doi=  }}
*{{cite journal  | author=Caltagarone J, Jing Z, Bowser R |title=Focal adhesions regulate Abeta signaling and cell death in Alzheimer's disease. |journal=Biochim. Biophys. Acta |volume=1772 |issue= 4 |pages= 438-45 |year= 2007 |pmid= 17215111 |doi= 10.1016/j.bbadis.2006.11.007 }}
*{{cite journal  | author=Wolfe MS |title=When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease. |journal=EMBO Rep. |volume=8 |issue= 2 |pages= 136-40 |year= 2007 |pmid= 17268504 |doi= 10.1038/sj.embor.7400896 }}
}}
{{refend}}
 

AR

• REDIRECT: Protein Redirected to: Androgen_receptor {August 21, 2007 2:49:28 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:49:29 PM PDT}
• UPDATE SUMMARY: Updating Summary, No Errors. {August 21, 2007 2:49:29 PM PDT}
• UPDATE CITATIONS: Updating Citations, No Errors. {August 21, 2007 2:49:29 PM PDT}
• INSPECTION: Manual Inspection Required for this protein: User:JonSDSUGrad/Sandbox/TEST9_Androgen_receptor {August 21, 2007 2:49:29 PM PDT}

 <!-- This template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
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| update_citations = yes
}}
Androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease), also known as AR, is a human gene.
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_AR_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e3g.
 | PDB = {{PDB2|1e3g}}, {{PDB2|1gs4}}, {{PDB2|1i37}}, {{PDB2|1i38}}, {{PDB2|1r4i}}, {{PDB2|1t5z}}, {{PDB2|1t63}}, {{PDB2|1t65}}, {{PDB2|1t73}}, {{PDB2|1t74}}, {{PDB2|1t76}}, {{PDB2|1t79}}, {{PDB2|1t7f}}, {{PDB2|1t7m}}, {{PDB2|1t7r}}, {{PDB2|1t7t}}, {{PDB2|1xj7}}, {{PDB2|1xnn}}, {{PDB2|1xow}}, {{PDB2|1xq3}}, {{PDB2|1z95}}, {{PDB2|2am9}}, {{PDB2|2ama}}, {{PDB2|2amb}}, {{PDB2|2ao6}}, {{PDB2|2ax6}}, {{PDB2|2ax7}}, {{PDB2|2ax8}}, {{PDB2|2ax9}}, {{PDB2|2axa}}, {{PDB2|2ihq}}, {{PDB2|2nw4}}, {{PDB2|2oz7}}
 | Name = Androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease)
 | HGNCid = 644
 | Symbol = AR
 | AltSymbols =; AIS; DHTR; HUMARA; KD; NR3C4; SBMA; SMAX1; TFM
 | OMIM = 313700
 | ECnumber =  
 | Homologene = 28
 | MGIid = 88064
 | GeneAtlas_image =  
 <!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
 | DateOfBotUpdate = ~~~~~
 | Function = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004882 |text = androgen receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005497 |text = androgen binding}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0019102 |text = male somatic sex determination}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0030850 |text = prostate gland development}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 367
    | Hs_Ensembl = ENSG00000169083
    | Hs_RefseqProtein = NP_000035
    | Hs_RefseqmRNA = NM_000044
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 66681190
    | Hs_GenLoc_end = 66867186
    | Hs_Uniprot = P10275
    | Mm_EntrezGene = 11835
    | Mm_Ensembl = ENSMUSG00000046532
    | Mm_RefseqmRNA = NM_013476
    | Mm_RefseqProtein = NP_038504
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 94352469
    | Mm_GenLoc_end = 94519866
    | Mm_Uniprot =  
  }}
}}
