関: gamma-globin、globin

WordNet

to remain unmolested, undisturbed, or uninterrupted -- used only in infinitive form; "let her be"
work in a specific place, with a specific subject, or in a specific function; "He is a herpetologist"; "She is our resident philosopher" (同)follow
have life, be alive; "Our great leader is no more"; "My grandfather lived until the end of war" (同)live
be identical to; be someone or something; "The president of the company is John Smith"; "This is my house"
happen, occur, take place; "I lost my wallet; this was during the visit to my parents house"; "There were two hundred people at his funeral"; "There was a lot of noise in the kitchen"
have the quality of being; (copula, used with an adjective or a predicate noun); "John is rich"; "This is not a good answer"
occupy a certain position or area; be somewhere; "Where is my umbrella?" "The toolshed is in the back"; "What is behind this behavior?"
spend or use time; "I may be an hour"
stake on the outcome of an issue; "I bet $100 on that new horse"; "She played all her money on the dark horse" (同)wager, play
the act of gambling; "he did it on a bet" (同)wager
maintain with or as if with a bet; "I bet she will be there!" (同)wager
second in order of importance; "the candidate, considered a beta male, was perceived to be unable to lead his party to victory"
the 2nd letter of the Greek alphabet
preliminary or testing stage of a software or hardware product; "a beta version"; "beta software"
a colorless protein obtained by removing heme from hemoglobin; the oxygen carrying compound in red blood cells (同)hematohiston, haematohiston

PrepTutorEJDIC

《連結語として補語を伴なって…『である』,…だ,…です / 《位置・場所を表す語句を伴って》(…に)『ある』,いる(occupy a place or situation) / 〈物事が〉『存在する』,ある(exist);〈生物が〉生存する,生きている(live) / 行われる,起こる,発生する(take place, occur) / 存続する,そのままでいる(remain as before) / 《『be to』 do》 / …する予定である,…することになっている / …すべきだ / 《受動態の不定詞を伴って》…できる / 《命令》…するのだ / 《条件節に》…する意図がある / 《『if…were to』 do》…するとしたなら / 《『be』 do『ing』》《進行形》 / 《進行中の動作》…している,しつつある / 《近い未来》…しようとしている,するつもり / 《動作の反復》(いつも)…している / 《『be』+『他動詞の過去分詞』》《受動態》…される,されている / 《『be』+『自動詞の過去分詞』》《完了形》…した[状態にある]
『かけ』・(…との)かけ《+『with』+『名』》 / かけた物(金) / かけの対象 / 〈金・物〉'を'『かける』 / (かけ事・ゲームなどで)〈人〉‘と'『かけをする』《+『名』〈人〉+『on』+『名』》 / (…に)『かける』《+『on』(『against』)+『名』(one's do『ing』)》
ベータ(ギリシア語アルファベットの第2文字;B,β;英語のB,b に遭当)
(液体の)小滴,しずく / (粘土・クリームなどの)球形の固まり

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/19 10:30:42」(JST)

wiki en

Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA.^[1] It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains.

HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria.^[2]^[3]

Gene locus

HBB protein is produced by the gene HBB which is located in the multigene locus of β-globin locus on chromosome 11, specifically on the short arm position 15.5. Expression of beta globin and the neighbouring globins in the β-globin locus is controlled by single locus control region (LCR), the most important regulatory element in the locus located upstream of the globin genes.^[4] The normal allelic variant is 1600 base pairs (bp) long and contains three exons. The order of the genes in the beta-globin cluster is 5' - epsilon – gamma-G – gamma-A – delta – beta - 3'.^[1]

Interactions

HBB interacts with Hemoglobin, alpha 1 (HBA1) to form haemoglobin A, the major haemoglobin in adult humans.^[5]^[6] The interaction is two-fold. First, one HBB and one HBA1 combine to form a single polypetide chain (dimer). Secondly, two dimers combine to form a larger polypeptide (tetramer), and this becomes the functional haemolglobin.^[7]

