B2L11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: B2L11_MOUSE
• UniProt AC: O54918
• Protein Name: Bcl-2-like protein 11
• Gene Name: Bcl2l11
• Organism: Mus musculus (Mouse).
• Sequence Length: 196
• Subcellular Localization: Membrane ; Peripheral membrane protein . Mitochondrion. Associated with intracytoplasmic membranes.
• Protein Description: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent..
• Protein Sequence: MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH

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
55	Phosphorylation	GDRCPHGSPQGPLAP CCCCCCCCCCCCCCC	15.83	12818176
65	Phosphorylation	GPLAPPASPGPFATR CCCCCCCCCCCCCCC	35.84	12818176
71	Phosphorylation	ASPGPFATRSPLFIF CCCCCCCCCCCEEEE	31.87	25338131
73	Phosphorylation	PGPFATRSPLFIFVR CCCCCCCCCEEEEEE	22.92	26824392
82	Phosphorylation	LFIFVRRSSLLSRSS EEEEEECHHHHCCCC	18.12	25159016
83	Phosphorylation	FIFVRRSSLLSRSSS EEEEECHHHHCCCCC	31.36	22942356
86	Phosphorylation	VRRSSLLSRSSSGYF EECHHHHCCCCCCCE	35.10	25159016
88	Phosphorylation	RSSLLSRSSSGYFSF CHHHHCCCCCCCEEE	26.02	28833060
89	Phosphorylation	SSLLSRSSSGYFSFD HHHHCCCCCCCEEEC	27.03	28833060
90	Phosphorylation	SLLSRSSSGYFSFDT HHHCCCCCCCEEECC	38.47	23684622
92	Phosphorylation	LSRSSSGYFSFDTDR HCCCCCCCEEECCCC	9.67	23984901
94	Phosphorylation	RSSSGYFSFDTDRSP CCCCCCEEECCCCCC	17.46	23984901
97	Phosphorylation	SGYFSFDTDRSPAPM CCCEEECCCCCCCCC	31.16	23984901
100	Phosphorylation	FSFDTDRSPAPMSCD EEECCCCCCCCCCCC	28.37	22817900
105	Phosphorylation	DRSPAPMSCDKSTQT CCCCCCCCCCCCCCC	20.36	22817900
110	Phosphorylation	PMSCDKSTQTPSPPC CCCCCCCCCCCCCCH	42.05	22942356
112	Phosphorylation	SCDKSTQTPSPPCQA CCCCCCCCCCCCHHH	26.31	19841067
114	Phosphorylation	DKSTQTPSPPCQAFN CCCCCCCCCCHHHHH	44.88	25266776
161	Phosphorylation	GDEFNETYTRRVFAN HHHHCHHHHHHHHCC	7.65	-
170	Phosphorylation	RRVFANDYREAEDHP HHHHCCCHHHCCCCH	15.34	24719451

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
55	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
55	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
55	S	Phosphorylation	Kinase	MAPK10	Q61831	GPS
55	S	Phosphorylation	Kinase	MAPK9	Q9WTU6	GPS
55	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
65	S	Phosphorylation	Kinase	MK10	Q61831	PhosphoELM
65	S	Phosphorylation	Kinase	MAPK9	Q9WTU6	GPS
65	S	Phosphorylation	Kinase	JNK2	P45984	PSP
65	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
65	S	Phosphorylation	Kinase	MAPK10	P53779	GPS
65	S	Phosphorylation	Kinase	JNK1	P45983	PSP
65	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
65	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
65	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
65	S	Phosphorylation	Kinase	MAPK	-	Uniprot
73	S	Phosphorylation	Kinase	MAPK10	Q61831	GPS
73	S	Phosphorylation	Kinase	MAPK9	Q9WTU6	GPS
73	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
83	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
92	Y	Phosphorylation	Kinase	LYN	P07948	PSP
100	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
100	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
100	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
112	T	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
112	T	Phosphorylation	Kinase	JNK1	P45983	PSP
112	T	Phosphorylation	Kinase	MAPK3	Q63844	GPS
112	T	Phosphorylation	Kinase	MAPK1	P63085	GPS
114	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
161	Y	Phosphorylation	Kinase	LYN	P07948	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Cbl	P22682	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
65	S	Phosphorylation	Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation.	21478148
65	S	ubiquitylation	Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation.	21478148

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of B2L11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCL1_HUMAN	MCL1	physical	15694340
B2LA1_HUMAN	BCL2A1	physical	15694340
B2CL2_HUMAN	BCL2L2	physical	15694340
B2CL1_HUMAN	BCL2L1	physical	15694340
BCL2_HUMAN	BCL2	physical	15694340
BCL2_HUMAN	BCL2	physical	10198631
B2CL1_HUMAN	BCL2L1	physical	10198631
B2LA1_HUMAN	BCL2A1	physical	10198631
MCL1_HUMAN	MCL1	physical	10198631
DYL1_HUMAN	DYNLL1	physical	10198631
TRIM2_MOUSE	Trim2	physical	21478148
1433B_MOUSE	Ywhab	physical	16282323
BCL2_MOUSE	Bcl2	physical	15136728
B2CL1_MOUSE	Bcl2l1	physical	15136728
DYL1_MOUSE	Dynll1	physical	15136728
BCL2_MOUSE	Bcl2	physical	23840878
BCL2_MOUSE	Bcl2	physical	17289999
MCL1_MOUSE	Mcl1	physical	17289999

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Identification of a novel Bcl-2-interacting mediator of cell death(Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), andits role in rapid ischemic tolerance-induced neuroprotection.";
Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M.,Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.;
J. Biol. Chem. 286:19331-19339(2011).
Cited for: INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, UBIQUITINATION,PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-55; SER-65 ANDSER-73.
PubMed: 21478148

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
PubMed: 19367708