What Is A Chromosome Apex

Poly peptide-coding gene in the species Man sapiens

APEX1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BIX, 1CQH, 4LND, 4QH9, 5DFF, 4QHD, 1E9N, 3U8U, 5DFI, 1HD7, 5DG0, 5DFJ, 4QHE, 5DFH, 1DE9, 4IEM, 2ISI, 1DE8, 2O3H, 1CQG, 1DEW, 5CFG
Identifiers
Aliases	APEX1, APE, APE1, APEN, Apex, APX, HAP1, REF1, apurinic/apyrimidinic endodeoxyribonuclease 1
External IDs	OMIM: 107748 MGI: 88042 HomoloGene: 1241 GeneCards: APEX1
Factor location (Man) Chr. Chromosome 14 (human)[1] Band 14q11.2 Start twenty,455,191 bp[ane] End xx,457,772 bp[one]
Cistron location (Mouse) Chr. Chromosome 14 (mouse)[two] Band xiv C1|14 26.three cM Start 51,162,425 bp[2] End 51,164,596 bp[2]
RNA expression design Bgee Homo Mouse (ortholog) Top expressed in ganglionic eminence islet of Langerhans Right adrenal gland gallbladder rectum stromal jail cell of endometrium parietal pleura body of stomach appendix lymph node Top expressed in archaic streak internal carotid artery external carotid avenue abdominal wall condyle maxillary prominence medial ganglionic eminence pilus follicle Paneth jail cell fossa More reference expression data BioGPS More reference expression data
Cistron ontology Molecular function DNA binding nuclease activity endonuclease activity hydrolase activity metal ion bounden lyase activity class I DNA-(apurinic or apyrimidinic site) endonuclease activity poly peptide-containing complex binding poly peptide binding exonuclease activity phosphodiesterase I activeness double-stranded Deoxyribonucleic acid 3'-five' exodeoxyribonuclease activity endodeoxyribonuclease activity chromatin Deoxyribonucleic acid binding endoribonuclease activity uracil Deoxyribonucleic acid N-glycosylase activity phosphoric diester hydrolase activity site-specific endodeoxyribonuclease activity, specific for altered base double-stranded telomeric DNA binding oxidoreductase activity double-stranded Dna exodeoxyribonuclease activity transcription coactivator action NF-kappaB binding RNA-DNA hybrid ribonuclease activeness damaged DNA bounden transcription corepressor activity 3'-five' exonuclease activity DNA-(apurinic or apyrimidinic site) endonuclease activeness RNA binding class III/Four Deoxyribonucleic acid-(apurinic or apyrimidinic site) endonuclease activity Cellular component cytoplasm centrosome intracellular anatomical construction mitochondrion nucleus perinuclear region of cytoplasm ribosome transcription regulator complex nuclear speck nucleoplasm nucleolus endoplasmic reticulum Biological process Dna repair nucleic acid phosphodiester bond hydrolysis cellular response to Dna damage stimulus DNA recombination positive regulation of G1/South transition of mitotic cell bike negative regulation of smooth musculus cell migration regulation of transcription, DNA-templated Deoxyribonucleic acid demethylation cellular response to army camp RNA phosphodiester bond hydrolysis, endonucleolytic transcription, Deoxyribonucleic acid-templated response to organonitrogen compound cellular response to hydrogen peroxide cellular response to peptide hormone stimulus regulation of mRNA stability cellular response to organonitrogen compound cell redox homeostasis ageing base-excision repair telomere maintenance negative regulation of nucleic acid-templated transcription telomere maintenance via base-excision repair regulation of apoptotic process positive regulation of nucleic acrid-templated transcription Sources:Amigo / QuickGO
Orthologs Species Man Mouse Entrez 328 11792 Ensembl ENSG00000100823 ENSMUSG00000035960 UniProt P27695 P28352 RefSeq (mRNA) NM_001244249 NM_001641 NM_080648 NM_080649 NM_009687 RefSeq (protein) NP_001231178 NP_001632 NP_542379 NP_542380 NP_033817 Location (UCSC) Chr 14: 20.46 – 20.46 Mb Chr fourteen: 51.16 – 51.16 Mb PubMed search [three] [4]
Wikidata
View/Edit Human View/Edit Mouse

DNA-(apurinic or apyrimidinic site) lyase is an enzyme that in humans is encoded by the APEX1 gene.

