B2CL1_HUMAN - dbPTM
B2CL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B2CL1_HUMAN
UniProt AC Q07817
Protein Name Bcl-2-like protein 1
Gene Name BCL2L1
Organism Homo sapiens (Human).
Sequence Length 233
Subcellular Localization Isoform Bcl-X(L): Mitochondrion inner membrane. Mitochondrion outer membrane. Mitochondrion matrix. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.; Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release. [PubMed: 17418785; Isoform Bcl-X(S) promotes apoptosis.]
Protein Sequence MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
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
2Phosphorylation------MSQSNRELV
------CCCCCHHHH
42.1722210691
4Phosphorylation----MSQSNRELVVD
----CCCCCHHHHHH
30.4622210691
14PhosphorylationELVVDFLSYKLSQKG
HHHHHHHHHHHHHCC
21.8830631047
16UbiquitinationVVDFLSYKLSQKGYS
HHHHHHHHHHHCCCC
37.9821890473
16 (in isoform 3)Ubiquitination-37.9821890473
16 (in isoform 1)Ubiquitination-37.9821890473
16 (in isoform 2)Ubiquitination-37.9821890473
18PhosphorylationDFLSYKLSQKGYSWS
HHHHHHHHHCCCCHH
26.2030631047
28PhosphorylationGYSWSQFSDVEENRT
CCCHHHCCCCHHCCC
32.86-
47PhosphorylationGTESEMETPSAINGN
CCCCCCCCCCCCCCC
22.6422617334
49PhosphorylationESEMETPSAINGNPS
CCCCCCCCCCCCCCC
49.5621840391
62PhosphorylationPSWHLADSPAVNGAT
CCCCCCCCCCCCCCC
14.787644501
87 (in isoform 3)Ubiquitination-25.7321890473
87 (in isoform 2)Ubiquitination-25.7321890473
87 (in isoform 1)Ubiquitination-25.7321890473
87UbiquitinationVIPMAAVKQALREAG
HHHHHHHHHHHHHCC
25.7321890473
115PhosphorylationLTSQLHITPGTAYQS
HHHCCCCCCCHHHHC
12.6222617334

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
47TPhosphorylationKinaseMAPK8P45983
GPS
47TPhosphorylationKinaseMAPK9P45984
GPS
49SPhosphorylationKinasePLK3Q9H4B4
Uniprot
62SPhosphorylationKinaseCDK1P06493
Uniprot
62SPhosphorylationKinaseGSK3AP49840
PSP
62SPhosphorylationKinaseGSK3BP49841
PSP
62SPhosphorylationKinaseMAPKAPK2P49137
PSP
62SPhosphorylationKinaseMAPK8P45983
GPS
62SPhosphorylationKinaseMAPK9P45984
GPS
62SPhosphorylationKinaseMAPK14Q16539
GPS
62SPhosphorylationKinasePINK1Q9BXM7
PSP
62SPhosphorylationKinasePLK1P53350
PSP
115TPhosphorylationKinaseMAPK8P45983
GPS
115TPhosphorylationKinaseMAPK9P45984
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
49SPhosphorylation

