BNI3L_HUMAN - dbPTM
BNI3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BNI3L_HUMAN
UniProt AC O60238
Protein Name BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
Gene Name BNIP3L
Organism Homo sapiens (Human).
Sequence Length 219
Subcellular Localization Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane
Single-pass membrane protein . Colocalizes with SPATA18 at the mitochondrion outer membrane.
Protein Description Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. 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. May function as a tumor suppressor..
Protein Sequence MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
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
34PhosphorylationPPPAGLNSSWVELPM
CCCCCCCCCEEECCC		30.53-
35PhosphorylationPPAGLNSSWVELPMN
CCCCCCCCEEECCCC		33.78-
62PhosphorylationGGLEHVPSSSSIHNG
CCCCCCCCCCCCCCC		41.5923401153
63PhosphorylationGLEHVPSSSSIHNGD
CCCCCCCCCCCCCCC		23.2623401153
64PhosphorylationLEHVPSSSSIHNGDM
CCCCCCCCCCCCCCH		37.3330266825
65PhosphorylationEHVPSSSSIHNGDME
CCCCCCCCCCCCCHH		29.7930266825
82PhosphorylationLLDAQHESGQSSSRG
EEEHHCCCCCCCCCC		39.7529255136
85PhosphorylationAQHESGQSSSRGSSH
HHCCCCCCCCCCCCC		33.5329255136
86PhosphorylationQHESGQSSSRGSSHC
HCCCCCCCCCCCCCC		19.0325849741
87PhosphorylationHESGQSSSRGSSHCD
CCCCCCCCCCCCCCC		46.0029255136
90PhosphorylationGQSSSRGSSHCDSPS
CCCCCCCCCCCCCCC		18.7930108239
91PhosphorylationQSSSRGSSHCDSPSP
CCCCCCCCCCCCCCC		30.8430108239
95PhosphorylationRGSSHCDSPSPQEDG
CCCCCCCCCCCCCCC		32.4430576142
95UbiquitinationRGSSHCDSPSPQEDG
CCCCCCCCCCCCCCC		32.44-
96UbiquitinationGSSHCDSPSPQEDGQ
CCCCCCCCCCCCCCC		36.46-
97PhosphorylationSSHCDSPSPQEDGQI
CCCCCCCCCCCCCCE		43.0730576142
114UbiquitinationDVEMHTSRDHSSQSE
EEEEECCCCCCCCCH		46.98-
117PhosphorylationMHTSRDHSSQSEEEV
EECCCCCCCCCHHHH		34.0723401153
118PhosphorylationHTSRDHSSQSEEEVV
ECCCCCCCCCHHHHH		34.0125159151
120PhosphorylationSRDHSSQSEEEVVEG
CCCCCCCCHHHHHHC		49.2629255136
129UbiquitinationEEVVEGEKEVEALKK
HHHHHCHHHHHHHHH		77.30-
135UbiquitinationEKEVEALKKSADWVS
HHHHHHHHHHCCHHH		52.29-
136UbiquitinationKEVEALKKSADWVSD
HHHHHHHHHCCHHHC		52.29-
137PhosphorylationEVEALKKSADWVSDW
HHHHHHHHCCHHHCC		29.8527251275
137UbiquitinationEVEALKKSADWVSDW
HHHHHHHHCCHHHCC		29.85-
139UbiquitinationEALKKSADWVSDWSS
HHHHHHCCHHHCCCC		54.0921890473
154UbiquitinationRPENIPPKEFHFRHP
CCCCCCCCHHCCCCC		68.6021890473
154UbiquitinationRPENIPPKEFHFRHP
CCCCCCCCHHCCCCC		68.6021890473
164PhosphorylationHFRHPKRSVSLSMRK
CCCCCCCCEEEEECC		23.3730266825
166PhosphorylationRHPKRSVSLSMRKSG
CCCCCCEEEEECCCC		18.9023401153
168PhosphorylationPKRSVSLSMRKSGAM
CCCCEEEEECCCCCC		14.7223401153
176AcetylationMRKSGAMKKGGIFSA
ECCCCCCCCCCCCCH		47.9712431203
177UbiquitinationRKSGAMKKGGIFSAE
CCCCCCCCCCCCCHH		49.65-
219PhosphorylationSTPSASTY-------
CCCCCCCC-------		17.67-
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 BNI3L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BNI3L_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 BNI3L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOK5_HUMANDOK5physical
16189514
EWS_HUMANEWSR1physical
16189514
BNI3L_HUMANBNIP3Lphysical
16189514
TMM11_HUMANTMEM11physical
16189514
ROBO2_HUMANROBO2physical
21900206
GNB5_HUMANGNB5physical
21900206
KLH23_HUMANKLHL23physical
21900206
GBP2_HUMANGBP2physical
21900206
MLP3A_HUMANMAP1LC3Aphysical
20010802
BNIP3_HUMANBNIP3physical
19060904
ECM1_HUMANECM1physical
21988832
CSKP_HUMANCASKphysical
21988832
KCC1D_HUMANCAMK1Dphysical
21988832
DUS3_HUMANDUSP3physical
21988832
BNI3L_HUMANBNIP3Lphysical
25416956
TMM11_HUMANTMEM11physical
25416956
SMCO4_HUMANSMCO4physical
25416956
CLC7A_HUMANCLEC7Aphysical
25416956
FATE1_HUMANFATE1physical
25416956
LRAD1_HUMANLDLRAD1physical
25416956
BNIP3_HUMANBNIP3physical
26186194
BNI3L_HUMANBNIP3Lphysical
21516116
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 BNI3L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.

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