Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y2K7

- KDM2A_HUMAN

UniProt

Q9Y2K7 - KDM2A_HUMAN

Protein

Lysine-specific demethylase 2A

Gene

KDM2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (07 Nov 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis.2 Publications

    Catalytic activityi

    Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
    Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei209 – 2091SubstrateBy similarity
    Metal bindingi212 – 2121Iron; catalyticCurated
    Metal bindingi214 – 2141Iron; catalyticPROSITE-ProRule annotation
    Binding sitei229 – 2291SubstrateBy similarity
    Metal bindingi284 – 2841Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri564 – 61047CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri617 – 67862PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone demethylase activity (H3-K36 specific) Source: UniProtKB-EC
    2. unmethylated CpG binding Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3-K36 demethylation Source: MGI
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 2A (EC:1.14.11.27)
    Alternative name(s):
    CXXC-type zinc finger protein 8
    F-box and leucine-rich repeat protein 11
    F-box protein FBL7
    F-box protein Lilina
    F-box/LRR-repeat protein 11
    JmjC domain-containing histone demethylation protein 1A
    [Histone-H3]-lysine-36 demethylase 1A
    Gene namesi
    Name:KDM2A
    Synonyms:CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:13606. KDM2A.

    Subcellular locationi

    Nucleusnucleoplasm 2 Publications
    Note: Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2.

    GO - Cellular componenti

    1. nuclear chromatin Source: Ensembl
    2. nucleolus Source: HPA
    3. nucleoplasm Source: UniProtKB-SubCell
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi212 – 2121H → A: Abolishes histone demethylase activity. 1 Publication
    Mutagenesisi571 – 5711C → A: Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577. 1 Publication
    Mutagenesisi574 – 5741C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. 1 Publication
    Mutagenesisi577 – 5771C → A: Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. 1 Publication

    Organism-specific databases

    PharmGKBiPA164721195.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11621162Lysine-specific demethylase 2APRO_0000119855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphoserine4 Publications
    Modified residuei390 – 3901Phosphoserine1 Publication
    Modified residuei394 – 3941Phosphoserine1 Publication
    Modified residuei550 – 5501Phosphothreonine4 Publications
    Modified residuei558 – 5581Phosphoserine3 Publications
    Modified residuei632 – 6321Phosphothreonine1 Publication
    Modified residuei692 – 6921Phosphoserine2 Publications
    Modified residuei713 – 7131Phosphothreonine2 Publications
    Modified residuei731 – 7311Phosphoserine2 Publications
    Modified residuei832 – 8321Phosphoserine1 Publication
    Modified residuei869 – 8691Phosphoserine2 Publications
    Modified residuei883 – 8831Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2K7.
    PaxDbiQ9Y2K7.
    PRIDEiQ9Y2K7.

    PTM databases

    PhosphoSiteiQ9Y2K7.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest levels in brain, testis and ovary, followed by lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2K7.
    BgeeiQ9Y2K7.
    CleanExiHS_FBXL11.
    GenevestigatoriQ9Y2K7.

    Organism-specific databases

    HPAiCAB012272.
    HPA042975.
    HPA044251.

    Interactioni

    Subunit structurei

    Part of a SCF (SKP1-cullin-F-box) protein ligase complex By similarity. Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to chromatin.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi116639. 15 interactions.
    DIPiDIP-34596N.
    IntActiQ9Y2K7. 10 interactions.
    MINTiMINT-1185543.
    STRINGi9606.ENSP00000384903.

