Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511). May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228).By similarity8 Publications

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Activity regulationi

The inhibitors KDOAM-25, CPI-455 and others inhibits its demethylase activity, resulting to cell growth arrest in cancer cells.2 Publications

Kineticsi

Kcat are 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.1 Publication
  1. KM=9 µM for 2-oxoglutarate1 Publication
  2. KM=2.9 µM for histone H3K4me31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei4092-oxoglutarate2 Publications1
    Metal bindingi483Iron; catalyticPROSITE-ProRule annotation4 Publications1
    Metal bindingi485Iron; catalytic4 Publications1
    Binding sitei4912-oxoglutarate2 Publications1
    Binding sitei4932-oxoglutarate2 Publications1
    Binding sitei5012-oxoglutarate2 Publications1
    Metal bindingi571Iron; catalyticPROSITE-ProRule annotation4 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
    Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
    Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
    Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionActivator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase
    Biological processBiological rhythms, Transcription, Transcription regulation
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiR-HSA-3214842 HDMs demethylate histones
    SIGNORiP29375

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 5A (EC:1.14.11.-)
    Alternative name(s):
    Histone demethylase JARID1A
    Jumonji/ARID domain-containing protein 1A
    Retinoblastoma-binding protein 2
    Short name:
    RBBP-2
    Gene namesi
    Name:KDM5AImported
    Synonyms:JARID1A, RBBP2, RBP21 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000073614.11
    HGNCiHGNC:9886 KDM5A
    MIMi180202 gene
    neXtProtiNX_P29375

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi112R → E: Decreases DNA-binding. 1 Publication1
    Mutagenesisi152K → E: Abolishes DNA-binding. 1 Publication1
    Mutagenesisi156S → D: Decreases DNA-binding. 1 Publication1
    Mutagenesisi157L → E: Decreases DNA-binding. 1 Publication1
    Mutagenesisi626C → S: No effect on lysine-specific histone demethylase activity; when associated with S-636. 1 Publication1
    Mutagenesisi636C → S: No effect on lysine-specific histone demethylase activity; when associated with S-626. 1 Publication1
    Mutagenesisi1609V → G: No effect on interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
    Mutagenesisi1625W → A: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
    Mutagenesisi1634 – 1635EW → AA: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication2

    Organism-specific databases

    DisGeNETi5927
    OpenTargetsiENSG00000073614
    PharmGKBiPA34250

    Chemistry databases

    ChEMBLiCHEMBL2424504
    GuidetoPHARMACOLOGYi2680

    Polymorphism and mutation databases

    BioMutaiKDM5A
    DMDMi215274124

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002005841 – 1690Lysine-specific demethylase 5AAdd BLAST1690

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei204PhosphoserineCombined sources1
    Cross-linki1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei1111PhosphoserineCombined sources1
    Modified residuei1330PhosphoserineCombined sources1
    Modified residuei1331PhosphoserineCombined sources1
    Modified residuei1343PhosphothreonineBy similarity1
    Modified residuei1345PhosphoserineBy similarity1
    Modified residuei1438PhosphoserineCombined sources1
    Modified residuei1488PhosphoserineCombined sources1
    Modified residuei1595PhosphotyrosineBy similarity1
    Modified residuei1598PhosphoserineCombined sources1
    Modified residuei1603PhosphoserineCombined sources1
    Modified residuei1666PhosphoserineCombined sources1

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP29375
    MaxQBiP29375
    PaxDbiP29375
    PeptideAtlasiP29375
    PRIDEiP29375
    ProteomicsDBi54559
    54560 [P29375-2]

    PTM databases

    iPTMnetiP29375
    PhosphoSitePlusiP29375
    SwissPalmiP29375

    Expressioni

    Gene expression databases

    BgeeiENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum
    CleanExiHS_JARID1A
    HS_RBP2
    ExpressionAtlasiP29375 baseline and differential
    GenevisibleiP29375 HS

    Organism-specific databases

    HPAiHPA006201

    Interactioni

    Subunit structurei

    Interacts with SUZ12; the interaction is direct (By similarity). Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Interacts with HDAC1 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK. Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RB1P064002EBI-1560836,EBI-491274

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi111862, 30 interactors
    DIPiDIP-472N
    IntActiP29375, 11 interactors
    MINTiP29375
    STRINGi9606.ENSP00000382688

