LOCUS       NP_055478               1064 aa            linear   PRI 17-SEP-2024
DEFINITION  lysine-specific demethylase 4A [Homo sapiens].
ACCESSION   NP_055478 XP_375723
VERSION     NP_055478.2
DBSOURCE    REFSEQ: accession NM_014663.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Cai,X., Yu,X., Tang,T., Xu,Y. and Wu,T.
  TITLE     JMJD2A promotes the development of castration-resistant prostate
            cancer by activating androgen receptor enhancer and inhibiting the
            cGAS-STING pathway
  JOURNAL   Mol Carcinog 63 (9), 1682-1696 (2024)
   PUBMED   38818897
  REMARK    GeneRIF: JMJD2A promotes the development of castration-resistant
            prostate cancer by activating androgen receptor enhancer and
            inhibiting the cGAS-STING pathway.
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Su,X., Ding,X., Ding,C., Wang,G., Fu,C., Liu,F., Shi,J. and He,W.
  TITLE     The role of JMJD2A in immune evasion and malignant behavior of
            esophageal squamous cell carcinoma
  JOURNAL   Int Immunopharmacol 137, 112401 (2024)
   PUBMED   38878485
  REMARK    GeneRIF: The role of JMJD2A in immune evasion and malignant
            behavior of esophageal squamous cell carcinoma.
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Liu,T.Y., Yan,J.S., Li,X., Xu,L., Hao,J.L., Zhao,S.Y., Hu,Q.L.,
            Na,F.J., Li,H.M., Zhao,Y. and Zhao,M.F.
  TITLE     FGL1: a novel biomarker and target for non-small cell lung cancer,
            promoting tumor progression and metastasis through KDM4A/STAT3
            transcription mechanism
  JOURNAL   J Exp Clin Cancer Res 43 (1), 213 (2024)
   PUBMED   39085849
  REMARK    GeneRIF: FGL1: a novel biomarker and target for non-small cell lung
            cancer, promoting tumor progression and metastasis through
            KDM4A/STAT3 transcription mechanism.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Gu,R., Kim,T.D., Song,H., Sui,Y., Shin,S., Oh,S. and Janknecht,R.
  TITLE     SET7/9-mediated methylation affects oncogenic functions of histone
            demethylase JMJD2A
  JOURNAL   JCI Insight 8 (20), e164990 (2023)
   PUBMED   37870957
  REMARK    GeneRIF: SET7/9-mediated methylation affects oncogenic functions of
            histone demethylase JMJD2A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Kim,J., Daniel,J., Espejo,A., Lake,A., Krishna,M., Xia,L., Zhang,Y.
            and Bedford,M.T.
  TITLE     Tudor, MBT and chromo domains gauge the degree of lysine
            methylation
  JOURNAL   EMBO Rep 7 (4), 397-403 (2006)
   PUBMED   16415788
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Gray,S.G., Iglesias,A.H., Lizcano,F., Villanueva,R., Camelo,S.,
            Jingu,H., Teh,B.T., Koibuchi,N., Chin,W.W., Kokkotou,E. and
            Dangond,F.
  TITLE     Functional characterization of JMJD2A, a histone deacetylase- and
            retinoblastoma-binding protein
  JOURNAL   J Biol Chem 280 (31), 28507-28518 (2005)
   PUBMED   15927959
  REMARK    GeneRIF: The ability of JMJD2A to associate with retinoblastoma
            proteins and histone deacetylase 1 implies an important role for
            this protein in cell proliferation and oncogenesis.
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   9  (residues 1 to 1064)
  AUTHORS   Zhang,D., Yoon,H.G. and Wong,J.
  TITLE     JMJD2A is a novel N-CoR-interacting protein and is involved in
            repression of the human transcription factor achaete scute-like
            homologue 2 (ASCL2/Hash2)
  JOURNAL   Mol Cell Biol 25 (15), 6404-6414 (2005)
   PUBMED   16024779
  REMARK    GeneRIF: JMJD2A selectively represses the expression of the achaete
            scute-like homologue 2 (ASCL2) gene but not other imprinted genes
            in the same imprinted locus in HeLa cells
REFERENCE   10 (residues 1 to 1064)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of JMJD2 family genes in silico
  JOURNAL   Int J Oncol 24 (6), 1623-1628 (2004)
   PUBMED   15138608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP198064.1, AB014577.1,
            CN361683.1 and CA944984.1.
            
            On May 19, 2006 this sequence version replaced NP_055478.1.
            
            Summary: This gene is a member of the Jumonji domain 2 (JMJD2)
            family and encodes a protein containing a JmjN domain, a JmjC
            domain, a JD2H domain, two TUDOR domains, and two PHD-type zinc
            fingers. This nuclear protein functions as a
            trimethylation-specific demethylase, converting specific
            trimethylated histone residues to the dimethylated form, and as a
            transcriptional repressor. [provided by RefSeq, Apr 2009].
            
