ERO1L

ERO1A
التراكيب المتوفرة
بنك بيانات البروتين	Ortholog search: PDBe RCSB
قائمة رموز معهدات بنك بيانات البروتين
	3AHQ, 3AHR
المعهدات
الأسماء المستعارة	ERO1A, ERO1-alpha, ERO1LA, ERO1-L, ERO1-L-alpha, ERO1L, Ero1alpha, endoplasmic reticulum oxidoreductase alpha, endoplasmic reticulum oxidoreductase 1 alpha
معهدات خارجية	الوراثة المندلية البشرية عبر الإنترنت 615435 MGI: MGI:1354385 HomoloGene: 49392 GeneCards: 30001
فهم الوجود الجيني
الوظيفة الجزيئية	• oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; • ‏GO:0001948 ربط بروتيني; • oxidoreductase activity; • protein disulfide oxidoreductase activity; • protein disulfide isomerase activity; • disulfide oxidoreductase activity;
المكونات الخلوية	• endoplasmic reticulum lumen; • غشاء; • intracellular membrane-bounded organelle; • تغصن; • شبكة إندوبلازمية; • endoplasmic reticulum membrane;
العمليات الحيوية	• release of sequestered calcium ion into cytosol; • 4-hydroxyproline metabolic process; • extracellular matrix organization; • protein maturation by protein folding; • cell redox homeostasis; • response to endoplasmic reticulum stress; • chaperone mediated protein folding requiring cofactor; • endoplasmic reticulum unfolded protein response; • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; • cellular protein modification process; • طي البروتين; • brown fat cell differentiation; • oxidation-reduction process; • cellular response to hypoxia; • response to temperature stimulus; • animal organ senescence; • استماتة; • protein folding in endoplasmic reticulum; • cellular response to oxidative stress;
	المصادر:Amigo / QuickGO
نمط التعبير عن الحمض النووي الريبوزي
	المزيد من بيانات التعبير المرجعية
أورثولوج
	Q96HE7; G3V503; G3V5B3
	Q8R180
	‏NM_014584، ‏XM_024449554 XM_011536684، ‏NM_014584، ‏XM_024449554
	NM_015774
	‏XP_011534986، ‏XP_024305322 NP_055399، ‏XP_011534986، ‏XP_024305322
	NP_056589
	ويكي بيانات
اعرض/عدّل إنسان	اعرض/عدّل فأر

ERO1L‏ (ERO1-like protein alpha) هوَ بروتين يُشَفر بواسطة جين ERO1L في الإنسان.

الوظيفة

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

الأهمية السريرية

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

المراجع

^ Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (Mar 2000). "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum". J Biol Chem. 275 (7): 4827–33. doi:10.1074/jbc.275.7.4827. PMID 10671517.
^ "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)". مؤرشف من الأصل في 05 ديسمبر 2010.

قراءة متعمقة

Pagani M, Fabbri M, Benedetti C, et al. (2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". J. Biol. Chem. 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.
Benham AM, Cabibbo A, Fassio A, et al. (2000). "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha". EMBO J. 19 (17): 4493–502. doi:10.1093/emboj/19.17.4493. PMC 302061. PMID 10970843.
Pagani M, Pilati S, Bertoli G, et al. (2001). "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function". FEBS Lett. 508 (1): 117–20. doi:10.1016/S0014-5793(01)03034-4. PMID 11707280.
Mezghrani A, Fassio A, Benham A, et al. (2002). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.
Anelli T, Alessio M, Mezghrani A, et al. (2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
Tsai B, Rapoport TA (2002). "Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1". J. Cell Biol. 159 (2): 207–16. doi:10.1083/jcb.200207120. PMC 2173060. PMID 12403808.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gess B, Hofbauer KH, Wenger RH, et al. (2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha". Eur. J. Biochem. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Anelli T, Alessio M, Bachi A, et al. (2003). "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44". EMBO J. 22 (19): 5015–22. doi:10.1093/emboj/cdg491. PMC 204474. PMID 14517240.
Bertoli G, Simmen T, Anelli T, et al. (2004). "Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum". J. Biol. Chem. 279 (29): 30047–52. doi:10.1074/jbc.M403192200. PMID 15136577.
Molteni SN, Fassio A, Ciriolo MR, et al. (2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum". J. Biol. Chem. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913.
van Lith M, Hartigan N, Hatch J, Benham AM (2005). "PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum". J. Biol. Chem. 280 (2): 1376–83. doi:10.1074/jbc.M408651200. PMID 15475357.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
May D, Itin A, Gal O, et al. (2005). "Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer". Oncogene. 24 (6): 1011–20. doi:10.1038/sj.onc.1208325. PMID 15592500.
Otsu M, Bertoli G, Fagioli C, et al. (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.