dbPTM

B2L11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	B2L11_HUMAN
UniProt AC	O43521
Protein Name	Bcl-2-like protein 11
Gene Name	BCL2L11
Organism	Homo sapiens (Human).
Sequence Length	198
Subcellular Localization	Endomembrane system Peripheral membrane protein. Associated with intracytoplasmic membranes.. Isoform BimEL: Mitochondrion. Translocates from microtubules to mitochondria on loss of cell adherence. Isoform BimL: Mitochondrion. Isoform BimS:
Protein Description	Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis..
Protein Sequence	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKQPSDVSS -----CCCCCCCCCH	62.53	25953088
12	S-nitrosylation	PSDVSSECDREGRQL CCCCCHHCCCCCCCC	6.89	24105792
34	Phosphorylation	QLRPGAPTSLQTEPQ CCCCCCCCCCCCCCC	41.35	-
35	Phosphorylation	LRPGAPTSLQTEPQG CCCCCCCCCCCCCCC	19.88	-
35 (in isoform 9)	Phosphorylation	-	19.88	-
35 (in isoform 3)	Phosphorylation	-	19.88	-
35 (in isoform 6)	Phosphorylation	-	19.88	-
35 (in isoform 7)	Phosphorylation	-	19.88	-
38 (in isoform 3)	Phosphorylation	-	55.73	-
38	Phosphorylation	GAPTSLQTEPQGNPE CCCCCCCCCCCCCCC	55.73	-
38 (in isoform 6)	Phosphorylation	-	55.73	-
38 (in isoform 7)	Phosphorylation	-	55.73	-
38 (in isoform 9)	Phosphorylation	-	55.73	-
43 (in isoform 6)	Phosphorylation	-	26.63	-
43 (in isoform 7)	Phosphorylation	-	26.63	-
43 (in isoform 3)	Phosphorylation	-	26.63	-
43 (in isoform 9)	Phosphorylation	-	26.63	-
44 (in isoform 5)	Phosphorylation	-	58.66	12591950
44 (in isoform 17)	Phosphorylation	-	58.66	12591950
44 (in isoform 16)	Phosphorylation	-	58.66	12591950
44 (in isoform 15)	Phosphorylation	-	58.66	12591950
44 (in isoform 18)	Phosphorylation	-	58.66	12591950
44 (in isoform 2)	Phosphorylation	-	58.66	12591950
50 (in isoform 12)	Phosphorylation	-	28.32	28787133
56 (in isoform 2)	Phosphorylation	-	38.53	12591950
58 (in isoform 2)	Phosphorylation	-	26.60	12591950
59	Phosphorylation	GDSCPHGSPQGPLAP CCCCCCCCCCCCCCC	15.83	12818176
60 (in isoform 12)	Phosphorylation	-	47.98	22210691
69	Phosphorylation	GPLAPPASPGPFATR CCCCCCCCCCCCCCC	35.84	17525735
77	Phosphorylation	PGPFATRSPLFIFMR CCCCCCCCCEEEEEE	22.92	22617229
86	Phosphorylation	LFIFMRRSSLLSRSS EEEEEECHHHHCCCC	18.25	30266825
87	Phosphorylation	FIFMRRSSLLSRSSS EEEEECHHHHCCCCC	31.36	23401153
90	Phosphorylation	MRRSSLLSRSSSGYF EECHHHHCCCCCCCE	35.10	23090842
92	Phosphorylation	RSSLLSRSSSGYFSF CHHHHCCCCCCCEEE	26.02	29978859
93	Phosphorylation	SSLLSRSSSGYFSFD HHHHCCCCCCCEEEC	27.03	29978859
94	Phosphorylation	SLLSRSSSGYFSFDT HHHCCCCCCCEEECC	38.47	17503221
96	Phosphorylation	LSRSSSGYFSFDTDR HCCCCCCCEEECCCC	9.67	29978859
98	Phosphorylation	RSSSGYFSFDTDRSP CCCCCCEEECCCCCC	17.46	-
104	Phosphorylation	FSFDTDRSPAPMSCD EEECCCCCCCCCCCC	28.37	21924351
109	Phosphorylation	DRSPAPMSCDKSTQT CCCCCCCCCCCCCCC	20.36	23186163
113	Phosphorylation	APMSCDKSTQTPSPP CCCCCCCCCCCCCCC	16.70	21712546
114	Phosphorylation	PMSCDKSTQTPSPPC CCCCCCCCCCCCCCH	42.05	29083192
116	Phosphorylation	SCDKSTQTPSPPCQA CCCCCCCCCCCCHHH	26.31	22817900
118	Phosphorylation	DKSTQTPSPPCQAFN CCCCCCCCCCHHHHH	44.88	25849741
127	Phosphorylation	PCQAFNHYLSAMASM CHHHHHHHHHHHHHH	11.94	29083192
129	Phosphorylation	QAFNHYLSAMASMRQ HHHHHHHHHHHHHHH	14.61	29083192
133	Phosphorylation	HYLSAMASMRQAEPA HHHHHHHHHHHCCCC	11.04	29083192
172	Phosphorylation	RRVFLNNYQAAEDHP HHHHHHCHHHHCCCH	9.84	28796482

