UniProt ID | AR6P6_HUMAN | |
---|---|---|
UniProt AC | Q8N6S5 | |
Protein Name | ADP-ribosylation factor-like protein 6-interacting protein 6 | |
Gene Name | ARL6IP6 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 226 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | ||
Protein Sequence | MSFAESGWRSALRRRGPGTPGPVARPSYSSFTQGDSWGEGEVDEEEGCDQVARDLRAEFSAGAWSEPRKRSVLPPDGNGSPVLPDKRNGIFPAAAGSRAQPRRWPVQVLSILCSLLFAILLAFLLAIAYLIVKELHAENLKNEDDVDTGLLGFWTLLIISLTAGFSCCSFSWTVTYFDSFEPGMFPPTPLSPARFKKLTGHSFHMGYSMAILNGIVAALTVAWCLM | |
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 | Phosphorylation | ------MSFAESGWR ------CCHHHHHHH | 32.91 | 23401153 | |
6 | Phosphorylation | --MSFAESGWRSALR --CCHHHHHHHHHHH | 39.98 | 22199227 | |
10 | Phosphorylation | FAESGWRSALRRRGP HHHHHHHHHHHHHCC | 25.75 | 22199227 | |
19 | Phosphorylation | LRRRGPGTPGPVARP HHHHCCCCCCCCCCC | 28.36 | 23401153 | |
27 | Phosphorylation | PGPVARPSYSSFTQG CCCCCCCCCCCCCCC | 31.90 | 28450419 | |
28 | Phosphorylation | GPVARPSYSSFTQGD CCCCCCCCCCCCCCC | 15.83 | 28450419 | |
29 | Phosphorylation | PVARPSYSSFTQGDS CCCCCCCCCCCCCCC | 24.26 | 28450419 | |
30 | Phosphorylation | VARPSYSSFTQGDSW CCCCCCCCCCCCCCC | 24.87 | 28450419 | |
32 | Phosphorylation | RPSYSSFTQGDSWGE CCCCCCCCCCCCCCC | 33.32 | 28450419 | |
36 | Phosphorylation | SSFTQGDSWGEGEVD CCCCCCCCCCCCCCC | 43.75 | 23927012 | |
48 | S-palmitoylation | EVDEEEGCDQVARDL CCCCCCCHHHHHHHH | 3.60 | 29575903 | |
60 | Phosphorylation | RDLRAEFSAGAWSEP HHHHHHHHCCCCCCC | 19.80 | 30266825 | |
65 | Phosphorylation | EFSAGAWSEPRKRSV HHHCCCCCCCCCCCC | 36.87 | 30266825 | |
71 | Phosphorylation | WSEPRKRSVLPPDGN CCCCCCCCCCCCCCC | 30.92 | 30266825 | |
80 | Phosphorylation | LPPDGNGSPVLPDKR CCCCCCCCCCCCCCC | 18.81 | 23401153 |
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 AR6P6_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AR6P6_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 AR6P6_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
A4_HUMAN | APP | physical | 21832049 | |
YKT6_HUMAN | YKT6 | physical | 26186194 | |
DUS3_HUMAN | DUSP3 | physical | 26186194 | |
PNPO_HUMAN | PNPO | physical | 26186194 | |
BLVRB_HUMAN | BLVRB | physical | 26186194 | |
GSTM1_HUMAN | GSTM1 | physical | 26186194 | |
PEBB_HUMAN | CBFB | physical | 26186194 | |
PMVK_HUMAN | PMVK | physical | 26186194 | |
NAA50_HUMAN | NAA50 | physical | 26186194 | |
UB2D2_HUMAN | UBE2D2 | physical | 26186194 | |
PYGB_HUMAN | PYGB | physical | 26186194 | |
SNX3_HUMAN | SNX3 | physical | 26186194 | |
PNPO_HUMAN | PNPO | physical | 28514442 | |
DUS3_HUMAN | DUSP3 | physical | 28514442 | |
PMVK_HUMAN | PMVK | physical | 28514442 | |
SNX3_HUMAN | SNX3 | physical | 28514442 | |
GSTM1_HUMAN | GSTM1 | physical | 28514442 | |
NAA50_HUMAN | NAA50 | physical | 28514442 | |
CHM4A_HUMAN | CHMP4A | physical | 28514442 | |
PEBB_HUMAN | CBFB | physical | 28514442 | |
YKT6_HUMAN | YKT6 | physical | 28514442 | |
BLVRB_HUMAN | BLVRB | physical | 28514442 | |
BID_HUMAN | BID | physical | 28514442 |
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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Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-65, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-36; SER-65 ANDSER-80, AND MASS SPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, AND MASSSPECTROMETRY. |