Apurinic/apyrimidinic (AP) sites (besides called "abasic sites") occur frequently in DNA molecules by spontaneous hydrolysis, by Deoxyribonucleic acid damaging agents or by Dna glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal Deoxyribonucleic acid replication. All cells, from simple prokaryotes to humans, have evolved systems to identify and repair such sites. Class 2 AP endonucleases cleave the phosphodiester backbone 5' to the AP site, thereby initiating a procedure known equally base excision repair (BER). The Apex gene (alternatively named APE1, HAP1, APEN) encodes the major AP endonuclease in human cells. Splice variants have been found for this factor; all encode the same protein.^[v]

Interactions [edit]

APEX1 has been shown to collaborate with MUTYH,^[6] Flap construction-specific endonuclease ane^[7] and XRCC1.^[viii]

Crumbling [edit]

Deficiency of APEX1 causes accummulation of DNA damage leading to both cellular senescence and features of premature aging.^[ix] This finding is consistent with the theory that DNA harm is a primary crusade of aging.^[10]

References [edit]

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000100823 - Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000035960 - Ensembl, May 2017
3. ^ "Homo PubMed Reference:". National Center for Biotechnology Information, U.South. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Middle for Biotechnology Information, U.Due south. National Library of Medicine.
5. ^ "Entrez Factor: APEX1 Noon nuclease (multifunctional Dna repair enzyme) one".
6. ^ Parker A, Gu Y, Mahoney Westward, Lee SH, Singh KK, Lu AL (February 2001). "Human being homolog of the MutY repair poly peptide (hMYH) physically interacts with proteins involved in long patch DNA base excision repair". The Periodical of Biological Chemical science. 276 (eight): 5547–55. doi:10.1074/jbc.M008463200. PMID 11092888.
7. ^ Dianova Two, Bohr VA, Dianov GL (October 2001). "Interaction of man AP endonuclease 1 with flap endonuclease ane and proliferating cell nuclear antigen involved in long-patch base excision repair". Biochemistry. xl (42): 12639–44. doi:x.1021/bi011117i. PMID 11601988.
8. ^ Vidal AE, Boiteux S, Hickson ID, Radicella JP (November 2001). "XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions". The EMBO Journal. xx (22): 6530–nine. doi:10.1093/emboj/twenty.22.6530. PMC125722. PMID 11707423.
9. ^ Li One thousand, Yang X, Lu X, Dai Northward, Zhang Southward, Cheng Y, et al. (June 2018). "APE1 deficiency promotes cellular senescence and premature aging features". Nucleic Acids Enquiry. 46 (xi): 5664–5677. doi:x.1093/nar/gky326. PMC6009672. PMID 29750271.
10. ^ Gensler HL, Bernstein H (September 1981). "Deoxyribonucleic acid damage as the primary crusade of aging". The Quarterly Review of Biological science. 56 (iii): 279–303. doi:10.1086/412317. PMID 7031747. S2CID 20822805.

Further reading [edit]

