Cytoglobin: Difference between revisions

CYGB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1UMO, 1URV, 1URY, 1UT0, 1UX9, 1V5H, 2DC3, 3AG0, 4B3W
Identifiers
Aliases	CYGB, HGB, STAP, cytoglobin
External IDs	OMIM: 608759; MGI: 2149481; HomoloGene: 12706; GeneCards: CYGB; OMA:CYGB - orthologs
Gene location (Human)
Chr.	Chromosome 17 (human)
End	76,551,175 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	116,545,139 bp
RNA expression pattern
	Top expressed in
	cardiac muscle tissue of right atrium; ; myocardium of left ventricle; ; right auricle; ; apex of heart; ; subcutaneous adipose tissue; ; right lobe of thyroid gland; ; left lobe of thyroid gland; ; gastric mucosa; ; canal of the cervix; ; mucosa of ileum;
	Top expressed in
	interventricular septum; ; aortic valve; ; ascending aorta; ; habenula; ; dorsal tegmental nucleus; ; ankle; ; lateral hypothalamus; ; central gray substance of midbrain; ; neural layer of retina; ; medial vestibular nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	fatty acid peroxidase activity; metal ion binding; heme binding; peroxidase activity; catalase activity; nitric oxide dioxygenase activity; oxygen binding; oxygen carrier activity; iron ion binding; protein binding;
Cellular component	cytoplasm; cytosol; neuron projection; neuronal cell body; nuclear speck;
Biological process	response to hypoxia; response to oxidative stress; negative regulation of hepatic stellate cell activation; negative regulation of collagen biosynthetic process; fatty acid oxidation; regulation of nitric-oxide synthase activity; negative regulation of fibroblast migration; cellular oxidant detoxification; oxygen transport;
	Sources:Amigo / QuickGO
Orthologs
	114757
	114886
	ENSG00000161544
	ENSMUSG00000020810
	Q8WWM9
	Q9CX80
	NM_134268
	NM_030206
	NP_599030
	NP_084482
	Wikidata
View/Edit Human	View/Edit Mouse

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Revision as of 22:32, 10 June 2008

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Cytoglobin is the protein product of CYGB, a human and mammalian gene.^[5]

Cytoglobin is a globin molecule located in the brain and most notably utilised in marine mammals. It is thought to be a method of protection under conditions of hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain.^[6]

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References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000161544 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020810 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: CYGB cytoglobin".
^ = "Why Diving Marine Mammals Resist Brain Damage from Low Oxygen". {{cite web}}: Check |url= value (help)

