dbPTM

BNIP3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BNIP3_MOUSE
UniProt AC	O55003
Protein Name	BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
Gene Name	Bnip3
Organism	Mus musculus (Mouse).
Sequence Length	187
Subcellular Localization	Mitochondrion. Mitochondrion outer membrane Single-pass membrane protein. Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with
Protein Description	Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (By similarity). Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway (By similarity)..
Protein Sequence	MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	LLDAQHESGRSSSKS EHHHHHHCCCCCCCC	37.06	27818261
51	Phosphorylation	AQHESGRSSSKSSHC HHHHCCCCCCCCCCC	42.35	23984901
52	Phosphorylation	QHESGRSSSKSSHCD HHHCCCCCCCCCCCC	40.19	29472430
53	Phosphorylation	HESGRSSSKSSHCDS HHCCCCCCCCCCCCC	37.49	29472430
55	Phosphorylation	SGRSSSKSSHCDSPP CCCCCCCCCCCCCCC	27.54	25159016
56	Phosphorylation	GRSSSKSSHCDSPPR CCCCCCCCCCCCCCC	31.69	25159016
60	Phosphorylation	SKSSHCDSPPRSQTP CCCCCCCCCCCCCCC	42.04	27742792
64	Phosphorylation	HCDSPPRSQTPQDTN CCCCCCCCCCCCCCC	44.15	27742792
66	Phosphorylation	DSPPRSQTPQDTNRA CCCCCCCCCCCCCCH	24.94	27742792
70	Phosphorylation	RSQTPQDTNRAEIDS CCCCCCCCCCHHHHH	22.74	25159016
77	Phosphorylation	TNRAEIDSHSFGEKN CCCHHHHHHCCCCCC	27.05	27742792
79	Phosphorylation	RAEIDSHSFGEKNST CHHHHHHCCCCCCCC	38.61	25521595
83	Ubiquitination	DSHSFGEKNSTLSEE HHHCCCCCCCCCCHH	57.48	22790023
85	Phosphorylation	HSFGEKNSTLSEEDY HCCCCCCCCCCHHHH	41.62	25521595
86	Phosphorylation	SFGEKNSTLSEEDYI CCCCCCCCCCHHHHH	43.63	25521595
88	Phosphorylation	GEKNSTLSEEDYIER CCCCCCCCHHHHHHH	38.74	27087446
92	Phosphorylation	STLSEEDYIERRREV CCCCHHHHHHHHHHH	14.15	27742792
101	Phosphorylation	ERRREVESILKKNSD HHHHHHHHHHHHCCC	38.09	23140645
104	Ubiquitination	REVESILKKNSDWIW HHHHHHHHHCCCCCC	48.52	22790023
128	Ubiquitination	PPKEFLFKHPKRTAT CCHHHHCCCCCCEEE	62.23	27667366
135	Phosphorylation	KHPKRTATLSMRNTS CCCCCEEEEEECCCH	20.82	26060331
141	Phosphorylation	ATLSMRNTSVMKKGG EEEEECCCHHHHCCC	16.60	-
142	Phosphorylation	TLSMRNTSVMKKGGI EEEECCCHHHHCCCC	24.62	-
146	Ubiquitination	RNTSVMKKGGIFSAD CCCHHHHCCCCCCHH	44.25	22790023

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
Oops, there are no upstream regulatory protein records of BNIP3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BNIP3_MOUSE !!

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 BNIP3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BNIP3_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of BNIP3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-79, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-85 AND SER-88,AND MASS SPECTROMETRY.	17242355 [Abstract]
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86 AND SER-88, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92, AND MASSSPECTROMETRY.	17947660 [Abstract]