ARF1_MOUSE - dbPTM
ARF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARF1_MOUSE
UniProt AC P84078
Protein Name ADP-ribosylation factor 1
Gene Name Arf1
Organism Mus musculus (Mouse).
Sequence Length 181
Subcellular Localization Golgi apparatus. Cytoplasm, perinuclear region. Cell junction, synapse, synaptosome. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Membrane
Lipid-anchor .
Protein Description GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD)..
Protein Sequence MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MGNIFANLF
------CCCHHHHHH
35.62-
2Myristoylation------MGNIFANLF
------CCCHHHHHH
35.62-
35PhosphorylationAGKTTILYKLKLGEI
CCCEEEEEEEECCCE
15.49-
36UbiquitinationGKTTILYKLKLGEIV
CCEEEEEEEECCCEE
35.3827667366
38UbiquitinationTTILYKLKLGEIVTT
EEEEEEEECCCEEEE
50.74-
59UbiquitinationNVETVEYKNISFTVW
EEEEEEEEEEEEEEE
34.01-
62PhosphorylationTVEYKNISFTVWDVG
EEEEEEEEEEEEECC
25.0222817900
73UbiquitinationWDVGGQDKIRPLWRH
EECCCCCCCHHHHHH
32.50-
127UbiquitinationVLLVFANKQDLPNAM
HHHHEECCCCCCCCC
41.58-
140PhosphorylationAMNAAEITDKLGLHS
CCCHHHHHHHHCCHH
20.7020415495
142AcetylationNAAEITDKLGLHSLR
CHHHHHHHHCCHHCC
35.4966698811
142UbiquitinationNAAEITDKLGLHSLR
CHHHHHHHHCCHHCC
35.4927667366
147PhosphorylationTDKLGLHSLRHRNWY
HHHHCCHHCCCCCEE
31.9422942356

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ARF1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARF1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ARF1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARF1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARF1_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP