BNIP3_HUMAN - dbPTM
BNIP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BNIP3_HUMAN
UniProt AC Q12983
Protein Name BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
Gene Name BNIP3
Organism Homo sapiens (Human).
Sequence Length 259
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. 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 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. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway..
Protein Sequence MGDAAADPPGPALPCEFLRPGCGAPLSPGAQLGRGAPTSAFPPPAAEAHPAARRGLRSPQLPSGAMSQNGAPGMQEESLQGSWVELHFSNNGNGGSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRASETDTHSIGEKNSSQSEEDDIERRKEVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSAEFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF
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
17PhosphorylationGPALPCEFLRPGCGA
CCCCCCCCCCCCCCC
18.26-
24PhosphorylationFLRPGCGAPLSPGAQ
CCCCCCCCCCCCCCC
20.73-
39PhosphorylationLGRGAPTSAFPPPAA
CCCCCCCCCCCCCHH
12.94-
54PhosphorylationEAHPAARRGLRSPQL
HHCHHHHCCCCCCCC
37.0624961811
57PhosphorylationPAARRGLRSPQLPSG
HHHHCCCCCCCCCCC
42.3525627689
58PhosphorylationAARRGLRSPQLPSGA
HHHCCCCCCCCCCCC
40.1924961811
59PhosphorylationARRGLRSPQLPSGAM
HHCCCCCCCCCCCCC
37.4925627689
61PhosphorylationRGLRSPQLPSGAMSQ
CCCCCCCCCCCCCCC
27.5425262027
62PhosphorylationGLRSPQLPSGAMSQN
CCCCCCCCCCCCCCC
31.69-
66PhosphorylationPQLPSGAMSQNGAPG
CCCCCCCCCCCCCCC
42.0422798277
70PhosphorylationSGAMSQNGAPGMQEE
CCCCCCCCCCCCCCH
44.1525627689
72PhosphorylationAMSQNGAPGMQEESL
CCCCCCCCCCCCHHH
24.9422798277
82PhosphorylationQEESLQGSWVELHFS
CCHHHCCCEEEEEEE
43.64-
84PhosphorylationESLQGSWVELHFSNN
HHHCCCEEEEEEECC
25.5825262027
86PhosphorylationLQGSWVELHFSNNGN
HCCCEEEEEEECCCC
34.0920363803
89PhosphorylationSWVELHFSNNGNGGS
CEEEEEEECCCCCCC
47.60-
90UbiquitinationWVELHFSNNGNGGSV
EEEEEEECCCCCCCC
57.8421906983
92PhosphorylationELHFSNNGNGGSVPA
EEEEECCCCCCCCCE
40.6020363803
93PhosphorylationLHFSNNGNGGSVPAS
EEEECCCCCCCCCEE
47.3120363803
95PhosphorylationFSNNGNGGSVPASVS
EECCCCCCCCCEEEE
44.9220363803
104UbiquitinationVPASVSIYNGDMEKI
CCEEEEEECCCHHEE
72.79-
104PhosphorylationVPASVSIYNGDMEKI
CCEEEEEECCCHHEE
72.7925884760
111UbiquitinationYNGDMEKILLDAQHE
ECCCHHEEEHHHHHH
48.52-
119PhosphorylationLLDAQHESGRSSSKS
EHHHHHHCCCCCCCC
26.6725849741
122PhosphorylationAQHESGRSSSKSSHC
HHHHCCCCCCCCCCC
47.8325849741
123PhosphorylationQHESGRSSSKSSHCD
HHHCCCCCCCCCCCC
36.7229514088
124PhosphorylationHESGRSSSKSSHCDS
HHCCCCCCCCCCCCC
40.7225159151
126PhosphorylationSGRSSSKSSHCDSPP
CCCCCCCCCCCCCCC
55.5428450419
127PhosphorylationGRSSSKSSHCDSPPR
CCCCCCCCCCCCCCC
6.1928450419
131PhosphorylationSKSSHCDSPPRSQTP
CCCCCCCCCCCCCCC
54.0525159151
135UbiquitinationHCDSPPRSQTPQDTN
CCCCCCCCCCCCCCC
62.23-
135PhosphorylationHCDSPPRSQTPQDTN
CCCCCCCCCCCCCCC
62.2325262027
137PhosphorylationDSPPRSQTPQDTNRA
CCCCCCCCCCCCCCC
28.5425159151
139MethylationPPRSQTPQDTNRASE
CCCCCCCCCCCCCCC
33.76-
140PhosphorylationPRSQTPQDTNRASET
CCCCCCCCCCCCCCC
30.0720068231
141PhosphorylationRSQTPQDTNRASETD
CCCCCCCCCCCCCCC
15.5830108239
142PhosphorylationSQTPQDTNRASETDT
CCCCCCCCCCCCCCC
20.8220068231
144PhosphorylationTPQDTNRASETDTHS
CCCCCCCCCCCCCCC
16.02-
145PhosphorylationPQDTNRASETDTHSI
CCCCCCCCCCCCCCC
4.2723403867
147PhosphorylationDTNRASETDTHSIGE
CCCCCCCCCCCCCCC
28.2323403867
148PhosphorylationTNRASETDTHSIGEK
CCCCCCCCCCCCCCC
16.6020068231
149PhosphorylationNRASETDTHSIGEKN
CCCCCCCCCCCCCCC
24.6223927012
151PhosphorylationASETDTHSIGEKNSS
CCCCCCCCCCCCCCC
3.5829255136
152UbiquitinationSETDTHSIGEKNSSQ
CCCCCCCCCCCCCCC
46.22-
153UbiquitinationETDTHSIGEKNSSQS
CCCCCCCCCCCCCCC
44.25-
155UbiquitinationDTHSIGEKNSSQSEE
CCCCCCCCCCCCCCH
27.01-
157PhosphorylationHSIGEKNSSQSEEDD
CCCCCCCCCCCCHHH
6.8225159151
158PhosphorylationSIGEKNSSQSEEDDI
CCCCCCCCCCCHHHH
25.6025159151
160PhosphorylationGEKNSSQSEEDDIER
CCCCCCCCCHHHHHH
50.7628355574
169UbiquitinationEDDIERRKEVESILK
HHHHHHHHHHHHHHH
5.42-
173PhosphorylationERRKEVESILKKNSD
HHHHHHHHHHHHCCC
25.4929514088
176UbiquitinationKEVESILKKNSDWIW
HHHHHHHHHCCCCCC
10.52-
188PhosphorylationWIWDWSSRPENIPPK
CCCCCCCCCCCCCCH
19.52-
189PhosphorylationIWDWSSRPENIPPKE
CCCCCCCCCCCCCHH
34.30-
190PhosphorylationWDWSSRPENIPPKEF
CCCCCCCCCCCCHHH
18.35-
191PhosphorylationDWSSRPENIPPKEFL
CCCCCCCCCCCHHHH
29.69-
192PhosphorylationWSSRPENIPPKEFLF
CCCCCCCCCCHHHHC
27.81-
193PhosphorylationSSRPENIPPKEFLFK
CCCCCCCCCHHHHCC
33.19-
195UbiquitinationRPENIPPKEFLFKHP
CCCCCCCHHHHCCCC
-
200UbiquitinationPPKEFLFKHPKRTAT
CCHHHHCCCCCCEEE
-
204MethylationFLFKHPKRTATLSMR
HHCCCCCCEEEEEEC
-
205PhosphorylationLFKHPKRTATLSMRN
HCCCCCCEEEEEECC
20068231
207PhosphorylationKHPKRTATLSMRNTS
CCCCCEEEEEECCCH
24275569
209PhosphorylationPKRTATLSMRNTSVM
CCCEEEEEECCCHHH
20068231
213PhosphorylationATLSMRNTSVMKKGG
EEEEECCCHHHHCCC
20068231
214PhosphorylationTLSMRNTSVMKKGGI
EEEECCCHHHHCCCC
20068231
218UbiquitinationRNTSVMKKGGIFSAE
CCCHHHHCCCCCCHH
-
253PhosphorylationIYIGRRLTTSTSTF-
HHHCCCCCCCCCCC-
-
254PhosphorylationYIGRRLTTSTSTF--
HHCCCCCCCCCCC--
-
255PhosphorylationIGRRLTTSTSTF---
HCCCCCCCCCCC---
-
256PhosphorylationGRRLTTSTSTF----
CCCCCCCCCCC----
-
257PhosphorylationRRLTTSTSTF-----
CCCCCCCCCC-----
-
258PhosphorylationRLTTSTSTF------
CCCCCCCCC------
-

