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Phorbol-12-myristate-13-acetate-induced protein 1 (PMA-induced protein 1) (Immediate-early-response protein APR) (Protein Noxa)

 APR_HUMAN               Reviewed;          54 AA.
Q13794; B2R4T7; Q8N589;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
15-MAR-2017, entry version 130.
RecName: Full=Phorbol-12-myristate-13-acetate-induced protein 1;
Short=PMA-induced protein 1;
AltName: Full=Immediate-early-response protein APR;
AltName: Full=Protein Noxa;
Name=PMAIP1; Synonyms=NOXA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2398525;
Hijikata M., Kato N., Sato T., Kagami Y., Shimotohno K.;
"Molecular cloning and characterization of a cDNA for a novel phorbol-
12-myristate-13-acetate-responsive gene that is highly expressed in an
adult T-cell leukemia cell line.";
J. Virol. 64:4632-4639(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Ovary, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND INDUCTION.
PubMed=10807576; DOI=10.1126/science.288.5468.1053;
Oda E., Ohki R., Murasawa H., Nemoto J., Shibue T., Yamashita T.,
Tokino T., Taniguchi T., Tanaka N.;
"Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of
p53-induced apoptosis.";
Science 288:1053-1058(2000).
[6]
FUNCTION, INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH BAX, AND
MUTAGENESIS OF LEU-29.
PubMed=15705586; DOI=10.1074/jbc.M412630200;
Sun Y., Leaman D.W.;
"Involvement of Noxa in cellular apoptotic responses to interferon,
double-stranded RNA, and virus infection.";
J. Biol. Chem. 280:15561-15568(2005).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF PHE-32
AND LYS-35, AND INTERACTION WITH MCL1.
PubMed=15694340; DOI=10.1016/j.molcel.2004.12.030;
Chen L., Willis S.N., Wei A., Smith B.J., Fletcher J.I., Hinds M.G.,
Colman P.M., Day C.L., Adams J.M., Huang D.C.S.;
"Differential targeting of prosurvival Bcl-2 proteins by their BH3-
only ligands allows complementary apoptotic function.";
Mol. Cell 17:393-403(2005).
[8]
FUNCTION, INTERACTION WITH MCL1, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=17374615; DOI=10.1074/jbc.M611186200;
Han J., Goldstein L.A., Hou W., Rabinowich H.;
"Functional linkage between NOXA and Bim in mitochondrial apoptotic
events.";
J. Biol. Chem. 282:16223-16231(2007).
[9]
FUNCTION, MUTAGENESIS OF LEU-29; PHE-32 AND LEU-36, AND INTERACTION
WITH MCL1.
PubMed=17389404; DOI=10.1073/pnas.0701297104;
Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J.,
Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.;
"Structural insights into the degradation of Mcl-1 induced by BH3
domains.";
Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 19-43 IN COMPLEX WITH
BCL2A1.
Northeast structural genomics consortium (NESG);
"Crystal structure of human BFL-1 in complex with NOXA BH3 peptide.";
Submitted (JUL-2010) to the PDB data bank.
-!- FUNCTION: Promotes activation of caspases and apoptosis. Promotes
mitochondrial membrane changes and efflux of apoptogenic proteins
from the mitochondria. Contributes to p53/TP53-dependent apoptosis
after radiation exposure. Promotes proteasomal degradation of
MCL1. Competes with BAK1 for binding to MCL1 and can displace BAK1
from its binding site on MCL1 (By similarity). Competes with
BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from
its binding site on MCL1. {ECO:0000250,
ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15694340,
ECO:0000269|PubMed:15705586, ECO:0000269|PubMed:17374615,
ECO:0000269|PubMed:17389404}.
-!- SUBUNIT: Interacts with MCL1, BCL2A1 and BAX.
{ECO:0000269|PubMed:15694340, ECO:0000269|PubMed:15705586,
ECO:0000269|PubMed:17374615, ECO:0000269|PubMed:17389404,
ECO:0000269|Ref.10}.
-!- INTERACTION:
P10415:BCL2; NbExp=3; IntAct=EBI-707392, EBI-77694;
P10415-1:BCL2; NbExp=3; IntAct=EBI-707392, EBI-4370304;
Q07820:MCL1; NbExp=5; IntAct=EBI-707392, EBI-1003422;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15705586,
ECO:0000269|PubMed:17374615}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13794-1; Sequence=Displayed;
Name=2;
IsoId=Q13794-2; Sequence=VSP_056247;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in adult T-cell leukemia cell
line.
-!- INDUCTION: Up-regulated by p53/TP53, phorbol esters, double-
stranded RNA, IFNB1/IFN-beta and viruses.
{ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15705586,
ECO:0000269|PubMed:17374615}.
-!- DOMAIN: The BH3 motif is essential for pro-apoptotic activity.
-!- SIMILARITY: Belongs to the PMAIP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D90070; BAA14111.1; -; mRNA.
EMBL; AK311943; BAG34884.1; -; mRNA.
EMBL; AC107990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013120; AAH13120.1; -; mRNA.
