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PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4)

 PAWR_HUMAN              Reviewed;         340 AA.
Q96IZ0; O75796; Q6FHY9; Q8N700;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=PRKC apoptosis WT1 regulator protein;
AltName: Full=Prostate apoptosis response 4 protein;
Short=Par-4;
Name=PAWR; Synonyms=PAR4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INTERACTION WITH WT1.
PubMed=8943350; DOI=10.1128/MCB.16.12.6945;
Johnstone R.W., See R.H., Sells S.F., Wang J., Muthukkumar S.,
Englert C., Haber D.A., Licht J.D., Sugrue S.P., Roberts T.,
Rangnekar V.M., Shi Y.;
"A novel repressor, par-4, modulates transcription and growth
suppression functions of the Wilms' tumor suppressor WT1.";
Mol. Cell. Biol. 16:6945-6956(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-78.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-42; ARG-78;
ALA-137 AND ALA-202.
NIEHS SNPs program;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
TISSUE=Blood;
PubMed=12242017; DOI=10.1016/S0378-1119(02)00826-0;
Hsu S.-C., Kirschenbaum F., Miller J., Cordell B., McCarthy J.V.;
"Structural and functional characterization of the upstream regulatory
region of the human gene encoding prostate apoptosis response factor-
4.";
Gene 295:109-116(2002).
[6]
FUNCTION IN APOPTOSIS AND TUMOR REGRESSION.
PubMed=11585763;
Chakraborty M., Qiu S.G., Vasudevan K.M., Rangnekar V.M.;
"Par-4 drives trafficking and activation of Fas and Fasl to induce
prostate cancer cell apoptosis and tumor regression.";
Cancer Res. 61:7255-7263(2001).
[7]
INTERACTION WITH SQSTM1 AND PRKCZ.
PubMed=11755531; DOI=10.1016/S0014-5793(01)03224-0;
Chang S., Kim J.H., Shin J.;
"p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes
PAR-4-induced PKCzeta inhibition.";
FEBS Lett. 510:57-61(2002).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH THAP1.
PubMed=12717420; DOI=10.1038/sj.onc.1206271;
Roussigne M., Cayrol C., Clouaire T., Amalric F., Girard J.-P.;
"THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-
response-4 (Par-4) to PML nuclear bodies.";
Oncogene 22:2432-2442(2003).
[9]
INTERACTION WITH AATF.
PubMed=14627703; DOI=10.1074/jbc.M309811200;
Guo Q., Xie J.;
"AATF inhibits aberrant production of amyloid beta peptide 1-42 by
interacting directly with Par-4.";
J. Biol. Chem. 279:4596-4603(2004).
[10]
INTERACTION WITH BACE1.
PubMed=15671026; DOI=10.1074/jbc.M411933200;
Xie J., Guo Q.;
"PAR-4 is involved in regulation of beta-secretase cleavage of the
Alzheimer amyloid precursor protein.";
J. Biol. Chem. 280:13824-13832(2005).
[11]
INTERACTION WITH SPSB1 AND SPSB2, AND MUTAGENESIS OF ASN-72.
PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
"Structural basis for protein recognition by B30.2/SPRY domains.";
Mol. Cell 24:967-976(2006).
[12]
REVIEW ON FUNCTION IN APOPTOSIS AND NEURODEGENERATIVE DISEASES.
PubMed=12565819; DOI=10.1016/S0014-4827(02)00016-2;
El-Guendy N., Rangnekar V.M.;
"Apoptosis by Par-4 in cancer and neurodegenerative diseases.";
Exp. Cell Res. 283:51-66(2003).
[13]
REVIEW.
PubMed=14755681; DOI=10.1002/jcb.20000;
Gurumurthy S., Rangnekar V.M.;
"Par-4 inducible apoptosis in prostate cancer cells.";
J. Cell. Biochem. 91:504-512(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20] {ECO:0000244|PDB:2JK9}
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 67-74 IN COMPLEX WITH SPSB1,
INTERACTION WITH SPSB1; SPSB2 AND SPSB4, MUTAGENESIS OF ALA-66;
GLU-68; LEU-69; ASN-71 AND ASN-72, AND MOTIF.
PubMed=20561531; DOI=10.1016/j.jmb.2010.06.017;
Filippakopoulos P., Low A., Sharpe T.D., Uppenberg J., Yao S.,
Kuang Z., Savitsky P., Lewis R.S., Nicholson S.E., Norton R.S.,
Bullock A.N.;
"Structural basis for Par-4 recognition by the SPRY domain- and SOCS
box-containing proteins SPSB1, SPSB2, and SPSB4.";
J. Mol. Biol. 401:389-402(2010).
-!- FUNCTION: Pro-apoptopic protein capable of selectively inducing
apoptosis in cancer cells, sensitizing the cells to diverse
apoptotic stimuli and causing regression of tumors in animal
models. Induces apoptosis in certain cancer cells by activation of
the Fas prodeath pathway and coparallel inhibition of NF-kappa-B
transcriptional activity. Inhibits the transcriptional activation
and augments the transcriptional repression mediated by WT1. Down-
regulates the anti-apoptotic protein BCL2 via its interaction with
WT1. Seems also to be a transcriptional repressor by itself. May
be directly involved in regulating the amyloid precursor protein
(APP) cleavage activity of BACE1. {ECO:0000269|PubMed:11585763}.
