ID DAPK3_RAT Reviewed; 448 AA. AC O88764; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 174. DE RecName: Full=Death-associated protein kinase 3; DE Short=DAP kinase 3; DE EC=2.7.11.1 {ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:9840928}; DE AltName: Full=DAP-like kinase; DE Short=Dlk; DE AltName: Full=MYPT1 kinase; DE AltName: Full=ZIP-kinase; GN Name=Dapk3; Synonyms=Zipk; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000312|EMBL:CAA07360.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9840928; DOI=10.1038/sj.onc.1202204; RA Koegel D., Ploettner O., Landsberg G., Christian S., Scheidtmann K.H.; RT "Cloning and characterization of Dlk, a novel serine/threonine kinase that RT is tightly associated with chromatin and phosphorylates core histones."; RL Oncogene 17:2645-2654(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 [3] RP INTERACTION WITH AATF. RX PubMed=10580117; DOI=10.1016/s0014-5793(99)01529-x; RA Page G., Loedige I., Kogel D., Scheidtmann K.H.; RT "AATF -- a novel transcription factor that interacts with Dlk/ZIP kinase RT and interferes with apoptosis."; RL FEBS Lett. 462:187-191(1999). RN [4] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 406-ARG-ARG-407. RX PubMed=10602474; DOI=10.1038/sj.onc.1203169; RA Koegel D., Bierbaum H., Preuss U., Scheidtmann K.H.; RT "C-terminal truncation of Dlk/ZIP kinase leads to abrogation of nuclear RT transport and high apoptotic activity."; RL Oncogene 18:7212-7218(1999). RN [5] {ECO:0000305} RP FUNCTION IN APOPTOSIS, CATALYTIC ACTIVITY, INTERACTION WITH ATF4 AND PAWR, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-42. RX PubMed=10602480; DOI=10.1038/sj.onc.1203170; RA Page G., Kogel D., Rangnekar V., Scheidtmann K.H.; RT "Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP kinase RT and Par-4 results in cytoplasmic retention and apoptosis."; RL Oncogene 18:7265-7273(1999). RN [6] RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF MYL12B AND RP PPP1R12A, AND CATALYTIC ACTIVITY. RX PubMed=11384979; DOI=10.1074/jbc.m102753200; RA Niiro N., Ikebe M.; RT "Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle RT contraction via myosin light chain phosphorylation."; RL J. Biol. Chem. 276:29567-29574(2001). RN [7] RP INTERACTION WITH CDC5L. RX PubMed=11884640; DOI=10.1093/nar/30.6.1408; RA Engemann H., Heinzel V., Page G., Preuss U., Scheidtmann K.H.; RT "DAP-like kinase interacts with the rat homolog of Schizosaccharomyces RT pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for RT G2/M phase transition."; RL Nucleic Acids Res. 30:1408-1417(2002). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=14582533; DOI=10.1078/0171-9335-00332; RA Preuss U., Bierbaum H., Buchenau P., Scheidtmann K.H.; RT "DAP-like kinase, a member of the death-associated protein kinase family, RT associates with centrosomes, centromers, and the contractile ring during RT mitosis."; RL Eur. J. Cell Biol. 82:447-459(2003). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12560483; DOI=10.1093/nar/gkg176; RA Preuss U., Landsberg G., Scheidtmann K.H.; RT "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by RT Dlk/ZIP kinase."; RL Nucleic Acids Res. 31:878-885(2003). RN [10] RP FUNCTION IN PHOSPHORYLATION OF MYL12B, SUBCELLULAR LOCATION, AND CATALYTIC RP ACTIVITY. RX PubMed=15096528; DOI=10.1083/jcb.200309056; RA Komatsu S., Ikebe M.; RT "ZIP kinase is responsible for the phosphorylation of myosin II and RT necessary for cell motility in mammalian fibroblasts."; RL J. Cell Biol. 165:243-254(2004). RN [11] RP SUBCELLULAR LOCATION, INTERACTION WITH PAWR, AND MUTAGENESIS OF ALA-294 AND RP ALA-295. RX PubMed=17953487; DOI=10.1371/journal.pgen.0030180; RA Shoval Y., Pietrokovski S., Kimchi A.; RT "ZIPK: a unique case of murine-specific divergence of a conserved RT vertebrate gene."; RL PLoS Genet. 