21840391
62SPhosphorylation

19917720

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 B2CL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AVEN_HUMANAVENphysical
10949025
BNIP3_HUMANBNIP3physical
10625696
RTN1_HUMANRTN1physical
11126360
RTN4_HUMANRTN4physical
11126360
BIK_HUMANBIKphysical
16189514
RAD9A_HUMANRAD9Aphysical
16189514
BIK_HUMANBIKphysical
15694340
BID_HUMANBIDphysical
15694340
APR_HUMANPMAIP1physical
15694340
BAD_HUMANBADphysical
15705582
BAK_HUMANBAK1physical
12137781
BAX_HUMANBAXphysical
9824152
BAD_HUMANBADphysical
12137781
BAX_HUMANBAXphysical
12137781
BCL2_HUMANBCL2physical
12137781
BAK_HUMANBAK1physical
14596824
B2L11_HUMANBCL2L11physical
14596824
HRK_HUMANHRKphysical
14596824
VDAC1_HUMANVDAC1physical
15637055
BAK_HUMANBAK1physical
15901672
BIK_HUMANBIKphysical
12853473
VDAC1_HUMANVDAC1physical
12767928
BAD_HUMANBADphysical
12115603
PP1A_HUMANPPP1CAphysical
12115603
BECN1_HUMANBECN1physical
9765397
RAD9A_HUMANRAD9Aphysical
10620799
BIK_HUMANBIKphysical
11342619
CASP9_HUMANCASP9physical
9539746
APAF_HUMANAPAF1physical
9539746
IKZF3_HUMANIKZF3physical
11714801
FKBP8_HUMANFKBP8physical
12510191
B2L11_MOUSEBcl2l11physical
10198631
DYL1_HUMANDYNLL1physical
10198631
BAD_HUMANBADphysical
9389483
HRK_HUMANHRKphysical
10075695
BLID_HUMANBLIDphysical
20400521
PARK7_HUMANPARK7physical
21852238
BAX_HUMANBAXphysical
21852238
ZFYV1_HUMANZFYVE1physical
21900206
P53_HUMANTP53physical
21900206
MET23_HUMANMETTL23physical
21900206
PPHLN_HUMANPPHLN1physical
21900206
ZN219_HUMANZNF219physical
21900206
EDRF1_HUMANEDRF1physical
21900206
PDIA4_HUMANPDIA4physical
21900206
GLOD4_HUMANGLOD4physical
21900206
RBM5_HUMANRBM5physical
21900206
PLD3_HUMANPLD3physical
21900206
DOCK7_HUMANDOCK7physical
21900206
ZHX1_HUMANZHX1physical
21900206
UBR1_HUMANUBR1physical
21900206
F16P1_HUMANFBP1physical
21900206
TLE1_HUMANTLE1physical
21900206
ACTB_HUMANACTBphysical
21900206
ASPP2_HUMANTP53BP2physical
21900206
LARP1_HUMANLARP1physical
21900206
PTN_HUMANPTNphysical
21900206
CLUS_HUMANCLUphysical
21527247
B2L11_HUMANBCL2L11physical
16260615
BMF_HUMANBMFphysical
16260615
CRYAA_HUMANCRYAAphysical
14752512
CRYAB_HUMANCRYABphysical
14752512
BAD_HUMANBADphysical
18628207
BECN1_HUMANBECN1physical
18628207
ATX3_HUMANATXN3physical
23562578
BAK_HUMANBAK1physical
10085290
PRKN_HUMANPARK2physical
24999239
PINK1_HUMANPINK1physical
24999239
B2L11_HUMANBCL2L11physical
15721256
BID_HUMANBIDphysical
15721256
BAD_HUMANBADphysical
15721256
BIK_HUMANBIKphysical
15721256
BMF_HUMANBMFphysical
15721256
HRK_HUMANHRKphysical
15721256
APR_HUMANPMAIP1physical
15721256
BBC3B_HUMANBBC3physical
15721256
BBC3_HUMANBBC3physical
15721256
ASPP2_HUMANTP53BP2physical
18719108
TCTP_HUMANTPT1physical
15870695
CDN2A_HUMANCDKN2Aphysical
19049976
ARF_HUMANCDKN2Aphysical
19049976
BECN1_HUMANBECN1physical
19049976
BAX_HUMANBAXphysical
9027312
CASP1_HUMANCASP1physical
9027312
C8AP2_HUMANCASP8AP2physical
9027312
B2CL1_HUMANBCL2L1physical
9111042
BAD_HUMANBADphysical
9305851
BMF_HUMANBMFphysical
25416956
BAX_HUMANBAXphysical
19427863
B2L11_HUMANBCL2L11physical
19427863
VDAC1_HUMANVDAC1physical
20080789
MTOR_HUMANMTORphysical
20080789
GIMA5_HUMANGIMAP5physical
16509771
BID_HUMANBIDphysical
16697956
B2L11_HUMANBCL2L11physical
16697956
BAD_HUMANBADphysical
16697956
BIK_HUMANBIKphysical
16697956
HRK_HUMANHRKphysical
16697956
BBC3B_HUMANBBC3physical
16697956
BBC3_HUMANBBC3physical
16697956
BMF_HUMANBMFphysical
16697956
BAD_HUMANBADphysical
20603619
ATG5_HUMANATG5physical
16998475
PDS5A_HUMANPDS5Aphysical
26186194
BCL2_HUMANBCL2physical
26186194
BAX_HUMANBAXphysical
26186194
BAD_HUMANBADphysical
26186194
B2L11_HUMANBCL2L11physical
26186194
BNI3L_HUMANBNIP3Lphysical
9973195
BAX_HUMANBAXphysical
25241761
CASP9_HUMANCASP9physical
25241761
RAF1_HUMANRAF1physical
25241761
B2L11_HUMANBCL2L11physical
20836993
BAK_HUMANBAK1physical
20836993
P53_HUMANTP53physical
20837658
BAD_HUMANBADphysical
20837658
PRKN_HUMANPARK2physical
28038320
BBC3B_HUMANBBC3physical
28202514
BBC3_HUMANBBC3physical
28202514
BAX_HUMANBAXphysical
28202514
B2L11_HUMANBCL2L11physical
28514442
BAD_HUMANBADphysical
28514442
BCL2_HUMANBCL2physical
28514442
PDS5A_HUMANPDS5Aphysical
28514442
BAX_HUMANBAXphysical
28514442
CDK1_HUMANCDK1physical
22617334
P53_HUMANTP53physical
25115399
BAX_HUMANBAXphysical
25115399

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
D09935 Navitoclax (USAN/INN)
D09936 Navitoclax dihydrochloride (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of B2CL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycleprogression and checkpoints.";
Wang J., Beauchemin M., Bertrand R.;
Cell. Signal. 23:2030-2038(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-49, ANDMUTAGENESIS OF SER-49.
"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation actsas a functional link coupling mitotic arrest and apoptosis.";
Terrano D.T., Upreti M., Chambers T.C.;
Mol. Cell. Biol. 30:640-656(2010).
Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-62 BY CDK1, ANDSUBCELLULAR LOCATION.

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