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 28-JAN-2026, entry version 183. 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. Also seems 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; Q99619: SPSB2; NbExp=2; IntAct=EBI-595869, EBI-2323209; CC Q96IZ0; Q96A44: SPSB4; NbExp=2; IntAct=EBI-595869, EBI-2323233; 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="https://atlasgeneticsoncology.org/gene/41641/PAWR"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001341661.1; NM_001354732.2. DR RefSeq; NP_002574.2; NM_002583.4. DR RefSeq; XP_047284872.1; XM_047428916.1. DR RefSeq; XP_054228126.1; XM_054372151.1. DR PDB; 2JK9; X-ray; 1.79 A; B=67-81. DR PDBsum; 2JK9; -. DR AlphaFoldDB; Q96IZ0; -. DR SMR; Q96IZ0; -. DR BioGRID; 111108; 137. DR CORUM; Q96IZ0; -. DR DIP; DIP-29003N; -. DR ELM; Q96IZ0; -. DR FunCoup; Q96IZ0; 1301. DR IntAct; Q96IZ0; 40. DR MINT; Q96IZ0; -. DR STRING; 9606.ENSP00000328088; -. DR BindingDB; Q96IZ0; -. DR DrugBank; DB14942; BMS-986141. DR GlyGen; Q96IZ0; 12 sites, 1 O-linked glycan (12 sites). DR iPTMnet; Q96IZ0; -. DR PhosphoSitePlus; Q96IZ0; -. DR BioMuta; PAWR; -. DR DMDM; 66773935; -. DR jPOST; Q96IZ0; -. DR MassIVE; Q96IZ0; -. DR PaxDb; 9606-ENSP00000328088; -. DR PeptideAtlas; Q96IZ0; -. DR ProteomicsDB; 76870; -. DR Pumba; Q96IZ0; -. DR TopDownProteomics; Q96IZ0; -. DR Antibodypedia; 1824; 392 antibodies from 41 providers. DR DNASU; 5074; -. DR Ensembl; ENST00000328827.9; ENSP00000328088.4; ENSG00000177425.12. 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 AGR; HGNC:8614; -. DR ClinPGx; PA32954; -. 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 OpenTargets; ENSG00000177425; -. DR VEuPathDB; HostDB:ENSG00000177425; -. DR eggNOG; ENOG502QVUF; Eukaryota. DR GeneTree; ENSGT00390000000406; -. DR HOGENOM; CLU_076619_0_0_1; -. DR InParanoid; Q96IZ0; -. DR OMA; NCIPLAR; -. DR OrthoDB; 6286739at2759; -. DR PAN-GO; Q96IZ0; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q96IZ0; -. DR PathwayCommons; Q96IZ0; -. DR SignaLink; Q96IZ0; -. DR SIGNOR; Q96IZ0; -. DR Agora; ENSG00000177425; -. DR BioGRID-ORCS; 5074; 29 hits in 1161 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. 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 186 other cell types or tissues. DR ExpressionAtlas; Q96IZ0; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0000785; C:chromatin; IEA:Ensembl. DR GO; GO:0097542; C:ciliary tip; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:SF1; PRKC APOPTOSIS WT1 REGULATOR PROTEIN; 1. DR PANTHER; PTHR15093; PROSTATE APOPTOSIS RESPONSE PROTEIN PAR-4; 1. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transcription; KW 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..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 47..82 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..192 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..203 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..253 FT /note="Basic and acidic 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 slightly 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 //