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 | citations =
-*{{cite journal  | author=Kawada N, Kristensen DB, Asahina K, ''et al.'' |title=Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25318-23 |year= 2001 |pmid= 11320098 |doi= 10.1074/jbc.M102630200 }}
+*{{cite journal  | author=Kawada N, Kristensen DB, Asahina K, ''et al.'' |title=Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25318–23 |year= 2001 |pmid= 11320098 |doi= 10.1074/jbc.M102630200 }}
-*{{cite journal  | author=Trent JT, Hargrove MS |title=A ubiquitously expressed human hexacoordinate hemoglobin. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19538-45 |year= 2002 |pmid= 11893755 |doi= 10.1074/jbc.M201934200 }}
+*{{cite journal  | author=Trent JT, Hargrove MS |title=A ubiquitously expressed human hexacoordinate hemoglobin. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19538–45 |year= 2002 |pmid= 11893755 |doi= 10.1074/jbc.M201934200 }}
-*{{cite journal  | author=Burmester T, Ebner B, Weich B, Hankeln T |title=Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. |journal=Mol. Biol. Evol. |volume=19 |issue= 4 |pages= 416-21 |year= 2002 |pmid= 11919282 |doi=  }}
+*{{cite journal  | author=Burmester T, Ebner B, Weich B, Hankeln T |title=Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. |journal=Mol. Biol. Evol. |volume=19 |issue= 4 |pages= 416–21 |year= 2002 |pmid= 11919282 |doi=  }}
-*{{cite journal  | author=Asahina K, Kawada N, Kristensen DB, ''et al.'' |title=Characterization of human stellate cell activation-associated protein and its expression in human liver. |journal=Biochim. Biophys. Acta |volume=1577 |issue= 3 |pages= 471-5 |year= 2002 |pmid= 12359339 |doi=  }}
+*{{cite journal  | author=Asahina K, Kawada N, Kristensen DB, ''et al.'' |title=Characterization of human stellate cell activation-associated protein and its expression in human liver. |journal=Biochim. Biophys. Acta |volume=1577 |issue= 3 |pages= 471–5 |year= 2002 |pmid= 12359339 |doi=  }}
-*{{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  | 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  | author=Sawai H, Kawada N, Yoshizato K, ''et al.'' |title=Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. |journal=Biochemistry |volume=42 |issue= 17 |pages= 5133-42 |year= 2003 |pmid= 12718557 |doi= 10.1021/bi027067e }}
+*{{cite journal  | author=Sawai H, Kawada N, Yoshizato K, ''et al.'' |title=Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. |journal=Biochemistry |volume=42 |issue= 17 |pages= 5133–42 |year= 2003 |pmid= 12718557 |doi= 10.1021/bi027067e }}
-*{{cite journal  | author=Geuens E, Brouns I, Flamez D, ''et al.'' |title=A globin in the nucleus! |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30417-20 |year= 2003 |pmid= 12796507 |doi= 10.1074/jbc.C300203200 }}
+*{{cite journal  | author=Geuens E, Brouns I, Flamez D, ''et al.'' |title=A globin in the nucleus! |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30417–20 |year= 2003 |pmid= 12796507 |doi= 10.1074/jbc.C300203200 }}
-*{{cite journal  | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51713-21 |year= 2004 |pmid= 14530264 |doi= 10.1074/jbc.M309396200 }}
+*{{cite journal  | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51713–21 |year= 2004 |pmid= 14530264 |doi= 10.1074/jbc.M309396200 }}
-*{{cite journal  | author=Schmidt M, Gerlach F, Avivi A, ''et al.'' |title=Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 8063-9 |year= 2004 |pmid= 14660570 |doi= 10.1074/jbc.M310540200 }}
+*{{cite journal  | author=Schmidt M, Gerlach F, Avivi A, ''et al.'' |title=Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 8063–9 |year= 2004 |pmid= 14660570 |doi= 10.1074/jbc.M310540200 }}
-*{{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  | 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  | author=Hünermund G, Schirmacher A, Ringelstein B, ''et al.'' |title=Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy. |journal=Muscle Nerve |volume=29 |issue= 4 |pages= 601-4 |year= 2004 |pmid= 15052627 |doi= 10.1002/mus.20009 }}
+*{{cite journal  | author=Hünermund G, Schirmacher A, Ringelstein B, ''et al.'' |title=Genomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy. |journal=Muscle Nerve |volume=29 |issue= 4 |pages= 601–4 |year= 2004 |pmid= 15052627 |doi= 10.1002/mus.20009 }}
