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AMBIGUITY: Did not locate an acceptable page to update. {November 4, 2007 10:02:41 AM PST}
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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 = PBB_Protein_AURKA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mq4.
| PDB = {{PDB2|1mq4}}, {{PDB2|1muo}}, {{PDB2|1ol5}}, {{PDB2|1ol6}}, {{PDB2|1ol7}}, {{PDB2|2bmc}}, {{PDB2|2c6d}}, {{PDB2|2c6e}}, {{PDB2|2j4z}}, {{PDB2|2j50}}, {{PDB2|2np8}}
| Name = Aurora kinase A
| HGNCid = 11393
| Symbol = AURKA
| AltSymbols =; AIK; ARK1; AURA; AURORA2; BTAK; MGC34538; STK15; STK6; STK7
| OMIM = 603072
| ECnumber =
| Homologene = 2670
| MGIid = 894678
| GeneAtlas_image1 = PBB_GE_AURKA_204092_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AURKA_208079_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0031625 |text = ubiquitin protein ligase binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005819 |text = spindle}}
| Process = {{GNF_GO|id=GO:0000278 |text = mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007051 |text = spindle organization and biogenesis}} {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0031647 |text = regulation of protein stability}} {{GNF_GO|id=GO:0048015 |text = phosphoinositide-mediated signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6790
| Hs_Ensembl = ENSG00000087586
| Hs_RefseqProtein = NP_003591
| Hs_RefseqmRNA = NM_003600
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 54377852
| Hs_GenLoc_end = 54400758
| Hs_Uniprot = O14965
| Mm_EntrezGene = 20878
| Mm_Ensembl = ENSMUSG00000027496
| Mm_RefseqmRNA = NM_011497
| Mm_RefseqProtein = NP_035627
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 172047401
| Mm_GenLoc_end = 172061711
| Mm_Uniprot = Q3TEY6
}}
}}
'''Aurora kinase A''', also known as '''AURKA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a cell cycle-regulated kinase that appears to be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. The encoded protein is found at the centrosome in interphase cells and at the spindle poles in mitosis. This gene may play a role in tumor development and progression. A processed pseudogene of this gene has been found on chromosome 1, and an unprocessed pseudogene has been found on chromosome 10. Multiple transcript variants encoding the same protein have been found for this gene.<ref>{{cite web | title = Entrez Gene: AURKA aurora kinase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6790| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nigg EA |title=Mitotic kinases as regulators of cell division and its checkpoints. |journal=Nat. Rev. Mol. Cell Biol. |volume=2 |issue= 1 |pages= 21-32 |year= 2001 |pmid= 11413462 |doi= 10.1038/35048096 }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 4, 2007 9:36:50 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = PBB_Protein_CALR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hhn.
| PDB = {{PDB2|1hhn}}, {{PDB2|1k91}}, {{PDB2|1k9c}}
| Name = Calreticulin
| HGNCid = 1455
| Symbol = CALR
| AltSymbols =; FLJ26680; RO; SSA; cC1qR
| OMIM = 109091
| ECnumber =
| Homologene = 37911
| MGIid = 88252
| GeneAtlas_image1 = PBB_GE_CALR_200935_at_tn.png
| GeneAtlas_image2 = PBB_GE_CALR_212953_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CALR_214315_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005788 |text = endoplasmic reticulum lumen}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006611 |text = protein export from nucleus}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0030866 |text = cortical actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0040020 |text = regulation of meiosis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 811
| Hs_Ensembl = ENSG00000179218
| Hs_RefseqProtein = NP_004334
| Hs_RefseqmRNA = NM_004343
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 12910392
| Hs_GenLoc_end = 12916274
| Hs_Uniprot = P27797
| Mm_EntrezGene = 12317
| Mm_Ensembl = ENSMUSG00000003814
| Mm_RefseqmRNA = NM_007591
| Mm_RefseqProtein = NP_031617
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 87731955
| Mm_GenLoc_end = 87736972
| Mm_Uniprot = Q3TVD2
}}
}}
'''Calreticulin''', also known as '''CALR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin but calreticulin is not a Ro/SS-A antigen. Earlier papers referred to calreticulin as an Ro/SS-A antigen but this was later disproven. Increased autoantibody titer against human calreticulin is found in infants with complete congenital heart block of both the IgG and IgM classes.<ref>{{cite web | title = Entrez Gene: CALR calreticulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=811| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coppolino MG, Dedhar S |title=Calreticulin. |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 5 |pages= 553-8 |year= 1998 |pmid= 9693955 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 4, 2007 9:37:25 AM PST}
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{{PBB_Controls
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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 = PBB_Protein_CASP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bmq.