    Chemistry databases

    BindingDBiP29375

    Structurei

    Secondary structure

    11690
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP29375
    SMRiP29375
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29375

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini19 – 60JmjNPROSITE-ProRule annotationAdd BLAST42
    Domaini84 – 174ARIDPROSITE-ProRule annotationAdd BLAST91
    Domaini437 – 603JmjCPROSITE-ProRule annotationAdd BLAST167

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1623 – 1690Interaction with LMO21 PublicationAdd BLAST68

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi419 – 423GSGFP motifBy similarity5

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi1492 – 1587Lys-richAdd BLAST96

    Domaini

    The GSGFP motif is required for the interaction with SUZ12 (By similarity). The ARID domain specifically binds to the CCGCCC motif and is required for the lysine-specific histone demethylase activity (PubMed:18270511). The PHD-type 3 zinc finger is required for the interaction with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity2 Publications

    Sequence similaritiesi

    Belongs to the JARID1 histone demethylase family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
    Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
    Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
    Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiKOG1246 Eukaryota
    ENOG410XR9J LUCA
    GeneTreeiENSGT00530000063118
    HOGENOMiHOG000290719
    InParanoidiP29375
    KOiK11446
    OMAiPICDWRV
    PhylomeDBiP29375
    TreeFamiTF106476

    Family and domain databases

    Gene3Di1.10.150.60, 1 hit
    3.30.40.10, 2 hits
    InterProiView protein in InterPro
    IPR001606 ARID_dom
    IPR036431 ARID_dom_sf
    IPR003347 JmjC_dom
    IPR003349 JmjN
    IPR013637 Lys_sp_deMease-like_dom
    IPR019786 Zinc_finger_PHD-type_CS
    IPR004198 Znf_C5HC2
    IPR011011 Znf_FYVE_PHD
    IPR001965 Znf_PHD
    IPR019787 Znf_PHD-finger
    IPR013083 Znf_RING/FYVE/PHD
    PfamiView protein in Pfam
    PF01388 ARID, 1 hit
    PF02373 JmjC, 1 hit
    PF02375 JmjN, 1 hit
    PF00628 PHD, 2 hits
    PF08429 PLU-1, 1 hit
    PF02928 zf-C5HC2, 1 hit
    SMARTiView protein in SMART
    SM00501 BRIGHT, 1 hit
    SM00558 JmjC, 1 hit
    SM00545 JmjN, 1 hit
    SM00249 PHD, 3 hits
    SUPFAMiSSF46774 SSF46774, 1 hit
    SSF57903 SSF57903, 3 hits
    PROSITEiView protein in PROSITE
    PS51011 ARID, 1 hit
    PS51184 JMJC, 1 hit
    PS51183 JMJN, 1 hit
    PS01359 ZF_PHD_1, 2 hits
    PS50016 ZF_PHD_2, 3 hits

    Sequences (2+)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P29375-1) [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
            10         20         30         40         50
    MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK
    60 70 80 90 100
    IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL
    110 120 130 140 150
    QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP
    160 170 180 190 200
    GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD
    210 220 230 240 250
    TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG
    260 270 280 290 300
    LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
    310 320 330 340 350
    RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE
    360 370 380 390 400
    AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS
    410 420 430 440 450
    IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV
    460 470 480 490 500
    LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP
    510 520 530 540 550
    KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV
    560 570 580 590 600
    PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
    610 620 630 640 650
    HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR
    660 670 680 690 700
    ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL
    710 720 730 740 750
    YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL
    760 770 780 790 800
    SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL
    810 820 830 840 850
    LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL
    860 870 880 890 900
    DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
    910 920 930 940 950
    ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT
    960 970 980 990 1000
    VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK
    1010 1020 1030 1040 1050
    AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA
    1060 1070 1080 1090 1100
    RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE
    1110 1120 1130 1140 1150
    KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA
    1160 1170 1180 1190 1200
    KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
    1210 1220 1230 1240 1250
    SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT
    1260 1270 1280 1290 1300
    ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL
    1310 1320 1330 1340 1350
    QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR
    1360 1370 1380 1390 1400
    ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH
    1410 1420 1430 1440 1450
    AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM
    1460 1470 1480 1490 1500
    VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD
    1510 1520 1530 1540 1550
    SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK
    1560 1570 1580 1590 1600
    LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA
    1610 1620 1630 1640 1650
    EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN
    1660 1670 1680 1690
    EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS
    Length:1,690
    Mass (Da):192,095
    Last modified:November 25, 2008 - v3
    Checksum:iFCF6DC22DEF001DF
    GO
    Isoform 2 (identifier: P29375-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1623-1690: VDWVQCDGGC...LPMEDLKETS → GVVFVTEEERDKKY