3:1884-1893(2007). RN [12] RP FUNCTION IN ANDROGEN RECEPTOR-MEDIATED TRANSCRIPTION, AND INTERACTION WITH RP AR. RX PubMed=18084323; DOI=10.1038/sj.onc.1210995; RA Leister P., Felten A., Chasan A.I., Scheidtmann K.H.; RT "ZIP kinase plays a crucial role in androgen receptor-mediated RT transcription."; RL Oncogene 27:3292-3300(2008). RN [13] RP INTERACTION WITH PAWR. RX PubMed=18505470; DOI=10.1111/j.1582-4934.2008.00374.x; RA Vetterkind S., Morgan K.G.; RT "The pro-apoptotic protein Par-4 facilitates vascular contractility by RT cytoskeletal targeting of ZIPK."; RL J. Cell. Mol. Med. 13:887-895(2009). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=20854903; DOI=10.1016/j.cellsig.2010.09.016; RA Weitzel D.H., Chambers J., Haystead T.A.; RT "Phosphorylation-dependent control of ZIPK nuclear import is species RT specific."; RL Cell. Signal. 23:297-303(2011). CC -!- FUNCTION: Serine/threonine kinase which is involved in the regulation CC of apoptosis, autophagy, transcription, translation and actin CC cytoskeleton reorganization. Regulates both type I (caspase-dependent) CC apoptotic and type II (caspase-independent) autophagic cell deaths CC signal, depending on the cellular setting. Involved in formation of CC promyelocytic leukemia protein nuclear body (PML-NB). Involved in CC apoptosis involving PAWR which mediates cytoplasmic relocation; in CC vitro phosphorylates PAWR. Phosphorylates MYL12B in non-muscle cells CC leading to reorganization of actin cytoskeleton such as in regulation CC of cell polarity and cell migration. Positively regulates canonical CC Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; CC disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation CC of TCF7L2 by NLK. Phosphorylates RPL13A on 'Ser-77' upon interferon- CC gamma activation which is causing RPL13A release from the ribosome, CC RPL13A association with the GAIT complex and its subsequent involvement CC in transcript-selective translation inhibition (By similarity). CC Phosphorylates STAT3 and enhances its transcriptional activity (By CC similarity). Enhances transcription from AR-responsive promoters in a CC hormone- and kinase-dependent manner. Phosphorylates histone H3 on CC 'Thr-11' at centromeres during mitosis. {ECO:0000250|UniProtKB:O43293, CC ECO:0000250|UniProtKB:O54784, ECO:0000269|PubMed:10602480, CC ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:12560483, CC ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:18084323, CC ECO:0000269|PubMed:9840928}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, CC ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:9840928}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10602480, CC ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:15096528, CC ECO:0000269|PubMed:9840928}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:9840928}; CC -!- ACTIVITY REGULATION: A sequential activation is proposed: CC autophosphorylation at consensus sites is leading to dimerization of CC the catalytic domain and activation segment exchange (producing an CC active confirmation of both kinase modules in trans) followed by CC phosphorylation at Thr-180 in the activation segment and at other CC regulatory sites (Probable). Phosphorylation at Thr-180, Thr-225 and CC Thr-265 is essential for activity. Inhibited by pyridone 6 (K00225), a CC potent, ATP-competitive inhibitor. Phosphorylation at Thr-180, Thr-225 CC and Thr-265 is essential for activity (By similarity). CC {ECO:0000250|UniProtKB:O43293}. CC -!- SUBUNIT: Homooligomer in its kinase-active form (homotrimers and CC homodimers are reported); monomeric in its kinase-inactive form. CC Homodimerization is required for activation segment autophosphorylation CC (By similarity). Interacts with DAXX, ATF4, NLK, TCF7L2, UBE2D1, CC UBE2D2, UBE2D3 and CDC5L. Interacts with PAWR; also demonstrated in CC aorta smooth muscle cells indicative for the cytoskeletal targeting CC function of PAWR. Interacts with AR; enhanced by AATF. CC {ECO:0000250|UniProtKB:O43293, ECO:0000269|PubMed:10580117, CC ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11884640, CC ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:18084323, CC ECO:0000269|PubMed:18505470}. CC -!