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O75164

- KDM4A_HUMAN

UniProt

O75164 - KDM4A_HUMAN

Protein

Lysine-specific demethylase 4A

Gene

KDM4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.
    Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei132 – 1321Alpha-ketoglutarate1 Publication
    Metal bindingi188 – 1881Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi190 – 1901Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei198 – 1981Alpha-ketoglutarate1 Publication
    Binding sitei206 – 2061Alpha-ketoglutarate1 Publication
    Metal bindingi234 – 2341Zinc
    Metal bindingi240 – 2401Zinc
    Metal bindingi276 – 2761Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi306 – 3061Zinc
    Metal bindingi308 – 3081Zinc
    Binding sitei945 – 9451Histone H3K4me3
    Binding sitei967 – 9671Histone H3K4me3
    Binding sitei973 – 9731Histone H3K4me3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri709 – 76759PHD-type 1Add
    BLAST
    Zinc fingeri829 – 88557PHD-type 2Add
    BLAST

    GO - Molecular functioni

    1. histone demethylase activity (H3-K36 specific) Source: UniProtKB
    2. methylated histone binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac muscle hypertrophy in response to stress Source: Ensembl
    2. histone demethylation Source: UniProtKB
    3. histone H3-K36 demethylation Source: GOC
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 4A (EC:1.14.11.-)
    Alternative name(s):
    JmjC domain-containing histone demethylation protein 3A
    Jumonji domain-containing protein 2A
    Gene namesi
    Name:KDM4A
    Synonyms:JHDM3A, JMJD2, JMJD2A, KIAA0677
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:22978. KDM4A.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: HPA
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication
    Mutagenesisi138 – 1381G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication
    Mutagenesisi165 – 1651G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication
    Mutagenesisi170 – 1701G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication
    Mutagenesisi188 – 1881H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. 2 Publications
    Mutagenesisi288 – 2892ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3.
    Mutagenesisi288 – 2892ST → TV, NV or GG: Abolishes histone demethylase activity.
    Mutagenesisi939 – 9391D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. 1 Publication
    Mutagenesisi945 – 9451D → A: Impairs binding to H3K4me3. 1 Publication
    Mutagenesisi945 – 9451D → R: Abolishes binding to H3K4me3. 1 Publication
    Mutagenesisi967 – 9671W → H: Abolishes binding to H3K4me3. 1 Publication
    Mutagenesisi973 – 9731Y → A: Abolishes binding to H3K4me3. 2 Publications

    Organism-specific databases

    PharmGKBiPA164721403.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10641063Lysine-specific demethylase 4APRO_0000183172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiO75164.
    PaxDbiO75164.
    PRIDEiO75164.

    PTM databases

    PhosphoSiteiO75164.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiO75164.
    BgeeiO75164.
    CleanExiHS_JMJD2A.
    GenevestigatoriO75164.

    Organism-specific databases

    HPAiHPA007610.

    Interactioni

    Subunit structurei

    Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST1H3DP684317EBI-936709,EBI-79722
    HIST2H4BP628057EBI-936709,EBI-302023
    HIST3H3Q166956EBI-936709,EBI-358900

    Protein-protein interaction databases

    BioGridi115035. 19 interactions.
    DIPiDIP-29372N.
    IntActiO75164. 28 interactions.
    MINTiMINT-2829088.
    STRINGi9606.ENSP00000361473.

