UniProt ID | BAD_MOUSE | |
---|---|---|
UniProt AC | Q61337 | |
Protein Name | Bcl2-associated agonist of cell death | |
Gene Name | Bad | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 204 | |
Subcellular Localization | Mitochondrion outer membrane. Cytoplasm . Colocalizes with HIF3A isoform 2 in the cytoplasm (PubMed:21546903). Upon phosphorylation, locates to the cytoplasm. | |
Protein Description | Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.. | |
Protein Sequence | MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ | |
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 |
---|---|---|---|---|---|
20 | Phosphorylation | HALGLRKSDPGIRSL HHHCCCCCCCCHHHC | 42.47 | 24719451 | |
26 | Phosphorylation | KSDPGIRSLGSDAGG CCCCCHHHCCCCCCC | 34.85 | - | |
29 | Phosphorylation | PGIRSLGSDAGGRRW CCHHHCCCCCCCCCC | 29.58 | 22871156 | |
67 | Phosphorylation | TDRGLGPSLTEDQPG CCCCCCCCCCCCCCC | 46.23 | - | |
76 | Phosphorylation | TEDQPGPYLAPGLLG CCCCCCCCCCCCCCC | 22.78 | 22817900 | |
94 | Phosphorylation | HQQGRAATNSHHGGA HHCCCHHCCCCCCCC | 35.95 | 22817900 | |
96 | Phosphorylation | QGRAATNSHHGGAGA CCCHHCCCCCCCCCC | 16.71 | 22817900 | |
108 | Phosphorylation | AGAMETRSRHSSYPA CCCCCCCCCCCCCCC | 41.59 | 26239621 | |
111 | Phosphorylation | METRSRHSSYPAGTE CCCCCCCCCCCCCCC | 30.38 | 27742792 | |
112 | Phosphorylation | ETRSRHSSYPAGTEE CCCCCCCCCCCCCCC | 29.07 | 27087446 | |
113 | Phosphorylation | TRSRHSSYPAGTEED CCCCCCCCCCCCCCC | 10.50 | 27742792 | |
117 | Phosphorylation | HSSYPAGTEEDEGME CCCCCCCCCCCCCCC | 38.00 | 27742792 | |
123 | Oxidation | GTEEDEGMEEELSPF CCCCCCCCCCCCCCC | 5.72 | 17242355 | |
128 | Phosphorylation | EGMEEELSPFRGRSR CCCCCCCCCCCCCCC | 25.85 | 25168779 | |
131 | Asymmetric dimethylarginine | EEELSPFRGRSRSAP CCCCCCCCCCCCCCC | 42.89 | - | |
131 | Methylation | EEELSPFRGRSRSAP CCCCCCCCCCCCCCC | 42.89 | - | |
133 | Asymmetric dimethylarginine | ELSPFRGRSRSAPPN CCCCCCCCCCCCCCC | 25.33 | - | |
133 | Methylation | ELSPFRGRSRSAPPN CCCCCCCCCCCCCCC | 25.33 | - | |
134 | Phosphorylation | LSPFRGRSRSAPPNL CCCCCCCCCCCCCCH | 33.15 | 27087446 | |
136 | Phosphorylation | PFRGRSRSAPPNLWA CCCCCCCCCCCCHHH | 46.50 | 27087446 | |
155 | Phosphorylation | GRELRRMSDEFEGSF HHHHHHCCHHCCCCC | 31.98 | 27087446 | |
161 | Phosphorylation | MSDEFEGSFKGLPRP CCHHCCCCCCCCCCC | 19.31 | 25619855 | |
170 | Phosphorylation | KGLPRPKSAGTATQM CCCCCCCCCCHHHHH | 34.31 | 25521595 | |
173 | Phosphorylation | PRPKSAGTATQMRQS CCCCCCCHHHHHHHH | 26.67 | 26643407 | |
175 | Phosphorylation | PKSAGTATQMRQSAG CCCCCHHHHHHHHHC | 23.80 | 26643407 | |
180 | Phosphorylation | TATQMRQSAGWTRII HHHHHHHHHCCHHHH | 20.55 | 29514104 | |
201 | Phosphorylation | NLGKGGSTPSQ---- CCCCCCCCCCC---- | 30.18 | 16166315 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
26 | S | Phosphorylation | Kinase | IKKB | O88351 | PSP |
94 | T | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
96 | S | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
112 | S | Phosphorylation | Kinase | PIM3 | Q86V86 | PSP |
112 | S | Phosphorylation | Kinase | RPS6KA2 | Q9WUT3 | GPS |
112 | S | Phosphorylation | Kinase | RPS6KA3 | P18654 | GPS |
112 | S | Phosphorylation | Kinase | RPS6KA5 | Q8C050 | GPS |
112 | S | Phosphorylation | Kinase | MAPK8 | Q91Y86 | GPS |
112 | S | Phosphorylation | Kinase | PAK1 | Q13153 | PSP |
112 | S | Phosphorylation | Kinase | PAK1 | O88643 | Uniprot |
112 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
112 | S | Phosphorylation | Kinase | PAK4 | Q8BTW9 | Uniprot |
112 | S | Phosphorylation | Kinase | PAK5 | Q8C015 | Uniprot |
112 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
112 | S | Phosphorylation | Kinase | PIM1 | P06803 | PSP |
112 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
