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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: Plasma membrane calcium-transporting ATPase 1

UniprotKB/SwissProt ID: P11505 (P11505)

Gene Name: Atp2b1

Organism: Rattus norvegicus (Rat)

Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis. Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to regulation of vascular smooth muscle cells vasoconstriction. Positively regulates bone mineralization through absorption of calcium from the intestine. Plays dual roles in osteoclast differentiation and survival by regulating RANKL-induced calcium oscillations in preosteoclasts and mediating calcium extrusion in mature osteoclasts (By similarity). Regulates insulin sensitivity through calcium/calmodulin signaling pathway by regulating AKT1 activation and NOS3 activation in endothelial cells (By similarity). May play a role in synaptic transmission by modulating calcium and proton dynamics at the synaptic vesicles

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Basolateral cell membrane. Synapse. Presynaptic cell membrane. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR022141 ATP_Ca_trans_C
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
IPR006408 P-type_ATPase_IIB
IPR001757 P_typ_ATPase
IPR044492 P_typ_ATPase_HD_dom

The S-nitrosylation sites of P11505

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 463 DNNLVRHLDA C ETMGNATAIC