    Structurei

    Secondary structure

    1
    1064
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Turni9 – 113
    Beta strandi15 – 173
    Helixi21 – 244
    Helixi27 – 3610
    Helixi39 – 424
    Beta strandi43 – 475
    Beta strandi59 – 613
    Helixi62 – 643
    Beta strandi66 – 694
    Beta strandi71 – 788
    Beta strandi81 – 888
    Helixi94 – 1029
    Turni104 – 1063
    Helixi114 – 12411
    Beta strandi131 – 1377
    Helixi156 – 1583
    Helixi159 – 1646
    Turni169 – 1713
    Beta strandi175 – 1795
    Beta strandi184 – 1885
    Helixi191 – 1933
    Beta strandi195 – 20410
    Beta strandi206 – 2116
    Helixi213 – 2153
    Helixi216 – 22611
    Helixi228 – 2336
    Helixi237 – 2404
    Beta strandi243 – 2453
    Helixi247 – 2526
    Beta strandi258 – 2625
    Beta strandi267 – 2704
    Beta strandi275 – 2806
    Beta strandi282 – 29110
    Helixi296 – 3027
    Beta strandi308 – 3114
    Helixi318 – 3247
    Helixi326 – 3283
    Helixi329 – 3335
    Helixi348 – 3503
    Helixi351 – 3544
    Beta strandi904 – 9085
    Beta strandi912 – 93221
    Beta strandi937 – 9415
    Helixi943 – 9453
    Helixi951 – 9544
    Beta strandi962 – 9665
    Beta strandi972 – 99019
    Beta strandi995 – 9984
    Helixi1000 – 10023
    Beta strandi1003 – 10053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GF7X-ray2.20A/B/C/D895-1011[»]
    2GFAX-ray2.10A/B895-1011[»]
    2GP3X-ray2.35A/B2-350[»]
    2GP5X-ray2.28A/B2-350[»]
    2OQ6X-ray2.00A/B1-359[»]
    2OQ7X-ray2.15A/B1-359[»]
    2OS2X-ray2.30A/B1-359[»]
    2OT7X-ray2.13A/B1-359[»]
    2OX0X-ray1.95A/B1-359[»]
    2P5BX-ray1.99A/B2-350[»]
    2PXJX-ray2.00A/B2-348[»]
    2Q8CX-ray2.05A/B1-350[»]
    2Q8DX-ray2.29A/B1-350[»]
    2Q8EX-ray2.05A/B1-350[»]
    2QQRX-ray1.80A/B897-1011[»]
    2QQSX-ray2.82A/B897-1011[»]
    2VD7X-ray2.25A/B1-359[»]
    2WWJX-ray2.60A/B7-353[»]
    2YBKX-ray2.40A/B1-359[»]
    2YBPX-ray2.02A/B1-359[»]
    2YBSX-ray2.32A/B1-359[»]
    3NJYX-ray2.60A/B1-359[»]
    3PDQX-ray1.99A/B1-359[»]
    3RVHX-ray2.25A/B1-359[»]
    3U4SX-ray2.15A/B1-359[»]
    4AI9X-ray2.25A/B1-359[»]
    4BISX-ray2.49A/B1-359[»]
    4GD4X-ray2.33A/B1-359[»]
    ProteinModelPortaliO75164.
    SMRiO75164. Positions 7-355, 821-869, 897-1011.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75164.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 5643JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 308167JmjCPROSITE-ProRule annotationAdd
    BLAST
    Domaini897 – 95458Tudor 1Add
    BLAST
    Domaini955 – 101157Tudor 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni597 – 63842Interaction with NCOR1Add
    BLAST

    Domaini

    The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1.4 Publications

    Sequence similaritiesi

    Belongs to the JHDM3 histone demethylase family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 JmjN domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.Curated
    Contains 2 Tudor domains.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri709 – 76759PHD-type 1Add
    BLAST
    Zinc fingeri829 – 88557PHD-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5141.
    HOGENOMiHOG000231125.
    InParanoidiO75164.
    KOiK06709.
    OMAiRKRTAGC.
    OrthoDBiEOG7TQV03.
    PhylomeDBiO75164.
    TreeFamiTF106449.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    SM00333. TUDOR. 2 hits.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75164-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP     50
    KEWKPRASYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI 100
    ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEKHVDEWNI 150
    GRLRTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL 200
    HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML 250
    KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG 300
    KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA 350
    AEFLKESELP PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR 400
    VCLEIPQEVS QSELFPKEDL SSEQYEMTEC PAALAPVRPT HSSVRQVEDG 450
    LTFPDYSDST EVKFEELKNV KLEEEDEEEE QAAAALDLSV NPASVGGRLV 500
    FSGSKKKSSS SLGSGSSRDS ISSDSETSEP LSCRAQGQTG VLTVHSYAKG 550
    DGRVTVGEPC TRKKGSAARS FSERELAEVA DEYMFSLEEN KKSKGRRQPL 600
    SKLPRHHPLV LQECVSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN 650
    FEAEKEFNET MAQQAPHCAV CMIFQTYHQV EFGGFNQNCG NASDLAPQKQ 700
    RTKPLIPEMC FTSTGCSTDI NLSTPYLEED GTSILVSCKK CSVRVHASCY 750
    GVPPAKASED WMCSRCSANA LEEDCCLCSL RGGALQRAND DRWVHVSCAV 800
    AILEARFVNI AERSPVDVSK IPLPRFKLKC IFCKKRRKRT AGCCVQCSHG 850
    RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALQSIT 900
    AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD 950
    CLQFGPPAEG EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR 1000
    DDVYTLDEEL PKRVKSRLSV ASDMRFNEIF TEKEVKQEKK RQRVINSRYR 1050
    EDYIEPALYR AIME 1064
    Length:1,064
    Mass (Da):120,662
    Last modified:October 5, 2010 - v2
    Checksum:i4A811BEECFEDC6B3
    GO
    Isoform 2 (identifier: O75164-2) [UniParc]FASTAAdd to Basket