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described.<ref>{{cite web | title = Entrez Gene: AR androgen receptor (dihydrotestosterone receptor; testicular feminization; spinal and bulbar muscular atrophy; Kennedy disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=367| accessdate = 2007-08-10}}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Pinsky L, Trifiro M, Kaufman M, ''et al.'' |title=Androgen resistance due to mutation of the androgen receptor. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=15 |issue= 5 |pages= 456-72 |year= 1993 |pmid= 1458719 |doi=  }}
*{{cite journal  | author=Veldscholte J, Berrevoets CA, Ris-Stalpers C, ''et al.'' |title=The androgen receptor in LNCaP cells contains a mutation in the ligand binding domain which affects steroid binding characteristics and response to antiandrogens. |journal=J. Steroid Biochem. Mol. Biol. |volume=41 |issue= 3-8 |pages= 665-9 |year= 1992 |pmid= 1562539 |doi=  }}
*{{cite journal  | author=Brinkmann AO, Jenster G, Ris-Stalpers C, ''et al.'' |title=Androgen receptor mutations. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 443-8 |year= 1995 |pmid= 7626493 |doi=  }}
*{{cite journal  | author=Quigley CA, De Bellis A, Marschke KB, ''et al.'' |title=Androgen receptor defects: historical, clinical, and molecular perspectives. |journal=Endocr. Rev. |volume=16 |issue= 3 |pages= 271-321 |year= 1995 |pmid= 7671849 |doi=  }}
*{{cite journal  | author=Sultan C, Lumbroso S, Poujol N, ''et al.'' |title=Mutations of androgen receptor gene in androgen insensitivity syndromes. |journal=J. Steroid Biochem. Mol. Biol. |volume=46 |issue= 5 |pages= 519-30 |year= 1994 |pmid= 8240973 |doi=  }}
*{{cite journal  | author=Yong EL, Tut TG, Ghadessy FJ, ''et al.'' |title=Partial androgen insensitivity and correlations with the predicted three dimensional structure of the androgen receptor ligand-binding domain. |journal=Mol. Cell. Endocrinol. |volume=137 |issue= 1 |pages= 41-50 |year= 1999 |pmid= 9607727 |doi=  }}
*{{cite journal  | author=Jänne OA, Moilanen AM, Poukka H, ''et al.'' |title=Androgen-receptor-interacting nuclear proteins. |journal=Biochem. Soc. Trans. |volume=28 |issue= 4 |pages= 401-5 |year= 2001 |pmid= 10961928 |doi=  }}
*{{cite journal  | author=Yeh S, Sampson ER, Lee DK, ''et al.'' |title=Functional analysis of androgen receptor N-terminal and ligand binding domain interacting coregulators in prostate cancer. |journal=J. Formos. Med. Assoc. |volume=99 |issue= 12 |pages= 885-94 |year= 2001 |pmid= 11155740 |doi=  }}
*{{cite journal  | author=Loy CJ, Yong EL |title=Sex, infertility and the molecular biology of the androgen receptor. |journal=Curr. Opin. Obstet. Gynecol. |volume=13 |issue= 3 |pages= 315-21 |year= 2001 |pmid= 11396657 |doi=  }}
*{{cite journal  | author=Roy AK, Tyagi RK, Song CS, ''et al.'' |title=Androgen receptor: structural domains and functional dynamics after ligand-receptor interaction. |journal=Ann. N. Y. Acad. Sci. |volume=949 |issue=  |pages= 44-57 |year= 2002 |pmid= 11795379 |doi=  }}
*{{cite journal  | author=He B, Wilson EM |title=The NH(2)-terminal and carboxyl-terminal interaction in the human androgen receptor. |journal=Mol. Genet. Metab. |volume=75 |issue= 4 |pages= 293-8 |year= 2002 |pmid= 12051960 |doi= 10.1016/S1096-7192(02)00009-4 }}
*{{cite journal  | author=Culig Z, Klocker H, Bartsch G, Hobisch A |title=Androgen receptor mutations in carcinoma of the prostate: significance for endocrine therapy. |journal=American journal of pharmacogenomics : genomics-related research in drug development and clinical practice |volume=1 |issue= 4 |pages= 241-9 |year= 2002 |pmid= 12083956 |doi=  }}
