DAPK3_RAT
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 03-AUG-2022, entry version 167.
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}.
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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. [O88764-1]
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 jPOST; O88764; -.
DR PaxDb; O88764; -.
DR Ensembl; ENSRNOT00000027634; ENSRNOP00000027634; ENSRNOG00000020383. [O88764-1]
DR GeneID; 64391; -.
DR KEGG; rno:64391; -.
DR UCSC; RGD:621766; rat. [O88764-1]
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; PSQIMAG; -.
DR OrthoDB; 813445at2759; -.
DR PhylomeDB; O88764; -.
DR TreeFam; TF314166; -.
DR PRO; PR:O88764; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000020383; Expressed in pancreas and 20 other tissues.
DR Genevisible; O88764; RN.
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; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
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: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:0008022; F:protein C-terminus binding; IPI: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 interferon-gamma; 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:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; 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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