Associated genetic disorders

Beta thalassemia

Total or partial absence of HBB causes a genetic disease called beta thalassemia. Total loss called, thalassemia major or beta-0-thalassemia, is due to mutation in both alleles, and this results in failure to form beta chain of haemoglobin. It prevents oxygen supply in the tissues. It is highly lethal. Symptoms, such as severe anaemia and heart attack, appear within two years after birth. They can be treated only by life-long blood transfusion and bone marrow transplantation.^[8]^[9] Reduced HBB function called thalassemia minor or beta+ thalassemia is due to mutation in one of the alleles. It is less severe but patients are prone to other diseases such as asthma and liver problems.^[10]

According to a recent study, the stop gain mutation Gln40stop in HBB gene is a common cause of autosomal recessive Beta- thalassemia in Sardinian people(almost exclusive in Sardinia). Carriers of this mutation show a enhaced red blood cell count. As a curiosity, the same mutation was also associated to a decrease in serum LDL levels in carriers, so the authors suggest that is due to the need of cholesterol to regenerate cell membranes.^[11]

Haemoglobin C

Sickle cell disease is closely related to another mutant haemoglobin called haemoglobin C (HbC), because they can be inherited together.^[12] HbC mutation is at the same position in HBB, but glutamic acid is replaced by lysine (β6Glu→Lys). The mutation is particularly prevalent in West African populations. HbC provides near full protection against Plasmodium falciparum in homozygous (CC) individuals and intermediate protection in heterozygous (AC) individuals.^[13] This indicates that HbC has stronger influence than HbS, and is predicted to replace HbS in malaria-endemic regions.^[14]

Haemoglobin E

Another point mutation in HBB, in which glutamic acid is replaced with lysine at position 26 (β26Glu→Lys), leads to the formation of haemoglobin E (HbE).^[15] HbE has a very unstable α- and β-globin association. Even though the unstable protein itself has mild effect, inherited with HbS and thalassemia traits, it turns into a life-threatening form of β-thalassemia. The mutation is of relatively recent origin suggesting that it resulted from selective pressure against severe falciparum malaria, as heterozygous allele prevents the development of malaria.^[16]

Sickle cell disease

More than a thousand naturally occurring HBB variants have been discovered. The most common is HbS, which causes sickle cell disease. HbS is produced by a point mutation in HBB in which the codon GAG is replaced by GTG. This results in the replacement of hydrophilic amino acid glutamic acid with the hydrophobic amino acid valine at the sixth position (β6Glu→Val). This substitution creates a hydrophobic spot on the outside of the protein that sticks to the hydrophobic region of an adjacent haemoglobin molecule's beta chain. This further causes clumping of HbS molecules into rigid fibers, causing "sickling" of the entire red blood cells in the homozygous (HbS/HbS) condition.^[17] Homozygous allele has become one of the deadliest genetic factors.^[18] Whereas, people heterozygous for the mutant allele (HbS/HbA) are resistant to malaria and develop minimal effects of the anaemia.^[19]

Human evolution

Malaria due to Plasmodium falciparum is a major selective factor in human evolution.^[3]^[20] It has influenced mutations in HBB in various degrees resulting in the existence of numerous HBB variants. Some of these mutations are not directly lethal and instead confer resistance to malaria, particularly in Africa where malaria is epidemic.^[21] People of African descent have evolved to have higher rates of the mutant HBB because the heterozygous individuals have a misshaped red blood cell that prevent attacks from malarial parasites. Thus, HBB mutants are the sources of positive selection in these regions and are important for their long-term survival.^[2]^[22] Such selection markers are important for tracing human ancestry and diversification from Africa.^[23]