*{{cite journal  | author=Ferro P, Catalano MG, Dell'Eva R, ''et al.'' |title=The androgen receptor CAG repeat: a modifier of carcinogenesis? |journal=Mol. Cell. Endocrinol. |volume=193 |issue= 1-2 |pages= 109-20 |year= 2003 |pmid= 12161010 |doi=  }}
*{{cite journal  | author=Sultan Ch, Gobinet J, Terouanne B, ''et al.'' |title=[The androgen receptor: molecular pathology] |journal=J. Soc. Biol. |volume=196 |issue= 3 |pages= 223-40 |year= 2003 |pmid= 12465595 |doi=  }}
*{{cite journal  | author=Walcott JL, Merry DE |title=Trinucleotide repeat disease. The androgen receptor in spinal and bulbar muscular atrophy. |journal=Vitam. Horm. |volume=65 |issue=  |pages= 127-47 |year= 2003 |pmid= 12481545 |doi=  }}
*{{cite journal  | author=Bonaccorsi L, Muratori M, Carloni V, ''et al.'' |title=Androgen receptor and prostate cancer invasion. |journal=Int. J. Androl. |volume=26 |issue= 1 |pages= 21-5 |year= 2003 |pmid= 12534934 |doi=  }}
*{{cite journal  | author=Verrijdt G, Haelens A, Claessens F |title=Selective DNA recognition by the androgen receptor as a mechanism for hormone-specific regulation of gene expression. |journal=Mol. Genet. Metab. |volume=78 |issue= 3 |pages= 175-85 |year= 2004 |pmid= 12649062 |doi=  }}
*{{cite journal  | author=Santos AF, Huang H, Tindall DJ |title=The androgen receptor: a potential target for therapy of prostate cancer. |journal=Steroids |volume=69 |issue= 2 |pages= 79-85 |year= 2004 |pmid= 15013685 |doi= 10.1016/j.steroids.2003.10.005 }}
*{{cite journal  | author=Mazen I, Lumbroso S, Abdel Ghaffar S, ''et al.'' |title=Mutation of the androgen receptor (R840S) in an Egyptian patient with partial androgen insensitivity syndrome: review of the literature on the clinical expression of different R840 substitutions. |journal=J. Endocrinol. Invest. |volume=27 |issue= 1 |pages= 57-60 |year= 2004 |pmid= 15053245 |doi=  }}
*{{cite journal  | author=Black BE, Paschal BM |title=Intranuclear organization and function of the androgen receptor. |journal=Trends Endocrinol. Metab. |volume=15 |issue= 9 |pages= 411-7 |year= 2005 |pmid= 15519887 |doi= 10.1016/j.tem.2004.09.006 }}
*{{cite journal  | author=Tufan AC, Satiroglu-Tufan NL, Aydinuraz B, ''et al.'' |title=No association of the CAG repeat length in exon 1 of the androgen receptor gene with idiopathic infertility in Turkish men: implications and literature review. |journal=Tohoku J. Exp. Med. |volume=206 |issue= 2 |pages= 105-15 |year= 2005 |pmid= 15888966 |doi=  }}
*{{cite journal  | author=Morel Y, Michel-Calemard L, Mallet D |title=[Genetic anomalies of the androgen receptor and sexual ambiguity with normal testicular function at birth] |journal=Ann. Endocrinol. (Paris) |volume=66 |issue= 3 |pages= 217-24 |year= 2005 |pmid= 15988382 |doi=  }}
*{{cite journal  | author=Rajender S, Singh L, Thangaraj K |title=Phenotypic heterogeneity of mutations in androgen receptor gene. |journal=Asian J. Androl. |volume=9 |issue= 2 |pages= 147-79 |year= 2007 |pmid= 17334586 |doi= 10.1111/j.1745-7262.2007.00250.x }}
*{{cite journal  | author=Comstock CE, Knudsen KE |title=The complex role of AR signaling after cytotoxic insult: implications for cell-cycle-based chemotherapeutics. |journal=Cell Cycle |volume=6 |issue= 11 |pages= 1307-13 |year= 2007 |pmid= 17568191 |doi=  }}
}}
{{refend}}
 