EMBL; BC032663; AAH32663.1; -; mRNA.
CCDS; CCDS11975.1; -. [Q13794-1]
PIR; I37018; I37018.
RefSeq; NP_066950.1; NM_021127.2. [Q13794-1]
UniGene; Hs.96; -.
PDB; 3MQP; X-ray; 2.24 A; B=19-43.
PDBsum; 3MQP; -.
ProteinModelPortal; Q13794; -.
SMR; Q13794; -.
BioGrid; 111379; 11.
IntAct; Q13794; 11.
MINT; MINT-1391244; -.
STRING; 9606.ENSP00000326119; -.
iPTMnet; Q13794; -.
PhosphoSitePlus; Q13794; -.
BioMuta; PMAIP1; -.
EPD; Q13794; -.
MaxQB; Q13794; -.
PaxDb; Q13794; -.
PeptideAtlas; Q13794; -.
PRIDE; Q13794; -.
DNASU; 5366; -.
Ensembl; ENST00000269518; ENSP00000269518; ENSG00000141682. [Q13794-2]
Ensembl; ENST00000316660; ENSP00000326119; ENSG00000141682. [Q13794-1]
GeneID; 5366; -.
KEGG; hsa:5366; -.
UCSC; uc002lic.3; human. [Q13794-1]
CTD; 5366; -.
DisGeNET; 5366; -.
GeneCards; PMAIP1; -.
HGNC; HGNC:9108; PMAIP1.
HPA; HPA051063; -.
MIM; 604959; gene.
neXtProt; NX_Q13794; -.
OpenTargets; ENSG00000141682; -.
PharmGKB; PA33434; -.
eggNOG; ENOG410J6XT; Eukaryota.
eggNOG; ENOG4111AWA; LUCA.
GeneTree; ENSGT00530000065105; -.
HOGENOM; HOG000034020; -.
HOVERGEN; HBG004273; -.
InParanoid; Q13794; -.
KO; K10131; -.
OMA; WRQTELP; -.
OrthoDB; EOG091G0V5H; -.
PhylomeDB; Q13794; -.
Reactome; R-HSA-111448; Activation of NOXA and translocation to mitochondria.
Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
SIGNOR; Q13794; -.
EvolutionaryTrace; Q13794; -.
GeneWiki; Phorbol-12-myristate-13-acetate-induced_protein_1; -.
GenomeRNAi; 5366; -.
PRO; PR:Q13794; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141682; -.
CleanEx; HS_PMAIP1; -.
ExpressionAtlas; Q13794; baseline and differential.
Genevisible; Q13794; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:InterPro.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:BHF-UCL.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:InterPro.
GO; GO:0043331; P:response to dsRNA; IDA:HGNC.
GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
InterPro; IPR024140; Noxa.
PANTHER; PTHR14299; PTHR14299; 1.
Pfam; PF15150; PMAIP1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Mitochondrion; Reference proteome.
CHAIN 1 54 Phorbol-12-myristate-13-acetate-induced
protein 1.
/FTId=PRO_0000064644.
REGION 41 50 Required for mitochondrial location.
MOTIF 29 37 BH3.
VAR_SEQ 20 54 ELEVECATQLRRFGDKLNFRQKLLNLISKLFCSGT -> GP
AGTAGTARDQAGFAIGMQLRFTRGKKLLSSSLSSSPLALPR
GHEEQVQVAGSRVCYSTQEIWRQTELPAETSESDIQTLLLR
NLTASKTCMRGLLQKSFLRRCTFHQFEERLHCN (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056247.
MUTAGEN 29 29 L->A: Reduced interaction with BAX.
{ECO:0000269|PubMed:15705586,
ECO:0000269|PubMed:17389404}.
MUTAGEN 29 29 L->E: Loss of interaction with MCL1 and
of increased MCL1 degradation; when
associated with E-32 and E-32.
{ECO:0000269|PubMed:15705586,
ECO:0000269|PubMed:17389404}.
MUTAGEN 32 32 F->E: Loss of interaction with MCL1 and
of increased MCL1 degradation; when
associated with E-29 and E-36.
{ECO:0000269|PubMed:15694340,
ECO:0000269|PubMed:17389404}.
MUTAGEN 32 32 F->I: Alters specificity of protein
interaction and enhances pro-apoptotic
activity; when associated with E-35.
{ECO:0000269|PubMed:15694340,
ECO:0000269|PubMed:17389404}.
MUTAGEN 35 35 K->E: Alters specificity of protein
interaction and enhances pro-apoptotic
activity; when associated with I-32.
{ECO:0000269|PubMed:15694340}.
MUTAGEN 36 36 L->E: Loss of interaction with MCL1 and
of increased MCL1 degradation; when
associated with E-29 and E-32.
{ECO:0000269|PubMed:17389404}.
HELIX 21 40 {ECO:0000244|PDB:3MQP}.
SEQUENCE 54 AA; 6030 MW; 291A142B27167E70 CRC64;
MPGKKARKNA QPSPARAPAE LEVECATQLR RFGDKLNFRQ KLLNLISKLF CSGT


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