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Q9H3R0

- KDM4C_HUMAN

UniProt

Q9H3R0 - KDM4C_HUMAN

Protein

Lysine-specific demethylase 4C

Gene

KDM4C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      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.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341Alpha-ketoglutarateBy similarity
    Metal bindingi190 – 1901Iron; catalytic
    Metal bindingi192 – 1921Iron; catalytic
    Binding sitei200 – 2001Alpha-ketoglutarateBy similarity
    Binding sitei208 – 2081Alpha-ketoglutarateBy similarity
    Metal bindingi236 – 2361Zinc1 Publication
    Metal bindingi242 – 2421Zinc1 Publication
    Metal bindingi278 – 2781Iron; catalytic
    Metal bindingi308 – 3081Zinc1 Publication
    Metal bindingi310 – 3101Zinc1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri689 – 74759PHD-type 1Add
    BLAST
    Zinc fingeri809 – 86557PHD-type 2Add
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: BHF-UCL
    2. dioxygenase activity Source: UniProtKB-KW
    3. enzyme binding Source: BHF-UCL
    4. histone demethylase activity (H3-K9 specific) Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3-K9 demethylation Source: UniProtKB
    2. positive regulation of cell proliferation Source: BHF-UCL
    3. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 4C (EC:1.14.11.-)
    Alternative name(s):
    Gene amplified in squamous cell carcinoma 1 protein
    Short name:
    GASC-1 protein
    JmjC domain-containing histone demethylation protein 3C
    Jumonji domain-containing protein 2C
    Gene namesi
    Name:KDM4C
    Synonyms:GASC1, JHDM3C, JMJD2C, KIAA0780
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17071. KDM4C.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nuclear chromatin Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164721503.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10561056Lysine-specific demethylase 4CPRO_0000183177Add
    BLAST

    Proteomic databases

    MaxQBiQ9H3R0.
    PaxDbiQ9H3R0.
    PRIDEiQ9H3R0.

    PTM databases

    PhosphoSiteiQ9H3R0.

    Expressioni

    Tissue specificityi

    Overexpressed in several esophageal squamous cell carcinomas (ESCs).1 Publication

    Gene expression databases

    ArrayExpressiQ9H3R0.
    BgeeiQ9H3R0.
    CleanExiHS_JMJD2C.
    GenevestigatoriQ9H3R0.

    Interactioni

    Protein-protein interaction databases

    BioGridi116712. 9 interactions.
    DIPiDIP-60098N.
    IntActiQ9H3R0. 1 interaction.
    MINTiMINT-4658283.
    STRINGi9606.ENSP00000370710.

    Structurei

    Secondary structure

    1
    1056
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 193
    Helixi23 – 264
    Helixi29 – 3810
    Helixi41 – 444
    Beta strandi45 – 495
    Helixi62 – 665
    Beta strandi68 – 714
    Beta strandi73 – 808
    Beta strandi83 – 908
    Helixi96 – 1049
    Turni106 – 1083
    Helixi116 – 12611
    Beta strandi133 – 1397
    Helixi158 – 1669
    Beta strandi172 – 1754
    Beta strandi177 – 1815
    Beta strandi186 – 1905
    Helixi193 – 1953
    Beta strandi197 – 20610
    Beta strandi208 – 2136
    Helixi215 – 2173
    Helixi218 – 22811
    Helixi230 – 2356
    Helixi239 – 2424
    Beta strandi245 – 2473
    Helixi249 – 2546
    Beta strandi260 – 2645
    Beta strandi269 – 2724
    Beta strandi277 – 2826
    Beta strandi284 – 29310
    Helixi296 – 2983
    Helixi299 – 3024
    Helixi320 – 3267
    Turni328 – 3303
    Helixi331 – 3355
    Beta strandi898 – 91215
    Beta strandi917 – 9215
    Helixi923 – 9253
    Helixi931 – 9344
    Beta strandi942 – 9465
    Beta strandi952 – 96918
    Beta strandi975 – 9795
    Helixi980 – 9823
    Beta strandi986 – 9883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XDPX-ray1.56A875-995[»]
    2XMLX-ray2.55A/B1-347[»]
    ProteinModelPortaliQ9H3R0.
    SMRiQ9H3R0. Positions 10-347, 713-749, 876-994.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H3R0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 5843JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 310167JmjCPROSITE-ProRule annotationAdd
    BLAST
    Domaini877 – 93458Tudor 1Add
    BLAST
    Domaini935 – 99157Tudor 2Add
    BLAST

    Domaini

    The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails By similarity.By similarity