BCL2

• REDIRECT: Protein Redirected to: Bcl-2 {August 21, 2007 2:49:40 PM PDT}
• SKIP PROTEIN BOX: Skipping Protein Box, No errors. {August 21, 2007 2:49:42 PM PDT}
• UPDATE SUMMARY: Updating Summary, No Errors. {August 21, 2007 2:49:42 PM PDT}
• UPDATE CITATIONS: Updating Citations, No Errors. {August 21, 2007 2:49:42 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_Bcl-2 {August 21, 2007 2:49:50 PM PDT}

BRCA1

• REDIRECT: Protein Redirected to: BRCA1 {August 21, 2007 2:50:24 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:50:26 PM PDT}
• SKIP SUMMARY: SKIPPING Summary, No Errors. {August 21, 2007 2:50:26 PM PDT}
• UPDATE CITATIONS: Updating Citations, No Errors. {August 21, 2007 2:50:26 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_BRCA1 {August 21, 2007 2:50:36 PM PDT}

CASP3

• REDIRECT: Protein Redirected to: Caspase 3 {August 21, 2007 2:50:42 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:50:43 PM PDT}
• UPDATE SUMMARY: Updating Summary, No Errors. {August 21, 2007 2:50:43 PM PDT}
• SKIP CITATIONS: Skipping Citations, No Errors. {August 21, 2007 2:50:43 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_Caspase 3 {August 21, 2007 2:50:48 PM PDT}

CDKN1A

• REDIRECT: Protein Redirected to: p21 {August 21, 2007 2:50:54 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:50:58 PM PDT}
• SKIP SUMMARY: Skipping Summary, No Errors. {August 21, 2007 2:50:58 PM PDT}
• SKIP CITATIONS: Skipping Citations, No Errors. {August 21, 2007 2:50:58 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_p21 {August 21, 2007 2:51:04 PM PDT}

CDKN2A

• REDIRECT: Protein Redirected to: P16INK4a {August 21, 2007 2:52:24 PM PDT}
• NO JOB: Aborted upload due to all updates being turned off. No errors. {August 21, 2007 2:52:27 PM PDT}
• NO JOB: Location: User:JonSDSUGrad/Sandbox/TEST9_P16INK4a {August 21, 2007 2:52:27 PM PDT}

