UniProt ID | PLS1_HUMAN | |
---|---|---|
UniProt AC | O15162 | |
Protein Name | Phospholipid scramblase 1 | |
Gene Name | PLSCR1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 318 | |
Subcellular Localization |
Cell membrane Single-pass type II membrane protein. Membrane Lipid-anchor Cytoplasmic side. Nucleus. |
|
Protein Description | May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation.. | |
Protein Sequence | MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW | |
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 |
---|---|---|---|---|---|
51 | Ubiquitination | VSYPPPPAGHSGPGP CCCCCCCCCCCCCCC | 33.82 | 33845483 | |
69 | Phosphorylation | PVPNQPVYNQPVYNQ CCCCCCCCCCCCCCC | 18.11 | 22817900 | |
74 | Phosphorylation | PVYNQPVYNQPVGAA CCCCCCCCCCCCCCC | 18.11 | 22817900 | |
125 | Ubiquitination | EVLTGFETNNKYEIK HHHHCCCCCCCEEEE | 41.66 | 33845483 | |
132 | Ubiquitination | TNNKYEIKNSFGQRV CCCCEEEECCCCCEE | 34.30 | 29901268 | |
142 | Ubiquitination | FGQRVYFAAEDTDCC CCCEEEEEECCCCCC | 7.70 | 27667366 | |
142 | Ubiquitination | FGQRVYFAAEDTDCC CCCEEEEEECCCCCC | 7.70 | 21890473 | |
148 | S-palmitoylation | FAAEDTDCCTRNCCG EEECCCCCCCCCCCC | 2.50 | 29575903 | |
149 | S-palmitoylation | AAEDTDCCTRNCCGP EECCCCCCCCCCCCC | 4.45 | 29575903 | |
153 | S-palmitoylation | TDCCTRNCCGPSRPF CCCCCCCCCCCCCCE | 2.27 | 29575903 | |
154 | S-palmitoylation | DCCTRNCCGPSRPFT CCCCCCCCCCCCCEE | 11.66 | 29575903 | |
161 | Phosphorylation | CGPSRPFTLRIIDNM CCCCCCEEEEEECCC | 20.15 | 10770950 | |
177 | Ubiquitination | QEVITLERPLRCSSC CEEEEECCCCCCCCC | 38.37 | 22817900 | |
177 | Ubiquitination | QEVITLERPLRCSSC CEEEEECCCCCCCCC | 38.37 | - | |
180 | Ubiquitination | ITLERPLRCSSCCCP EEECCCCCCCCCCCC | 22.43 | 21890473 | |
180 | Ubiquitination | ITLERPLRCSSCCCP EEECCCCCCCCCCCC | 22.43 | 21890473 | |
184 | S-palmitoylation | RPLRCSSCCCPCCLQ CCCCCCCCCCCCEEE | 1.27 | 12564925 | |
185 | S-palmitoylation | PLRCSSCCCPCCLQE CCCCCCCCCCCEEEE | 2.91 | 12564925 | |
186 | S-palmitoylation | LRCSSCCCPCCLQEI CCCCCCCCCCEEEEE | 3.20 | 12564925 | |
188 | S-palmitoylation | CSSCCCPCCLQEIEI CCCCCCCCEEEEEEE | 1.95 | 12564925 | |
189 | S-palmitoylation | SSCCCPCCLQEIEIQ CCCCCCCEEEEEEEE | 2.38 | 12564925 | |
207 | Ubiquitination | GVPIGYVIQTWHPCL CCCEEEEEEECCCCC | 1.97 | 21963094 | |
207 | Ubiquitination | GVPIGYVIQTWHPCL CCCEEEEEEECCCCC | 1.97 | - | |
209 | Ubiquitination | PIGYVIQTWHPCLPK CEEEEEEECCCCCCE | 18.02 | 22817900 | |
213 | S-palmitoylation | VIQTWHPCLPKFTIQ EEEECCCCCCEEEEC | 7.03 | 29575903 | |
216 | Ubiquitination | TWHPCLPKFTIQNEK ECCCCCCEEEECCCC | 42.04 | 27667366 | |
223 | 2-Hydroxyisobutyrylation | KFTIQNEKREDVLKI EEEECCCCHHCEEEE | 69.50 | - | |
223 | Ubiquitination | KFTIQNEKREDVLKI EEEECCCCHHCEEEE | 69.50 | 21906983 | |
249 | Phosphorylation | DVDFEIKSLDEQCVV CCCEEEEECCCCEEH | 46.87 | 25159151 | |
251 | Ubiquitination | DFEIKSLDEQCVVGK CEEEEECCCCEEHHH | 51.52 | 22817900 | |
254 | Ubiquitination | IKSLDEQCVVGKISK EEECCCCEEHHHHHH | 2.23 | 21890473 | |
258 | Ubiquitination | DEQCVVGKISKHWTG CCCEEHHHHHHHHHH | 32.00 | 27667366 | |
261 | Ubiquitination | CVVGKISKHWTGILR EEHHHHHHHHHHHHH | 46.78 | 21906983 | |
281 | Ubiquitination | ADNFGIQFPLDLDVK CHHCCCCCCCCCCHH | 6.49 | 21963094 | |
283 | Ubiquitination | NFGIQFPLDLDVKMK HCCCCCCCCCCHHHH | 12.33 | 22817900 | |
288 | Ubiquitination | FPLDLDVKMKAVMIG CCCCCCHHHHHHHHH | 34.06 | 21963094 | |
290 | Ubiquitination | LDLDVKMKAVMIGAC CCCCHHHHHHHHHHH | 31.92 | 22817900 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
69 | Y | Phosphorylation | Kinase | ABL1 | P00519 | PhosphoELM |
69 | Y | Phosphorylation | Kinase | ABL | P00520 | PSP |
69 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
69 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
69 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
74 | Y | Phosphorylation | Kinase | ABL1 | P00519 | PhosphoELM |
74 | Y | Phosphorylation | Kinase | ABL | P00520 | PSP |
74 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
74 | Y | Phosphorylation | Kinase | ABL-FAMILY | - | GPS |
74 | Y | Phosphorylation | Kinase | SRC64 | - | PhosphoELM |
161 | T | Phosphorylation | Kinase | PRKCD | Q05655 | Uniprot |
161 | T | Phosphorylation | Kinase | PRKCD | P09215 | GPS |
161 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
161 | T | Phosphorylation |
| 10770950 |
* 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 PLS1_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 |
"Regulation of phospholipid scramblase activity during apoptosis andcell activation by protein kinase Cdelta."; Frasch S.C., Henson P.M., Kailey J.M., Richter D.A., Janes M.S.,Fadok V.A., Bratton D.L.; J. Biol. Chem. 275:23065-23073(2000). Cited for: PHOSPHORYLATION AT THR-161, AND MUTAGENESIS. | |
"c-Abl tyrosine kinase binds and phosphorylates phospholipidscramblase 1."; Sun J., Zhao J., Schwartz M.A., Wang J.Y., Wiedmer T., Sims P.J.; J. Biol. Chem. 276:28984-28990(2001). Cited for: PHOSPHORYLATION AT TYR-69 AND TYR-74, AND MUTAGENESIS. |