PAWR_HUMAN
ID PAWR_HUMAN Reviewed; 340 AA.
AC Q96IZ0; O75796; Q6FHY9; Q8N700;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=PRKC apoptosis WT1 regulator protein;
DE AltName: Full=Prostate apoptosis response 4 protein;
DE Short=Par-4;
GN Name=PAWR; Synonyms=PAR4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH WT1.
RX PubMed=8943350; DOI=10.1128/mcb.16.12.6945;
RA Johnstone R.W., See R.H., Sells S.F., Wang J., Muthukkumar S., Englert C.,
RA Haber D.A., Licht J.D., Sugrue S.P., Roberts T., Rangnekar V.M., Shi Y.;
RT "A novel repressor, par-4, modulates transcription and growth suppression
RT functions of the Wilms' tumor suppressor WT1.";
RL Mol. Cell. Biol. 16:6945-6956(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-78.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-42; ARG-78; ALA-137 AND
RP ALA-202.
RG NIEHS SNPs program;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC TISSUE=Blood;
RX PubMed=12242017; DOI=10.1016/s0378-1119(02)00826-0;
RA Hsu S.-C., Kirschenbaum F., Miller J., Cordell B., McCarthy J.V.;
RT "Structural and functional characterization of the upstream regulatory
RT region of the human gene encoding prostate apoptosis response factor-4.";
RL Gene 295:109-116(2002).
RN [6]
RP FUNCTION IN APOPTOSIS AND TUMOR REGRESSION.
RX PubMed=11585763;
RA Chakraborty M., Qiu S.G., Vasudevan K.M., Rangnekar V.M.;
RT "Par-4 drives trafficking and activation of Fas and Fasl to induce prostate
RT cancer cell apoptosis and tumor regression.";
RL Cancer Res. 61:7255-7263(2001).
RN [7]
RP INTERACTION WITH SQSTM1 AND PRKCZ.
RX PubMed=11755531; DOI=10.1016/s0014-5793(01)03224-0;
RA Chang S., Kim J.H., Shin J.;
RT "p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-
RT induced PKCzeta inhibition.";
RL FEBS Lett. 510:57-61(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH THAP1.
RX PubMed=12717420; DOI=10.1038/sj.onc.1206271;
RA Roussigne M., Cayrol C., Clouaire T., Amalric F., Girard J.-P.;
RT "THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-
RT response-4 (Par-4) to PML nuclear bodies.";
RL Oncogene 22:2432-2442(2003).
RN [9]
RP INTERACTION WITH AATF.
RX PubMed=14627703; DOI=10.1074/jbc.m309811200;
RA Guo Q., Xie J.;
RT "AATF inhibits aberrant production of amyloid beta peptide 1-42 by
RT interacting directly with Par-4.";
RL J. Biol. Chem. 279:4596-4603(2004).
RN [10]
RP INTERACTION WITH BACE1.
RX PubMed=15671026; DOI=10.1074/jbc.m411933200;
RA Xie J., Guo Q.;
RT "PAR-4 is involved in regulation of beta-secretase cleavage of the
RT Alzheimer amyloid precursor protein.";
RL J. Biol. Chem. 280:13824-13832(2005).
RN [11]
RP INTERACTION WITH SPSB1 AND SPSB2, AND MUTAGENESIS OF ASN-72.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
RN [12]
RP REVIEW ON FUNCTION IN APOPTOSIS AND NEURODEGENERATIVE DISEASES.
RX PubMed=12565819; DOI=10.1016/s0014-4827(02)00016-2;
RA El-Guendy N., Rangnekar V.M.;
RT "Apoptosis by Par-4 in cancer and neurodegenerative diseases.";
RL Exp. Cell Res. 283:51-66(2003).
RN [13]
RP REVIEW.
