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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: Calcium/calmodulin-dependent protein kinase type II subunit beta

UniprotKB/SwissProt ID: P28652 (P28652)

Gene Name: Camk2b

Organism: Mus musculus (Mouse)

Function: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons (PubMed:29100089). Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2 (PubMed:21752990). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). Phosphorylates reticulophagy regulator RETREG1 at 'Thr-134' under endoplasmic reticulum stress conditions which enhances RETREG1 oligomerization and its membrane scission and reticulophagy activity (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Sarcoplasmic reticulum membrane. Synapse

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR013543 Ca/CaM-dep_prot_kinase-assoc
IPR011009 Kinase-like_dom_sf
IPR032710 NTF2-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The S-nitrosylation sites of P28652

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 290 SMMHRQETVE C LKKFNARRKL  CCCEEEECCC C CCCHHHHHHC  6.16% 24895380
2 31 GKGAFSVVRR C VKLCTGHEYA  CCCEEEECCC C CCCHHHHHHC  1.91%
3 35 FSVVRRCVKL C TGHEYAAKII  CCCEEEECCC C CCCHHHHHHC  3.38% 24895380
4 533 DGKWQNVHFH C SGAPVAPLQ-  CCCEEEECCC C CCCHHHHHHC  3.82% 24895380