UniProt functional annotation for Q07820



	UniProt functional annotation for Q07820

UniProt code: Q07820.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. {ECO:0000269|PubMed:10766760, ECO:0000269|PubMed:16543145}.

Subunit: Interacts with HIF3A (via C-terminus domain) (By similarity). Interacts with BAD, BOK, BIK and BMF (By similarity). Interacts with PMAIP1 (PubMed:17389404). Interacts with BBC3 (By similarity). Isoform 1 interacts with BAX, BAK1 and TPT1 (PubMed:10837489, PubMed:12149273, PubMed:15077116). Heterodimer of isoform 1 and isoform 2. Homodimers of isoform 1 or isoform 2 are not detected. Isoform 2 does not interact with pro-apoptotic BCL2-related proteins (PubMed:10837489). Interacts with RTL10/BOP (PubMed:23055042). Interacts with BCL2L11; may sequester BCL2L11 to prevent its pro-apoptotic activity (PubMed:10837489, PubMed:27013495, PubMed:17389404, PubMed:20562877). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and MCL1 is impaired in the absence of GIMAP5 (By similarity). {ECO:0000250|UniProtKB:P97287, ECO:0000250|UniProtKB:Q9Z1P3, ECO:0000269|PubMed:10837489, ECO:0000269|PubMed:12149273, ECO:0000269|PubMed:15077116, ECO:0000269|PubMed:17389404, ECO:0000269|PubMed:20562877, ECO:0000269|PubMed:23055042, ECO:0000269|PubMed:27013495}.

Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm. Mitochondrion. Nucleus, nucleoplasm. Note=Cytoplasmic, associated with mitochondria.

Induction: Expression increases early during phorbol ester-induced differentiation along the monocyte/macrophage pathway in myeloid leukemia cell line ML-1. Rapidly up-regulated by CSF2 in ML-1 cells. Up-regulated by heat shock-induced differentiation. Expression increases early during retinoic acid-induced differentiation. {ECO:0000269|PubMed:8790944, ECO:0000269|PubMed:9671497}.

Ptm: Cleaved by CASP3 during apoptosis. In intact cells cleavage occurs preferentially after Asp-127, yielding a pro-apoptotic 28 kDa C- terminal fragment.

Ptm: Rapidly degraded in the absence of phosphorylation on Thr-163 in the PEST region. {ECO:0000269|PubMed:12223490, ECO:0000269|PubMed:15241487, ECO:0000269|PubMed:23024798}.

Ptm: Phosphorylated on Ser-159, by GSK3, in response to IL3/interleukin-3 withdrawal. Phosphorylation at Ser-159 induces ubiquitination and proteasomal degradation, abrogating the anti- apoptotic activity. Treatment with taxol or okadaic acid induces phosphorylation on additional sites. {ECO:0000269|PubMed:16543145}.

Ptm: Ubiquitinated. Ubiquitination is induced by phosphorylation at Ser-159. {ECO:0000269|PubMed:16543145}.

Similarity: Belongs to the Bcl-2 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis. {ECO:0000269\|PubMed:10766760, ECO:0000269\|PubMed:16543145}.


Subunit:		Interacts with HIF3A (via C-terminus domain) (By similarity). Interacts with BAD, BOK, BIK and BMF (By similarity). Interacts with PMAIP1 (PubMed:17389404). Interacts with BBC3 (By similarity). Isoform 1 interacts with BAX, BAK1 and TPT1 (PubMed:10837489, PubMed:12149273, PubMed:15077116). Heterodimer of isoform 1 and isoform 2. Homodimers of isoform 1 or isoform 2 are not detected. Isoform 2 does not interact with pro-apoptotic BCL2-related proteins (PubMed:10837489). Interacts with RTL10/BOP (PubMed:23055042). Interacts with BCL2L11; may sequester BCL2L11 to prevent its pro-apoptotic activity (PubMed:10837489, PubMed:27013495, PubMed:17389404, PubMed:20562877). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and MCL1 is impaired in the absence of GIMAP5 (By similarity). {ECO:0000250\|UniProtKB:P97287, ECO:0000250\|UniProtKB:Q9Z1P3, ECO:0000269\|PubMed:10837489, ECO:0000269\|PubMed:12149273, ECO:0000269\|PubMed:15077116, ECO:0000269\|PubMed:17389404, ECO:0000269\|PubMed:20562877, ECO:0000269\|PubMed:23055042, ECO:0000269\|PubMed:27013495}.
Subcellular location:		Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm. Mitochondrion. Nucleus, nucleoplasm. Note=Cytoplasmic, associated with mitochondria.
Induction:		Expression increases early during phorbol ester-induced differentiation along the monocyte/macrophage pathway in myeloid leukemia cell line ML-1. Rapidly up-regulated by CSF2 in ML-1 cells. Up-regulated by heat shock-induced differentiation. Expression increases early during retinoic acid-induced differentiation. {ECO:0000269\|PubMed:8790944, ECO:0000269\|PubMed:9671497}.
Ptm:		Cleaved by CASP3 during apoptosis. In intact cells cleavage occurs preferentially after Asp-127, yielding a pro-apoptotic 28 kDa C- terminal fragment.
Ptm:		Rapidly degraded in the absence of phosphorylation on Thr-163 in the PEST region. {ECO:0000269\|PubMed:12223490, ECO:0000269\|PubMed:15241487, ECO:0000269\|PubMed:23024798}.
Ptm:		Phosphorylated on Ser-159, by GSK3, in response to IL3/interleukin-3 withdrawal. Phosphorylation at Ser-159 induces ubiquitination and proteasomal degradation, abrogating the anti- apoptotic activity. Treatment with taxol or okadaic acid induces phosphorylation on additional sites. {ECO:0000269\|PubMed:16543145}.
Ptm:		Ubiquitinated. Ubiquitination is induced by phosphorylation at Ser-159. {ECO:0000269\|PubMed:16543145}.
Similarity:		Belongs to the Bcl-2 family. {ECO:0000305}.