DMTF1_MOUSE
ID DMTF1_MOUSE Reviewed; 761 AA.
AC Q8CE22; P70413; Q3TUR9; Q80VR8; Q8BQX6; Q8CA56; Q8CCZ0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cyclin-D-binding Myb-like transcription factor 1;
DE AltName: Full=Cyclin-D-interacting Myb-like protein 1;
DE Short=mDmp1;
GN Name=Dmtf1; Synonyms=Dmp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING, INTERACTION
RP WITH CCND1; CCND2 AND CCND3, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP PHOSPHORYLATION.
RC STRAIN=C57BL/Kaplan;
RX PubMed=8887674; DOI=10.1128/mcb.16.11.6457;
RA Hirai H., Sherr C.J.;
RT "Interaction of D-type cyclins with a novel myb-like transcription factor,
RT DMP1.";
RL Mol. Cell. Biol. 16:6457-6467(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 (ISOFORM 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Embryo, Medulla oblongata, Skin, and
RC Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Olfactory epithelium;
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 [4]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-319.
RX PubMed=9786929; DOI=10.1074/jbc.273.44.29188;
RA Inoue K., Sherr C.J., Shapiro L.H.;
RT "Regulation of the CD13/aminopeptidase N gene by DMP1, a transcription
RT factor antagonized by D-type cyclins.";
RL J. Biol. Chem. 273:29188-29194(1998).
RN [5]
RP FUNCTION, DNA-BINDING, INTERACTION WITH CCND1 AND CCND2, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-319.
RX PubMed=9488476; DOI=10.1128/mcb.18.3.1590;
RA Inoue K., Sherr C.J.;
RT "Gene expression and cell cycle arrest mediated by transcription factor
RT DMP1 is antagonized by D-type cyclins through a cyclin-dependent-kinase-
RT independent mechanism.";
RL Mol. Cell. Biol. 18:1590-1600(1998).
RN [6]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=10097151; DOI=10.1073/pnas.96.7.3993;
RA Inoue K., Roussel M.F., Sherr C.J.;
RT "Induction of ARF tumor suppressor gene expression and cell cycle arrest by
RT transcription factor DMP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3993-3998(1999).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10898794;
RA Inoue K., Wen R., Rehg J.E., Adachi M., Cleveland J.L., Roussel M.F.,
RA Sherr C.J.;
RT "Disruption of the ARF transcriptional activator DMP1 facilitates cell
RT immortalization, Ras transformation, and tumorigenesis.";
RL Genes Dev. 14:1797-1809(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11711428; DOI=10.1101/gad.929901;
RA Inoue K., Zindy F., Randle D.H., Rehg J.E., Sherr C.J.;
RT "Dmp1 is haplo-insufficient for tumor suppression and modifies the
RT frequencies of Arf and p53 mutations in Myc-induced lymphomas.";
RL Genes Dev. 15:2934-2939(2001).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=15601844; DOI=10.1128/mcb.25.1.220-232.2005;
RA Sreeramaneni R., Chaudhry A., McMahon M., Sherr C.J., Inoue K.;
RT "Ras-Raf-Arf signaling critically depends on the Dmp1 transcription
RT factor.";
RL Mol. Cell. Biol. 25:220-232(2005).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=16878159; DOI=10.1038/sj.onc.1209750;
RA Mallakin A., Taneja P., Matise L.A., Willingham M.C., Inoue K.;
RT "Expression of Dmp1 in specific differentiated, nonproliferating cells and
RT its regulation by E2Fs.";
RL Oncogene 25:7703-7713(2006).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17936562; DOI=10.1016/j.ccr.2007.08.034;
RA Mallakin A., Sugiyama T., Taneja P., Matise L.A., Frazier D.P.,
RA Choudhary M., Hawkins G.A., D'Agostino R.B. Jr., Willingham M.C., Inoue K.;
RT "Mutually exclusive inactivation of DMP1 and ARF/p53 in lung cancer.";
RL Cancer Cell 12:381-394(2007).
RN [12]
RP INDUCTION.
RX PubMed=17546045; DOI=10.1038/sj.onc.1210568;
RA Taneja P., Mallakin A., Matise L.A., Frazier D.P., Choudhary M., Inoue K.;
RT "Repression of Dmp1 and Arf transcription by anthracyclins: critical roles
RT of the NF-kappaB subunit p65.";
RL Oncogene 26:7457-7466(2007).