RX PubMed=14755681; DOI=10.1002/jcb.20000;
RA Gurumurthy S., Rangnekar V.M.;
RT "Par-4 inducible apoptosis in prostate cancer cells.";
RL J. Cell. Biochem. 91:504-512(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20] {ECO:0007744|PDB:2JK9}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 67-74 IN COMPLEX WITH SPSB1,
RP INTERACTION WITH SPSB1; SPSB2 AND SPSB4, MUTAGENESIS OF ALA-66; GLU-68;
RP LEU-69; ASN-71 AND ASN-72, AND MOTIF.
RX PubMed=20561531; DOI=10.1016/j.jmb.2010.06.017;
RA Filippakopoulos P., Low A., Sharpe T.D., Uppenberg J., Yao S., Kuang Z.,
RA Savitsky P., Lewis R.S., Nicholson S.E., Norton R.S., Bullock A.N.;
RT "Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-
RT containing proteins SPSB1, SPSB2, and SPSB4.";
RL J. Mol. Biol. 401:389-402(2010).
CC -!- FUNCTION: Pro-apoptotic protein capable of selectively inducing
CC apoptosis in cancer cells, sensitizing the cells to diverse apoptotic
CC stimuli and causing regression of tumors in animal models. Induces
CC apoptosis in certain cancer cells by activation of the Fas prodeath
CC pathway and coparallel inhibition of NF-kappa-B transcriptional
CC activity. Inhibits the transcriptional activation and augments the
CC transcriptional repression mediated by WT1. Down-regulates the anti-
CC apoptotic protein BCL2 via its interaction with WT1. Seems also to be a
CC transcriptional repressor by itself. May be directly involved in
CC regulating the amyloid precursor protein (APP) cleavage activity of
CC BACE1. {ECO:0000269|PubMed:11585763}.
CC -!- SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with WT1
CC (PubMed:8943350). Interacts with THAP1 (PubMed:12717420). Interacts
CC with AATF (PubMed:14627703). Interacts with BACE1 (PubMed:15671026).
CC Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is
CC direct and occurs in association with the Elongin BC complex
CC (PubMed:17189197, PubMed:20561531). Interacts with SPSB2 (via
CC B30.2/SPRY domain); this interaction occurs in association with the
CC Elongin BC complex (PubMed:17189197, PubMed:20561531). Interacts with
CC SPSB4 (via B30.2/SPRY domain) (PubMed:20561531); this interaction
CC occurs in association with the Elongin BC complex (PubMed:20561531).
CC Component of a ternary complex composed of SQSTM1 and PRKCZ
CC (PubMed:11755531). Interacts with actin (By similarity).
CC {ECO:0000250|UniProtKB:Q62627, ECO:0000250|UniProtKB:Q925B0,
CC ECO:0000269|PubMed:11755531, ECO:0000269|PubMed:12717420,
CC ECO:0000269|PubMed:14627703, ECO:0000269|PubMed:15671026,
CC ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:20561531,
CC ECO:0000269|PubMed:8943350}.
CC -!- INTERACTION:
CC Q96IZ0; Q01094: E2F1; NbExp=2; IntAct=EBI-595869, EBI-448924;
CC Q96IZ0; P11021: HSPA5; NbExp=8; IntAct=EBI-595869, EBI-354921;
CC Q96IZ0; Q96BD6: SPSB1; NbExp=2; IntAct=EBI-595869, EBI-2659201;
CC Q96IZ0; P08670: VIM; NbExp=2; IntAct=EBI-595869, EBI-353844;
CC Q96IZ0; Q9D5L7: Spsb1; Xeno; NbExp=2; IntAct=EBI-595869, EBI-8821912;
CC Q96IZ0; O88838: Spsb2; Xeno; NbExp=6; IntAct=EBI-595869, EBI-8820410;
CC Q96IZ0; Q8R5B6: Spsb4; Xeno; NbExp=3; IntAct=EBI-595869, EBI-8821982;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic in
CC absence of apoptosis signal and in normal cells. Nuclear in most cancer
CC cell lines. Nuclear entry seems to be essential but not sufficient for
CC apoptosis (By similarity). Nuclear localization includes nucleoplasm
CC and PML nuclear bodies. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expression is elevated in various
CC neurodegenerative diseases such as amyotrophic lateral sclerosis,
CC Alzheimer, Parkinson and Huntington diseases and stroke. Down-regulated
CC in several cancers. {ECO:0000269|PubMed:8943350}.
