ARS2

ARS2
사용 가능한 구조물
PDB	직교 검색: PDBe RCSB
PDB ID 코드 목록
	1H7D, 1H7J
식별자
별칭	ARS2, ALASE-E, ALASE, ANH1, ASB, XLDP, XLPP, XLSA, SIDBA1, 5'-아미노렐불산염 2
외부 ID	OMIM: 301300 MGI: 87990 호몰로진: 17 GeneCard: ARSA2
유전자 위치(인간)
쳇.	X염색체(인간)
끝	55,030,977 bp
유전자 위치(마우스)
쳇.	X염색체(쥐)
끝	150,195,638 bp
RNA 표현 패턴
	표현된 상단
	골수; ; 폐골.; ; 핏덩어리; ; 간; ; 결장의; ; 뱃속; ; 폐를 끼치다; ; 하트;
	추가 참조 표현식 데이터
	n/a
유전자 온톨로지
분자함수	전이효소 활동; 글리신 제본; GO:0001948 단백질 결합; 촉매 활성; 피리독살 인산염 바인딩; 아킬전달효소 활동; 5-절제결합성분해효소 활동;
셀룰러 컴포넌트	미토콘드리아 행렬; 미토콘드리온; 미토콘드리아 내막;
생물학적 과정	저산소증에 대한 반응; 프로토폴피피린겐 IX 생합성 과정; 생합성 과정; 테트라피롤 생합성 과정; 헤메 생합성 과정; 헤모글로빈 생합성 과정; 적혈구 분화; 신진대사를 하다; 산소동작.; 세포 철 이온 항진; 포르피린 복합 대사 과정;
	출처:아미고 / 퀵고
직교체
	212
	11656
	ENSG00000158578
	ENSMUSG00000025270
	P22557
	P08680
	NM_000032; NM_001037967; NM_001037968; NM_001037969
	NM_001102446; NM_009653
	NP_000023; NP_001033056; NP_001033057
	NP_001095916; NP_033783
	위키다타
인간 보기/편집	마우스 보기/편집

ARS2로도 알려진 델타-아미노레불린체 싱타아제 2는 인간에서 ARS2 유전자에 의해 암호화된 단백질이다.^[5]^[6]^[7]ARS2는 아미노레불린산신타아제다.null

이 유전자의 산물은 적혈구 특이 미토콘드리아에 위치한 효소를 명시한다.암호화된 단백질은 헤메 생합성 경로의 첫 번째 단계를 촉진한다.이 유전자의 결함은 X연계 피리독신 반응 시더블라스틱 빈혈의 원인이 된다.대안으로 서로 다른 ISO 양식을 인코딩하는 분할된 대본 변형이 식별되었다.^[7]null

그것의 유전자는 철분 수치가 너무 낮으면 IRP가 결합하는 5'-UTR 영역에 IRE를 포함하고 있어, 따라서 그것의 번역을 억제한다.null

참조

^ ^a ^b ^c GRCh38: 앙상블 릴리스 89: ENSG00000158578 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리스 89: ENSMUSG000025270 - 앙상블, 2017년 5월
^ "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.
^ Bishop DF, Henderson AS, Astrin KH (Jun 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics. 7 (2): 207–14. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.
^ Cotter PD, Willard HF, Gorski JL, Bishop DF (May 1992). "Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations" (PDF). Genomics. 13 (1): 211–2. doi:10.1016/0888-7543(92)90223-F. hdl:2027.42/30074. PMID 1577484.
^ ^a ^b "Entrez Gene: Delta-aminolevulinate synthase 2".