CC -!- FUNCTION: Transcriptional activator which activates the CDKN2A/ARF
CC locus in response to Ras-Raf signaling, thereby promoting p53/TP53-
CC dependent growth arrest. May also cooperate with MYB to activate
CC transcription of the ANPEP gene. Binds to the consensus sequence 5'-
CC CCCG[GT]ATGT-3'. {ECO:0000269|PubMed:10097151,
CC ECO:0000269|PubMed:10898794, ECO:0000269|PubMed:11711428,
CC ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:17936562,
CC ECO:0000269|PubMed:8887674, ECO:0000269|PubMed:9488476,
CC ECO:0000269|PubMed:9786929}.
CC -!- SUBUNIT: Interacts with the D-type cyclins CCND1, CCND2 and CCND3.
CC Interaction with D-type cyclins may modulate transcriptional activation
CC by this protein. {ECO:0000269|PubMed:8887674,
CC ECO:0000269|PubMed:9488476}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:10097151, ECO:0000269|PubMed:16878159,
CC ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:9488476}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CE22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CE22-2; Sequence=VSP_032097;
CC Name=3;
CC IsoId=Q8CE22-3; Sequence=VSP_032097, VSP_032100, VSP_032101;
CC Name=4;
CC IsoId=Q8CE22-4; Sequence=VSP_032094, VSP_032098, VSP_032099;
CC Name=5;
CC IsoId=Q8CE22-5; Sequence=VSP_032095, VSP_032096;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at mRNA level). Expressed
CC in brain, intestine, kidney, lung, pancreas, skin, spleen and tongue
CC (at protein level). Expressed at high levels in testis and thymus (at
CC protein level). In all tissues examined, expression is predominant in
CC non-proliferating and differentiated cell types. These include
CC epithelial, interstitial and smooth muscle cells of the intestine,
CC differentiated spermatids, sperm and interstitial cells of the testis,
CC and lymphoid cells of the medullary compartment of the thymus.
CC {ECO:0000269|PubMed:10898794, ECO:0000269|PubMed:16878159,
CC ECO:0000269|PubMed:8887674}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle. Expression is
CC highest in G0 and G1 phases and decreases during S and G2/M phases.
CC {ECO:0000269|PubMed:16878159, ECO:0000269|PubMed:8887674}.
CC -!- INDUCTION: Expression is induced by activation of the Ras-Raf signaling
CC pathway, and this may require JUN and JUNB. Expression can be repressed
CC by E2F1, E2F2, E2F3 and E2F4. Expression is also repressed by non-
CC classical inhibitors of NF-kappa-B signaling such as doxorubicin,
CC daunorubicin and UVC, and by the NF-kappa-B p65 subunit (RELA).
CC {ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:16878159,
CC ECO:0000269|PubMed:17546045}.
CC -!- PTM: Phosphorylated by the cyclin-D2/CDK4, cyclin-D3/CDK4 and cyclin-
CC D2/CDK6 complexes and to a lesser extent by the cyclin-D1/CDK4 complex.
CC {ECO:0000269|PubMed:8887674, ECO:0000269|PubMed:9488476}.
CC -!- DISRUPTION PHENOTYPE: Mice spontaneously develop tumors with a mean
CC latency around 80 weeks. The most common tumor types are pulmonary
CC adenomas, adenocarcinomas, hepatocellular tumors, B-cell lymphomas and
CC vascular tumors. The protein appears to be haplo-insufficient for tumor
CC suppression, as heterozygous animals are also prone to spontaneous
CC tumor development. Mice lacking this protein also exhibit enhanced
CC susceptibility to tumor induction by activated Ras or the application
CC of dimethylbenzanthracene (DMBA) or ionizing radiation. Early passage
CC murine embryonic fibroblasts (MEFs) from animals lacking this protein
CC are susceptible to transformation by activated Ras alone due to
CC functional inactivation of the ARF-p53 pathway. Late passage MEFs from
CC animals lacking this protein escape senescence without disrupting
CC CDKN2A/ARF or p53 function. {ECO:0000269|PubMed:10898794,
CC ECO:0000269|PubMed:11711428, ECO:0000269|PubMed:17936562}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DMTF1 family. {ECO:0000305}.