    Structurei

    Secondary structure

    1
    1162
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Helixi40 – 456
    Helixi59 – 613
    Helixi64 – 707
    Beta strandi76 – 805
    Turni82 – 854
    Helixi95 – 1017
    Helixi123 – 1308
    Turni134 – 1363
    Beta strandi141 – 1466
    Helixi154 – 1563
    Helixi161 – 1666
    Helixi168 – 1725
    Helixi175 – 1773
    Beta strandi199 – 2035
    Beta strandi208 – 2125
    Helixi215 – 2173
    Beta strandi219 – 2279
    Beta strandi229 – 2346
    Helixi238 – 24912
    Beta strandi254 – 2563
    Helixi258 – 2614
    Beta strandi266 – 2705
    Beta strandi275 – 2784
    Beta strandi283 – 2875
    Beta strandi292 – 2998
    Beta strandi302 – 3043
    Helixi305 – 31713
    Helixi329 – 34517
    Helixi352 – 36211
    Helixi455 – 46915
    Helixi473 – 4753
    Beta strandi480 – 4834
    Helixi485 – 49814
    Beta strandi499 – 5013
    Helixi504 – 5074
    Helixi575 – 5784
    Helixi586 – 5905
    Helixi592 – 5943
    Helixi605 – 6073
    Turni621 – 6233
    Helixi629 – 6324
    Helixi635 – 6373
    Beta strandi640 – 6423
    Turni643 – 6453
    Helixi651 – 6533
    Beta strandi664 – 6718
    Turni673 – 6753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YU1X-ray2.70A1-517[»]
    2YU2X-ray2.70A1-517[»]
    4BBQX-ray2.24A/B567-681[»]
    ProteinModelPortaliQ9Y2K7.
    SMRiQ9Y2K7. Positions 34-364, 450-517, 567-676, 891-1145.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2K7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini148 – 316169JmjCPROSITE-ProRule annotationAdd
    BLAST
    Domaini889 – 93648F-boxAdd
    BLAST
    Repeati961 – 98222LRR 1Add
    BLAST
    Repeati984 – 101027LRR 2Add
    BLAST
    Repeati1048 – 107326LRR 3Add
    BLAST
    Repeati1074 – 110330LRR 4Add
    BLAST
    Repeati1104 – 112825LRR 5Add
    BLAST
    Repeati1129 – 115628LRR 6Add
    BLAST

    Domaini

    The JmjC domain mediates demethylation activity and is required for satellite silencing.
    The CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated.

    Sequence similaritiesi

    Belongs to the JHDM1 histone demethylase family.Curated
    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 F-box domain.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 6 LRR (leucine-rich) repeats.Curated
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri564 – 61047CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri617 – 67862PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290496.
    InParanoidiQ9Y2K7.
    KOiK10276.
    OMAiCEAFISE.
    OrthoDBiEOG78SQH0.
    PhylomeDBiQ9Y2K7.
    TreeFamiTF106480.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001810. F-box_dom.
    IPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR002857. Znf_CXXC.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2K7-1) [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

    MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN     50
    ANFVTFMEGK DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM 100
    CVGSRRMVDV MDVNTQKGIE MTMAQWTRYY ETPEEEREKL YNVISLEFSH 150
    TRLENMVQRP STVDFIDWVD NMWPRHLKES QTESTNAILE MQYPKVQKYC 200
    LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN LELYENWLLS 250
    GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL 300
    HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL 350
    TKEFQKESLS MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV 400
    NLDYDGLGKT CRSLPSLKKT LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ 450
    VHLTHFELEG LRCLVDKLES LPLHKKCVPT GIEDEDALIA DVKILLEELA 500
    NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP HTMKPAPRLT 550
    PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM 600
    KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH 650
    PGCLQMDGEG LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK 700
    VLRPLRSCDE PLTPPPHSPT SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS 750
    ASRDERFKRR QLLRLQATER TMVREKENNP SGKKELSEVE KAKIRGSYLT 800
    VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC PARTPQRGDE 850
    EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS 900
    VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII 950
    KRQPVSLDLS WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC 1000
    PLLRTLDLRW AVGIKDPQIR DLLTPPADKP GQDNRSKLRN MTDFRLAGLD 1050
    ITDATLRLII RHMPLLSRLD LSHCSHLTDQ SSNLLTAVGS STRYSLTELN 1100
    MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF ISDLSINSLY 1150
    CLSDEKLIQK IS 1162
    Length:1,162
    Mass (Da):132,793
    Last modified:November 7, 2003 - v3
    Checksum:i88620A363A5C5842
    GO
    Isoform 2 (identifier: Q9Y2K7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-306: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:856
    Mass (Da):96,859
    Checksum:iC1351A450B4482E0
    GO
    Isoform 4 (identifier: Q9Y2K7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-542: Missing.

