O60238 · BNI3L_HUMAN
- ProteinBCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- GeneBNIP3L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids219 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60238
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Note: Colocalizes with SPATA18 at the mitochondrion outer membrane.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 188-208 | Helical | ||||
Sequence: VFIPSLFLSHVLALGLGIYIG |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 187 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000064957 | 1-219 | UniProt | BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like | |||
Sequence: MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY | |||||||
Modified residue | 62 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 120 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 166 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Self-associates. Interacts with BNIP3 and STEAP3. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).
(Microbial infection) Interacts with human adenovirus-2 E1B 19 kDa protein.
(Microbial infection) Interacts with Kaposi's sarcoma-associated herpesvirus protein VIRF-1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-101 | Disordered | ||||
Sequence: MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQED | ||||||
Compositional bias | 9-69 | Polar residues | ||||
Sequence: PPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNG | ||||||
Compositional bias | 79-98 | Polar residues | ||||
Sequence: QHESGQSSSRGSSHCDSPSP | ||||||
Motif | 126-148 | BH3 | ||||
Sequence: EGEKEVEALKKSADWVSDWSSRP |
Sequence similarities
Belongs to the NIP3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O60238-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length219
- Mass (Da)23,930
- Last updated1998-08-01 v1
- Checksum19372E897BC63609
O60238-2
- Name2
- Differences from canonical
- 1-40: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056248 | 1-40 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 9-69 | Polar residues | ||||
Sequence: PPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNG | ||||||
Compositional bias | 79-98 | Polar residues | ||||
Sequence: QHESGQSSSRGSSHCDSPSP | ||||||
Sequence conflict | 107 | in Ref. 4; AAN04051 | ||||
Sequence: D → E | ||||||
Sequence conflict | 150 | in Ref. 9; CAI46217 | ||||
Sequence: N → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB004788 EMBL· GenBank· DDBJ | BAA28692.1 EMBL· GenBank· DDBJ | mRNA | ||
AF079221 EMBL· GenBank· DDBJ | AAC27723.1 EMBL· GenBank· DDBJ | mRNA | ||
AF067396 EMBL· GenBank· DDBJ | AAD03589.1 EMBL· GenBank· DDBJ | mRNA | ||
AF536326 EMBL· GenBank· DDBJ | AAN04051.1 EMBL· GenBank· DDBJ | mRNA | ||
AF452712 EMBL· GenBank· DDBJ | AAL50978.1 EMBL· GenBank· DDBJ | mRNA | ||
AF255051 EMBL· GenBank· DDBJ | AAF70290.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK315870 EMBL· GenBank· DDBJ | BAF98761.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316315 EMBL· GenBank· DDBJ | BAH14686.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019501 EMBL· GenBank· DDBJ | AAV38308.1 EMBL· GenBank· DDBJ | mRNA | ||
AL132665 EMBL· GenBank· DDBJ | CAI46217.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AC011726 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC015743 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022911 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001559 EMBL· GenBank· DDBJ | AAH01559.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009603 EMBL· GenBank· DDBJ | AAH09603.1 EMBL· GenBank· DDBJ | mRNA |