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Q6ZMT4

- KDM7A_HUMAN

UniProt

Q6ZMT4 - KDM7A_HUMAN

Protein

Lysine-specific demethylase 7A

Gene

KDM7A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate.3 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.2 Publications

    Kineticsi

    1. KM=1.2 µM for histone H3 H3K9Me21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei279 – 2791SubstrateBy similarity
    Metal bindingi282 – 2821Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi284 – 2841Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei299 – 2991SubstrateBy similarity
    Metal bindingi354 – 3541Iron; catalytic1 PublicationPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 8852PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone demethylase activity (H3-K27 specific) Source: UniProtKB
    2. histone demethylase activity (H3-K36 specific) Source: UniProtKB
    3. histone demethylase activity (H3-K9 specific) Source: UniProtKB
    4. histone demethylase activity (H4-K20 specific) Source: UniProtKB
    5. iron ion binding Source: UniProtKB
    6. methylated histone binding Source: UniProtKB
    7. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. histone H3-K27 demethylation Source: UniProtKB
    2. histone H3-K36 demethylation Source: UniProtKB
    3. histone H3-K9 demethylation Source: UniProtKB
    4. histone H4-K20 demethylation Source: UniProtKB
    5. midbrain development Source: UniProtKB
    6. positive regulation of transcription, DNA-templated Source: Ensembl
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 7A (EC:1.14.11.-)
    Alternative name(s):
    JmjC domain-containing histone demethylation protein 1D
    Lysine-specific demethylase 7
    Gene namesi
    Name:KDM7A
    Synonyms:JHDM1D, KDM7, KIAA1718
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:22224. KDM7A.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi282 – 2821H → A: Abolishes enzymatic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162392512.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 941941Lysine-specific demethylase 7APRO_0000226771Add
    BLAST

    Proteomic databases

    PaxDbiQ6ZMT4.
    PRIDEiQ6ZMT4.

    PTM databases

    PhosphoSiteiQ6ZMT4.

    Expressioni

    Gene expression databases

    BgeeiQ6ZMT4.
    CleanExiHS_JHDM1D.
    GenevestigatoriQ6ZMT4.

    Organism-specific databases

    HPAiHPA012114.

    Interactioni

    Protein-protein interaction databases

    BioGridi123331. 1 interaction.
    IntActiQ6ZMT4. 1 interaction.
    STRINGi9606.ENSP00000380692.

    Structurei

    Secondary structure

    1
    941
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni40 – 434
    Beta strandi52 – 554
    Turni56 – 583
    Beta strandi61 – 633
    Helixi64 – 674
    Helixi71 – 766
    Beta strandi77 – 804
    Helixi83 – 897
    Beta strandi100 – 1045
    Helixi120 – 1289
    Helixi134 – 1363
    Turni143 – 1453
    Helixi148 – 1547
    Beta strandi160 – 1645
    Turni166 – 1683
    Helixi179 – 1868
    Turni187 – 1893
    Beta strandi190 – 1967
    Turni197 – 2004
    Beta strandi201 – 2066
    Helixi207 – 2159
    Beta strandi216 – 2183
    Beta strandi223 – 2297
    Beta strandi231 – 2333
    Helixi234 – 2385
    Helixi243 – 2486
    Helixi250 – 2545
    Beta strandi269 – 2735
    Beta strandi278 – 2825
    Helixi285 – 2873
    Beta strandi289 – 30416
    Helixi308 – 31811
    Helixi321 – 3255
    Helixi328 – 3314
    Beta strandi336 – 3416
    Beta strandi345 – 3484
    Beta strandi353 – 36917
    Helixi375 – 38814
    Helixi391 – 3955
    Helixi399 – 41820
    Turni419 – 4213
    Helixi426 – 44217
    Turni445 – 4473
    Helixi448 – 4503
    Helixi452 – 4543
    Beta strandi457 – 4593
    Helixi461 – 47717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KV5X-ray2.39A/D1-488[»]
    3KV6X-ray2.89A/D1-488[»]
    3KV9X-ray2.29A92-488[»]
    3KVAX-ray2.79A92-488[»]
    3KVBX-ray2.69A92-488[»]
    3U78X-ray2.69A92-488[»]
    ProteinModelPortaliQ6ZMT4.
    SMRiQ6ZMT4. Positions 38-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6ZMT4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini230 – 386157JmjCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 11418LinkerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 3130Ala-richAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 prevents its access to H3K9me2.1 Publication
    The linker region is a critical determinant of demethylase specificity. It prevents the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3, while it favors selectivity toward H3K27me2.1 Publication