112 | S | Phosphorylation | Kinase | PIM2 | Q62070 | Uniprot |
112 | S | Phosphorylation | Kinase | PAK2 | Q8CIN4 | Uniprot |
112 | S | Phosphorylation | Kinase | PIM3 | P58750 | Uniprot |
112 | S | Phosphorylation | Kinase | RAF1 | P04049 | PSP |
112 | S | Phosphorylation | Kinase | RAF1 | Q99N57 | Uniprot |
112 | S | Phosphorylation | Kinase | AKT-FAMILY | - | GPS |
112 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
112 | S | Phosphorylation | Kinase | RAF-FAMILY | - | GPS |
112 | S | Phosphorylation | Kinase | RSK-SUBFAMILY | - | GPS |
112 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
112 | S | Phosphorylation | Kinase | PKB_GROUP | - | PhosphoELM |
112 | S | Phosphorylation | Kinase | RSK_GROUP | - | PhosphoELM |
112 | S | Phosphorylation | Kinase | P90RSK | P18653 | PSP |
112 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
112 | S | Phosphorylation | Kinase | AKT1 | P31750 | PSP |
112 | S | Phosphorylation | Kinase | RPS6KA1 | Q15418 | GPS |
112 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
112 | S | Phosphorylation | Kinase | PKACA | P00517 | PSP |
117 | T | Phosphorylation | Kinase | CSK21 | Q60737 | PhosphoELM |
117 | T | Phosphorylation | Kinase | CSNK2A1 | P19139 | GPS |
128 | S | Phosphorylation | Kinase | MAPK8 | Q91Y86 | GPS |
128 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
128 | S | Phosphorylation | Kinase | CDK1 | P11440 | PSP |
136 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
136 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
136 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
136 | S | Phosphorylation | Kinase | PIM3 | Q86V86 | PSP |
136 | S | Phosphorylation | Kinase | PKACA | P00517 | PSP |
136 | S | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
136 | S | Phosphorylation | Kinase | AKT-FAMILY | - | GPS |
136 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
136 | S | Phosphorylation | Kinase | RAF-FAMILY | - | GPS |
136 | S | Phosphorylation | Kinase | AKT1 | P31750 | PSP |
136 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
136 | S | Phosphorylation | Kinase | PKB_GROUP | - | PhosphoELM |
136 | S | Phosphorylation | Kinase | PIM1 | P06803 | PSP |
136 | S | Phosphorylation | Kinase | PAK1 | Q13153 | PSP |
136 | S | Phosphorylation | Kinase | PRKCQ | Q02111 | Uniprot |
136 | S | Phosphorylation | Kinase | RPS6KA1 | Q15418 | GPS |
136 | S | Phosphorylation | Kinase | PAK1 | O88643 | Uniprot |
136 | S | Phosphorylation | Kinase | PAK4 | Q8BTW9 | GPS |
136 | S | Phosphorylation | Kinase | RPS6KB1 | Q8BSK8 | Uniprot |
136 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
136 | S | Phosphorylation | Kinase | RPS6KA1 | P18653 | Uniprot |
136 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
155 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
155 | S | Phosphorylation | Kinase | RPS6KA5 | O75582 | GPS |
155 | S | Phosphorylation | Kinase | RPS6KA1 | Q15418 | GPS |
155 | S | Phosphorylation | Kinase | RSK-SUBFAMILY | - | GPS |
155 | S | Phosphorylation | Kinase | RSK_GROUP | - | PhosphoELM |
155 | S | Phosphorylation | Kinase | RAF-FAMILY | - | GPS |
155 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
155 | S | Phosphorylation | Kinase | AKT1 | P31750 | PSP |
155 | S | Phosphorylation | Kinase | PIM2 | Q9P1W9 | PSP |
155 | S | Phosphorylation | Kinase | P90RSK | P18653 | PSP |
155 | S | Phosphorylation | Kinase | AKT-FAMILY | - | GPS |
155 | S | Phosphorylation | Kinase | PRKG1 | P0C605 | GPS |
155 | S | Phosphorylation | Kinase | PKG1 | Q13976 | PSP |
155 | S | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
155 | S | Phosphorylation | Kinase | PKACA | P00517 | PSP |
155 | S | Phosphorylation | Kinase | PIM1 | P11309 | PSP |
155 | S | Phosphorylation | Kinase | PIM3 | Q86V86 | PSP |