추가 읽기

Han L, Zhong Y, Huang B, Han L, Pan L, Xu X, Wang X, Huang B, Lu J (2008). "Sodium butyrate activates erythroid-specific 5-aminolevulinate synthase gene through Sp1 elements at its promoter". Blood Cells, Molecules & Diseases. 41 (2): 148–53. doi:10.1016/j.bcmd.2008.04.002. PMID 18555711.
Kaneko K, Furuyama K, Aburatani H, Shibahara S (Mar 2009). "Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling". The FEBS Journal. 276 (5): 1370–82. doi:10.1111/j.1742-4658.2009.06878.x. PMID 19187226.
Cox TC, Sadlon TJ, Schwarz QP, Matthews CS, Wise PD, Cox LL, Bottomley SS, May BK (Feb 2004). "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis". The International Journal of Biochemistry & Cell Biology. 36 (2): 281–95. doi:10.1016/S1357-2725(03)00246-2. PMID 14643893.
Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T (Oct 1999). "A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia". American Journal of Hematology. 62 (2): 112–4. doi:10.1002/(SICI)1096-8652(199910)62:2<112::AID-AJH9>3.0.CO;2-L. PMID 10577279.
Hurford MT, Marshall-Taylor C, Vicki SL, Zhou JZ, Silverman LM, Rezuke WN, Altman A, Tsongalis GJ (Jul 2002). "A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia". Clinica Chimica Acta; International Journal of Clinical Chemistry. 321 (1–2): 49–53. doi:10.1016/S0009-8981(02)00095-5. PMID 12031592.
Bekri S, May A, Cotter PD, Al-Sabah AI, Guo X, Masters GS, Bishop DF (Jul 2003). "A promoter mutation in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causes X-linked sideroblastic anemia". Blood. 102 (2): 698–704. doi:10.1182/blood-2002-06-1623. PMID 12663458.
Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW (Sep 2005). "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans". The EMBO Journal. 24 (18): 3166–77. doi:10.1038/sj.emboj.7600792. PMC 1224682. PMID 16121195.
Cazzola M, May A, Bergamaschi G, Cerani P, Ferrillo S, Bishop DF (Dec 2002). "Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation". Blood. 100 (12): 4236–8. doi:10.1182/blood-2002-03-0685. PMID 12393718.
Sussman NL, Lee PL, Dries AM, Schwartz MR, Barton JC (2008). "Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G". Acta Haematologica. 120 (3): 168–73. doi:10.1159/000181183. PMID 19066423.
Whatley SD, Ducamp S, Gouya L, Grandchamp B, Beaumont C, Badminton MN, Elder GH, Holme SA, Anstey AV, Parker M, Corrigall AV, Meissner PN, Hift RJ, Marsden JT, Ma Y, Mieli-Vergani G, Deybach JC, Puy H (Sep 2008). "C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload". American Journal of Human Genetics. 83 (3): 408–14. doi:10.1016/j.ajhg.2008.08.003. PMC 2556430. PMID 18760763.
Furuyama K, Sassa S (Mar 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia". The Journal of Clinical Investigation. 105 (6): 757–64. doi:10.1172/JCI6816. PMC 377455. PMID 10727444.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
Lee PL, Barton JC, Rao SV, Acton RT, Adler BK, Beutler E (2006). "Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload". Blood Cells, Molecules & Diseases. 36 (2): 292–7. doi:10.1016/j.bcmd.2005.12.004. PMID 16446107.
Bergmann AK, Campagna DR, McLoughlin EM, Agarwal S, Fleming MD, Bottomley SS, Neufeld EJ (Feb 2010). "Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations". Pediatric Blood & Cancer. 54 (2): 273–8. doi:10.1002/pbc.22244. PMC 2843911. PMID 19731322.
Rabstein S, Unfried K, Ranft U, Illig T, Kolz M, Mambetova C, Vlad M, Roman C, Weiss T, Becker D, Brüning T, Pesch B (2008). "Lack of association of delta-aminolevulinate dehydratase polymorphisms with blood lead levels and hemoglobin in Romanian women from a lead-contaminated region". Journal of Toxicology and Environmental Health. Part A. 71 (11–12): 716–24. doi:10.1080/15287390801985190. PMID 18569569.
Abu-Farha M, Niles J, Willmore WG (Oct 2005). "Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition". Biochemistry and Cell Biology. 83 (5): 620–30. doi:10.1139/o05-045. PMID 16234850.
Nachman MW, D'Agostino SL, Tillquist CR, Mobasher Z, Hammer MF (May 2004). "Nucleotide variation at Msn and Alas2, two genes flanking the centromere of the X chromosome in humans". Genetics. 167 (1): 423–37. doi:10.1534/genetics.167.1.423. PMC 1470878. PMID 15166166.

외부 링크

UCSC 게놈 브라우저의 인간 ARS2 게놈 위치 및 ARS2 유전자 세부 정보 페이지.
X-Linked Sideroblastic 빈혈 및 아탁시아에 대한 GeneReviews/NCBI/NIH/UW 입력

이 기사는 공공영역에 있는 미국 국립 의학 도서관의 텍스트를 통합하고 있다.

인간 X 염색체 및/또는 그 관련 단백질에 대한 유전자에 대한 이 기사는 스터브다.위키피디아를 확장하여 도울 수 있다.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리스 89: ENSG00000158578 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리스 89: ENSMUSG000025270 - 앙상블, 2017년 5월

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2347585-5] Bishop DF, Henderson AS, Astrin KH (Jun 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics. 7 (2): 207–14. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.

[pmid1577484-6] Cotter PD, Willard HF, Gorski JL, Bishop DF (May 1992). "Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations" (PDF). Genomics. 13 (1): 211–2. doi:10.1016/0888-7543(92)90223-F. hdl:2027.42/30074. PMID 1577484.

[entrez-7] "Entrez Gene: Delta-aminolevulinate synthase 2".

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