References

^ ^a ^b "Entrez Gene: HBB hemoglobin, beta".
^ ^a ^b Sabeti, Pardis C (2008). "Natural selection: uncovering mechanisms of evolutionary adaptation to infectious disease". Nature Education 1 (1): 13.
^ ^a ^b Kwiatkowski DP (2005). "How malaria has affected the human genome and what human genetics can teach us about malaria". The American Journal of Human Genetics 77 (2): 171–192. doi:10.1086/432519. PMC: 1224522. PMID 16001361.
^ Levings PP, Bungert J (2002). "The human beta-globin locus control region". Eur. J. Biochem. 269 (6): 1589–99. doi:10.1046/j.1432-1327.2002.02797.x. PMID 11895428.
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–968. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
^ Shaanan B (1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. (ENGLAND) 171 (1): 31–59. doi:10.1016/S0022-2836(83)80313-1. ISSN 0022-2836. PMID 6644819.
^ "Hemoglobin Synthesis". harvard.edu. Harvard University. 2002. Retrieved 18 November 2014.
^ Muncie HL, Campbell J (2009). "Alpha and beta thalassemia". American Family Physician 80 (4): 339–44. PMID 19678601.
^ "Beta thalassemia". Genetics Home Reference. U.S. National Library of Medicine. 11 November 2014. Retrieved 18 November 2014.
^ Valenti L, Canavesi E, Galmozzi E, Dongiovanni P, Rametta R, Maggioni P, Maggioni M, Fracanzani AL, Fargion S (2010). "Beta-globin mutations are associated with parenchymal siderosis and fibrosis in patients with non-alcoholic fatty liver disease". Journal of Hepatology 53 (5): 927–933. doi:10.1016/j.jhep.2010.05.023. PMID 20739079.
^ Sidore, C., y colaboradores (2015). "Genome sequencing elucidates Sardinian genetic architecture and augments association analyses for lipid and blood inflammatory markers". Nature Genetics 47: 1272–1281. doi:10.1038/ng.3368.
^ Piel FB, Howes RE, Patil AP, Nyangiri OA, Gething PW, Bhatt S, Williams TN, Weatherall DJ, Hay SI (2013). "The distribution of haemoglobin C and its prevalence in newborns in Africa". Scientific Reports 3 (1671). doi:10.1038/srep01671. PMC: 3628164. PMID 23591685.
^ Modiano D, Luoni G, Sirima BS, Simporé J, Verra F, Konaté A, Rastrelli E, Olivieri A, Calissano C, Paganotti GM, D'Urbano L, Sanou I, Sawadogo A, Modiano G, Coluzzi M (2001). "Haemoglobin C protects against clinical Plasmodium falciparum malaria". Nature 414 (6861): 305–308. doi:10.1038/35104556. PMID 11713529.
^ Verra F, Bancone G, Avellino P, Blot I, Simporé J, Modiano D (2007). "Haemoglobin C and S in natural selection against Plasmodium falciparum malaria: a plethora or a single shared adaptive mechanism?". Parassitologia 49 (4): 209–13. PMID 18689228.
^ Olivieri NF, Pakbaz Z, Vichinsky E (2011). "Hb E/beta-thalassaemia: a common & clinically diverse disorder". The Indian Journal of Medical Research 134 (4): 522–531. PMC: 3237252. PMID 22089616.
^ Chotivanich K, Udomsangpetch R, Pattanapanyasat K, Chierakul W, Simpson J, Looareesuwan S, White N (2002). "Hemoglobin E: a balanced polymorphism protective against high parasitemias and thus severe P falciparum malaria". Blood 100 (4): 1172–1176. PMID 12149194.
^ Thom CS, Dickson CF, Gell DA, Weiss MJ (2013). "Hemoglobin variants: biochemical properties and clinical correlates". Cold Spring Harb Perspect Med 3 (3): a011858. doi:10.1101/cshperspect.a011858. PMID 23388674.
