LOCUS       NP_059021                450 aa            linear   ROD 31-MAR-2024
DEFINITION  runt-related transcription factor 1 [Rattus norvegicus].
ACCESSION   NP_059021
VERSION     NP_059021.1
DBSOURCE    REFSEQ: accession NM_017325.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Xiao,C., Liu,J., Cheng,Y., Wu,Y., Li,Q., Chen,X., Yuan,J., Dong,Q.,
            Li,L., Liu,Y. and Shen,F.
  TITLE     RUNX1 targeting AKT3 promotes alveolar hypercoagulation and
            fibrinolytic inhibition in LPS induced ARDS
  JOURNAL   Respir Res 25 (1), 54 (2024)
   PUBMED   38267920
  REMARK    GeneRIF: RUNX1 targeting AKT3 promotes alveolar hypercoagulation
            and fibrinolytic inhibition in LPS induced ARDS.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Suzuki,S., Tanaka,S., Kametani,Y., Umeda,A., Nishinaka,K.,
            Egawa,K., Okada,Y., Obana,M. and Fujio,Y.
  TITLE     Runx1 is upregulated by STAT3 and promotes proliferation of
            neonatal rat cardiomyocytes
  JOURNAL   Physiol Rep 11 (23), e15872 (2023)
   PUBMED   38040660
  REMARK    GeneRIF: Runx1 is upregulated by STAT3 and promotes proliferation
            of neonatal rat cardiomyocytes.
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Song,J., Zhang,X., Lv,S., Liu,M., Hua,X., Yue,L., Wang,S. and He,W.
  TITLE     Age-related promoter-switch regulates Runx1 expression in adult rat
            hearts
  JOURNAL   BMC Cardiovasc Disord 23 (1), 541 (2023)
   PUBMED   37936072
  REMARK    GeneRIF: Age-related promoter-switch regulates Runx1 expression in
            adult rat hearts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Xiao,C., Li,Q., Xiao,J., Chen,X., Yuan,J., Li,S., Li,W., Gao,D.,
            Li,L., Liu,Y. and Shen,F.
  TITLE     miR-9 targeting RUNX1 improves LPS-induced alveolar
            hypercoagulation and fibrinolysis inhibition through NF-kappaB
            inactivation in ARDS
  JOURNAL   Int Immunopharmacol 120, 110318 (2023)
   PUBMED   37201407
  REMARK    GeneRIF: miR-9 targeting RUNX1 improves LPS-induced alveolar
            hypercoagulation and fibrinolysis inhibition through NF-kappaB
            inactivation in ARDS.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Zhang,Y., Huang,H., Liu,W., Liu,S., Wang,X.Y., Diao,Z.L.,
            Zhang,A.H., Guo,W., Han,X., Dong,X. and Katilov,O.
  TITLE     Endothelial progenitor cells-derived exosomal microRNA-21-5p
            alleviates sepsis-induced acute kidney injury by inhibiting RUNX1
            expression
  JOURNAL   Cell Death Dis 12 (4), 335 (2021)
   PUBMED   33785732
  REMARK    GeneRIF: Endothelial progenitor cells-derived exosomal
            microRNA-21-5p alleviates sepsis-induced acute kidney injury by
            inhibiting RUNX1 expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Zhang,Y.W., Bae,S.C., Huang,G., Fu,Y.X., Lu,J., Ahn,M.Y., Kanno,Y.,
            Kanno,T. and Ito,Y.
  TITLE     A novel transcript encoding an N-terminally truncated AML1/PEBP2
            alphaB protein interferes with transactivation and blocks
            granulocytic differentiation of 32Dcl3 myeloid cells
  JOURNAL   Mol Cell Biol 17 (7), 4133-4145 (1997)
   PUBMED   9199349
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Giese,K., Kingsley,C., Kirshner,J.R. and Grosschedl,R.
  TITLE     Assembly and function of a TCR alpha enhancer complex is dependent
            on LEF-1-induced DNA bending and multiple protein-protein
            interactions
  JOURNAL   Genes Dev 9 (8), 995-1008 (1995)
   PUBMED   7774816
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Lu,J., Maruyama,M., Satake,M., Bae,S.C., Ogawa,E., Kagoshima,H.,
            Shigesada,K. and Ito,Y.
  TITLE     Subcellular localization of the alpha and beta subunits of the
            acute myeloid leukemia-linked transcription factor PEBP2/CBF
  JOURNAL   Mol Cell Biol 15 (3), 1651-1661 (1995)
   PUBMED   7862156
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Zhu,X., Yeadon,J.E. and Burden,S.J.
  TITLE     AML1 is expressed in skeletal muscle and is regulated by
            innervation
  JOURNAL   Mol Cell Biol 14 (12), 8051-8057 (1994)
   PUBMED   7969143
  REMARK    Erratum:[Mol Cell Biol 1995 Feb;15(2):1136]
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Meyers,S., Downing,J.R. and Hiebert,S.W.
  TITLE     Identification of AML-1 and the (8;21) translocation protein
            (AML-1/ETO) as sequence-specific DNA-binding proteins: the runt
            homology domain is required for DNA binding and protein-protein
            interactions
  JOURNAL   Mol Cell Biol 13 (10), 6336-6345 (1993)
   PUBMED   8413232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L35271.1, SRR26643429.40770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..450
                     /product="runt-related transcription factor 1"
                     /note="core-binding factor runt domain alpha subunit 2
                     (acute myeloid leukemia 1 oncogene); oncogene AML-1; acute
                     myeloid leukemia 1 protein; core-binding factor subunit
                     alpha-2; polyomavirus enhancer-binding protein 2 alpha B
                     subunit; PEA2-alpha B; PEBP2-alpha B"
                     /calculated_mol_wt=48426
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            24
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Region          51..179
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          80..84
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Region          135..143
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Region          168..177
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Region          170..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Region          209..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Region          290..369
                     /region_name="Interaction with KAT6A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     Region          306..398
                     /region_name="Interaction with KAT6B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Region          360..450
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     Region          360..400
                     /region_name="Interaction with FOXP3.
                     /evidence=ECO:0000250|UniProtKB:Q01196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Region          410..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63046.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01196; propagated from
                     UniProtKB/Swiss-Prot (Q63046.1)"
     CDS             1..450
                     /gene="Runx1"
                     /gene_synonym="Aml1; CBF-alpha-2; Cbfa2; PEA2-alpha;
                     PEBP2-alpha"
                     /coded_by="NM_017325.2:400..1752"
                     /db_xref="GeneID:50662"
                     /db_xref="RGD:2283"
ORIGIN      
        1 mripvdasts rrftppstal spgkmsealp lgapdggaal asklrsgdrs mvevladhpg
       61 elvrtdspnf lcsvlpthwr cnktlpiafk vvalgdvpdg tlvtvmagnd enysaelrna
      121 taamknqvar fndlrfvgrs grgksftlti tvftnppqva tyhraikitv dgpreprrhr
      181 qklddqtkpg slsfserlse leqlrrtamr vsphhpaptp npraslnhst afnpqpqsqm
      241 qdarqiqpsp pwsydqsyqy lgsitssvhp atpispgras gmtslsaels srlstapdlt
      301 afgdprqfpt lpsisdprmh ypgaftyspp vtsgigigms amsstsryht ylpppypgss
      361 qaqagpfqtg spsyhlyygt sagsyqfsmv ggersppril ppctnastga allnpslpsq
      421 sdvvetegsh snsptnmppa rleeavwrpy
//