• Mol CD, Hosfield DJ, Tainer JA (August 2000). "Abasic site recognition by two apurinic/apyrimidinic endonuclease families in Deoxyribonucleic acid base excision repair: the 3' ends justify the means". Mutation Research. 460 (3–4): 211–29. doi:10.1016/s0921-8777(00)00028-8. PMID 10946230.
• Fritz Thousand (September 2000). "Human APE/Ref-1 protein". The International Journal of Biochemistry & Cell Biology. 32 (9): 925–9. doi:10.1016/S1357-2725(00)00045-5. PMID 11084372.
• Fritz G, Grösch S, Tomicic Yard, Kaina B (Nov 2003). "APE/Ref-one and the mammalian response to genotoxic stress". Toxicology. 193 (1–2): 67–78. doi:10.1016/S0300-483X(03)00290-7. PMID 14599768.
• Tell 1000, Damante G, Caldwell D, Kelley MR (2005). "The intracellular localization of APE1/Ref-i: more than a passive phenomenon?". Antioxidants & Redox Signaling. 7 (iii–four): 367–84. doi:10.1089/ars.2005.7.367. hdl:1805/4802. PMID 15706084.
• Hung RJ, Hall J, Brennan P, Boffetta P (November 2005). "Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review". American Journal of Epidemiology. 162 (10): 925–42. doi:10.1093/aje/kwi318. PMID 16221808.
• Dyrkheeva NS, Khodyreva SN, Lavrik OI (2007). "[Multifunctional homo apurinic/apyrimidinic endonuclease ane: the role of additional functions]". Molekuliarnaia Biologiia. 41 (3): 450–66. PMID 17685223.
• Harrison 50, Ascione G, Menninger JC, Ward DC, Demple B (December 1992). "Human being apurinic endonuclease cistron (APE): structure and genomic mapping (chromosome 14q11.2-12)". Human Molecular Genetics. 1 (nine): 677–eighty. doi:10.1093/hmg/1.nine.677. PMID 1284593.
• Cheng XB, Bunville J, Patterson TA (January 1992). "Nucleotide sequence of a cDNA for an apurinic/apyrimidinic endonuclease from HeLa cells". Nucleic Acids Enquiry. 20 (two): 370. doi:10.1093/nar/20.2.370. PMC310384. PMID 1371347.
• Xanthoudakis S, Miao G, Wang F, Pan YC, Curran T (September 1992). "Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme". The EMBO Journal. 11 (9): 3323–35. doi:ten.1002/j.1460-2075.1992.tb05411.x. PMC556867. PMID 1380454.
• Zhao B, Grandy DK, Hagerup JM, Magenis RE, Smith Fifty, Chauhan BC, Henner WD (August 1992). "The human gene for apurinic/apyrimidinic endonuclease (HAP1): sequence and localization to chromosome xiv band q12". Nucleic Acids Inquiry. 20 (15): 4097–8. doi:10.1093/nar/20.15.4097. PMC334100. PMID 1380694.
• Robson CN, Hochhauser D, Craig R, Rack K, Buckle VJ, Hickson ID (September 1992). "Construction of the human DNA repair factor HAP1 and its localisation to chromosome 14q 11.two-12". Nucleic Acids Inquiry. twenty (17): 4417–21. doi:10.1093/nar/twenty.17.4417. PMC334166. PMID 1383925.
• Seki S, Hatsushika M, Watanabe S, Akiyama 1000, Nagao 1000, Tsutsui K (July 1992). "cDNA cloning, sequencing, expression and possible domain structure of human Noon nuclease homologous to Escherichia coli exonuclease III". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1131 (three): 287–99. doi:x.1016/0167-4781(92)90027-w. PMID 1627644.
• Robson CN, Hickson ID (October 1991). "Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease 3) mutants". Nucleic Acids Enquiry. 19 (20): 5519–23. doi:10.1093/nar/19.20.5519. PMC328951. PMID 1719477.
• Demple B, Herman T, Chen DS (December 1991). "Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of Dna repair enzymes". Proceedings of the National University of Sciences of the The states of America. 88 (24): 11450–4. Bibcode:1991PNAS...8811450D. doi:x.1073/pnas.88.24.11450. PMC53153. PMID 1722334.
• Okazaki T, Chung U, Nishishita T, Ebisu S, Usuda Southward, Mishiro S, Xanthoudakis S, Igarashi T, Ogata Due east (November 1994). "A redox factor protein, ref1, is involved in negative factor regulation past extracellular calcium". The Journal of Biological Chemistry. 269 (45): 27855–62. doi:10.1016/S0021-9258(xviii)46865-2. PMID 7961715.
• Akiyama Thou, Seki S, Oshida T, Yoshida MC (September 1994). "Structure, promoter analysis and chromosomal assignment of the man Apex gene". Biochimica et Biophysica Acta (BBA) - Cistron Structure and Expression. 1219 (1): 15–25. doi:10.1016/0167-4781(94)90241-0. PMID 8086453.
• Andersson B, Wentland MA, Ricafrente JY, Liu Due west, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–thirteen. doi:10.1006/abio.1996.0138. PMID 8619474.
• Chung U, Igarashi T, Nishishita T, Iwanari H, Iwamatsu A, Suwa A, Mimori T, Hata K, Ebisu South, Ogata E, Fujita T, Okazaki T (April 1996). "The interaction between Ku antigen and REF1 protein mediates negative gene regulation past extracellular calcium". The Journal of Biological Chemistry. 271 (15): 8593–8. doi:10.1074/jbc.271.fifteen.8593. PMID 8621488.
• Rothwell DG, Hickson ID (November 1996). "Asparagine 212 is essential for abasic site recognition by the man DNA repair endonuclease HAP1". Nucleic Acids Inquiry. 24 (21): 4217–21. doi:10.1093/nar/24.21.4217. PMC146231. PMID 8932375.
• Izumi T, Henner WD, Mitra S (November 1996). "Negative regulation of the major human AP-endonuclease, a multifunctional protein". Biochemistry. 35 (47): 14679–83. doi:10.1021/bi961995u. PMID 8942627.

External links [edit]

• Human APEX1 genome location and APEX1 gene details folio in the UCSC Genome Browser.

What Is A Chromosome Apex,

Source: https://en.wikipedia.org/wiki/APEX1

Posted by: wyckoffsupuldn.blogspot.com

Share this post