| PDB = {{PDB2|1bmq}}, {{PDB2|1ibc}}, {{PDB2|1ice}}, {{PDB2|1rwk}}, {{PDB2|1rwm}}, {{PDB2|1rwn}}, {{PDB2|1rwo}}, {{PDB2|1rwp}}, {{PDB2|1rwv}}, {{PDB2|1rww}}, {{PDB2|1rwx}}, {{PDB2|1sc1}}, {{PDB2|1sc3}}, {{PDB2|1sc4}}, {{PDB2|2fqq}}, {{PDB2|2h48}}, {{PDB2|2hbq}}, {{PDB2|2hbr}}, {{PDB2|2hby}}, {{PDB2|2hbz}}
| Name = Caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)
| HGNCid = 1499
| Symbol = CASP1
| AltSymbols =; ICE; IL1BC; P45
| OMIM = 147678
| ECnumber =
| Homologene = 7653
| MGIid = 96544
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0008656 |text = caspase activator activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 834
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001214
| Hs_RefseqmRNA = NM_001223
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 12362
| Mm_Ensembl = ENSMUSG00000025888
| Mm_RefseqmRNA = NM_009807
| Mm_RefseqProtein = NP_033937
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 5298517
| Mm_GenLoc_end = 5307285
| Mm_Uniprot = P29452
}}
}}
'''Caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)''', also known as '''CASP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing of this gene results in five transcript variants encoding distinct isoforms.<ref>{{cite web | title = Entrez Gene: CASP1 caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=834| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
INFO: Beginning work on CRYAB... {November 4, 2007 9:37:25 AM PST}
AMBIGUITY: Did not locate an acceptable page to update. {November 4, 2007 9:38:16 AM PST}
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{{PBB_Controls
| update_page = yes
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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 = Crystallin, alpha B
| HGNCid = 2389
| Symbol = CRYAB
| AltSymbols =; CRYA2; CTPP2; HSPB5
| OMIM = 123590
| ECnumber =
| Homologene = 68209
| MGIid = 88516
| GeneAtlas_image1 = PBB_GE_CRYAB_209283_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0030018 |text = Z disc}} {{GNF_GO|id=GO:0043292 |text = contractile fiber}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0007601 |text = visual perception}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1410
| Hs_Ensembl = ENSG00000109846
| Hs_RefseqProtein = NP_001876
| Hs_RefseqmRNA = NM_001885
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 111284560
| Hs_GenLoc_end = 111287704
| Hs_Uniprot = P02511
| Mm_EntrezGene = 12955
| Mm_Ensembl = ENSMUSG00000032060
| Mm_RefseqmRNA = NM_009964
| Mm_RefseqProtein = NP_034094
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 50503555
| Mm_GenLoc_end = 50508863
| Mm_Uniprot = Q52L78
}}
}}
'''Crystallin, alpha B''', also known as '''CRYAB''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.<ref>{{cite web | title = Entrez Gene: CRYAB crystallin, alpha B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1410| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Derham BK, Harding JJ |title=Alpha-crystallin as a molecular chaperone. |journal=Progress in retinal and eye research |volume=18 |issue= 4 |pages= 463-509 |year= 1999 |pmid= 10217480 |doi= }}
*{{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= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 4, 2007 10:03:32 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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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 = PBB_Protein_WRN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2axl.
| PDB = {{PDB2|2axl}}, {{PDB2|2dgz}}, {{PDB2|2e1e}}, {{PDB2|2e1f}}, {{PDB2|2fbt}}, {{PDB2|2fbv}}, {{PDB2|2fbx}}, {{PDB2|2fby}}, {{PDB2|2fc0}}
| Name = Werner syndrome
| HGNCid = 12791
| Symbol = WRN
| AltSymbols =; RECQL2; RECQL3; DKFZp686C2056; RECQ3
| OMIM = 604611
| ECnumber =
| Homologene = 6659
| MGIid = 109635
| GeneAtlas_image1 = PBB_GE_WRN_205667_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003678 |text = DNA helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008026 |text = ATP-dependent helicase activity}} {{GNF_GO|id=GO:0008408 |text = 3'-5' exonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000723 |text = telomere maintenance}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0007568 |text = aging}} {{GNF_GO|id=GO:0040009 |text = regulation of growth rate}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7486
| Hs_Ensembl = ENSG00000165392
| Hs_RefseqProtein = NP_000544
| Hs_RefseqmRNA = NM_000553
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 31010320
| Hs_GenLoc_end = 31150818
| Hs_Uniprot = Q14191
| Mm_EntrezGene = 22427
| Mm_Ensembl = ENSMUSG00000031583
| Mm_RefseqmRNA = XM_986059
| Mm_RefseqProtein = XP_991153
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 34701594
| Mm_GenLoc_end = 34851407
| Mm_Uniprot = Q3TB25
}}
}}
'''Werner syndrome''', also known as '''WRN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the RecQ subfamily and the DEAH (Asp-Glu-Ala-His) subfamily of DNA and RNA helicases. DNA helicases are involved in many aspects of DNA metabolism, including transcription, replication, recombination, and repair. This protein contains a nuclear localization signal in the C-terminus and shows a predominant nucleolar localization. It possesses an intrinsic 3' to 5' DNA helicase activity, and is also a 3' to 5' exonuclease. Based on interactions between this protein and Ku70/80 heterodimer in DNA end processing, this protein may be involved in the repair of double strand DNA breaks. Defects in this gene are the cause of werner syndrome, an autosomal recessive disorder characterized by premature aging.<ref>{{cite web | title = Entrez Gene: WRN Werner syndrome| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7486| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Moser MJ, Oshima J, Monnat RJ |title=WRN mutations in Werner syndrome. |journal=Hum. Mutat. |volume=13 |issue= 4 |pages= 271-9 |year= 1999 |pmid= 10220139 |doi= 10.1002/(SICI)1098-1004(1999)13:4<271::AID-HUMU2>3.0.CO;2-Q }}
*{{cite journal | author=Kastan MB, Lim DS |title=The many substrates and functions of ATM. |journal=Nat. Rev. Mol. Cell Biol. |volume=1 |issue= 3 |pages= 179-86 |year= 2001 |pmid= 11252893 |doi= 10.1038/35043058 }}
*{{cite journal | author=Comai L, Li B |title=The Werner syndrome protein at the crossroads of DNA repair and apoptosis. |journal=Mech. Ageing Dev. |volume=125 |issue= 8 |pages= 521-8 |year= 2005 |pmid= 15336909 |doi= 10.1016/j.mad.2004.06.004 }}
}}
{{refend}}
{{protein-stub}}