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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: Cell division control protein 42 homolog

UniprotKB/SwissProt ID: Q2KJ93 (Q2KJ93)

Gene Name: CDC42

Organism: Bos taurus (Bovine)

Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Regulates cell migration. In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections (By similarity). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation (By similarity). Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (By similarity). Upon activation by PLEKHG4B, involved in actin cytoskeletal remodeling during epithelial cell-cell junction formation (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Midbody. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Cell projection, lamellipodium membrane. Cell projection, dendrite

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR037874 Cdc42
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd
IPR001806 Small_GTPase
IPR003578 Small_GTPase_Rho

The S-nitrosylation sites of Q2KJ93

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 6 -----MQTIK C VVVGDGAVGK