-!- SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with
WT1 (PubMed:8943350). Interacts with THAP1 (PubMed:12717420).
Interacts with AATF (PubMed:14627703). Interacts with BACE1
(PubMed:15671026). Interacts with SPSB1 (via B30.2/SPRY domain);
this interaction is direct and occurs in association with the
Elongin BC complex (PubMed:17189197, PubMed:20561531). Interacts
with SPSB2 (via B30.2/SPRY domain); this interaction occurs in
association with the Elongin BC complex (PubMed:17189197,
PubMed:20561531). Interacts with SPSB4 (via B30.2/SPRY domain)
(PubMed:20561531); this interaction occurs in association with the
Elongin BC complex (PubMed:20561531). Component of a ternary
complex composed of SQSTM1 and PRKCZ (PubMed:11755531). Interacts
with actin (By similarity). {ECO:0000250|UniProtKB:Q62627,
ECO:0000269|PubMed:11755531, ECO:0000269|PubMed:12717420,
ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15671026,
ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:20561531,
ECO:0000269|PubMed:8943350}.
-!- INTERACTION:
P11021:HSPA5; NbExp=8; IntAct=EBI-595869, EBI-354921;
Q96BD6:SPSB1; NbExp=2; IntAct=EBI-595869, EBI-2659201;
Q9D5L7:Spsb1 (xeno); NbExp=2; IntAct=EBI-595869, EBI-8821912;
O88838:Spsb2 (xeno); NbExp=6; IntAct=EBI-595869, EBI-8820410;
Q8R5B6:Spsb4 (xeno); NbExp=3; IntAct=EBI-595869, EBI-8821982;
P08670:VIM; NbExp=2; IntAct=EBI-595869, EBI-353844;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic
in absence of apoptosis signal and in normal cells. Nuclear in
most cancer cell lines. Nuclear entry seems to be essential but
not sufficient for apoptosis (By similarity). Nuclear localization
includes nucleoplasm and PML nuclear bodies. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Expression is elevated in
various neurodegenerative diseases such as amyotrophic lateral
sclerosis, Alzheimer, Parkinson and Huntington diseases and
stroke. Down-regulated in several cancers.
{ECO:0000269|PubMed:8943350}.
-!- INDUCTION: By apoptosis.
-!- DOMAIN: The leucine-zipper domain is not essential for apoptosis,
but is required for sensitization of cells to exogenous apoptotic
insults and for interaction with its partners. {ECO:0000250}.
-!- DOMAIN: The SAC domain is a death-inducing domain selective for
apoptosis induction in cancer cells. This domain is essential for
nuclear entry, Fas activation, inhibition of NF-kappa-B activity
and induction of apoptosis in cancer cells (By similarity).
{ECO:0000250}.
-!- DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition
by proteins containing a B30.2/SPRY domain.
{ECO:0000269|PubMed:20561531}.
-!- PTM: Preferentially phosphorylated at the Thr-163 by PKC in cancer
cells. {ECO:0000250}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PAWRID41641ch12q21.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pawr/";
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EMBL; U63809; AAC24947.1; -; mRNA.
EMBL; CR536549; CAG38786.1; -; mRNA.
EMBL; AY300794; AAP43693.1; -; Genomic_DNA.
EMBL; BC007018; AAH07018.1; -; mRNA.
EMBL; AF503628; AAM27453.1; -; Genomic_DNA.
CCDS; CCDS31863.1; -.
RefSeq; NP_002574.2; NM_002583.2.
RefSeq; XP_006719498.1; XM_006719435.2.
RefSeq; XP_016874866.1; XM_017019377.1.
UniGene; Hs.643130; -.
UniGene; Hs.662065; -.
PDB; 2JK9; X-ray; 1.79 A; B=67-74.
PDBsum; 2JK9; -.
ProteinModelPortal; Q96IZ0; -.
SMR; Q96IZ0; -.
BioGrid; 111108; 47.
CORUM; Q96IZ0; -.
DIP; DIP-29003N; -.
ELM; Q96IZ0; -.
IntAct; Q96IZ0; 20.
MINT; MINT-1418971; -.
STRING; 9606.ENSP00000328088; -.
iPTMnet; Q96IZ0; -.
PhosphoSitePlus; Q96IZ0; -.
BioMuta; PAWR; -.
DMDM; 66773935; -.
EPD; Q96IZ0; -.
MaxQB; Q96IZ0; -.
PaxDb; Q96IZ0; -.
PeptideAtlas; Q96IZ0; -.
PRIDE; Q96IZ0; -.
TopDownProteomics; Q96IZ0; -.