    Show »
    Length:620
    Mass (Da):69,898
    Checksum:i48020F8357601D46
    GO
    Isoform 5 (identifier: Q9Y2K7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-439: Missing.
         440-492: DPQCAPRKDR...EDEDALIADV → MCSGRFQNIQ...PRQLQSDGKR

    Show »
    Length:723
    Mass (Da):81,678
    Checksum:iBC40E0405B687BB9
    GO
    Isoform 3 (identifier: Q9Y2K7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         774-782: REKENNPSG → LRQETLDKN
         783-1162: Missing.

    Show »
    Length:782
    Mass (Da):89,948
    Checksum:i667E9A3E503C6550
    GO

    Sequence cautioni

    The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410.
    The sequence AAD56012.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA76848.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAJ05817.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti518 – 5181K → I in AAH47371. (PubMed:15489334)Curated
    Sequence conflicti657 – 6571D → G in AAH47371. (PubMed:15489334)Curated
    Sequence conflicti1128 – 11281Missing in AAH01203. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 542542Missing in isoform 4. 1 PublicationVSP_046938Add
    BLAST
    Alternative sequencei1 – 439439Missing in isoform 5. 1 PublicationVSP_046939Add
    BLAST
    Alternative sequencei1 – 306306Missing in isoform 2. 1 PublicationVSP_017468Add
    BLAST
    Alternative sequencei440 – 49253DPQCA…LIADV → MCSGRFQNIQVNPDFPRGRI SNSFRRTSSTENKTKTLGKL HQEPRQLQSDGKR in isoform 5. 1 PublicationVSP_046940Add
    BLAST
    Alternative sequencei774 – 7829REKENNPSG → LRQETLDKN in isoform 3. 2 PublicationsVSP_017469
    Alternative sequencei783 – 1162380Missing in isoform 3. 2 PublicationsVSP_017470Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023221 mRNA. Translation: BAA76848.2. Different initiation.
    AB490246 mRNA. Translation: BAJ05817.1. Different initiation.
    JQ710743 mRNA. Translation: AFK81542.1.
    JQ710744 mRNA. Translation: AFK81543.1.
    AK024505 mRNA. Translation: BAB15795.1. Frameshift.
    AP000729 Genomic DNA. No translation available.
    AP001885 Genomic DNA. No translation available.
    BC001203 mRNA. Translation: AAH01203.1.
    BC047371 mRNA. Translation: AAH47371.1.
    BC047486 mRNA. Translation: AAH47486.1.
    BC064360 mRNA. Translation: AAH64360.1.
    AF179221 mRNA. Translation: AAD56012.1. Different initiation.
    AL117517 mRNA. Translation: CAH10721.1.
    CCDSiCCDS44657.1. [Q9Y2K7-1]
    CCDS58148.1. [Q9Y2K7-5]
    RefSeqiNP_001243334.1. NM_001256405.1. [Q9Y2K7-5]
    NP_036440.1. NM_012308.2. [Q9Y2K7-1]
    UniGeneiHs.124147.

    Genome annotation databases

    EnsembliENST00000308783; ENSP00000309302; ENSG00000173120. [Q9Y2K7-4]
    ENST00000398645; ENSP00000381640; ENSG00000173120. [Q9Y2K7-3]
    ENST00000529006; ENSP00000432786; ENSG00000173120. [Q9Y2K7-1]
    ENST00000530342; ENSP00000435776; ENSG00000173120. [Q9Y2K7-5]
    GeneIDi22992.
    KEGGihsa:22992.
    UCSCiuc001ojw.3. human. [Q9Y2K7-1]

    Polymorphism databases

    DMDMi38257795.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023221 mRNA. Translation: BAA76848.2 . Different initiation.
    AB490246 mRNA. Translation: BAJ05817.1 . Different initiation.
    JQ710743 mRNA. Translation: AFK81542.1 .
    JQ710744 mRNA. Translation: AFK81543.1 .
    AK024505 mRNA. Translation: BAB15795.1 . Frameshift.
    AP000729 Genomic DNA. No translation available.
    AP001885 Genomic DNA. No translation available.
    BC001203 mRNA. Translation: AAH01203.1 .
    BC047371 mRNA. Translation: AAH47371.1 .
    BC047486 mRNA. Translation: AAH47486.1 .
    BC064360 mRNA. Translation: AAH64360.1 .
    AF179221 mRNA. Translation: AAD56012.1 . Different initiation.
    AL117517 mRNA. Translation: CAH10721.1 .
    CCDSi CCDS44657.1. [Q9Y2K7-1 ]
    CCDS58148.1. [Q9Y2K7-5 ]
    RefSeqi NP_001243334.1. NM_001256405.1. [Q9Y2K7-5 ]
    NP_036440.1. NM_012308.2. [Q9Y2K7-1 ]
    UniGenei Hs.124147.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YU1 X-ray 2.70 A 1-517 [» ]
    2YU2 X-ray 2.70 A 1-517 [» ]
    4BBQ X-ray 2.24 A/B 567-681 [» ]
    ProteinModelPortali Q9Y2K7.
    SMRi Q9Y2K7. Positions 34-364, 450-517, 567-676, 891-1145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116639. 15 interactions.
    DIPi DIP-34596N.
    IntActi Q9Y2K7. 10 interactions.
    MINTi MINT-1185543.
    STRINGi 9606.ENSP00000384903.

