BAD_MOUSE - dbPTM
BAD_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
20PhosphorylationHALGLRKSDPGIRSL
HHHCCCCCCCCHHHC
42.4724719451
26PhosphorylationKSDPGIRSLGSDAGG
CCCCCHHHCCCCCCC
34.85-
29PhosphorylationPGIRSLGSDAGGRRW
CCHHHCCCCCCCCCC
29.5822871156
67PhosphorylationTDRGLGPSLTEDQPG
CCCCCCCCCCCCCCC
46.23-
76PhosphorylationTEDQPGPYLAPGLLG
CCCCCCCCCCCCCCC
22.7822817900
94PhosphorylationHQQGRAATNSHHGGA
HHCCCHHCCCCCCCC
35.9522817900
96PhosphorylationQGRAATNSHHGGAGA
CCCHHCCCCCCCCCC
16.7122817900
108PhosphorylationAGAMETRSRHSSYPA
CCCCCCCCCCCCCCC
41.5926239621
111PhosphorylationMETRSRHSSYPAGTE
CCCCCCCCCCCCCCC
30.3827742792
112PhosphorylationETRSRHSSYPAGTEE
CCCCCCCCCCCCCCC
29.0727087446
113PhosphorylationTRSRHSSYPAGTEED
CCCCCCCCCCCCCCC
10.5027742792
117PhosphorylationHSSYPAGTEEDEGME
CCCCCCCCCCCCCCC
38.0027742792
123OxidationGTEEDEGMEEELSPF
CCCCCCCCCCCCCCC
5.7217242355
128PhosphorylationEGMEEELSPFRGRSR
CCCCCCCCCCCCCCC
25.8525168779
131Asymmetric dimethylarginineEEELSPFRGRSRSAP
CCCCCCCCCCCCCCC
42.89-
131MethylationEEELSPFRGRSRSAP
CCCCCCCCCCCCCCC
42.89-
133Asymmetric dimethylarginineELSPFRGRSRSAPPN
CCCCCCCCCCCCCCC
25.33-
133MethylationELSPFRGRSRSAPPN
CCCCCCCCCCCCCCC
25.33-
134PhosphorylationLSPFRGRSRSAPPNL
CCCCCCCCCCCCCCH
33.1527087446
136PhosphorylationPFRGRSRSAPPNLWA
CCCCCCCCCCCCHHH
46.5027087446
155PhosphorylationGRELRRMSDEFEGSF
HHHHHHCCHHCCCCC
31.9827087446
161PhosphorylationMSDEFEGSFKGLPRP
CCHHCCCCCCCCCCC
19.3125619855
170PhosphorylationKGLPRPKSAGTATQM
CCCCCCCCCCHHHHH
34.3125521595
173PhosphorylationPRPKSAGTATQMRQS
CCCCCCCHHHHHHHH
26.6726643407
175PhosphorylationPKSAGTATQMRQSAG
CCCCCHHHHHHHHHC
23.8026643407
180PhosphorylationTATQMRQSAGWTRII
HHHHHHHHHCCHHHH
20.5529514104
201PhosphorylationNLGKGGSTPSQ----
CCCCCCCCCCC----
30.1816166315

