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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: Ras-related protein Rab-14

UniprotKB/SwissProt ID: P61107 (P61107)

Gene Name: Rab14

Organism: Rattus norvegicus (Rat)

Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development (PubMed:15004230). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion. Mediates endosomal tethering and fusion through the interaction with RUFY1 and RAB4B (By similarity). Interaction with RAB11FIP1 may function in the process of neurite formation (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Recycling endosome. Early endosome membrane. Golgi apparatus membrane. Golgi apparatus, trans-Golgi network membrane. Cytoplasmic vesicle, phagosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR027417 P-loop_NTPase
IPR030702 Rab14
IPR050209 Rab_GTPases_membrane_traffic
IPR005225 Small_GTP-bd
IPR001806 Small_GTPase

The S-nitrosylation sites of P61107

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 26 IIGDMGVGKS C LLHQFTEKKF