    Sequence similaritiesi

    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri37 – 8852PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290496.
    HOGENOMiHOG000231232.
    HOVERGENiHBG045631.
    InParanoidiQ6ZMT4.
    KOiK11445.
    OMAiLWMKKEL.
    OrthoDBiEOG73JKV9.
    PhylomeDBiQ6ZMT4.
    TreeFamiTF106480.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZMT4-1) [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

    MAGAAAAVAA GAAAGAAAAA VSVAAPGRAS APPPPPPVYC VCRQPYDVNR    50
    FMIECDICKD WFHGSCVGVE EHHAVDIDLY HCPNCAVLHG SSLMKKRRNW 100
    HRHDYTEIDD GSKPVQAGTR TFIKELRSRV FPSADEIIIK MHGSQLTQRY 150
    LEKHGFDVPI MVPKLDDLGL RLPSPTFSVM DVERYVGGDK VIDVIDVARQ 200
    ADSKMTLHNY VKYFMNPNRP KVLNVISLEF SDTKMSELVE VPDIAKKLSW 250
    VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI 300
    FYLIKPTDEN LARYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT 350
    GWIHAVLTSQ DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE 400
    AICWFVAKNL LETLKELRED GFQPQTYLVQ GVKALHTALK LWMKKELVSE 450
    HAFEIPDNVR PGHLIKELSK VIRAIEEENG KPVKSQGIPI VCPVSRSSNE 500
    ATSPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE MCPWEEDILS 550
    SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQPFADQSLY 600
    TADSENEEDK RRTKKAKMKI EESSGVEGVE HEESQKPLNG FFTRVKSELR 650
    SRSSGYSDIS ESEDSGPECT ALKSIFTTEE SESSGDEKKQ EITSNFKEES 700
    NVMRNFLQKS QKPSRSEIPI KRECPTSTST EEEAIQGMLS MAGLHYSTCL 750
    QRQIQSTDCS GERNSLQDPS SCHGSNHEVR QLYRYDKPVE CGYHVKTEDP 800
    DLRTSSWIKQ FDTSRFHPQD LSRSQKCIRK EGSSEISQRV QSRNYVDSSG 850
    SSLQNGKYMQ NSNLTSGACQ ISNGSLSPER PVGETSFSVP LHPTKRPASN 900
    PPPISNQATK GKRPKKGMAT AKQRLGKILK LNRNGHARFF V 941
    Length:941
    Mass (Da):106,557
    Last modified:March 7, 2006 - v2
    Checksum:iAB8161020D157F11
    GO
    Isoform 2 (identifier: Q6ZMT4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         792-809: GYHVKTEDPDLRTSSWIK → ETRSHLCCPDWSPTPELK
         810-941: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:809
    Mass (Da):92,001
    Checksum:i1561533C92AB3466
    GO

    Sequence cautioni

    The sequence BAD18641.1 differs from that shown. Reason: Frameshift at position 902.
    The sequence EAL24032.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti677 – 6771T → I in CAE46011. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti392 – 3921D → Y.
    Corresponds to variant rs5020212 [ dbSNP | Ensembl ].
    VAR_049652
    Natural varianti644 – 6441R → S.1 Publication
    Corresponds to variant rs6950119 [ dbSNP | Ensembl ].
    VAR_049653

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei792 – 80918GYHVK…SSWIK → ETRSHLCCPDWSPTPELK in isoform 2. 1 PublicationVSP_017458Add
    BLAST
    Alternative sequencei810 – 941132Missing in isoform 2. 1 PublicationVSP_017459Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131497 mRNA. Translation: BAD18641.1. Frameshift.
    AC004849 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24032.1. Sequence problems.
    AB051505 mRNA. Translation: BAB21809.1.
    BX641017 mRNA. Translation: CAE46011.1.
    CCDSiCCDS43658.1. [Q6ZMT4-1]
    RefSeqiNP_085150.1. NM_030647.1. [Q6ZMT4-1]
    UniGeneiHs.308710.