CC -!- INDUCTION: By apoptosis.
CC -!- DOMAIN: The leucine-zipper domain is not essential for apoptosis, but
CC is required for sensitization of cells to exogenous apoptotic insults
CC and for interaction with its partners. {ECO:0000250}.
CC -!- DOMAIN: The SAC domain is a death-inducing domain selective for
CC apoptosis induction in cancer cells. This domain is essential for
CC nuclear entry, Fas activation, inhibition of NF-kappa-B activity and
CC induction of apoptosis in cancer cells (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition by
CC proteins containing a B30.2/SPRY domain. {ECO:0000269|PubMed:20561531}.
CC -!- PTM: Preferentially phosphorylated at the Thr-163 by PKC in cancer
CC cells. {ECO:0000250}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PAWRID41641ch12q21.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pawr/";
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DR EMBL; U63809; AAC24947.1; -; mRNA.
DR EMBL; CR536549; CAG38786.1; -; mRNA.
DR EMBL; AY300794; AAP43693.1; -; Genomic_DNA.
DR EMBL; BC007018; AAH07018.1; -; mRNA.
DR EMBL; AF503628; AAM27453.1; -; Genomic_DNA.
DR CCDS; CCDS31863.1; -.
DR RefSeq; NP_002574.2; NM_002583.2.
DR RefSeq; XP_006719498.1; XM_006719435.2.
DR RefSeq; XP_016874866.1; XM_017019377.1.
DR PDB; 2JK9; X-ray; 1.79 A; B=67-81.
DR PDBsum; 2JK9; -.
DR AlphaFoldDB; Q96IZ0; -.
DR SMR; Q96IZ0; -.
DR BioGRID; 111108; 87.
DR CORUM; Q96IZ0; -.
DR DIP; DIP-29003N; -.
DR ELM; Q96IZ0; -.
DR IntAct; Q96IZ0; 27.
DR MINT; Q96IZ0; -.
DR STRING; 9606.ENSP00000328088; -.
DR BindingDB; Q96IZ0; -.
DR GlyGen; Q96IZ0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96IZ0; -.
DR PhosphoSitePlus; Q96IZ0; -.
DR BioMuta; PAWR; -.
DR DMDM; 66773935; -.
DR EPD; Q96IZ0; -.
DR jPOST; Q96IZ0; -.
DR MassIVE; Q96IZ0; -.
DR MaxQB; Q96IZ0; -.
DR PaxDb; Q96IZ0; -.
DR PeptideAtlas; Q96IZ0; -.
DR PRIDE; Q96IZ0; -.
DR ProteomicsDB; 76870; -.
DR TopDownProteomics; Q96IZ0; -.
DR Antibodypedia; 1824; 395 antibodies from 40 providers.
DR DNASU; 5074; -.
DR Ensembl; ENST00000328827.9; ENSP00000328088.4; ENSG00000177425.11.
DR GeneID; 5074; -.
DR KEGG; hsa:5074; -.
DR MANE-Select; ENST00000328827.9; ENSP00000328088.4; NM_002583.4; NP_002574.2.
DR UCSC; uc001syx.4; human.
DR CTD; 5074; -.
DR DisGeNET; 5074; -.
DR GeneCards; PAWR; -.
DR HGNC; HGNC:8614; PAWR.
DR HPA; ENSG00000177425; Low tissue specificity.
DR MIM; 601936; gene.
DR neXtProt; NX_Q96IZ0; -.
DR OpenTargets; ENSG00000177425; -.
DR PharmGKB; PA32954; -.