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
44	S	Phosphorylation	Kinase	CDK1	P06493	PSP
44	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
56	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
56	T	Phosphorylation	Kinase	MAPK9	P45984	GPS
58	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
58	S	Phosphorylation	Kinase	MAPK10	P53779	GPS
69	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
69	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
69	S	Phosphorylation	Kinase	MAPK	-	Uniprot
87	S	Phosphorylation	Kinase	AKT1	P31749	PSP
87	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
93	S	Phosphorylation	Kinase	AURKA	O14965	GPS
94	S	Phosphorylation	Kinase	AURKA	O14965	GPS
98	S	Phosphorylation	Kinase	AURKA	O14965	GPS
104	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
104	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
116	T	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
116	T	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
118	S	Phosphorylation	Kinase	JNK-SUBFAMILY	-	GPS
118	S	Phosphorylation	Kinase	JNK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:18198176
-	K	Ubiquitination	E3 ubiquitin ligase	CISH	Q9NSE2	PMID:18420585
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM2	Q9C040	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
69	S	Phosphorylation	15486195
Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with TRIM2 and polyubiquitination, followed by proteasomal degradation.
69	S	ubiquitylation	15486195
Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with TRIM2 and polyubiquitination, followed by proteasomal degradation.

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 B2L11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCL2_HUMAN	BCL2	physical	15694340
B2CL1_HUMAN	BCL2L1	physical	15694340
MCL1_HUMAN	MCL1	physical	15694340
MCL1_HUMAN	MCL1	physical	10837489
VDAC1_RAT	Vdac1	physical	12118373
B2CL1_HUMAN	BCL2L1	physical	9430630
B2CL2_HUMAN	BCL2L2	physical	9430630
MCL1_HUMAN	MCL1	physical	9731710
BCL2_HUMAN	BCL2	physical	9731710
B2CL2_HUMAN	BCL2L2	physical	9731710
B2LA1_HUMAN	BCL2A1	physical	9731710
B2CL1_HUMAN	BCL2L1	physical	9731710
BCL2_HUMAN	BCL2	physical	19805519
SNF5_HUMAN	SMARCB1	physical	15096481
GTF2I_HUMAN	GTF2I	physical	15096481
TRIM2_RAT	Trim2	physical	21478148
TRIM2_HUMAN	TRIM2	physical	21478148
FBW1A_HUMAN	BTRC	physical	22388891
CISH_HUMAN	CISH	physical	19622774
ELOB_HUMAN	TCEB2	physical	19622774
VHL_HUMAN	VHL	physical	19305426
RACK1_HUMAN	GNB2L1	physical	18420585
CISH_HUMAN	CISH	physical	18420585
CD302_HUMAN	CD302	physical	18420585
FBW1A_HUMAN	BTRC	physical	19150432
MCL1_HUMAN	MCL1	physical	19150432
A4_HUMAN	APP	physical	21832049
1433B_HUMAN	YWHAB	physical	16282323
FBW1A_HUMAN	BTRC	physical	23912711
AURKA_HUMAN	AURKA	physical	23912711
FGL1_HUMAN	FGL1	physical	21988832
RIOK3_HUMAN	RIOK3	physical	21988832
FEM1C_HUMAN	FEM1C	physical	21988832
B2CL1_HUMAN	BCL2L1	physical	19427863
F1_VACCW	F1L	physical	17074758
BCL2_HUMAN	BCL2	physical	17074758
MCL1_HUMAN	MCL1	physical	17097560
BCL2_HUMAN	BCL2	physical	17097560
AT2A3_HUMAN	ATP2A3	physical	26186194
ANKL2_HUMAN	ANKLE2	physical	26186194
MTHR_HUMAN	MTHFR	physical	26186194
DYL2_HUMAN	DYNLL2	physical	26186194
DYL1_HUMAN	DYNLL1	physical	26186194
FBW1A_HUMAN	BTRC	physical	26186194
FBW1B_HUMAN	FBXW11	physical	26186194
MCL1_HUMAN	MCL1	physical	26186194
RHPN2_HUMAN	RHPN2	physical	26186194
BAX_HUMAN	BAX	physical	26186194
BCL2_HUMAN	BCL2	physical	26186194
UBP27_HUMAN	USP27X	physical	27013495
B2CL1_HUMAN	BCL2L1	physical	27013495
MCL1_HUMAN	MCL1	physical	27013495
BCL2_HUMAN	BCL2	physical	20836993
B2CL1_HUMAN	BCL2L1	physical	20836993
MCL1_HUMAN	MCL1	physical	20836993
MK01_HUMAN	MAPK1	physical	24269611
MK03_HUMAN	MAPK3	physical	24269611
MCL1_HUMAN	MCL1	physical	28514442
RHPN2_HUMAN	RHPN2	physical	28514442
MTHR_HUMAN	MTHFR	physical	28514442
ANKL2_HUMAN	ANKLE2	physical	28514442
BCL2_HUMAN	BCL2	physical	28514442
FBW1A_HUMAN	BTRC	physical	28514442
AT2A3_HUMAN	ATP2A3	physical	28514442
FBW1B_HUMAN	FBXW11	physical	28514442
MTA2_HUMAN	MTA2	physical	28514442

Drug and Disease Associations

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.

Regulatory Network of B2L11_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.	18220336 [Abstract]

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