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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
UniprotKB/SwissProt ID: P16615 (P16615)

Gene Name: ATP2A2

Organism: Homo sapiens (Human)

Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity) Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Endoplasmic reticulum membrane. Sarcoplasmic reticulum membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006068 ATPase_P-typ_cation-transptr_C
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR005782 P-type_ATPase_IIA
IPR001757 P_typ_ATPase
IPR044492 P_typ_ATPase_HD_dom
The S-nitrosylation sites of P16615
No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 344 RSLPSVETLG C TSVICSDKTG  CCCCCCCCHH H HHHHCCCCCC  2.63%
2 349 VETLGCTSVI C SDKTGTLTTN  CCCCCCCCHH H HHHHCCCCCC  3.95%
3 364 GTLTTNQMSV C RMFILDRVEG  CCCCCCCCHH H HHHHCCCCCC  1.73%
4 377 FILDRVEGDT C SLNEFTITGS  CCCCCCCCHH H HHHHCCCCCC  5.32%
5 447 VGEATETALT C LVEKMNVFDT  CCCCCCCCHH H HHHHCCCCCC  4.1%
6 471 GLSKIERANA C NSVIKQLMKK  CCCCCCCCHH H HHHHCCCCCC  3.8%
7 498 SRDRKSMSVY C TPNKPSRTSM  CCCCCCCCHH H HHHHCCCCCC  4.83% 24105792
8 560 EWGSGSDTLR C LALATHDNPL  CCCCCCCCHH H HHHHCCCCCC  2.68% 20140087
9 875 SFYQLSHFLQ C KEDNPDFEGV  CCCCCCCCHH H HHHHCCCCCC  5.92%
10 997 ARNYLEPGKE C VQPATKSCSF  CCCCCCCCHH H HHHHCCCCCC  3.82%