    Also known as: deltaN-JMJD2A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-583: Missing.

    Show »
    Length:481
    Mass (Da):54,697
    Checksum:i394B208A6E5483FB
    GO

    Sequence cautioni

    The sequence BAA31652.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti482 – 4821A → E.2 Publications
    Corresponds to variant rs586339 [ dbSNP | Ensembl ].
    VAR_023775
    Natural varianti877 – 8771V → G.
    Corresponds to variant rs12759032 [ dbSNP | Ensembl ].
    VAR_031217

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 583583Missing in isoform 2. CuratedVSP_044239Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014577 mRNA. Translation: BAA31652.2. Different initiation.
    AL451062, AC092815 Genomic DNA. Translation: CAH71021.1.
    BC002558 mRNA. Translation: AAH02558.1.
    CCDSiCCDS491.1. [O75164-1]
    RefSeqiNP_055478.2. NM_014663.2. [O75164-1]
    XP_005271411.1. XM_005271354.1. [O75164-1]
    XP_005271412.1. XM_005271355.1. [O75164-1]
    UniGeneiHs.155983.

    Genome annotation databases

    EnsembliENST00000372396; ENSP00000361473; ENSG00000066135. [O75164-1]
    GeneIDi9682.
    KEGGihsa:9682.
    UCSCiuc001cjx.3. human. [O75164-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014577 mRNA. Translation: BAA31652.2 . Different initiation.
    AL451062 , AC092815 Genomic DNA. Translation: CAH71021.1 .
    BC002558 mRNA. Translation: AAH02558.1 .
    CCDSi CCDS491.1. [O75164-1 ]
    RefSeqi NP_055478.2. NM_014663.2. [O75164-1 ]
    XP_005271411.1. XM_005271354.1. [O75164-1 ]
    XP_005271412.1. XM_005271355.1. [O75164-1 ]
    UniGenei Hs.155983.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GF7 X-ray 2.20 A/B/C/D 895-1011 [» ]
    2GFA X-ray 2.10 A/B 895-1011 [» ]
    2GP3 X-ray 2.35 A/B 2-350 [» ]
    2GP5 X-ray 2.28 A/B 2-350 [» ]
    2OQ6 X-ray 2.00 A/B 1-359 [» ]
    2OQ7 X-ray 2.15 A/B 1-359 [» ]
    2OS2 X-ray 2.30 A/B 1-359 [» ]
    2OT7 X-ray 2.13 A/B 1-359 [» ]
    2OX0 X-ray 1.95 A/B 1-359 [» ]
    2P5B X-ray 1.99 A/B 2-350 [» ]
    2PXJ X-ray 2.00 A/B 2-348 [» ]
    2Q8C X-ray 2.05 A/B 1-350 [» ]
    2Q8D X-ray 2.29 A/B 1-350 [» ]
    2Q8E X-ray 2.05 A/B 1-350 [» ]
    2QQR X-ray 1.80 A/B 897-1011 [» ]
    2QQS X-ray 2.82 A/B 897-1011 [» ]
    2VD7 X-ray 2.25 A/B 1-359 [» ]
    2WWJ X-ray 2.60 A/B 7-353 [» ]
    2YBK X-ray 2.40 A/B 1-359 [» ]
    2YBP X-ray 2.02 A/B 1-359 [» ]
    2YBS X-ray 2.32 A/B 1-359 [» ]
    3NJY X-ray 2.60 A/B 1-359 [» ]
    3PDQ X-ray 1.99 A/B 1-359 [» ]
    3RVH X-ray 2.25 A/B 1-359 [» ]
    3U4S X-ray 2.15 A/B 1-359 [» ]
    4AI9 X-ray 2.25 A/B 1-359 [» ]
    4BIS X-ray 2.49 A/B 1-359 [» ]
    4GD4 X-ray 2.33 A/B 1-359 [» ]
    ProteinModelPortali O75164.
    SMRi O75164. Positions 7-355, 821-869, 897-1011.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115035. 19 interactions.
    DIPi DIP-29372N.
    IntActi O75164. 28 interactions.
    MINTi MINT-2829088.
    STRINGi 9606.ENSP00000361473.