    Show »
    Length:1,636
    Mass (Da):186,289
    Checksum:iF308F907C2F899E0
    GO

    Computationally mapped potential isoform sequencesi

    There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E7EV89E7EV89_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    715Annotation score:
    F5GZR8F5GZR8_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    131Annotation score:
    F5H322F5H322_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    122Annotation score:
    F5GZ99F5GZ99_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    126Annotation score:

    Sequence cautioni

    The sequence AAB28544 differs from that shown. Reason: Frameshift at several positions.Curated
    The sequence BAE06081 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti1411Q → QVFFGK in AAB28544 (PubMed:8414517).Curated1
    Sequence conflicti1547E → K in AAB28544 (PubMed:8414517).Curated1
    Sequence conflicti1612 – 1614AQN → EPD in AAB28544 (PubMed:8414517).Curated3

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_032984865M → T. Corresponds to variant dbSNP:rs11062385Ensembl.1
    Natural variantiVAR_0329851190P → A. Corresponds to variant dbSNP:rs2229353Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0357461623 – 1690VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationAdd BLAST68

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S66431 mRNA Translation: AAB28544.1 Frameshift.
    AB209999 mRNA Translation: BAE06081.1 Different initiation.
    AC005844 Genomic DNA No translation available.
    AC007406 Genomic DNA No translation available.
    BC048307 mRNA Translation: AAH48307.1 Different termination.
    BC053893 mRNA Translation: AAH53893.1 Different termination.
    BC110916 mRNA Translation: AAI10917.1 Different termination.
    CCDSiCCDS41736.1 [P29375-1]
    PIRiI78879
    RefSeqiNP_001036068.1, NM_001042603.2 [P29375-1]
    UniGeneiHs.76272

    Genome annotation databases

    EnsembliENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
    GeneIDi5927
    KEGGihsa:5927
    UCSCiuc001qif.3 human [P29375-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Similar proteinsi

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S66431 mRNA Translation: AAB28544.1 Frameshift.
    AB209999 mRNA Translation: BAE06081.1 Different initiation.
    AC005844 Genomic DNA No translation available.
    AC007406 Genomic DNA No translation available.
    BC048307 mRNA Translation: AAH48307.1 Different termination.
    BC053893 mRNA Translation: AAH53893.1 Different termination.
    BC110916 mRNA Translation: AAI10917.1 Different termination.
    CCDSiCCDS41736.1 [P29375-1]
    PIRiI78879
    RefSeqiNP_001036068.1, NM_001042603.2 [P29375-1]
    UniGeneiHs.76272

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2JXJNMR-A85-175[»]
    2KGGNMR-A1609-1659[»]
    2KGINMR-A1609-1659[»]
    3GL6X-ray1.90A1609-1659[»]
    5C11X-ray2.80A1609-1659[»]
    5CEHX-ray3.14A12-797[»]
    5E6HX-ray2.24A1-87[»]
    A348-588[»]
    5ISLX-ray1.69A1-87[»]
    A348-588[»]
    5IVBX-ray1.39A1-87[»]
    A348-588[»]
    5IVCX-ray1.57A1-87[»]
    A348-588[»]
    5IVEX-ray1.78A1-87[»]
    A348-588[»]
    5IVFX-ray1.68A1-87[»]
    A348-588[»]
    5IVJX-ray1.57A1-87[»]
    A348-588[»]
    5IVVX-ray1.85A1-87[»]
    A348-588[»]
    5IVYX-ray1.45A1-87[»]
    A348-588[»]
    5IW0X-ray1.63A1-87[»]
    A348-588[»]
    5IWFX-ray2.29A1-87[»]
    A348-588[»]
    5K4LX-ray3.18A/B12-797[»]
    5V9PX-ray3.00A12-797[»]
    5V9TX-ray3.05A/B12-797[»]
    6BGUX-ray1.68A1-588[»]
    6BGVX-ray1.59A1-588[»]
    6BGWX-ray1.64A1-588[»]
    6BGXX-ray1.88A1-588[»]
    6BGYX-ray1.22A1-588[»]
    6BGZX-ray1.69A1-588[»]
    6BH0X-ray1.99A1-588[»]
    6BH1X-ray1.93A1-588[»]
    6BH2X-ray1.45A1-588[»]
    6BH3X-ray1.70A1-588[»]
    6BH4X-ray2.05A1-588[»]
    6BH5X-ray1.65A1-588[»]
    ProteinModelPortaliP29375
    SMRiP29375
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111862, 30 interactors
    DIPiDIP-472N
    IntActiP29375, 11 interactors
    MINTiP29375
    STRINGi9606.ENSP00000382688