^ Lozano R, Naghavi M, Foreman K, Lim S, Shibuya K, Aboyans V, Abraham J, Adair T, Aggarwal R, Ahn SY, Alvarado M, Anderson HR, Anderson LM, Andrews KG, Atkinson C, Baddour LM, Barker-Collo S, Bartels DH, Bell ML, Benjamin EJ, Bennett D, Bhalla K, Bikbov B, Bin Abdulhak A, Birbeck G, Blyth F, Bolliger I, Boufous S, Bucello C, Burch M, Burney P, Carapetis J, Chen H, Chou D, Chugh SS, Coffeng LE, Colan SD, Colquhoun S, Colson KE, Condon J, Connor MD, Cooper LT, Corriere M, Cortinovis M, de Vaccaro KC, Couser W, Cowie BC, Criqui MH, Cross M, Dabhadkar KC, Dahodwala N, De Leo D, Degenhardt L, Delossantos A, Denenberg J, Des Jarlais DC, Dharmaratne SD, Dorsey ER, Driscoll T, Duber H, Ebel B, Erwin PJ, Espindola P, Ezzati M, Feigin V, Flaxman AD, Forouzanfar MH, Fowkes FG, Franklin R, Fransen M, Freeman MK, Gabriel SE, Gakidou E, Gaspari F, Gillum RF, Gonzalez-Medina D, Halasa YA, Haring D, Harrison JE, Havmoeller R, Hay RJ, Hoen B, Hotez PJ, Hoy D, Jacobsen KH, James SL, Jasrasaria R, Jayaraman S, Johns N, Karthikeyan G, Kassebaum N, Keren A, Khoo JP, Knowlton LM, Kobusingye O, Koranteng A, Krishnamurthi R, Lipnick M, Lipshultz SE, Ohno SL, Mabweijano J, MacIntyre MF, Mallinger L, March L, Marks GB, Marks R, Matsumori A, Matzopoulos R, Mayosi BM, McAnulty JH, McDermott MM, McGrath J, Mensah GA, Merriman TR, Michaud C, Miller M, Miller TR, Mock C, Mocumbi AO, Mokdad AA, Moran A, Mulholland K, Nair MN, Naldi L, Narayan KM, Nasseri K, Norman P, O'Donnell M, Omer SB, Ortblad K, Osborne R, Ozgediz D, Pahari B, Pandian JD, Rivero AP, Padilla RP, Perez-Ruiz F, Perico N, Phillips D, Pierce K, Pope CA, Porrini E, Pourmalek F, Raju M, Ranganathan D, Rehm JT, Rein DB, Remuzzi G, Rivara FP, Roberts T, De León FR, Rosenfeld LC, Rushton L, Sacco RL, Salomon JA, Sampson U, Sanman E, Schwebel DC, Segui-Gomez M, Shepard DS, Singh D, Singleton J, Sliwa K, Smith E, Steer A, Taylor JA, Thomas B, Tleyjeh IM, Towbin JA, Truelsen T, Undurraga EA, Venketasubramanian N, Vijayakumar L, Vos T, Wagner GR, Wang M, Wang W, Watt K, Weinstock MA, Weintraub R, Wilkinson JD, Woolf AD, Wulf S, Yeh PH, Yip P, Zabetian A, Zheng ZJ, Lopez AD, Murray CJ, AlMazroa MA, Memish ZA (2012). "Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010". Lancet 380 (9859): 2095–128. doi:10.1016/S0140-6736(12)61728-0. PMID 23245604.
^ Luzzatto L (2012). "Sickle cell anaemia and malaria". Mediterr J Hematol Infect Dis 4 (1): e2012065. doi:10.4084/MJHID.2012.065. PMC: 3499995. PMID 23170194.
^ Verra F, Mangano VD, Modiano D (2009). "Genetics of susceptibility to Plasmodium falciparum: from classical malaria resistance genes towards genome-wide association studies.". Parasite Immunology 31 (5): 234–53. doi:10.1111/j.1365-3024.2009.01106.x. PMID 19388945.
^ Tishkoff SA, Williams SM (2002). "Genetic analysis of African populations: human evolution and complex disease.". Nature Reviews Genetics 3 (8): 611–21. doi:10.1038/nrg865. PMID 12154384.
^ Excoffier L (2002). "Human demographic history: refining the recent African origin model". Current Opinion in Genetics & Development 12 (6): 675–682. doi:10.1016/S0959-437X(02)00350-7. PMID 12433581.
^ Reed FA, Tishkoff SA (2006). "African human diversity, origins and migrations". Current Opinion in Genetics & Development 16 (6): 597–605. doi:10.1016/j.gde.2006.10.008. PMID 17056248.