    Chemistry

    BindingDBi O75164.
    ChEMBLi CHEMBL5896.

    PTM databases

    PhosphoSitei O75164.

    Proteomic databases

    MaxQBi O75164.
    PaxDbi O75164.
    PRIDEi O75164.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372396 ; ENSP00000361473 ; ENSG00000066135 . [O75164-1 ]
    GeneIDi 9682.
    KEGGi hsa:9682.
    UCSCi uc001cjx.3. human. [O75164-1 ]

    Organism-specific databases

    CTDi 9682.
    GeneCardsi GC01P044115.
    H-InvDB HIX0020610.
    HGNCi HGNC:22978. KDM4A.
    HPAi HPA007610.
    MIMi 609764. gene.
    neXtProti NX_O75164.
    PharmGKBi PA164721403.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5141.
    HOGENOMi HOG000231125.
    InParanoidi O75164.
    KOi K06709.
    OMAi RKRTAGC.
    OrthoDBi EOG7TQV03.
    PhylomeDBi O75164.
    TreeFami TF106449.

    Miscellaneous databases

    ChiTaRSi Kdm4A. human.
    EvolutionaryTracei O75164.
    GeneWikii JMJD2A.
    GenomeRNAii 9682.
    NextBioi 36361.
    PROi O75164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75164.
    Bgeei O75164.
    CleanExi HS_JMJD2A.
    Genevestigatori O75164.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    PF02375. JmjN. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 2 hits.
    SM00333. TUDOR. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
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    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-482.
      Tissue: Brain.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-482.
      Tissue: Placenta.
    4. "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
      Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
      J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HDAC1; HDAC2; HDAC3; RB1 AND HTLV-1 TAX.
    5. "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)."
      Zhang D., Yoon H.-G., Wong J.
      Mol. Cell. Biol. 25:6404-6414(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCOR1.
    6. "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases."
      Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.
      Cell 125:467-481(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-188.
    7. "Tudor, MBT and chromo domains gauge the degree of lysine methylation."
      Kim J., Daniel J., Espejo A., Lake A., Krishna M., Xia L., Zhang Y., Bedford M.T.
      EMBO Rep. 7:397-403(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites."
      Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G., Sixma T.K., Richard S.
      EMBO J. 31:1865-1878(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DOMAIN, MUTAGENESIS OF HIS-188 AND ASP-939.
    12. "A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation."
      Verrier L., Escaffit F., Chailleux C., Trouche D., Vandromme M.
      PLoS Genet. 7:E1001390-E1001390(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2).
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 1-350 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, ZINC-BINDING, MUTAGENESIS OF GLY-133; GLY-138; GLY-165; GLY-170; 279-SER-THR-280 AND TYR-973.
    14. "Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A."
      Huang Y., Fang J., Bedford M.T., Zhang Y., Xu R.-M.
      Science 312:748-751(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 895-1011 IN COMPLEX WITH TRIMETHYLATED H3 'LYS-4', DOMAIN, MUTAGENESIS OF ASP-945; TRP-967 AND TYR-973.

    Entry informationi

    Entry nameiKDM4A_HUMAN
    AccessioniPrimary (citable) accession number: O75164
    Secondary accession number(s): Q5VVB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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