    Chemistry

    BindingDBi Q9Y2K7.
    ChEMBLi CHEMBL1938210.
    GuidetoPHARMACOLOGYi 2671.

    PTM databases

    PhosphoSitei Q9Y2K7.

    Polymorphism databases

    DMDMi 38257795.

    Proteomic databases

    MaxQBi Q9Y2K7.
    PaxDbi Q9Y2K7.
    PRIDEi Q9Y2K7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308783 ; ENSP00000309302 ; ENSG00000173120 . [Q9Y2K7-4 ]
    ENST00000398645 ; ENSP00000381640 ; ENSG00000173120 . [Q9Y2K7-3 ]
    ENST00000529006 ; ENSP00000432786 ; ENSG00000173120 . [Q9Y2K7-1 ]
    ENST00000530342 ; ENSP00000435776 ; ENSG00000173120 . [Q9Y2K7-5 ]
    GeneIDi 22992.
    KEGGi hsa:22992.
    UCSCi uc001ojw.3. human. [Q9Y2K7-1 ]

    Organism-specific databases

    CTDi 22992.
    GeneCardsi GC11P066888.
    HGNCi HGNC:13606. KDM2A.
    HPAi CAB012272.
    HPA042975.
    HPA044251.
    MIMi 605657. gene.
    neXtProti NX_Q9Y2K7.
    PharmGKBi PA164721195.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290496.
    InParanoidi Q9Y2K7.
    KOi K10276.
    OMAi CEAFISE.
    OrthoDBi EOG78SQH0.
    PhylomeDBi Q9Y2K7.
    TreeFami TF106480.

    Miscellaneous databases

    ChiTaRSi KDM2A. human.
    EvolutionaryTracei Q9Y2K7.
    GeneWikii KDM2A.
    GenomeRNAii 22992.
    NextBioi 35533673.
    PROi Q9Y2K7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2K7.
    Bgeei Q9Y2K7.
    CleanExi HS_FBXL11.
    Genevestigatori Q9Y2K7.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001810. F-box_dom.
    IPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR002857. Znf_CXXC.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    PF02373. JmjC. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
      Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
      Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Tsuneoka M., Tanaka Y., Okamoto K., Teye K.
      Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    3. Iuchi S., Green H.
      Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    4. "Prediction of the coding sequences of unidentified human genes. XIII. 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., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Characterization of long cDNA clones from human adult spleen."
      Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
      DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Spleen.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Eye, Testis and Uterus.
    9. Pagano M.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162.
      Tissue: Testis.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Histone demethylation by a family of JmjC domain-containing proteins."
      Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
      Nature 439:811-816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-212.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. "KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state."
      Frescas D., Guardavaccaro D., Kuchay S.M., Kato H., Poleshko A., Basrur V., Elenitoba-Johnson K.S., Katz R.A., Pagano M.
      Cell Cycle 7:3539-3547(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-571; CYS-574 AND CYS-577.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713 AND SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-550; SER-558; THR-713; SER-731 AND SER-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-692 AND SER-869, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. Cited for: SUBCELLULAR LOCATION, DOMAIN CXXC ZINC-FINGER.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-394; THR-550; SER-558; SER-869 AND SER-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKDM2A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2K7
    Secondary accession number(s): D4QA03
    , E9PIL6, I3VM55, Q49A21, Q4G0M3, Q69YY8, Q9BVH5, Q9H7H5, Q9UK66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3