UniProt ID | APOL2_HUMAN | |
---|---|---|
UniProt AC | Q9BQE5 | |
Protein Name | Apolipoprotein L2 | |
Gene Name | APOL2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 337 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles.. | |
Protein Sequence | MNPESSIFIEDYLKYFQDQVSRENLLQLLTDDEAWNGFVAAAELPRDEADELRKALNKLASHMVMKDKNRHDKDQQHRQWFLKEFPRLKRELEDHIRKLRALAEEVEQVHRGTTIANVVSNSVGTTSGILTLLGLGLAPFTEGISFVLLDTGMGLGAAAAVAGITCSVVELVNKLRARAQARNLDQSGTNVAKVMKEFVGGNTPNVLTLVDNWYQVTQGIGRNIRAIRRARANPQLGAYAPPPHIIGRISAEGGEQVERVVEGPAQAMSRGTMIVGAATGGILLLLDVVSLAYESKHLLEGAKSESAEELKKRAQELEGKLNFLTKIHEMLQPGQDQ | |
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 | -------MNPESSIF -------CCHHHHHC | 19.94 | - | |
58 | Ubiquitination | ELRKALNKLASHMVM HHHHHHHHHHHHHHH | 46.40 | - | |
66 | Ubiquitination | LASHMVMKDKNRHDK HHHHHHHCCCCCCCH | 54.89 | - | |
73 | Methylation | KDKNRHDKDQQHRQW CCCCCCCHHHHHHHH | 51.84 | - | |
83 | Ubiquitination | QHRQWFLKEFPRLKR HHHHHHHHHCHHHHH | 48.08 | 21890473 | |
187 | Phosphorylation | QARNLDQSGTNVAKV HHCCCCCCCCHHHHH | 47.45 | 28857561 | |
193 | Ubiquitination | QSGTNVAKVMKEFVG CCCCHHHHHHHHHHC | 38.28 | 21890473 | |
196 | Ubiquitination | TNVAKVMKEFVGGNT CHHHHHHHHHHCCCC | 51.49 | - | |
203 | Phosphorylation | KEFVGGNTPNVLTLV HHHHCCCCCCCEEHH | 21.37 | 27251275 | |
239 | Phosphorylation | ANPQLGAYAPPPHII CCCCCCCCCCCCCEE | 20.17 | - | |
250 | Phosphorylation | PHIIGRISAEGGEQV CCEEEEEECCCCCCE | 20.93 | 25159151 | |
268 | Sulfoxidation | VEGPAQAMSRGTMIV HCCHHHHHHCCCEEE | 1.54 | 21406390 | |
269 | Phosphorylation | EGPAQAMSRGTMIVG CCHHHHHHCCCEEEE | 30.49 | 20071362 | |
272 | Phosphorylation | AQAMSRGTMIVGAAT HHHHHCCCEEEEECH | 11.56 | 22210691 | |
279 | Phosphorylation | TMIVGAATGGILLLL CEEEEECHHHHHHHH | 35.09 | 22210691 | |
303 | Ubiquitination | KHLLEGAKSESAEEL HHHHCCCCCCCHHHH | 66.66 | - | |
303 | Acetylation | KHLLEGAKSESAEEL HHHHCCCCCCCHHHH | 66.66 | 23236377 | |
304 | Phosphorylation | HLLEGAKSESAEELK HHHCCCCCCCHHHHH | 35.93 | 22210691 | |
306 | Phosphorylation | LEGAKSESAEELKKR HCCCCCCCHHHHHHH | 48.33 | 22210691 | |
320 | 2-Hydroxyisobutyrylation | RAQELEGKLNFLTKI HHHHHHHHHHHHHHH | 30.77 | - | |
320 | Ubiquitination | RAQELEGKLNFLTKI HHHHHHHHHHHHHHH | 30.77 | 21890473 | |
326 | Ubiquitination | GKLNFLTKIHEMLQP HHHHHHHHHHHHHCC | 44.18 | 21890473 | |
330 | Sulfoxidation | FLTKIHEMLQPGQDQ HHHHHHHHHCCCCCC | 2.32 | 21406390 |
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 APOL2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APOL2_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 APOL2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
UBB_HUMAN | UBB | physical | 26186194 | |
BASI_HUMAN | BSG | physical | 26496610 | |
UBL4A_HUMAN | UBL4A | physical | 26496610 | |
RTL8C_HUMAN | FAM127A | physical | 26496610 | |
MAST3_HUMAN | MAST3 | physical | 26496610 | |
RT09_HUMAN | MRPS9 | physical | 26496610 | |
BPNT1_HUMAN | BPNT1 | physical | 28514442 | |
UBB_HUMAN | UBB | physical | 28514442 | |
SODC_HUMAN | SOD1 | 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-250, 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-250, AND MASSSPECTROMETRY. | |
"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 SER-250, AND MASSSPECTROMETRY. |