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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: Triple functional domain protein

UniprotKB/SwissProt ID: F1M0Z1 (F1M0Z1)

Gene Name: Trio

Organism: Rattus norvegicus (Rat)

Function: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth (By similarity). Plays a key role in the regulation of neurite outgrowth and lamellipodia formation (By similarity). In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (PubMed:26721934). May act as a regulator of adipogenesis (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cell projection

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001251 CRAL-TRIO_dom
IPR036865 CRAL-TRIO_dom_sf
IPR035899 DBL_dom_sf
IPR000219 DH_dom
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR047054 Kalirin_TRIO_PH_1
IPR028570 Kalirin_TRIO_SH3_1
IPR047053 Kalirin_TRIO_SH3_2
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR051336 RhoGEF_Guanine_NuclExch_SF
IPR008271 Ser/Thr_kinase_AS
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR055251 SOS1_NGEF_PH
IPR018159 Spectrin/alpha-actinin
IPR002017 Spectrin_repeat

The S-nitrosylation sites of F1M0Z1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1024 VAFYKTSEQV C SVLESLEQEY   
2 1041 EQEYKREEDW C GGADKLGPNS   
3 1991 TERDYVRDLG C VVEGYMALMK   
4 2137 SELEKAVEVM C IVPKRCNDMM   
5 465 EKYMSNVDSW C KACGEVDLPS