UpToDate Contents

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1. βサラセミアの病態生理 pathophysiology of beta thalassemia
2. 鎌状細胞貧血における臨床的ばらつき clinical variability in sickle cell anemia
3. αサラセミアの病態生理 pathophysiology of alpha thalassemia
4. サラセミア症候群の分子病理 molecular pathology of the thalassemic syndromes
5. 正常なヘモグロビンの構造および機能 structure and function of normal hemoglobins

English Journal

Prenatal diagnosis of sickle cell disease by the technique of PCR.

Singh PJ1, Shrivastava AC1, Shrikhande AV1.
Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion.Indian J Hematol Blood Transfus.2015 Jun;31(2):233-41. doi: 10.1007/s12288-014-0427-8. Epub 2014 Jul 8.
Sickle cell disease (SCD) is prevalent in Central India and causes major morbidity and mortality. There is a lack of prenatal diagnostic facility near population affected with SCD. This is the pilot study in our region with the aim to establish prenatal diagnostic facility for the couples carrying s
PMID 25825564

Novel Βeta (β)-Thalassemia Mutation in Turkish Children.

Ulasli M1, Oztuzcu S1, Kirkbes S1, Bay A2, Igci YZ1, Bayraktar R1, Igci M1, Ergun S1, Cakmak EA1, Aytekin E2, Arslan A1.
Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion.Indian J Hematol Blood Transfus.2015 Jun;31(2):218-22. doi: 10.1007/s12288-014-0380-6. Epub 2014 Apr 11.
Beta (β)-thalassemia is the most frequently observed hereditary blood disorder in the world. It is characterized by deficiency of hemoglobin β-globin gene and is also a profoundly heterogeneous both at the molecular and clinical level. In the case of β-thalassemia, there is reduced (β(+) type) o
PMID 25825561

Effects of α-thalassaemia mutations on the haematological parameters of β-thalassaemia carriers.

Saleh-Gohari N1, Khademi Bami M2, Nikbakht R3, Karimi-Maleh H4.
Journal of clinical pathology.J Clin Pathol.2015 May 2. pii: jclinpath-2014-202825. doi: 10.1136/jclinpath-2014-202825. [Epub ahead of print]
BACKGROUND: Thalassaemia is a haemoglobin disorder caused by a reduction in, or a complete absence of, the production of α- or β-globin genes. Detection of β-thalassaemia carriers is the first step in the prenatal diagnosis of the disease and is based primarily on the differences between levels o
PMID 25935548

Japanese Journal

Identification of an evolutionarily conserved, functional noncoding element regulated by Six1 homeoprotein

Jeong Yongsu,Oh Sangtaek
Genes & genetic systems 85(3), 233-240, 2010-06-25
… To address their regulatory potential, each of the Six1-bound sequences was cloned into a reporter cassette containing beta-globin minimal promoter and lacZ gene and assayed for enhancer activity in transgenic mouse embryos. …
NAID 10029515218

Analysis of murine S-glutathionyl hemoglobins and beta globin haplotype by dynamic capillary isoelectric focusing

HEMPE James M.,MCGEHEE Amanda M.,STOYANOV Alexandre V.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 877(28), 3462-3466, 2009-10-15
NAID 10028027442

Clinical and hematological characteristics of uncommon beta-globin variants in Thailand