 <!-- This template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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}}
'''Cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)''', also known as '''CDKN2A''', is a human [[gene]].
<!-- This infobox is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_CDKN2A_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a5e.
 | PDB = {{PDB2|1a5e}}, {{PDB2|1bi7}}, {{PDB2|1dc2}}, {{PDB2|2a5e}}
 | Name = Cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)
 | HGNCid = 1787
 | Symbol = CDKN2A
 | AltSymbols =; ARF; CDK4I; CDKN2; CMM2; INK4; INK4a; MLM; MTS1; TP16; p14; p14ARF; p16; p16INK4; p16INK4a; p19
 | OMIM = 600160
 | ECnumber =  
 | Homologene = 55430
 | MGIid =  
 | GeneAtlas_image =  
 <!-- The Following entry is a time stamp of the last bot update.  It is typically hidden data -->
 | DateOfBotUpdate = ~~~~~
 | Function = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006364 |text = rRNA processing}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007569 |text = cell aging}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0045736 |text = negative regulation of cyclin-dependent protein kinase activity}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1029
    | Hs_Ensembl = ENSG00000147889
    | Hs_RefseqProtein = NP_000068
    | Hs_RefseqmRNA = NM_000077
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 21957751
    | Hs_GenLoc_end = 21984490
    | Hs_Uniprot = P42771
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
<!-- This summary is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene generates several transcript variants which differ in their first exons. At least three alternatively spliced variants encoding distinct proteins have been reported, two of which encode structurally related isoforms known to function as inhibitors of CDK4 kinase. The remaining transcript includes an alternate first exon located 20 Kb upstream of the remainder of the gene; this transcript contains an alternate open reading frame (ARF) that specifies a protein which is structurally unrelated to the products of the other variants. This ARF product functions as a stabilizer of the tumor suppressor protein p53 as it can interact with, and sequester, MDM1, a protein responsible for the degradation of p53. In spite of the structural and functional differences, the CDK inhibitor isoforms and the ARF product encoded by this gene, through the regulatory roles of CDK4 and p53 in cell cycle G1 progression, share a common functionality in cell cycle G1 control. This gene is frequently mutated or deleted in a wide variety of tumors, and is known to be an important tumor suppressor gene.<ref>{{cite web | title = Entrez Gene: CDKN2A cyclin-dependent kinase inhibitor 2A (melanoma, p16, inhibits CDK4)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1029| accessdate = 2007-08-10}}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Smith-Sørensen B, Hovig E |title=CDKN2A (p16INK4A) somatic and germline mutations. |journal=Hum. Mutat. |volume=7 |issue= 4 |pages= 294-303 |year= 1996 |pmid= 8723678 |doi= 10.1002/(SICI)1098-1004(1996)7:4&lt;294::AID-HUMU2&gt;3.0.CO;2-9 }}
*{{cite journal  | author=Dracopoli NC, Fountain JW |title=CDKN2 mutations in melanoma. |journal=Cancer Surv. |volume=26 |issue=  |pages= 115-32 |year= 1996 |pmid= 8783570 |doi=  }}
*{{cite journal  | author=Akita H |title=[Prognostic importance of altered expression of cell cycle regulators in lung cancer] |journal=Nippon Rinsho |volume=60 Suppl 5 |issue=  |pages= 267-71 |year= 2003 |pmid= 12101670 |doi=  }}
*{{cite journal  | author=Kusy S, Larsen CJ, Roche J |title=p14ARF, p15INK4b and p16INK4a methylation status in chronic myelogenous leukemia. |journal=Leuk. Lymphoma |volume=45 |issue= 10 |pages= 1989-94 |year= 2005 |pmid= 15370242 |doi= 10.1080/10428190410001714025 }}
*{{cite journal  | author=Gjerset RA |title=DNA damage, p14ARF, nucleophosmin (NPM/B23), and cancer. |journal=J. Mol. Histol. |volume=37 |issue= 5-7 |pages= 239-51 |year= 2007 |pmid= 16855788 |doi= 10.1007/s10735-006-9040-y }}
*{{cite journal  | author=Yildiz IZ, Usubütün A, Firat P, ''et al.'' |title=Efficiency of immunohistochemical p16 expression and HPV typing in cervical squamous intraepithelial lesion grading and review of the p16 literature. |journal=Pathol. Res. Pract. |volume=203 |issue= 6 |pages= 445-9 |year= 2007 |pmid= 17543474 |doi= 10.1016/j.prp.2007.03.010 }}
}}
{{refend}}
 

MMP9

• REDIRECT: Protein Redirected to: MMP9 {August 21, 2007 2:52:32 PM PDT}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {August 21, 2007 2:52:34 PM PDT}
• UPDATE SUMMARY: Updating Summary, No Errors. {August 21, 2007 2:52:34 PM PDT}
• UPDATE CITATIONS: Updating Citations, No Errors. {August 21, 2007 2:52:34 PM PDT}
• UPDATED: Updated protein page: User:JonSDSUGrad/Sandbox/TEST9_MMP9 {August 21, 2007 2:53:59 PM PDT}

end log.