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
253TPhosphorylationKinasePKACAP17612
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BNIP3_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 BNIP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMM11_HUMANTMEM11physical
16189514
BNI3L_HUMANBNIP3Lphysical
16189514
BNIP3_HUMANBNIP3physical
16189514
BNIP3_HUMANBNIP3physical
9396766
B2CL1_HUMANBCL2L1physical
10625696
BNIP3_HUMANBNIP3physical
10625696
HDAC1_HUMANHDAC1physical
19339613
RHEB_HUMANRHEBphysical
17928295
TGM2_HUMANTGM2physical
21988832
ZEP1_HUMANHIVEP1physical
21988832
BCL2_HUMANBCL2physical
23504944
BNIP3_HUMANBNIP3physical
25416956
BNI3L_HUMANBNIP3Lphysical
25416956
KTN1_HUMANKTN1physical
25416956
TMM11_HUMANTMEM11physical
25416956
CLC7A_HUMANCLEC7Aphysical
25416956
FATE1_HUMANFATE1physical
25416956
LRAD1_HUMANLDLRAD1physical
25416956
OPA1_HUMANOPA1physical
20436456
BNI3L_HUMANBNIP3Lphysical
21516116
BNI3L_HUMANBNIP3Lphysical
28514442
PPTC7_HUMANPPTC7physical
28514442
TMM11_HUMANTMEM11physical
28514442
P4R3B_HUMANSMEK2physical
28514442
PINK1_HUMANPINK1physical
27528605

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 BNIP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-93, AND MASSSPECTROMETRY.

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