155 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
155 | S | Phosphorylation | Kinase | PRKACA | P05132 | GPS |
170 | S | Phosphorylation | Kinase | CAMK2G | Q13555 | PSP |
170 | S | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
173 | T | Phosphorylation | Kinase | PIM3 | P58750 | PSP |
201 | T | Phosphorylation | Kinase | MAPK8 | Q91Y86 | GPS |
201 | T | Phosphorylation | Kinase | JNK1 | P45983 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
112 | S | Phosphorylation |
| 9381178 |
112 | S | Phosphorylation |
| 9381178 |
131 | R | Methylation |
| 10611223 |
131 | R | Phosphorylation |
| 10611223 |
133 | R | Methylation |
| 10611223 |
133 | R | Phosphorylation |
| 10611223 |
136 | S | Methylation |
| 9381178 |
136 | S | Phosphorylation |
| 9381178 |
136 | S | Phosphorylation |
| 9381178 |
136 | S | Phosphorylation |
| 9381178 |
136 | S | Phosphorylation |
| 9381178 |
155 | S | Phosphorylation |
| 11717309 |
155 | S | Phosphorylation |
| 11717309 |
155 | S | Phosphorylation |
| 11717309 |
170 | S | Phosphorylation |
| 11717309 |
* 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 BAD_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SODM_MOUSE | Sod2 | physical | 12931191 | |
KAPCA_MOUSE | Prkaca | physical | 12931191 | |
WASF1_MOUSE | Wasf1 | physical | 12931191 | |
HXK4_MOUSE | Gck | physical | 12931191 | |
BCL2_MOUSE | Bcl2 | physical | 21084607 | |
B2CL1_MOUSE | Bcl2l1 | physical | 21084607 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY. | |
"p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1regulates its mitochondrial localization, phosphorylation of BAD, andBcl-2 association."; Jin S., Zhuo Y., Guo W., Field J.; J. Biol. Chem. 280:24698-24705(2005). Cited for: PHOSPHORYLATION AT SER-112 BY RAF1. | |
"The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death."; Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J.,Lilly M.; J. Biol. Chem. 278:45358-45367(2003). Cited for: PHOSPHORYLATION AT SER-112 BY PIM2. | |
"Identification of a novel phosphorylation site, Ser-170, as aregulator of bad pro-apoptotic activity."; Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K.,Goodlett D.R., Aebersold R., Duronio V.; J. Biol. Chem. 277:6399-6405(2002). Cited for: PHOSPHORYLATION AT SER-170, MUTAGENESIS OF SER-112; SER-155 ANDSER-170, AND MASS SPECTROMETRY. | |
"p70S6 kinase signals cell survival as well as growth, inactivatingthe pro-apoptotic molecule BAD."; Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.; Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001). Cited for: PHOSPHORYLATION AT SER-136. | |
"Protein kinase C-theta mediates a selective T cell survival signalvia phosphorylation of BAD."; Villalba M., Bushway P., Altman A.; J. Immunol. 166:5955-5963(2001). Cited for: PHOSPHORYLATION AT SER-136. | |
"p21-activated protein kinase gamma-PAK suppresses programmed celldeath of BALB3T3 fibroblasts."; Jakobi R., Moertl E., Koeppel M.A.; J. Biol. Chem. 276:16624-16634(2001). Cited for: PHOSPHORYLATION AT SER-112. | |
"p21-activated kinase 1 phosphorylates the death agonist bad andprotects cells from apoptosis."; Schurmann A., Mooney A.F., Sanders L.C., Sells M.A., Wang H.G.,Reed J.C., Bokoch G.M.; Mol. Cell. Biol. 20:453-461(2000). Cited for: PHOSPHORYLATION AT SER-112 AND SER-136. | |
"Rsk1 mediates a MEK-MAP kinase cell survival signal."; Shimamura A., Ballif B.A., Richards S.A., Blenis J.; Curr. Biol. 10:127-135(2000). Cited for: PHOSPHORYLATION AT SER-112 AND SER-136. | |
"Interleukin-3-induced phosphorylation of BAD through the proteinkinase Akt."; Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.; Science 278:687-689(1997). Cited for: PHOSPHORYLATION AT SER-112 AND SER-136, AND MUTAGENESIS OF SER-112 ANDSER-136. |