-*{{cite journal  | author=de Sanctis D, Dewilde S, Pesce A, ''et al.'' |title=Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination. |journal=J. Mol. Biol. |volume=336 |issue= 4 |pages= 917-27 |year= 2004 |pmid= 15095869 |doi=  }}
+*{{cite journal  | author=de Sanctis D, Dewilde S, Pesce A, ''et al.'' |title=Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination. |journal=J. Mol. Biol. |volume=336 |issue= 4 |pages= 917–27 |year= 2004 |pmid= 15095869 |doi=  }}
-*{{cite journal  | author=Sugimoto H, Makino M, Sawai H, ''et al.'' |title=Structural basis of human cytoglobin for ligand binding. |journal=J. Mol. Biol. |volume=339 |issue= 4 |pages= 873-85 |year= 2004 |pmid= 15165856 |doi= 10.1016/j.jmb.2004.04.024 }}
+*{{cite journal  | author=Sugimoto H, Makino M, Sawai H, ''et al.'' |title=Structural basis of human cytoglobin for ligand binding. |journal=J. Mol. Biol. |volume=339 |issue= 4 |pages= 873–85 |year= 2004 |pmid= 15165856 |doi= 10.1016/j.jmb.2004.04.024 }}
-*{{cite journal  | author=Fago A, Hundahl C, Dewilde S, ''et al.'' |title=Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44417-26 |year= 2004 |pmid= 15299006 |doi= 10.1074/jbc.M407126200 }}
+*{{cite journal  | author=Fago A, Hundahl C, Dewilde S, ''et al.'' |title=Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. |journal=J. Biol. Chem. |volume=279 |issue= 43 |pages= 44417–26 |year= 2004 |pmid= 15299006 |doi= 10.1074/jbc.M407126200 }}
-*{{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  | 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  | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=Hyperthermal stability of neuroglobin and cytoglobin. |journal=FEBS J. |volume=272 |issue= 8 |pages= 2076-84 |year= 2005 |pmid= 15819897 |doi= 10.1111/j.1742-4658.2005.04635.x }}
+*{{cite journal  | author=Hamdane D, Kiger L, Dewilde S, ''et al.'' |title=Hyperthermal stability of neuroglobin and cytoglobin. |journal=FEBS J. |volume=272 |issue= 8 |pages= 2076–84 |year= 2005 |pmid= 15819897 |doi= 10.1111/j.1742-4658.2005.04635.x }}
-*{{cite journal  | author=Sawai H, Makino M, Mizutani Y, ''et al.'' |title=Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin. |journal=Biochemistry |volume=44 |issue= 40 |pages= 13257-65 |year= 2006 |pmid= 16201751 |doi= 10.1021/bi050997o }}
+*{{cite journal  | author=Sawai H, Makino M, Mizutani Y, ''et al.'' |title=Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin. |journal=Biochemistry |volume=44 |issue= 40 |pages= 13257–65 |year= 2006 |pmid= 16201751 |doi= 10.1021/bi050997o }}
-*{{cite journal  | author=Shaw RJ, Liloglou T, Rogers SN, ''et al.'' |title=Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing. |journal=Br. J. Cancer |volume=94 |issue= 4 |pages= 561-8 |year= 2006 |pmid= 16449996 |doi= 10.1038/sj.bjc.6602972 }}
+*{{cite journal  | author=Shaw RJ, Liloglou T, Rogers SN, ''et al.'' |title=Promoter methylation of P16, RARbeta, E-cadherin, cyclin A1 and cytoglobin in oral cancer: quantitative evaluation using pyrosequencing. |journal=Br. J. Cancer |volume=94 |issue= 4 |pages= 561–8 |year= 2006 |pmid= 16449996 |doi= 10.1038/sj.bjc.6602972 }}
-*{{cite journal  | author=McRonald FE, Liloglou T, Xinarianos G, ''et al.'' |title=Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression. |journal=Hum. Mol. Genet. |volume=15 |issue= 8 |pages= 1271-7 |year= 2006 |pmid= 16510494 |doi= 10.1093/hmg/ddl042 }}
+*{{cite journal  | author=McRonald FE, Liloglou T, Xinarianos G, ''et al.'' |title=Down-regulation of the cytoglobin gene, located on 17q25, in tylosis with oesophageal cancer (TOC): evidence for trans-allele repression. |journal=Hum. Mol. Genet. |volume=15 |issue= 8 |pages= 1271–7 |year= 2006 |pmid= 16510494 |doi= 10.1093/hmg/ddl042 }}
-*{{cite journal  | author=Xinarianos G, McRonald FE, Risk JM, ''et al.'' |title=Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer. |journal=Hum. Mol. Genet. |volume=15 |issue= 13 |pages= 2038-44 |year= 2006 |pmid= 16698880 |doi= 10.1093/hmg/ddl128 }}
+*{{cite journal  | author=Xinarianos G, McRonald FE, Risk JM, ''et al.'' |title=Frequent genetic and epigenetic abnormalities contribute to the deregulation of cytoglobin in non-small cell lung cancer. |journal=Hum. Mol. Genet. |volume=15 |issue= 13 |pages= 2038–44 |year= 2006 |pmid= 16698880 |doi= 10.1093/hmg/ddl128 }}
 }}
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Revision as of 22:32, 10 June 2008

References

Further reading