Sarcolipin

SLN
التراكيب المتوفرة
بنك بيانات البروتين	Human UniProt search: PDBe RCSB
قائمة رموز معهدات بنك بيانات البروتين
	1JDM
المعهدات
الأسماء المستعارة	SLN, sarcolipin
معهدات خارجية	الوراثة المندلية البشرية عبر الإنترنت 602203 GeneCards: 6588
فهم الوجود الجيني
الوظيفة الجزيئية	• ATPase binding; • enzyme inhibitor activity; • enzyme regulator activity; • ‏GO:0001948 ربط بروتيني;
المكونات الخلوية	• مكون تكاملي للغشاء; • endoplasmic reticulum membrane; • غشاء; • شبكة إندوبلازمية; • sarcoplasmic reticulum membrane; • شبكة إندوبلازمية عضلية;
العمليات الحيوية	• positive regulation of protein depolymerization; • negative regulation of protein complex disassembly; • negative regulation of calcium ion binding; • regulation of calcium ion transport; • negative regulation of catalytic activity; • negative regulation of calcium ion transmembrane transporter activity; • نقل شاردة الكالسيوم; • negative regulation of calcium ion import; • sarcoplasmic reticulum calcium ion transport; • regulation of relaxation of muscle; • regulation of calcium-transporting ATPase activity; • positive regulation of cold-induced thermogenesis;
	المصادر:Amigo / QuickGO
نمط التعبير عن الحمض النووي الريبوزي
	المزيد من بيانات التعبير المرجعية
أورثولوج
	O00631
	n/a
	NM_003063
	n/a
	NP_003054
	n/a
	ويكي بيانات
اعرض/عدّل إنسان

Sarcolipin‏ (Sarcolipin) هوَ بروتين يُشَفر بواسطة جين Sarcolipin في الإنسان.

الوظيفة

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

الأهمية السريرية

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

المراجع

^ "Entrez Gene: SLN sarcolipin". مؤرشف من الأصل في 05 ديسمبر 2010.
^ Odermatt A, Taschner PE, Scherer SW, Beatty B, Khanna VK, Cornblath DR, Chaudhry V, Yee WC, Schrank B, Karpati G, Breuning MH, Knoers N, MacLennan DH (November 1997). "Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease". Genomics. 45 (3): 541–53. doi:10.1006/geno.1997.4967. PMID 9367679.

قراءة متعمقة

Lanfranchi G, Muraro T, Caldara F, Pacchioni B, Pallavicini A, Pandolfo D, Toppo S, Trevisan S, Scarso S, Valle G (January 1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization". Genome Research. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
Odermatt A, Becker S, Khanna VK, Kurzydlowski K, Leisner E, Pette D, MacLennan DH (May 1998). "Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase". The Journal of Biological Chemistry. 273 (20): 12360–9. doi:10.1074/jbc.273.20.12360. PMID 9575189.
Smith WS, Broadbridge R, East JM, Lee AG (January 2002). "Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum". The Biochemical Journal. 361 (Pt 2): 277–86. doi:10.1042/0264-6021:3610277. PMC 1222307. PMID 11772399.
Mascioni A, Karim C, Barany G, Thomas DD, Veglia G (January 2002). "Structure and orientation of sarcolipin in lipid environments". Biochemistry. 41 (2): 475–82. doi:10.1021/bi011243m. PMID 11781085.
Asahi M, Kurzydlowski K, Tada M, MacLennan DH (July 2002). "Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs)". The Journal of Biological Chemistry. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137.
Minamisawa S, Wang Y, Chen J, Ishikawa Y, Chien KR, Matsuoka R (March 2003). "Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling". The Journal of Biological Chemistry. 278 (11): 9570–5. doi:10.1074/jbc.M213132200. PMID 12645548.
Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH (April 2003). "Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban". Proceedings of the National Academy of Sciences of the United States of America. 100 (9): 5040–5. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (September 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.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Vittorini S, Storti S, Parri MS, Cerillo AG, Clerico A (2007). "SERCA2a, phospholamban, sarcolipin, and ryanodine receptors gene expression in children with congenital heart defects". Molecular Medicine. 13 (1–2): 105–11. doi:10.2119/2006-00054.Vittorini. PMC 1869624. PMID 17515962.