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DR EMBL; U70017; AAC52878.1; -; mRNA.
DR EMBL; AK029147; BAC26325.1; -; mRNA.
DR EMBL; AK031887; BAC27593.1; -; mRNA.
DR EMBL; AK039563; BAC30386.1; -; mRNA.
DR EMBL; AK046201; BAC32635.1; -; mRNA.
DR EMBL; AK160595; BAE35902.1; -; mRNA.
DR EMBL; BC045141; AAH45141.1; -; mRNA.
DR CCDS; CCDS19088.1; -. [Q8CE22-1]
DR CCDS; CCDS51412.1; -. [Q8CE22-2]
DR RefSeq; NP_001103797.1; NM_001110327.1. [Q8CE22-2]
DR RefSeq; NP_035936.3; NM_011806.3. [Q8CE22-1]
DR RefSeq; XP_011238970.1; XM_011240668.2. [Q8CE22-1]
DR AlphaFoldDB; Q8CE22; -.
DR SMR; Q8CE22; -.
DR IntAct; Q8CE22; 1.
DR STRING; 10090.ENSMUSP00000071815; -.
DR iPTMnet; Q8CE22; -.
DR PhosphoSitePlus; Q8CE22; -.
DR EPD; Q8CE22; -.
DR PaxDb; Q8CE22; -.
DR PRIDE; Q8CE22; -.
DR ProteomicsDB; 279548; -. [Q8CE22-1]
DR ProteomicsDB; 279549; -. [Q8CE22-2]
DR ProteomicsDB; 279550; -. [Q8CE22-3]
DR ProteomicsDB; 279551; -. [Q8CE22-4]
DR ProteomicsDB; 279552; -. [Q8CE22-5]
DR Antibodypedia; 15263; 255 antibodies from 26 providers.
DR DNASU; 23857; -.
DR Ensembl; ENSMUST00000071921; ENSMUSP00000071815; ENSMUSG00000042508. [Q8CE22-1]
DR Ensembl; ENSMUST00000095017; ENSMUSP00000092627; ENSMUSG00000042508. [Q8CE22-2]
DR Ensembl; ENSMUST00000183448; ENSMUSP00000139042; ENSMUSG00000042508. [Q8CE22-5]
DR Ensembl; ENSMUST00000184159; ENSMUSP00000139231; ENSMUSG00000042508. [Q8CE22-4]
DR Ensembl; ENSMUST00000184401; ENSMUSP00000139281; ENSMUSG00000042508. [Q8CE22-5]
DR Ensembl; ENSMUST00000184888; ENSMUSP00000139164; ENSMUSG00000042508. [Q8CE22-5]
DR GeneID; 23857; -.
DR KEGG; mmu:23857; -.
DR UCSC; uc008wky.2; mouse. [Q8CE22-1]
DR UCSC; uc008wkz.2; mouse. [Q8CE22-2]
DR UCSC; uc008wld.2; mouse. [Q8CE22-3]
DR CTD; 9988; -.
DR MGI; MGI:1344415; Dmtf1.
DR VEuPathDB; HostDB:ENSMUSG00000042508; -.
DR eggNOG; KOG0051; Eukaryota.
DR GeneTree; ENSGT00940000156016; -.
DR HOGENOM; CLU_021360_0_0_1; -.
DR InParanoid; Q8CE22; -.
DR OMA; WEDLAWG; -.
DR OrthoDB; 1474117at2759; -.
DR PhylomeDB; Q8CE22; -.
DR TreeFam; TF333537; -.
DR BioGRID-ORCS; 23857; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Dmtf1; mouse.
DR PRO; PR:Q8CE22; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CE22; protein.
DR Bgee; ENSMUSG00000042508; Expressed in rostral migratory stream and 254 other tissues.
DR ExpressionAtlas; Q8CE22; baseline and differential.
DR Genevisible; Q8CE22; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 3.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Tumor suppressor.
