UniProt ID | ARL17_HUMAN | |
---|---|---|
UniProt AC | Q8IVW1 | |
Protein Name | ADP-ribosylation factor-like protein 17 | |
Gene Name | ARL17A | |
Organism | Homo sapiens (Human). | |
Sequence Length | 177 | |
Subcellular Localization | Golgi apparatus. | |
Protein Description | GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity).. | |
Protein Sequence | MGNIFEKLFKSLLGKKKMRILILSLDTAGKTTILYKLKLGETVPAVPTVGFCVETVEYKNNTFAVWDVGSHFKIRPLWQHFFQNTKGARSPGSTHQGSLASGVLPIKCSHVEFGMWKGGRSHPFLPHSSRCAGSGGQLDSILPHQSPAWGPWGCKDLSSGFPSFLTSSILWKSAVVK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Myristoylation | ------MGNIFEKLF ------CCHHHHHHH | 35.62 | - | |
15 | Ubiquitination | LFKSLLGKKKMRILI HHHHHHCCCCEEEEE | 49.55 | - | |
16 | Ubiquitination | FKSLLGKKKMRILIL HHHHHCCCCEEEEEE | 50.43 | - | |
35 | Phosphorylation | AGKTTILYKLKLGET CCCEEEEEEEECCCC | 15.49 | - | |
36 | Acetylation | GKTTILYKLKLGETV CCEEEEEEEECCCCC | 35.38 | 30769653 | |
36 | Ubiquitination | GKTTILYKLKLGETV CCEEEEEEEECCCCC | 35.38 | - | |
90 | Phosphorylation | QNTKGARSPGSTHQG HCCCCCCCCCCCCCC | 32.83 | - | |
93 | Phosphorylation | KGARSPGSTHQGSLA CCCCCCCCCCCCCCC | 26.54 | - | |
94 | Phosphorylation | GARSPGSTHQGSLAS CCCCCCCCCCCCCCC | 24.92 | - |
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 ARL17_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARL17_HUMAN !! |
* 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 ARL17_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ARL17_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
There are no disease associations of PTM sites. | ||||||
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
There are no disease associations of PTM sites. | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY. |