- INTERACTION: CC O88764; Q62627: Pawr; NbExp=5; IntAct=EBI-4404236, EBI-1187240; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10602474, CC ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:17953487, CC ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9840928}. Nucleus, PML CC body {ECO:0000269|PubMed:10602474}. Cytoplasm CC {ECO:0000303|PubMed:10602480}. Cytoplasm, cytoskeleton, microtubule CC organizing center {ECO:0000269|PubMed:14582533}. Chromosome, centromere CC {ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:14582533}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:15096528}. Note=Predominantly CC localized to the nucleus. Relocates to the cytoplasm on binding PAWR CC where the complex appears to interact with actin filaments (Probable). CC Associated with the centrosomes throughout the mitotic cell cycle, with CC the centromeres from prophase to anaphase and with the contractile ring CC during cytokinesis. {ECO:0000269|PubMed:14582533, CC ECO:0000269|PubMed:17953487, ECO:0000303|PubMed:10602474}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O88764-1; Sequence=Displayed; CC Name=2; CC IsoId=O88764-2; Sequence=VSP_042061; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissue types CC examined. High levels in brain, heart, lung and spleen, lower CC expression in kidney, liver, skeletal muscle and testis. Isoform 2 is CC expressed in the smooth muscle. {ECO:0000269|PubMed:9840928}. CC -!- PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase CC does not lead to proteasomal degradation, but influences promyelocytic CC leukemia protein nuclear bodies (PML-NBs) formation in the nucleus (By CC similarity). {ECO:0000250|UniProtKB:O54784}. CC -!- PTM: The phosphorylation status is critical for kinase activity, CC oligomerization and intracellular localization. Phosphorylation at Thr- CC 180, Thr-225 and Thr-265 is essential for activity. The phosphorylated CC form is localized in the cytoplasm and nuclear translocation or CC retention is maximal when it is not phosphorylated. Phosphorylation CC increases the trimeric form, and its dephosphorylation favors a kinase- CC inactive monomeric form. {ECO:0000250|UniProtKB:O43293}. CC -!- MISCELLANEOUS: A species-specific loss of a key phosphorylation site in CC murine DAPK3 seems to direct it mainly to the nucleus which is proposed CC to be compensated by the interaction with PAWR to maintain at least the CC cytoplasmic basic membrane blebbing function in the apoptosis pathway. CC {ECO:0000303|PubMed:10602480}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. DAP kinase subfamily. {ECO:0000305}. 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; AJ006971; CAA07360.1; -; mRNA. DR EMBL; BC062076; AAH62076.1; -; mRNA. DR RefSeq; NP_071991.1; NM_022546.1. [O88764-1] DR RefSeq; XP_006241055.1; XM_006240993.2. [O88764-1] DR RefSeq; XP_017450587.1; XM_017595098.1. DR RefSeq; XP_017450588.1; XM_017595099.1. [O88764-1] DR AlphaFoldDB; O88764; -. DR SMR; O88764; -. DR BioGRID; 249061; 6. DR IntAct; O88764; 5. DR STRING; 10116.ENSRNOP00000027634; -. DR PhosphoSitePlus; O88764; -. DR jPOST; O88764; -. DR PaxDb; 10116-ENSRNOP00000027634; -. DR Ensembl; ENSRNOT00000027634.5; ENSRNOP00000027634.5; ENSRNOG00000020383.6. [O88764-1] DR Ensembl; ENSRNOT00055056655; ENSRNOP00055046761; ENSRNOG00055032768. [O88764-1] DR Ensembl; ENSRNOT00060053652; ENSRNOP00060044536; ENSRNOG00060030872. [O88764-1] DR Ensembl; ENSRNOT00065037526; ENSRNOP00065030317; ENSRNOG00065022007. [O88764-1] DR GeneID; 64391; -. DR KEGG; rno:64391; -. DR UCSC; RGD:621766; rat. [O88764-1] DR AGR; RGD:621766; -. DR CTD; 1613; -. DR RGD; 621766; Dapk3. DR eggNOG; KOG0032; Eukaryota. DR GeneTree; ENSGT00940000161753; -. DR HOGENOM; CLU_000288_63_55_1; -. DR InParanoid; O88764; -. DR OMA; CRQKSNG; -. DR OrthoDB; 5474191at2759; -. DR PhylomeDB; O88764; -. DR TreeFam; TF314166; -. DR PRO; PR:O88764; -. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000020383; Expressed in pancreas and 20 other cell types or tissues. DR GO; GO:0005884; C:actin filament; IDA:RGD. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0016301; F:kinase activity; IDA:RGD. DR GO; GO:0043522; F:leucine zipper domain binding; ISO:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; ISO:RGD. DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD. DR GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD. DR GO; GO:0030182; P:neuron differentiation; IEP:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD. DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD. DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:RGD. DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD. DR GO; GO:0043519; P:regulation of myosin II filament organization; ISO:RGD. DR CDD; cd14105; STKc_DAPK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR042870; DAPK3_STKc. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24342:SF18; DEATH-ASSOCIATED PROTEIN KINASE 3; 1. DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; O88764; RN. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Apoptosis; ATP-binding; Centromere; KW Chromatin regulator; Chromosome; Cytoplasm; Cytoskeleton; Kinase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transcription; Transcription regulation; KW Transferase; Ubl conjugation. FT CHAIN 1..448 FT /note="Death-associated protein kinase 3" FT /id="PRO_0000085916" FT DOMAIN 13..275 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 161..204 FT /note="Activation segment" FT /evidence="ECO:0000250|UniProtKB:O96017" FT REGION 390..448 FT /note="Interaction with CDC5L" FT /evidence="ECO:0000269|PubMed:11884640" FT REGION 418..448 FT /note="Required for interaction with ATF4 but not with FT PAWR" FT /evidence="ECO:0000269|PubMed:10602480" FT REGION 422..436 FT /note="Leucine-zipper" FT /evidence="ECO:0000250|UniProtKB:O43293" FT ACT_SITE 139 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 19..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 180 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 225 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 265 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 265 FT /note="Phosphothreonine; by ROCK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 304 FT /note="Phosphoserine; by DAPK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 306 FT /note="Phosphoserine; by autocatalysis and DAPK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 307 FT /note="Phosphoserine; by DAPK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 313 FT /note="Phosphoserine; by DAPK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT MOD_RES 321 FT /note="Phosphoserine; by DAPK1" FT /evidence="ECO:0000250|UniProtKB:O43293" FT VAR_SEQ 1 FT /note="M -> MIDSSCVPRILQKDSAMM (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_042061" FT MUTAGEN 42 FT /note="K->A: Loss of kinase activity, loss of PAWR-linked FT translocation into the cytoplasm; maintains nuclear FT localization but loss of localization to PML-NB." FT /evidence="ECO:0000269|PubMed:10602474, FT ECO:0000269|PubMed:10602480" FT MUTAGEN 294 FT /note="A->T: Causes dissociation from promyelocytic FT leukemia oncogenic bodies and increased blebbing-inducing FT potency; when associated with T-300." FT /evidence="ECO:0000269|PubMed:17953487" FT MUTAGEN 295 FT /note="A->T: Causes dissociation from promyelocytic FT leukemia oncogenic bodies and increased blebbing-inducing FT potency; when associated with T-299." FT /evidence="ECO:0000269|PubMed:17953487" FT MUTAGEN 406..407 FT /note="RR->AL: Cytoplasmic localization." FT /evidence="ECO:0000269|PubMed:10602474" SQ SEQUENCE 448 AA; 51450 MW; 843C0FD0BF0C1EEA CRC64; MSTFRQEDVE DHYEMGEELG SGQFAIVRKC QQKGTGMEYA AKFIKKRRLP SSRRGVSREE IEREVSILRE IRHPNIITLH DVFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL KQILDGVHYL HSKRIAHFDL KPENIMLLDK HAASPRIKLI DFGIAHRIEA GSEFKNIFGT PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY FSSTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKVRRR EDGARKPERR RLRAARLREY SLKSHSSMPR NTSYASFERF SRVLEDVAAA EQGLRELQRG RRQCRERVCA LRVAAEQREA RCRDGSAGLG RDLRRLRTEL GRTEALRTRA QEEARAALLG AGGLKRRLCR LENRYDALAA QVAAEVQFVR DLVRALEQER LQAECGVR //