DR VEuPathDB; HostDB:ENSG00000177425; -.
DR eggNOG; ENOG502QVUF; Eukaryota.
DR GeneTree; ENSGT00390000000406; -.
DR HOGENOM; CLU_076619_0_0_1; -.
DR InParanoid; Q96IZ0; -.
DR OMA; TVQNESM; -.
DR OrthoDB; 1363165at2759; -.
DR PhylomeDB; Q96IZ0; -.
DR TreeFam; TF332824; -.
DR PathwayCommons; Q96IZ0; -.
DR SignaLink; Q96IZ0; -.
DR SIGNOR; Q96IZ0; -.
DR BioGRID-ORCS; 5074; 27 hits in 1081 CRISPR screens.
DR ChiTaRS; PAWR; human.
DR EvolutionaryTrace; Q96IZ0; -.
DR GeneWiki; PAWR; -.
DR GenomeRNAi; 5074; -.
DR Pharos; Q96IZ0; Tbio.
DR PRO; PR:Q96IZ0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96IZ0; protein.
DR Bgee; ENSG00000177425; Expressed in germinal epithelium of ovary and 184 other tissues.
DR ExpressionAtlas; Q96IZ0; baseline and differential.
DR Genevisible; Q96IZ0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl.
DR DisProt; DP01603; -.
DR IDEAL; IID00177; -.
DR InterPro; IPR026117; Par-4.
DR PANTHER; PTHR15093; PTHR15093; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..340
FT /note="PRKC apoptosis WT1 regulator protein"
FT /id="PRO_0000058236"
FT REGION 1..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..203
FT /note="Selective for apoptosis induction in cancer cells
FT (SAC)"
FT REGION 300..340
FT /note="Leucine-zipper"
FT COILED 186..206
FT /evidence="ECO:0000255"
FT MOTIF 68..72
FT /note="B30.2/SPRY domain-binding motif"
FT /evidence="ECO:0000269|PubMed:20561531"
FT MOTIF 145..161
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 163
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q62627"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 42
FT /note="P -> L (in dbSNP:rs8176804)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022465"
FT VARIANT 78
FT /note="P -> R (in dbSNP:rs8176805)"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT /id="VAR_022466"
FT VARIANT 137
FT /note="G -> A (in dbSNP:rs8176806)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022467"
FT VARIANT 202
FT /note="E -> A (in dbSNP:rs8176870)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022468"
FT MUTAGEN 66
FT /note="A->D: No loss of interaction with SPSB1, SPSB2 and
FT SPSB4."
FT /evidence="ECO:0000269|PubMed:20561531"
FT MUTAGEN 68
FT /note="E->D: Increased interaction with SPSB2. Only
FT slightly increased interaction with SPSB4. Increased
FT interaction with SPSB1, SPSB2 and SPSB4; when associated
FT with A-69."
FT /evidence="ECO:0000269|PubMed:20561531"
FT MUTAGEN 69
FT /note="L->I: Only slighlty increased interaction with
FT SPSB2. Only slightly increased interaction with SPSB4.
FT Increased interaction with SPSB1, SPSB2 and SPSB4; when
FT associated with A-68."
FT /evidence="ECO:0000269|PubMed:20561531"
FT MUTAGEN 71
FT /note="N->A: Loss of interaction with SPSB1, SPSB2 and
FT SPSB4."
FT /evidence="ECO:0000269|PubMed:20561531"
FT MUTAGEN 72
FT /note="N->A: Loss of interaction with SPSB1-Elongin BC
FT complex and SPSB2 and SPSB4."
FT /evidence="ECO:0000269|PubMed:17189197,
FT ECO:0000269|PubMed:20561531"
FT CONFLICT 102..103
FT /note="AP -> PPAR (in Ref. 1; AAC24947)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="I -> M (in Ref. 2; CAG38786)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="R -> T (in Ref. 1; AAC24947)"
FT /evidence="ECO:0000305"
SQ 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