            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 :: SRR1803617.163321.1,
                                           SRR1803613.177794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372396.4/ ENSP00000361473.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2-p34.1"
     Protein         1..1064
                     /product="lysine-specific demethylase 4A"
                     /EC_number="1.14.11.66"
                     /EC_number="1.14.11.69"
                     /note="jumonji domain containing 2A; jumonji C
                     domain-containing histone demethylase 3A; lysine
                     (K)-specific demethylase 4A; jumonji domain-containing
                     protein 2A; [histone H3]-trimethyl-L-lysine(9) demethylase
                     4A; [histone H3]-trimethyl-L-lysine(36) demethylase 4A;
                     jmjC domain-containing histone demethylation protein 3A;
                     tudor domain containing 14A"
                     /calculated_mol_wt=120532
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75164.2)"
     Region          13..55
                     /region_name="JmjN"
                     /note="Small domain found in the jumonji family of
                     transcription factors; smart00545"
                     /db_xref="CDD:128818"
     Region          175..291
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          358..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75164.2)"
     Region          501..537
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75164.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75164.2)"
     Region          597..638
                     /region_name="Interaction with NCOR1.
                     /evidence=ECO:0000269|PubMed:16024779"
                     /note="propagated from UniProtKB/Swiss-Prot (O75164.2)"
     Region          616..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75164.2)"
     Region          667..766
                     /region_name="PHD_JMJD2A"
                     /note="PHD finger found in Jumonji domain-containing
                     protein 2A (JMJD2A); cd15575"
                     /db_xref="CDD:277050"
     Site            order(667,734..738,742,761)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277050"
     Region          775..884
                     /region_name="ePHD_JMJD2A"
                     /note="Extended PHD finger (ePHD) found in Jumonji
                     domain-containing protein 2A (JMJD2A); cd15713"
                     /db_xref="CDD:277183"
     Site            order(829,843..847,853,879)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277183"
     Region          899..953
                     /region_name="Tudor_JMJD2A_rpt1"
                     /note="first Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20463"
                     /db_xref="CDD:410534"
     Site            order(931..932,934..937,939)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410534"
     Site            945
                     /site_type="other"
                     /note="Histone H3K4me3 binding; propagated from
                     UniProtKB/Swiss-Prot (O75164.2)"
     Region          956..1011
                     /region_name="Tudor_JMJD2A_rpt2"
                     /note="second Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20466"
                     /db_xref="CDD:410537"
     Site            order(967..969,973)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410537"
     Site            967
                     /site_type="other"
                     /note="Histone H3K4me3 binding; propagated from
                     UniProtKB/Swiss-Prot (O75164.2)"
     Site            973
                     /site_type="other"
                     /note="Histone H3K4me3 binding; propagated from
                     UniProtKB/Swiss-Prot (O75164.2)"
     CDS             1..1064
                     /gene="KDM4A"
                     /gene_synonym="JHDM3A; JMJD2; JMJD2A; TDRD14A"
                     /coded_by="NM_014663.3:144..3338"
                     /db_xref="CCDS:CCDS491.1"
                     /db_xref="GeneID:9682"
                     /db_xref="HGNC:HGNC:22978"
                     /db_xref="MIM:609764"
ORIGIN      
        1 masesetlnp sarimtfypt meefrnfsry iayiesqgah raglakvvpp kewkprasyd
       61 diddlvipap iqqlvtgqsg lftqyniqkk amtvrefrki ansdkyctpr ysefeelerk
      121 ywknltfnpp iygadvngtl yekhvdewni grlrtildlv ekesgitieg vntpylyfgm
      181 wktsfawhte dmdlysinyl hfgepkswys vppehgkrle rlakgffpgs aqsceaflrh
      241 kmtlisplml kkygipfdkv tqeagefmit fpygyhagfn hgfncaestn fatrrwieyg
      301 kqavlcscrk dmvkismdvf vrkfqperyk lwkagkdntv idhtlptpea aeflkeselp
      361 pragneeecp eedmegvedg eegdlktsla khrigtkrhr vcleipqevs qselfpkedl
      421 sseqyemtec paalapvrpt hssvrqvedg ltfpdysdst evkfeelknv kleeedeeee
      481 qaaaaldlsv npasvggrlv fsgskkksss slgsgssrds issdsetsep lscraqgqtg
      541 vltvhsyakg dgrvtvgepc trkkgsaars fserelaeva deymfsleen kkskgrrqpl
      601 sklprhhplv lqecvsddet seqltpeeea eeteawakpl sqlwqnrppn feaekefnet
      661 maqqaphcav cmifqtyhqv efggfnqncg nasdlapqkq rtkplipemc ftstgcstdi
      721 nlstpyleed gtsilvsckk csvrvhascy gvppakased wmcsrcsana leedcclcsl
      781 rggalqrand drwvhvscav ailearfvni aerspvdvsk iplprfklkc ifckkrrkrt
      841 agccvqcshg rcptafhvsc aqaagvmmqp ddwpfvvfit cfrhkipnle rakgalqsit
      901 agqkviskhk ngrfyqcevv rlttetfyev nfddgsfsdn lypedivsqd clqfgppaeg
      961 evvqvrwtdg qvygakfvas hpiqmyqvef edgsqlvvkr ddvytldeel pkrvksrlsv
     1021 asdmrfneif tekevkqekk rqrvinsryr edyiepalyr aime
//