DNASU; 5074; -.
Ensembl; ENST00000328827; ENSP00000328088; ENSG00000177425.
GeneID; 5074; -.
KEGG; hsa:5074; -.
UCSC; uc001syx.4; human.
CTD; 5074; -.
DisGeNET; 5074; -.
EuPathDB; HostDB:ENSG00000177425.10; -.
GeneCards; PAWR; -.
HGNC; HGNC:8614; PAWR.
HPA; CAB020779; -.
HPA; HPA012640; -.
MIM; 601936; gene.
neXtProt; NX_Q96IZ0; -.
OpenTargets; ENSG00000177425; -.
PharmGKB; PA32954; -.
eggNOG; ENOG410IFBP; Eukaryota.
eggNOG; ENOG4111M3H; LUCA.
GeneTree; ENSGT00390000000406; -.
HOGENOM; HOG000115462; -.
HOVERGEN; HBG058812; -.
InParanoid; Q96IZ0; -.
OMA; NCAVGPA; -.
OrthoDB; EOG091G0JYK; -.
PhylomeDB; Q96IZ0; -.
TreeFam; TF332824; -.
SIGNOR; Q96IZ0; -.
ChiTaRS; PAWR; human.
EvolutionaryTrace; Q96IZ0; -.
GeneWiki; PAWR; -.
GenomeRNAi; 5074; -.
PRO; PR:Q96IZ0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000177425; -.
CleanEx; HS_PAWR; -.
ExpressionAtlas; Q96IZ0; baseline and differential.
Genevisible; Q96IZ0; HS.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0042094; P:interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026117; Par-4.
PANTHER; PTHR15093; PTHR15093; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Coiled coil; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 340 PRKC apoptosis WT1 regulator protein.
/FTId=PRO_0000058236.
REGION 145 203 Selective for apoptosis induction in
cancer cells (SAC).
REGION 300 340 Leucine-zipper.
COILED 186 206 {ECO:0000255}.
MOTIF 68 72 B30.2/SPRY domain-binding motif.
{ECO:0000269|PubMed:20561531}.
MOTIF 145 161 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 49 120 Ala-rich.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 163 163 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q62627}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 42 42 P -> L (in dbSNP:rs8176804).
{ECO:0000269|Ref.3}.
/FTId=VAR_022465.
VARIANT 78 78 P -> R (in dbSNP:rs8176805).
{ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_022466.
VARIANT 137 137 G -> A (in dbSNP:rs8176806).
{ECO:0000269|Ref.3}.
/FTId=VAR_022467.
VARIANT 202 202 E -> A (in dbSNP:rs8176870).
{ECO:0000269|Ref.3}.
/FTId=VAR_022468.
MUTAGEN 66 66 A->D: No loss of interaction with SPSB1,
SPSB2 and SPSB4.
{ECO:0000269|PubMed:20561531}.
MUTAGEN 68 68 E->D: Increased interaction with SPSB2.
Increased only sligthly interaction with
SPSB4. Increased interaction with SPSB1,
SPSB2 and SPSB4; when associated with A-
69. {ECO:0000269|PubMed:20561531}.
MUTAGEN 69 69 L->I: Increased only sligthly interaction
with SPSB2. Increased only sligthly
interaction with SPSB4. Increased
interaction with SPSB1, SPSB2 and SPSB4;
when associated with A-68.
{ECO:0000269|PubMed:20561531}.
MUTAGEN 71 71 N->A: Loss of interaction with SPSB1,
SPSB2 and SPSB4.
{ECO:0000269|PubMed:20561531}.
MUTAGEN 72 72 N->A: Loss of interaction with SPSB1-
Elongin BC complex and SPSB2 and SPSB4.
{ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:20561531}.
CONFLICT 102 103 AP -> PPAR (in Ref. 1; AAC24947).
{ECO:0000305}.
CONFLICT 199 199 I -> M (in Ref. 2; CAG38786).
{ECO:0000305}.
CONFLICT 281 281 R -> T (in Ref. 1; AAC24947).
{ECO:0000305}.
SEQUENCE 340 AA; 36568 MW; 7E7515455402DBF8 CRC64;
MATGGYRTSS GLGGSTTDFL EEWKAKREKM RAKQNPPGPA PPGGGSSDAA GKPPAGALGT
PAAAAANELN NNLPGGAPAA PAVPGPGGVN CAVGSAMLTR AAPGPRRSED EPPAASASAA
PPPQRDEEEP DGVPEKGKSS GPSARKGKGQ IEKRKLREKR RSTGVVNIPA AECLDEYEDD
EAGQKERKRE DAITQQNTIQ NEAVNLLDPG SSYLLQEPPR TVSGRYKSTT SVSEEDVSSR
YSRTDRSGFP RYNRDANVSG TLVSSSTLEK KIEDLEKEVV RERQENLRLV RLMQDKEEMI
GKLKEEIDLL NRDLDDIEDE NEQLKQENKT LLKVVGQLTR


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