FT CHAIN 1..761
FT /note="Cyclin-D-binding Myb-like transcription factor 1"
FT /id="PRO_0000323730"
FT DOMAIN 225..263
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 268..333
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 339..388
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DNA_BIND 306..329
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..237
FT /note="Interaction with CCND2"
FT REGION 24..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..458
FT /note="Required for DNA-binding"
FT REGION 87..170
FT /note="Required for transcriptional activation"
FT REGION 176..761
FT /note="Interaction with CCND1, CCND2 and CCND3"
FT /evidence="ECO:0000269|PubMed:8887674"
FT REGION 459..761
FT /note="Required for transcriptional activation"
FT REGION 584..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 37..78
FT /note="DPDEVDSEDSTEPPHKRLCLSSEDDQSIDDATPCISVVALPL -> V (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032094"
FT VAR_SEQ 238..273
FT /note="LRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNT -> QLWTPHNKGHTF
FT KLWLSKVLLPTTCQPVRREKKNEE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032095"
FT VAR_SEQ 274..761
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032096"
FT VAR_SEQ 401..471
FT /note="VLIKGLKQLHENQKNNPVLLENKSGSGVPNSNCNSSVQHVQIRVARLEDNTA
FT ISPSPMAALQIPVQITHVS -> A (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032097"
FT VAR_SEQ 402..451
FT /note="LIKGLKQLHENQKNNPVLLENKSGSGVPNSNCNSSVQHVQIRVARLEDNT
FT -> YSMFRSESPAWKIIQPSLQAPWQRCRFQSRSPTSLQQTPLLLLLTQKQSH (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032098"
FT VAR_SEQ 452..761
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032099"
FT VAR_SEQ 500..524
FT /note="SFHLQPTGTPGTYLLQTSSSQGLPL -> KRKLLLLHLVMGTRGHALMVMEV
FT KG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032100"
FT VAR_SEQ 525..761
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032101"
FT MUTAGEN 319
FT /note="K->E: Abrogates DNA-binding."
FT /evidence="ECO:0000269|PubMed:9488476,
FT ECO:0000269|PubMed:9786929"
FT CONFLICT 44
FT /note="E -> Q (in Ref. 2; BAC30386)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="V -> F (in Ref. 2; BAC30386)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="E -> Q (in Ref. 2; BAC30386)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> G (in Ref. 2; BAC26325)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="V -> A (in Ref. 1; AAC52878)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="H -> P (in Ref. 1; AAC52878)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="V -> L (in Ref. 1; AAC52878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 84644 MW; DB93810B0991CBE3 CRC64;
MSTVEEDSDT VTVETVNSVT FTQDTDGNLI LHCPQNDPDE VDSEDSTEPP HKRLCLSSED
DQSIDDATPC ISVVALPLSE NDQSFEVTMT ATTEVADDEL SEGTVTQIQI LQNDQLDEIS
PLGTEEVSAV SQAWFTTKED KDSLTNKGHK WKQGMWSKEE IDILMNNIER YLKARGIKDA
TEIIFEMSKD ERKDFYRTIA WGLNRPLFAV YRRVLRMYDD RNHVGKYTPE EIEKLKELRI
KHGNDWATIG AALGRSASSV KDRCRLMKDT CNTGKWTEEE EKRLAEVVHE LTSTEPGDIV
TQGVSWAAVA ERVGTRSEKQ CRSKWLNYLN WKQSGGTEWT KEDEINLILR IAELDVADEN
DINWDLLAEG WSSVRSPQWL RSKWWTIKRQ IANHKDVSFP VLIKGLKQLH ENQKNNPVLL
ENKSGSGVPN SNCNSSVQHV QIRVARLEDN TAISPSPMAA LQIPVQITHV SSTDSPAASV
DSETITLNSG TLQTFEILPS FHLQPTGTPG TYLLQTSSSQ GLPLTLTTNP TVTLAAAAPA
SPEQIIVHAL SPEHLLNTSD NVTVQCHTPR VIIQTVATED ITSSLSQEEL TVDSDLHSSD
FPEPPDALEA DTFPDEIPRP KMTIQPSFNN AHVSKFSDQN STELMNSVMV RTEEEIADTD
LKQEEPPSDL ASAYVTEDLE SPTIVHQVHQ TIDDETILIV PSPHGFIQAS DVIDTESVLP
LTTLTDPIFQ HHQEASNIIG SSLGSPVSED SKDVEDLVNC H