UAPRASERT Noppacharn,ROJNUCKARIN Ponlapat,SETTAPIBOON Rung,AMORNSIRIWAT Supaporn,SUTCHARITCHAN Pranee
International journal of hematology 89(5), 568-571, 2009-06-15
NAID 10025161659

Related Pictures

★リンクテーブル★

リンク元	「βグロビン」「gamma-globin」「β-グロビン」
関連記事	「globin」「beta」「be」

「βグロビン」

Hemoglobin, beta
	HBB structure based on PyMOL rendering of PDB 1a00
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1A00, 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CBL, 1CBM, 1CH4, 1CLS, 1CMY, 1COH, 1DKE, 1DXT, 1DXU, 1DXV, 1FN3, 1G9V, 1GBU, 1GBV, 1GLI, 1GZX, 1HAB, 1HAC, 1HBA, 1HBB, 1HBS, 1HCO, 1HDB, 1HGA, 1HGB, 1HGC, 1HHO, 1IRD, 1J3Y, 1J3Z, 1J40, 1J41, 1J7S, 1J7W, 1J7Y, 1JY7, 1K0Y, 1K1K, 1KD2, 1LFL, 1LFQ, 1LFT, 1LFV, 1LFY, 1LFZ, 1LJW, 1M9P, 1MKO, 1NEJ, 1NIH, 1NQP, 1O1I, 1O1J, 1O1K, 1O1L, 1O1M, 1O1N, 1O1O, 1O1P, 1QI8, 1QSH, 1QSI, 1QXD, 1QXE, 1R1X, 1R1Y, 1RPS, 1RQ3, 1RQ4, 1RQA, 1RVW, 1SDK, 1SDL, 1THB, 1UIW, 1VWT, 1XXT, 1XY0, 1XYE, 1XZ2, 1XZ4, 1XZ5, 1XZ7, 1XZU, 1XZV, 1Y09, 1Y0A, 1Y0C, 1Y0D, 1Y0T, 1Y0W, 1Y22, 1Y2Z, 1Y31, 1Y35, 1Y45, 1Y46, 1Y4B, 1Y4F, 1Y4G, 1Y4P, 1Y4Q, 1Y4R, 1Y4V, 1Y5F, 1Y5J, 1Y5K, 1Y7C, 1Y7D, 1Y7G, 1Y7Z, 1Y83, 1Y85, 1Y8W, 1YDZ, 1YE0, 1YE1, 1YE2, 1YEN, 1YEO, 1YEQ, 1YEU, 1YEV, 1YFF, 1YG5, 1YGD, 1YGF, 1YH9, 1YHE, 1YHR, 1YIE, 1YIH, 1YVQ, 1YVT, 1YZI, 2D5Z, 2D60, 2DN1, 2DN2, 2DN3, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHB, 2HHD, 2HHE, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HHB, 3HXN, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3ONZ, 3OO4, 3OO5, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 3S65, 3S66, 3SZK, 3W4U, 4FC3, 4HHB, 6HBW
Identifiers
Symbols	HBB ; CD113t-C; beta-globin
External IDs	OMIM: 141900 MGI: 96022 HomoloGene: 68066 ChEMBL: 4331 GeneCards: HBB Gene
Gene ontology
Molecular function	• peroxidase activity; • oxygen transporter activity; • iron ion binding; • protein binding; • oxygen binding; • heme binding; • hemoglobin binding; • haptoglobin binding;
Cellular component	• extracellular region; • cytosol; • hemoglobin complex; • haptoglobin-hemoglobin complex; • endocytic vesicle lumen;
Biological process	• blood coagulation; • regulation of blood pressure; • positive regulation of cell death; • oxygen transport; • bicarbonate transport; • nitric oxide transport; • response to hydrogen peroxide; • hydrogen peroxide catabolic process; • small molecule metabolic process; • positive regulation of nitric oxide biosynthetic process; • regulation of blood vessel size; • protein heterooligomerization; • renal absorption;
	Sources: Amigo / QuickGO
Orthologs
	v; t; e;