    Genome annotation databases

    EnsembliENST00000397560; ENSP00000380692; ENSG00000006459. [Q6ZMT4-1]
    GeneIDi80853.
    KEGGihsa:80853.
    UCSCiuc003vvm.3. human. [Q6ZMT4-1]

    Polymorphism databases

    DMDMi90111764.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK131497 mRNA. Translation: BAD18641.1 . Frameshift.
    AC004849 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24032.1 . Sequence problems.
    AB051505 mRNA. Translation: BAB21809.1 .
    BX641017 mRNA. Translation: CAE46011.1 .
    CCDSi CCDS43658.1. [Q6ZMT4-1 ]
    RefSeqi NP_085150.1. NM_030647.1. [Q6ZMT4-1 ]
    UniGenei Hs.308710.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KV5 X-ray 2.39 A/D 1-488 [» ]
    3KV6 X-ray 2.89 A/D 1-488 [» ]
    3KV9 X-ray 2.29 A 92-488 [» ]
    3KVA X-ray 2.79 A 92-488 [» ]
    3KVB X-ray 2.69 A 92-488 [» ]
    3U78 X-ray 2.69 A 92-488 [» ]
    ProteinModelPortali Q6ZMT4.
    SMRi Q6ZMT4. Positions 38-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123331. 1 interaction.
    IntActi Q6ZMT4. 1 interaction.
    STRINGi 9606.ENSP00000380692.

    Chemistry

    ChEMBLi CHEMBL3038496.
    GuidetoPHARMACOLOGYi 2686.

    PTM databases

    PhosphoSitei Q6ZMT4.

    Polymorphism databases

    DMDMi 90111764.

    Proteomic databases

    PaxDbi Q6ZMT4.
    PRIDEi Q6ZMT4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397560 ; ENSP00000380692 ; ENSG00000006459 . [Q6ZMT4-1 ]
    GeneIDi 80853.
    KEGGi hsa:80853.
    UCSCi uc003vvm.3. human. [Q6ZMT4-1 ]

    Organism-specific databases

    CTDi 80853.
    GeneCardsi GC07M139784.
    H-InvDB HIX0007139.
    HGNCi HGNC:22224. KDM7A.
    HPAi HPA012114.
    neXtProti NX_Q6ZMT4.
    PharmGKBi PA162392512.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290496.
    HOGENOMi HOG000231232.
    HOVERGENi HBG045631.
    InParanoidi Q6ZMT4.
    KOi K11445.
    OMAi LWMKKEL.
    OrthoDBi EOG73JKV9.
    PhylomeDBi Q6ZMT4.
    TreeFami TF106480.

    Miscellaneous databases

    EvolutionaryTracei Q6ZMT4.
    GenomeRNAii 80853.
    NextBioi 71296.
    PROi Q6ZMT4.

    Gene expression databases

    Bgeei Q6ZMT4.
    CleanExi HS_JHDM1D.
    Genevestigatori Q6ZMT4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
      Tissue: Trachea.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-941 (ISOFORM 1), VARIANT SER-644.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-941 (ISOFORM 2).
      Tissue: Fetal kidney.
    6. "KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development."
      Tsukada Y., Ishitani T., Nakayama K.I.
      Genes Dev. 24:432-437(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF HIS-282.
    7. Cited for: FUNCTION.
    8. "Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases."
      Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X.
      Nat. Struct. Mol. Biol. 17:38-43(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-488 IN COMPLEX WITH IRON AND N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DOMAIN LINKER AND PHD-FINGER.

    Entry informationi

    Entry nameiKDM7A_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZMT4
    Secondary accession number(s): A4D1S9
    , C9JJH9, C9JQU2, Q6MZL8, Q9C0E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 92 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 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3