    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 fingeri689 – 74759PHD-type 1Add
    BLAST
    Zinc fingeri809 – 86557PHD-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5141.
    HOGENOMiHOG000231125.
    InParanoidiQ9H3R0.
    KOiK06709.
    OMAiDIIQGER.
    OrthoDBiEOG7TQV03.
    PhylomeDBiQ9H3R0.
    TreeFamiTF106449.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H3R0-1) [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

    MEVAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI     50
    PPKEWKPRQC YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR 100
    QLANSGKYCT PRYLDYEDLE RKYWKNLTFV APIYGADING SIYDEGVDEW 150
    NIARLNTVLD VVEEECGISI EGVNTPYLYF GMWKTTFAWH TEDMDLYSIN 200
    YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL RHKMTLISPS 250
    VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID 300
    YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP 350
    ASTPEVKAWL QRRRKVRKAS RSFQCARSTS KRPKADEEEE VSDEVDGAEV 400
    PNPDSVTDDL KVSEKSEAAV KLRNTEASSE EESSASRMQV EQNLSDHIKL 450
    SGNSCLSTSV TEDIKTEDDK AYAYRSVPSI SSEADDSIPL SSGYEKPEKS 500
    DPSELSWPKS PESCSSVAES NGVLTEGEES DVESHGNGLE PGEIPAVPSG 550
    ERNSFKVPSI AEGENKTSKS WRHPLSRPPA RSPMTLVKQQ APSDEELPEV 600
    LSIEEEVEET ESWAKPLIHL WQTKSPNFAA EQEYNATVAR MKPHCAICTL 650
    LMPYHKPDSS NEENDARWET KLDEVVTSEG KTKPLIPEMC FIYSEENIEY 700
    SPPNAFLEED GTSLLISCAK CCVRVHASCY GIPSHEICDG WLCARCKRNA 750
    WTAECCLCNL RGGALKQTKN NKWAHVMCAV AVPEVRFTNV PERTQIDVGR 800
    IPLQRLKLKC IFCRHRVKRV SGACIQCSYG RCPASFHVTC AHAAGVLMEP 850
    DDWPYVVNIT CFRHKVNPNV KSKACEKVIS VGQTVITKHR NTRYYSCRVM 900
    AVTSQTFYEV MFDDGSFSRD TFPEDIVSRD CLKLGPPAEG EVVQVKWPDG 950
    KLYGAKYFGS NIAHMYQVEF EDGSQIAMKR EDIYTLDEEL PKRVKARFST 1000
    ASDMRFEDTF YGADIIQGER KRQRVLSSRF KNEYVADPVY RTFLKSSFQK 1050
    KCQKRQ 1056
    Length:1,056
    Mass (Da):119,982
    Last modified:May 16, 2006 - v2
    Checksum:iCBE871D4FAADD06D
    GO
    Isoform 2 (identifier: Q9H3R0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         999-1056: STASDMRFED...SFQKKCQKRQ → VSAGRCHLGT...QCNIFLSGTY

    Note: No experimental confirmation available.

    Show »
    Length:1,047
    Mass (Da):118,416
    Checksum:i5A6E06262786B259
    GO
    Isoform 3 (identifier: Q9H3R0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         809-813: KCIFC → GRLGI
         814-1056: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:813
    Mass (Da):91,891
    Checksum:i672012048DEE27AC
    GO
    Isoform 4 (identifier: Q9H3R0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKHYGLPWKRTEEAAADTALTIM
         809-813: KCIFC → GRLGI
         814-1056: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:835
    Mass (Da):94,376
    Checksum:iB08576383C57FE4B
    GO

    Sequence cautioni

    The sequence BAA34500.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI39608.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551L → I in BAB16102. (PubMed:10987278)Curated
    Sequence conflicti514 – 5141C → S in BAG64946. (PubMed:14702039)Curated
    Sequence conflicti807 – 8071K → R in BAG64946. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti206 – 2061E → D.
    Corresponds to variant rs7864351 [ dbSNP | Ensembl ].
    VAR_049660
    Natural varianti396 – 3961D → N.
    Corresponds to variant rs2296067 [ dbSNP | Ensembl ].
    VAR_020340
    Natural varianti492 – 4921S → T.3 Publications
    Corresponds to variant rs35826653 [ dbSNP | Ensembl ].
    VAR_049661
    Natural varianti697 – 6971N → S.
    Corresponds to variant rs35389625 [ dbSNP | Ensembl ].
    VAR_049662
    Natural varianti767 – 7671Q → E.
    Corresponds to variant rs1407856 [ dbSNP | Ensembl ].
    VAR_024681
    Natural varianti772 – 7721K → R.1 Publication
    Corresponds to variant rs1417290 [ dbSNP | Ensembl ].
    VAR_049663
    Natural varianti1039 – 10391V → I.1 Publication
    Corresponds to variant rs913588 [ dbSNP | Ensembl ].
    VAR_024682

