| UniProt ID | B2L14_HUMAN | |
|---|---|---|
| UniProt AC | Q9BZR8 | |
| Protein Name | Apoptosis facilitator Bcl-2-like protein 14 | |
| Gene Name | BCL2L14 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 327 | |
| Subcellular Localization |
Cytoplasm . Isoform 1: Cytoplasm, cytosol. Diffusely distributed throughout the cytosol. Isoform 2: Endomembrane system. Predominantly localized to cytosolic organelles. |
|
| Protein Description | Plays a role in apoptosis.. | |
| Protein Sequence | MCSTSGCDLEEIPLDDDDLNTIEFKILAYYTRHHVFKSTPALFSPKLLRTRSLSQRGLGNCSANESWTEVSWPCRNSQSSEKAINLGKKKSSWKAFFGVVEKEDSQSTPAKVSAQGQRTLEYQDSHSQQWSRCLSNVEQCLEHEAVDPKVISIANRVAEIVYSWPPPQATQAGGFKSKEIFVTEGLSFQLQGHVPVASSSKKDEEEQILAKIVELLKYSGDQLERKLKKDKALMGHFQDGLSYSVFKTITDQVLMGVDPRGESEVKAQGFKAALVIDVTAKLTAIDNHPMNRVLGFGTKYLKENFSPWIQQHGGWEKILGISHEEVD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 38 | Phosphorylation | TRHHVFKSTPALFSP HHHHHHCCCCCHHCH | 28.32 | - | |
| 44 | Phosphorylation | KSTPALFSPKLLRTR CCCCCHHCHHHHHCC | 23.21 | 24670416 | |
| 50 | Phosphorylation | FSPKLLRTRSLSQRG HCHHHHHCCCCHHCC | 25.28 | 23312004 | |
| 52 | Phosphorylation | PKLLRTRSLSQRGLG HHHHHCCCCHHCCCC | 31.59 | 23312004 | |
| 54 | Phosphorylation | LLRTRSLSQRGLGNC HHHCCCCHHCCCCCC | 21.05 | 23312004 | |
| 62 | Phosphorylation | QRGLGNCSANESWTE HCCCCCCCCCCCCCE | 37.82 | 25693802 | |
| 66 | Phosphorylation | GNCSANESWTEVSWP CCCCCCCCCCEECCC | 38.82 | 27251275 | |
| 68 | Phosphorylation | CSANESWTEVSWPCR CCCCCCCCEECCCCC | 35.47 | 27251275 | |
| 71 | Phosphorylation | NESWTEVSWPCRNSQ CCCCCEECCCCCCCC | 21.04 | 28348404 | |
| 113 | Phosphorylation | QSTPAKVSAQGQRTL CCCCCEEEECCCEEE | 17.73 | 27135362 | |
| 125 | Phosphorylation | RTLEYQDSHSQQWSR EEEEECCCCHHHHHH | 14.98 | 27251275 | |
| 135 | Phosphorylation | QQWSRCLSNVEQCLE HHHHHHHHCHHHHHH | 42.32 | 26657352 | |
| 152 | Phosphorylation | AVDPKVISIANRVAE CCCHHHHHHHHHHHH | 20.73 | 23927012 | |
| 183 | Phosphorylation | KSKEIFVTEGLSFQL CCCEEEEECCCEEEE | 17.37 | 29083192 | |
| 187 | Phosphorylation | IFVTEGLSFQLQGHV EEEECCCEEEEEEEC | 23.08 | 29083192 | |
| 198 | Phosphorylation | QGHVPVASSSKKDEE EEECCCCCCCCCCHH | 35.06 | 29083192 | |
| 199 | Phosphorylation | GHVPVASSSKKDEEE EECCCCCCCCCCHHH | 36.12 | 29083192 | |
| 200 | Phosphorylation | HVPVASSSKKDEEEQ ECCCCCCCCCCHHHH | 41.03 | 29083192 | |
| 218 | Phosphorylation | KIVELLKYSGDQLER HHHHHHHHCHHHHHH | 20.18 | 26074081 | |
| 219 | Phosphorylation | IVELLKYSGDQLERK HHHHHHHCHHHHHHH | 34.01 | 26074081 |
| 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 B2L14_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of B2L14_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 B2L14_HUMAN !! | ||||||
| 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 |
| "Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASSSPECTROMETRY. | |