dbPTM

BNIP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BNIP2_HUMAN
UniProt AC	Q12982
Protein Name	BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
Gene Name	BNIP2
Organism	Homo sapiens (Human).
Sequence Length	314
Subcellular Localization	Cytoplasm. Cytoplasm, perinuclear region. Localizes to the nuclear envelope region and to other cytoplasmic structures.
Protein Description	Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins..
Protein Sequence	MEGVELKEEWQDEDFPIPLPEDDSIEADILAITGPEDQPGSLEVNGNKVRKKLMAPDISLTLDPSDGSVLSDDLDESGEIDLDGLDTPSENSNEFEWEDDLPKPKTTEVIRKGSITEYTAAEEKEDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESSQPNYRYLMDNLFKYVIGTLELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQVDQELNGKQDEPKNEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Phosphorylation	GPEDQPGSLEVNGNK CCCCCCCCEEECCHH	28.21	24275569
47 (in isoform 2)	Phosphorylation	-	34.15	22210691
59	Phosphorylation	KLMAPDISLTLDPSD EEECCCEEEEECCCC	23.76	22468782
65	Phosphorylation	ISLTLDPSDGSVLSD EEEEECCCCCCCCCC	55.03	22468782
71	Phosphorylation	PSDGSVLSDDLDESG CCCCCCCCCCCCCCC	27.24	22468782
77	Phosphorylation	LSDDLDESGEIDLDG CCCCCCCCCCCCCCC	41.20	24275569
85	Phosphorylation	GEIDLDGLDTPSENS CCCCCCCCCCCCCCC	7.09	24719451
87	Phosphorylation	IDLDGLDTPSENSNE CCCCCCCCCCCCCCC	33.48	24275569
89	Phosphorylation	LDGLDTPSENSNEFE CCCCCCCCCCCCCCC	52.05	24275569
92	Phosphorylation	LDTPSENSNEFEWED CCCCCCCCCCCCCCC	33.41	24275569
101	Phosphorylation	EFEWEDDLPKPKTTE CCCCCCCCCCCCCCE	10.19	27251275
106	Phosphorylation	DDLPKPKTTEVIRKG CCCCCCCCCEEEECC	36.39	26074081
107	Phosphorylation	DLPKPKTTEVIRKGS CCCCCCCCEEEECCC	34.09	26074081
109	Phosphorylation	PKPKTTEVIRKGSIT CCCCCCEEEECCCCC	4.88	27642862
114	Phosphorylation	TEVIRKGSITEYTAA CEEEECCCCCEEEEE	29.40	29255136
116	Phosphorylation	VIRKGSITEYTAAEE EEECCCCCEEEEEEE	25.33	22167270
118	Phosphorylation	RKGSITEYTAAEEKE ECCCCCEEEEEEECC	7.95	30278072
119	Phosphorylation	KGSITEYTAAEEKED CCCCCEEEEEEECCC	17.10	23927012
145	Ubiquitination	QDHRVDMKAIEPYKK CCCCCCHHHCCCCCC	41.57	-
162	Phosphorylation	SHGGYYGDGLNAIVV HCCCCCCCCHHHEEE	42.14	-
174 (in isoform 2)	Ubiquitination	-	8.01	-
185	Phosphorylation	SSQPNYRYLMDNLFK CCCCCHHHHHHHHHH	8.95	24667141
186 (in isoform 2)	Ubiquitination	-	2.28	-
198	Phosphorylation	FKYVIGTLELLVAEN HHHHHHHHHHHHCCC	3.53	-
207 (in isoform 2)	Ubiquitination	-	2.23	-
208	Phosphorylation	LVAENYMIVYLNGAT HHCCCEEEEEECCCC	0.99	-
210	Phosphorylation	AENYMIVYLNGATTR CCCEEEEEECCCCCC	5.41	-
213	Phosphorylation	YMIVYLNGATTRRKM EEEEEECCCCCCCCC	23.00	-
214 (in isoform 2)	Ubiquitination	-	12.53	-
228	Ubiquitination	PSLGWLRKCYQQIDR CCHHHHHHHHHHHHH	34.81	-
230	Phosphorylation	LGWLRKCYQQIDRRL HHHHHHHHHHHHHHH	13.39	-
233	Ubiquitination	LRKCYQQIDRRLRKN HHHHHHHHHHHHHHH	2.34	-
235	Phosphorylation	KCYQQIDRRLRKNLK HHHHHHHHHHHHHHH	40.96	20166139
237	Phosphorylation	YQQIDRRLRKNLKSL HHHHHHHHHHHHHHE	10.74	18088087
239	Phosphorylation	QIDRRLRKNLKSLII HHHHHHHHHHHHEEE	71.82	27642862
240	Phosphorylation	IDRRLRKNLKSLIIV HHHHHHHHHHHEEEE	46.39	19651622
245	Ubiquitination	RKNLKSLIIVHPSWF HHHHHHEEEECHHHH	3.89	-
266	Ubiquitination	VTRPFISSKFSQKIR HHHHHHCHHHHHHHH	32.67	-
267	Ubiquitination	TRPFISSKFSQKIRY HHHHHCHHHHHHHHH	42.09	21890473
281 (in isoform 2)	Ubiquitination	-	3.59	-
290 (in isoform 2)	Ubiquitination	-	3.41	-
306	Phosphorylation	VDQELNGKQDEPKNE HHHHHCCCCCCCCCC	54.20	-
329	Ubiquitination	---------------------- ----------------------		21890473
329 (in isoform 2)	Ubiquitination	-		-
333 (in isoform 2)	Ubiquitination	-		-
340	Ubiquitination	--------------------------------- ---------------------------------		-
349	Ubiquitination	------------------------------------------ ------------------------------------------		-
368 (in isoform 2)	Ubiquitination	-		-
388	Ubiquitination	--------------------------------------------------------------------------------- ---------------------------------------------------------------------------------		-
427	Ubiquitination	------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------		-

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 BNIP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BNIP2_HUMAN !!

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 BNIP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BCL2_HUMAN	BCL2	physical	12901880
CREB3_HUMAN	CREB3	physical	16189514
CDC42_HUMAN	CDC42	physical	10799524
BNIP2_HUMAN	BNIP2	physical	10954711
CDC42_HUMAN	CDC42	physical	10954711
RHG01_HUMAN	ARHGAP1	physical	10954711
RHG01_HUMAN	ARHGAP1	physical	10551883
FRK_HUMAN	FRK	physical	25416956
KLC1_HUMAN	KLC1	physical	25416956
MYO5B_HUMAN	MYO5B	physical	25416956
UPK1B_HUMAN	UPK1B	physical	25416956
FATE1_HUMAN	FATE1	physical	25416956

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 BNIP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-114, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-116, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.	19007248 [Abstract]