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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: Signal recognition particle subunit SRP54

UniprotKB/SwissProt ID: P61011 (P61011)

Gene Name: SRP54

Organism: Homo sapiens (Human)

Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (PubMed:34020957). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (PubMed:28972538, PubMed:29914977)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus speckle. Cytoplasm. Endoplasmic reticulum

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR036891 Signal_recog_part_SRP54_M_sf
IPR013822 Signal_recog_particl_SRP54_hlx
IPR004125 Signal_recog_particle_SRP54_M
IPR036225 SRP/SRP_N
IPR022941 SRP54
IPR006325 SRP54_euk
IPR000897 SRP54_GTPase_dom
IPR042101 SRP54_N_sf

The S-nitrosylation sites of P61011

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 136 QRKGWKTCLI C ADTFRAGAFD   
2 36 EVLNAMLKEV C TALLEADVNI