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MKHYGLPWKRTEEAAADTAL TIM in isoform 4. 1 PublicationVSP_046113
    Alternative sequencei809 – 8135KCIFC → GRLGI in isoform 3 and isoform 4. 1 PublicationVSP_045462
    Alternative sequencei814 – 1056243Missing in isoform 3 and isoform 4. 1 PublicationVSP_045463Add
    BLAST
    Alternative sequencei999 – 105658STASD…CQKRQ → VSAGRCHLGTCQVNSLSSPH VSQAQQETYLGFWINSKKSQ CNIFLSGTY in isoform 2. 1 PublicationVSP_018311Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037901 mRNA. Translation: BAB16102.1.
    AB018323 mRNA. Translation: BAA34500.1. Different initiation.
    AK304032 mRNA. Translation: BAG64946.1.
    AK310439 mRNA. No translation available.
    AL354707
    , AL137020, AL161443, AL445592, AL513412 Genomic DNA. Translation: CAH73283.1.
    AL354707
    , AL137020, AL161443, AL513412, AL445592 Genomic DNA. Translation: CAH73284.1.
    AL445592
    , AL161443, AL513412, AL354707, AL137020 Genomic DNA. Translation: CAI16322.1.
    AL445592
    , AL137020, AL354707, AL513412, AL161443 Genomic DNA. Translation: CAI16323.1.
    AL161443
    , AL137020, AL354707, AL513412, AL445592 Genomic DNA. Translation: CAI39606.1.
    AL161443
    , AL513412, AL445592, AL354707, AL137020 Genomic DNA. Translation: CAI39607.1.
    AL161443, AL137020, AL513412 Genomic DNA. Translation: CAI39608.1. Sequence problems.
    BC104859 mRNA. Translation: AAI04860.1.
    BC104861 mRNA. Translation: AAI04862.1.
    BC143571 mRNA. Translation: AAI43572.1.
    CCDSiCCDS55285.1. [Q9H3R0-4]
    CCDS55286.1. [Q9H3R0-3]
    CCDS55287.1. [Q9H3R0-2]
    CCDS6471.1. [Q9H3R0-1]
    RefSeqiNP_001140166.1. NM_001146694.1. [Q9H3R0-2]
    NP_001140167.1. NM_001146695.1. [Q9H3R0-3]
    NP_001140168.1. NM_001146696.1. [Q9H3R0-4]
    NP_055876.2. NM_015061.3. [Q9H3R0-1]
    UniGeneiHs.709425.

    Genome annotation databases

    EnsembliENST00000381306; ENSP00000370707; ENSG00000107077. [Q9H3R0-2]
    ENST00000381309; ENSP00000370710; ENSG00000107077. [Q9H3R0-1]
    ENST00000543771; ENSP00000445427; ENSG00000107077. [Q9H3R0-3]
    GeneIDi23081.
    KEGGihsa:23081.
    UCSCiuc003zkg.3. human. [Q9H3R0-2]
    uc003zkh.3. human. [Q9H3R0-1]

