S100A2

S100A2
التراكيب المتوفرة
بنك بيانات البروتين	Human UniProt search: PDBe RCSB
قائمة رموز معهدات بنك بيانات البروتين
	2RGI, 4DUQ
المعهدات
الأسماء المستعارة	S100A2, CAN19, S100L, S100 calcium binding protein A2
معهدات خارجية	الوراثة المندلية البشرية عبر الإنترنت 176993 HomoloGene: 48389 GeneCards: 6273
فهم الوجود الجيني
الوظيفة الجزيئية	• ربط أيون فلزي; • ربط أيون الكالسيوم; • identical protein binding; • ‏GO:0001948 ربط بروتيني; • transition metal ion binding;
المكونات الخلوية	• مكون خلوي;
العمليات الحيوية	• endothelial cell migration;
	المصادر:Amigo / QuickGO
نمط التعبير عن الحمض النووي الريبوزي
	المزيد من بيانات التعبير المرجعية
أورثولوج
	P29034
	n/a
	‏NM_001366406، ‏NM_001366407 NM_005978، ‏NM_001366406، ‏NM_001366407
	n/a
	‏NP_001353335، ‏NP_001353336 NP_005969، ‏NP_001353335، ‏NP_001353336
	n/a
	ويكي بيانات
اعرض/عدّل إنسان

S100A2‏ (S100 calcium binding protein A2) هوَ بروتين يُشَفر بواسطة جين S100A2 في الإنسان.

الوظيفة

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

الأهمية السريرية

هذا القسم فارغ أوغير مكتمل، ساهم بتحريره.

المراجع

^ "Entrez Gene: S100A2 S100 calcium binding protein A2". مؤرشف من الأصل في 05 ديسمبر 2010.
^ Engelkamp D, Schafer BW, Mattei MG, Erne P, Heizmann CW (Aug 1993). "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proc Natl Acad Sci U S A. 90 (14): 6547–51. doi:10.1073/pnas.90.14.6547. PMC 46969. PMID 8341667.

قراءة متعمقة

Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Lee SW, Tomasetto C, Swisshelm K, et al. (1992). "Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment". Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2504–8. doi:10.1073/pnas.89.6.2504. PMC 48687. PMID 1372446.
Schäfer BW, Wicki R, Engelkamp D, et al. (1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638–43. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
Gimona M, Lando Z, Dolginov Y, et al. (1997). "Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins". J. Cell Sci. 110 (5): 611–21. PMID 9092943.
Böni R, Burg G, Doguoglu A, et al. (1997). "Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions". Br. J. Dermatol. 137 (1): 39–43. doi:10.1111/j.1365-2133.1997.tb03698.x. PMID 9274623.
Groves P, Finn BE, Kuźnicki J, Forsén S (1998). "A model for target protein binding to calcium-activated S100 dimers". FEBS Lett. 421 (3): 175–9. doi:10.1016/S0014-5793(97)01535-4. PMID 9468301.
Wicki R, Franz C, Scholl FA, et al. (1998). "Repression of the candidate tumor suppressor gene S100A2 in breast cancer is mediated by site-specific hypermethylation". Cell Calcium. 22 (4): 243–54. doi:10.1016/S0143-4160(97)90063-4. PMID 9481475.
Franz C, Durussel I, Cox JA, et al. (1998). "Binding of Ca2+ and Zn2+ to human nuclear S100A2 and mutant proteins". J. Biol. Chem. 273 (30): 18826–34. doi:10.1074/jbc.273.30.18826. PMID 9668057.
Mueller A, Bächi T, Höchli M, et al. (1999). "Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation". Histochem. Cell Biol. 111 (6): 453–9. doi:10.1007/s004180050381. PMID 10429967.
Stradal TB, Troxler H, Heizmann CW, Gimona M (2000). "Mapping the zinc ligands of S100A2 by site-directed mutagenesis". J. Biol. Chem. 275 (18): 13219–27. doi:10.1074/jbc.275.18.13219. PMID 10788426.
Hoyaux D, Decaestecker C, Heizmann CW, et al. (2000). "S100 proteins in Corpora amylacea from normal human brain". Brain Res. 867 (1–2): 280–8. doi:10.1016/S0006-8993(00)02393-3. PMID 10837826.
Deshpande R, Woods TL, Fu J, et al. (2000). "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking". J. Invest. Dermatol. 115 (3): 477–85. doi:10.1046/j.1523-1747.2000.00078.x. PMID 10951287.
Nagy N, Hoyaux D, Gielen I, et al. (2002). "The Ca2+-binding S100A2 protein is differentially expressed in epithelial tissue of glandular or squamous origin". Histol. Histopathol. 17 (1): 123–30. PMID 11813862.
Kyriazanos ID, Tachibana M, Dhar DK, et al. (2002). "Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus". Oncol. Rep. 9 (3): 503–10. doi:10.3892/or.9.3.503. PMID 11956617.
Zhang T, Woods TL, Elder JT (2003). "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes". J. Invest. Dermatol. 119 (5): 1196–201. doi:10.1046/j.1523-1747.2002.19520.x. PMID 12445212.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hibi K, Fujitake S, Takase T, et al. (2004). "Identification of S100A2 as a target of the DeltaNp63 oncogenic pathway". Clin. Cancer Res. 9 (11): 4282–5. PMID 14519656.