UniProt ID | ARL8B_HUMAN | |
---|---|---|
UniProt AC | Q9NVJ2 | |
Protein Name | ADP-ribosylation factor-like protein 8B | |
Gene Name | ARL8B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 186 | |
Subcellular Localization | Late endosome membrane . Lysosome membrane . Cytoplasm, cytoskeleton, spindle. Localizes with microtubules at the spindle mid-zone during mitosis. | |
Protein Description | May play a role in lysosome motility. [PubMed: 16537643] | |
Protein Sequence | MLALISRLLDWFRSLFWKEEMELTLVGLQYSGKTTFVNVIASGQFSEDMIPTVGFNMRKVTKGNVTIKIWDIGGQPRFRSMWERYCRGVNAIVYMIDAADREKIEASRNELHNLLDKPQLQGIPVLVLGNKRDLPNALDEKQLIEKMNLSAIQDREICCYSISCKEKDNIDITLQWLIQHSKSRRS | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MLALISRL -------CHHHHHHH | 4.45 | 22223895 | |
61 | Phosphorylation | GFNMRKVTKGNVTIK CEEEEEECCCCEEEE | 35.95 | - | |
62 | Ubiquitination | FNMRKVTKGNVTIKI EEEEEECCCCEEEEE | 52.02 | 27667366 | |
66 | Phosphorylation | KVTKGNVTIKIWDIG EECCCCEEEEEEECC | 22.13 | 28060719 | |
68 | Ubiquitination | TKGNVTIKIWDIGGQ CCCCEEEEEEECCCC | 28.51 | 23503661 | |
68 | Ubiquitination | TKGNVTIKIWDIGGQ CCCCEEEEEEECCCC | 28.51 | - | |
107 | Phosphorylation | DREKIEASRNELHNL HHHHHHHHHHHHHHH | 23.89 | 21406692 | |
117 | Ubiquitination | ELHNLLDKPQLQGIP HHHHHCCCHHHCCCC | 34.33 | - | |
131 | Ubiquitination | PVLVLGNKRDLPNAL CEEEECCCCCCCCCC | 45.55 | 27667366 | |
141 | Acetylation | LPNALDEKQLIEKMN CCCCCCHHHHHHHCC | 50.50 | 26822725 | |
141 | Malonylation | LPNALDEKQLIEKMN CCCCCCHHHHHHHCC | 50.50 | 32601280 | |
141 | Neddylation | LPNALDEKQLIEKMN CCCCCCHHHHHHHCC | 50.50 | 32015554 | |
141 | Sumoylation | LPNALDEKQLIEKMN CCCCCCHHHHHHHCC | 50.50 | - | |
141 | Ubiquitination | LPNALDEKQLIEKMN CCCCCCHHHHHHHCC | 50.50 | 21906983 | |
146 | Ubiquitination | DEKQLIEKMNLSAIQ CHHHHHHHCCHHHHC | 26.54 | 23000965 | |
146 | Malonylation | DEKQLIEKMNLSAIQ CHHHHHHHCCHHHHC | 26.54 | 26320211 | |
150 | Phosphorylation | LIEKMNLSAIQDREI HHHHCCHHHHCCCEE | 20.51 | 21815630 | |
160 | Phosphorylation | QDREICCYSISCKEK CCCEEEEEEEEECCC | 12.48 | 28152594 | |
161 | Phosphorylation | DREICCYSISCKEKD CCEEEEEEEEECCCC | 8.29 | 28152594 | |
163 | Phosphorylation | EICCYSISCKEKDNI EEEEEEEEECCCCCC | 17.13 | 28152594 | |
165 | Ubiquitination | CCYSISCKEKDNIDI EEEEEEECCCCCCEE | 62.09 | 33845483 | |
167 | Ubiquitination | YSISCKEKDNIDITL EEEEECCCCCCEEEH | 41.38 | 33845483 | |
182 | Ubiquitination | QWLIQHSKSRRS--- HHHHHHHHHCCC--- | 45.95 | 21906983 |
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 ARL8B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARL8B_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 ARL8B_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TBB5_HUMAN | TUBB | physical | 15331635 | |
A4_HUMAN | APP | physical | 21832049 | |
BT3A3_HUMAN | BTN3A3 | physical | 21988832 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
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. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"An N-terminally acetylated Arf-like GTPase is localised to lysosomesand affects their motility."; Hofmann I., Munro S.; J. Cell Sci. 119:1494-1503(2006). Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,ACETYLATION AT MET-1, AND MUTAGENESIS OF LEU-2; 5-ILE--PHE-12 ANDGLN-75. |