    Polymorphism databases

    DMDMi97536525.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037901 mRNA. Translation: BAB16102.1 .
    AB018323 mRNA. Translation: BAA34500.1 . Different initiation.
    AK304032 mRNA. Translation: BAG64946.1 .
    AK310439 mRNA. No translation available.
    AL354707
    , AL137020 , AL161443 , AL445592 , AL513412 Genomic DNA. Translation: CAH73283.1 .
    AL354707
    , AL137020 , AL161443 , AL513412 , AL445592 Genomic DNA. Translation: CAH73284.1 .
    AL445592
    , AL161443 , AL513412 , AL354707 , AL137020 Genomic DNA. Translation: CAI16322.1 .
    AL445592
    , AL137020 , AL354707 , AL513412 , AL161443 Genomic DNA. Translation: CAI16323.1 .
    AL161443
    , AL137020 , AL354707 , AL513412 , AL445592 Genomic DNA. Translation: CAI39606.1 .
    AL161443
    , AL513412 , AL445592 , AL354707 , AL137020 Genomic DNA. Translation: CAI39607.1 .
    AL161443 , AL137020 , AL513412 Genomic DNA. Translation: CAI39608.1 . Sequence problems.
    BC104859 mRNA. Translation: AAI04860.1 .
    BC104861 mRNA. Translation: AAI04862.1 .
    BC143571 mRNA. Translation: AAI43572.1 .
    CCDSi CCDS55285.1. [Q9H3R0-4 ]
    CCDS55286.1. [Q9H3R0-3 ]
    CCDS55287.1. [Q9H3R0-2 ]
    CCDS6471.1. [Q9H3R0-1 ]
    RefSeqi NP_001140166.1. NM_001146694.1. [Q9H3R0-2 ]
    NP_001140167.1. NM_001146695.1. [Q9H3R0-3 ]
    NP_001140168.1. NM_001146696.1. [Q9H3R0-4 ]
    NP_055876.2. NM_015061.3. [Q9H3R0-1 ]
    UniGenei Hs.709425.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XDP X-ray 1.56 A 875-995 [» ]
    2XML X-ray 2.55 A/B 1-347 [» ]
    ProteinModelPortali Q9H3R0.
    SMRi Q9H3R0. Positions 10-347, 713-749, 876-994.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116712. 9 interactions.
    DIPi DIP-60098N.
    IntActi Q9H3R0. 1 interaction.
    MINTi MINT-4658283.
    STRINGi 9606.ENSP00000370710.

    Chemistry

    BindingDBi Q9H3R0.
    ChEMBLi CHEMBL6175.

    PTM databases

    PhosphoSitei Q9H3R0.

    Polymorphism databases

    DMDMi 97536525.

    Proteomic databases

    MaxQBi Q9H3R0.
    PaxDbi Q9H3R0.
    PRIDEi Q9H3R0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381306 ; ENSP00000370707 ; ENSG00000107077 . [Q9H3R0-2 ]
    ENST00000381309 ; ENSP00000370710 ; ENSG00000107077 . [Q9H3R0-1 ]
    ENST00000543771 ; ENSP00000445427 ; ENSG00000107077 . [Q9H3R0-3 ]
    GeneIDi 23081.
    KEGGi hsa:23081.
    UCSCi uc003zkg.3. human. [Q9H3R0-2 ]
    uc003zkh.3. human. [Q9H3R0-1 ]

    Organism-specific databases

    CTDi 23081.
    GeneCardsi GC09P006720.
    H-InvDB HIX0017555.
    HGNCi HGNC:17071. KDM4C.
    MIMi 605469. gene.
    neXtProti NX_Q9H3R0.
    PharmGKBi PA164721503.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5141.
    HOGENOMi HOG000231125.
    InParanoidi Q9H3R0.
    KOi K06709.
    OMAi DIIQGER.
    OrthoDBi EOG7TQV03.
    PhylomeDBi Q9H3R0.
    TreeFami TF106449.

    Miscellaneous databases

    ChiTaRSi KDM4C. human.
    EvolutionaryTracei Q9H3R0.
    GeneWikii JMJD2C.
    GenomeRNAii 23081.
    NextBioi 44205.
    PROi Q9H3R0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H3R0.
    Bgeei Q9H3R0.
    CleanExi HS_JMJD2C.
    Genevestigatori Q9H3R0.

    Family and domain databases

    InterProi IPR003347. JmjC_dom.
    IPR003349. TF_JmjN.
    IPR002999. Tudor.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines."
      Yang Z.Q., Imoto I., Fukuda Y., Pimkhaokham A., Shimada Y., Imamura M., Sugano S., Nakamura Y., Inazawa J.
      Cancer Res. 60:4735-4739(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS THR-492 AND ARG-772.
    2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-492.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT THR-492.
      Tissue: Testis and Trachea.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 ILE-1039.
      Tissue: Liver.
    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, ENZYME ACTIVITY.
    7. "Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family."
      Hillringhaus L., Yue W.W., Rose N.R., Ng S.S., Gileadi C., Loenarz C., Bello S.H., Bray J.E., Schofield C.J., Oppermann U.
      J. Biol. Chem. 286:41616-41625(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-347 IN COMPLEX WITH ZINC AND NICKEL ION, COFACTOR, SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiKDM4C_HUMAN
    AccessioniPrimary (citable) accession number: Q9H3R0
    Secondary accession number(s): B4E1Y4
    , B7ZL46, F5H347, F5H7P0, O94877, Q2M3M0, Q5JUC9, Q5VYJ2, Q5VYJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 123 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 9
      Human chromosome 9: 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

    Dasty 3