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
26SPhosphorylationKinaseIKKBO88351
PSP
94TPhosphorylationKinasePIM3P58750
PSP
96SPhosphorylationKinasePIM3P58750
PSP
112SPhosphorylationKinasePIM3Q86V86
PSP
112SPhosphorylationKinaseRPS6KA2Q9WUT3
GPS
112SPhosphorylationKinaseRPS6KA3P18654
GPS
112SPhosphorylationKinaseRPS6KA5Q8C050
GPS
112SPhosphorylationKinaseMAPK8Q91Y86
GPS
112SPhosphorylationKinasePAK1Q13153
PSP
112SPhosphorylationKinasePAK1O88643
Uniprot
112SPhosphorylationKinaseAKT1P31749
PSP
112SPhosphorylationKinasePAK4Q8BTW9
Uniprot
112SPhosphorylationKinasePAK5Q8C015
Uniprot
112SPhosphorylationKinasePIM1P11309
PSP
112SPhosphorylationKinasePIM1P06803
PSP
112SPhosphorylationKinasePIM2Q9P1W9
PSP
112SPhosphorylationKinasePIM2Q62070
Uniprot
112SPhosphorylationKinasePAK2Q8CIN4
Uniprot
112SPhosphorylationKinasePIM3P58750
Uniprot
112SPhosphorylationKinaseRAF1P04049
PSP
112SPhosphorylationKinaseRAF1Q99N57
Uniprot
112SPhosphorylationKinaseAKT-FAMILY-GPS
112SPhosphorylationKinasePKA-FAMILY-GPS
112SPhosphorylationKinaseRAF-FAMILY-GPS
112SPhosphorylationKinaseRSK-SUBFAMILY-GPS
112SPhosphorylationKinasePKA-Uniprot
112SPhosphorylationKinasePKB_GROUP-PhosphoELM
112SPhosphorylationKinaseRSK_GROUP-PhosphoELM
112SPhosphorylationKinaseP90RSKP18653
PSP
112SPhosphorylationKinasePRKACAP05132
GPS
112SPhosphorylationKinaseAKT1P31750
PSP
112SPhosphorylationKinaseRPS6KA1Q15418
GPS
112SPhosphorylationKinasePKACAP17612
PSP
112SPhosphorylationKinasePKACAP00517
PSP
117TPhosphorylationKinaseCSK21Q60737
PhosphoELM
117TPhosphorylationKinaseCSNK2A1P19139
GPS
128SPhosphorylationKinaseMAPK8Q91Y86
GPS
128SPhosphorylationKinaseCDK1P06493
PSP
128SPhosphorylationKinaseCDK1P11440
PSP
136SPhosphorylationKinasePIM2Q9P1W9
PSP
136SPhosphorylationKinaseAKT1P31749
PSP
136SPhosphorylationKinasePKACAP17612
PSP
136SPhosphorylationKinasePIM3Q86V86
PSP
136SPhosphorylationKinasePKACAP00517
PSP
136SPhosphorylationKinasePIM3P58750
PSP
136SPhosphorylationKinaseAKT-FAMILY-GPS
136SPhosphorylationKinasePKA-FAMILY-GPS
136SPhosphorylationKinaseRAF-FAMILY-GPS
136SPhosphorylationKinaseAKT1P31750
PSP
136SPhosphorylationKinasePKA-Uniprot
136SPhosphorylationKinasePKB_GROUP-PhosphoELM
136SPhosphorylationKinasePIM1P06803
PSP
136SPhosphorylationKinasePAK1Q13153
PSP
136SPhosphorylationKinasePRKCQQ02111
Uniprot
136SPhosphorylationKinaseRPS6KA1Q15418
GPS
136SPhosphorylationKinasePAK1O88643
Uniprot
136SPhosphorylationKinasePAK4Q8BTW9
GPS
136SPhosphorylationKinaseRPS6KB1Q8BSK8
Uniprot
136SPhosphorylationKinasePRKACAP05132
GPS
136SPhosphorylationKinaseRPS6KA1P18653
Uniprot
136SPhosphorylationKinasePIM1P11309
PSP
155SPhosphorylationKinasePKA-Uniprot
155SPhosphorylationKinaseRPS6KA5O75582
GPS
155SPhosphorylationKinaseRPS6KA1Q15418
GPS
155SPhosphorylationKinaseRSK-SUBFAMILY-GPS
155SPhosphorylationKinaseRSK_GROUP-PhosphoELM
155SPhosphorylationKinaseRAF-FAMILY-GPS
155SPhosphorylationKinasePKA-FAMILY-GPS
155SPhosphorylationKinaseAKT1P31750
PSP
155SPhosphorylationKinasePIM2Q9P1W9
PSP
155SPhosphorylationKinaseP90RSKP18653
PSP
155SPhosphorylationKinaseAKT-FAMILY-GPS
155SPhosphorylationKinasePRKG1P0C605
GPS
155SPhosphorylationKinasePKG1Q13976
PSP
155SPhosphorylationKinasePIM3P58750
PSP
155SPhosphorylationKinasePKACAP00517
PSP
155SPhosphorylationKinasePIM1P11309
PSP
155SPhosphorylationKinasePIM3Q86V86
PSP
155SPhosphorylationKinasePKACAP17612
PSP
155SPhosphorylationKinasePRKACAP05132
GPS
170SPhosphorylationKinaseCAMK2GQ13555
PSP
170SPhosphorylationKinasePIM3P58750
PSP
173TPhosphorylationKinasePIM3P58750
PSP
201TPhosphorylationKinaseMAPK8Q91Y86
GPS
201TPhosphorylationKinaseJNK1P45983
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
112SPhosphorylation

9381178
112SPhosphorylation

9381178
131RMethylation

10611223
131RPhosphorylation

10611223
133RMethylation

10611223
133RPhosphorylation

10611223
136SMethylation

9381178
136SPhosphorylation

9381178
136SPhosphorylation

9381178
136SPhosphorylation

9381178
136SPhosphorylation

9381178
155SPhosphorylation

11717309
155SPhosphorylation

11717309
155SPhosphorylation

11717309
170SPhosphorylation

11717309

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SODM_MOUSESod2physical
12931191
KAPCA_MOUSEPrkacaphysical
12931191
WASF1_MOUSEWasf1physical
12931191
HXK4_MOUSEGckphysical
12931191
BCL2_MOUSEBcl2physical
21084607
B2CL1_MOUSEBcl2l1physical
21084607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAD_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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