B2CL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: B2CL1_MOUSE
• UniProt AC: Q64373
• Protein Name: Bcl-2-like protein 1
• Gene Name: Bcl2l1
• Organism: Mus musculus (Mouse).
• Sequence Length: 233
• Subcellular Localization: Mitochondrion membrane ; Single-pass membrane protein . Nucleus membrane; Single-pass membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to the centrosome when phosphorylated at Ser-49.
• 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 (By similarity). May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).; Isoform Bcl-X(S) promotes apoptosis..
• Protein Sequence: MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK

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
14	Phosphorylation	ELVVDFLSYKLSQKG HHHHHHHHHHHHHCC	21.88	-
49	Phosphorylation	EAERETPSAINGNPS HHHHCCCCCCCCCCC	49.56	-
62	Phosphorylation	PSWHLADSPAVNGAT CCCCCCCCCCCCCCC	14.78	-
73	Phosphorylation	NGATGHSSSLDAREV CCCCCCCCCCCHHHH	29.28	-
87	Ubiquitination	VIPMAAVKQALREAG HHHHHHHHHHHHHCC	25.73	-
216	Phosphorylation	RFNRWFLTGMTVAGV HHHHHHHHCHHHHHH	18.55	30635358
219	Phosphorylation	RWFLTGMTVAGVVLL HHHHHCHHHHHHHHH	14.46	30635358
228	Phosphorylation	AGVVLLGSLFSRK-- HHHHHHHHHHCCC--	26.64	30635358
231	Phosphorylation	VLLGSLFSRK----- HHHHHHHCCC-----	44.44	30635358

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
14	S	Phosphorylation	Kinase	MST1	Q13043	PSP
49	S	Phosphorylation	Kinase	PLK3	Q60806	Uniprot
62	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
49	S	Phosphorylation	Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity).	-
62	S	Phosphorylation	Phosphorylated on Ser-62 by CDK1.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of B2CL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2L11_MOUSE	Bcl2l11	physical	11859372
BAX_MOUSE	Bax	physical	8798452
P53_MOUSE	Trp53	physical	16151013
BBC3_MOUSE	Bbc3	physical	16151013
BAX_MOUSE	Bax	physical	7650488
PAXI_MOUSE	Pxn	physical	14699151
P53_MOUSE	Trp53	physical	14963330
CDN2A_MOUSE	Cdkn2a	physical	19049976
ARF_MOUSE	Cdkn2a	physical	19049976
BECN1_MOUSE	Becn1	physical	19049976

Drug and Disease Associations

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