B2CL1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: B2CL1_RAT
• UniProt AC: P53563
• Protein Name: Bcl-2-like protein 1
• Gene Name: Bcl2l1
• Organism: Rattus norvegicus (Rat).
• 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 (By similarity).; Isoform Bcl-X(S) promotes apoptosis..
• Protein Sequence: MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK

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
49	Phosphorylation	EPERETPSAINGNPS CCCCCCCCCCCCCCC	49.56	-
62	Phosphorylation	PSWHLADSPAVNGAT CCCCCCCCCCCCCCC	14.78	18951975
87	Ubiquitination	VIPMAAVKQALREAG HHHHHHHHHHHHHCC	25.73	-
106	Phosphorylation	LRYRRAFSDLTSQLH HHHHHHHHHHHHHCC	30.63	18951975
228	Phosphorylation	AGVVLLGSLFSRK-- HHHHHHHHHHCCC--	26.64	18951975

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
49	S	Phosphorylation	Kinase	PLK3	Q9R011	Uniprot
62	S	Phosphorylation	Kinase	CDK1	P39951	Uniprot
106	S	Phosphorylation	Kinase	AKT1	P47196	PSP

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNM1L_RAT	Dnm1l	physical	18250306
P53_RAT	Tp53	physical	17073802

Drug and Disease Associations

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