    Chemistry databases

    BindingDBiP29375
    ChEMBLiCHEMBL2424504
    GuidetoPHARMACOLOGYi2680

    PTM databases

    iPTMnetiP29375
    PhosphoSitePlusiP29375
    SwissPalmiP29375

    Polymorphism and mutation databases

    BioMutaiKDM5A
    DMDMi215274124

    Proteomic databases

    EPDiP29375
    MaxQBiP29375
    PaxDbiP29375
    PeptideAtlasiP29375
    PRIDEiP29375
    ProteomicsDBi54559
    54560 [P29375-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
    GeneIDi5927
    KEGGihsa:5927
    UCSCiuc001qif.3 human [P29375-1]

    Organism-specific databases

    CTDi5927
    DisGeNETi5927
    EuPathDBiHostDB:ENSG00000073614.11
    GeneCardsiKDM5A
    H-InvDBiHIX0010308
    HGNCiHGNC:9886 KDM5A
    HPAiHPA006201
    MIMi180202 gene
    neXtProtiNX_P29375
    OpenTargetsiENSG00000073614
    PharmGKBiPA34250
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1246 Eukaryota
    ENOG410XR9J LUCA
    GeneTreeiENSGT00530000063118
    HOGENOMiHOG000290719
    InParanoidiP29375
    KOiK11446
    OMAiPICDWRV
    PhylomeDBiP29375
    TreeFamiTF106476

    Enzyme and pathway databases

    ReactomeiR-HSA-3214842 HDMs demethylate histones
    SIGNORiP29375

    Miscellaneous databases

    ChiTaRSiKDM5A human
    EvolutionaryTraceiP29375
    GeneWikiiJARID1A
    GenomeRNAii5927
    PROiPR:P29375
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum
    CleanExiHS_JARID1A
    HS_RBP2
    ExpressionAtlasiP29375 baseline and differential
    GenevisibleiP29375 HS

    Family and domain databases

    Gene3Di1.10.150.60, 1 hit
    3.30.40.10, 2 hits
    InterProiView protein in InterPro
    IPR001606 ARID_dom
    IPR036431 ARID_dom_sf
    IPR003347 JmjC_dom
    IPR003349 JmjN
    IPR013637 Lys_sp_deMease-like_dom
    IPR019786 Zinc_finger_PHD-type_CS
    IPR004198 Znf_C5HC2
    IPR011011 Znf_FYVE_PHD
    IPR001965 Znf_PHD
    IPR019787 Znf_PHD-finger
    IPR013083 Znf_RING/FYVE/PHD
    PfamiView protein in Pfam
    PF01388 ARID, 1 hit
    PF02373 JmjC, 1 hit
    PF02375 JmjN, 1 hit
    PF00628 PHD, 2 hits
    PF08429 PLU-1, 1 hit
    PF02928 zf-C5HC2, 1 hit
    SMARTiView protein in SMART
    SM00501 BRIGHT, 1 hit
    SM00558 JmjC, 1 hit
    SM00545 JmjN, 1 hit
    SM00249 PHD, 3 hits
    SUPFAMiSSF46774 SSF46774, 1 hit
    SSF57903 SSF57903, 3 hits
    PROSITEiView protein in PROSITE
    PS51011 ARID, 1 hit
    PS51184 JMJC, 1 hit
    PS51183 JMJN, 1 hit
    PS01359 ZF_PHD_1, 2 hits
    PS50016 ZF_PHD_2, 3 hits
    ProtoNetiSearch...

    Entry informationi

    Entry nameiKDM5A_HUMAN
    AccessioniPrimary (citable) accession number: P29375
    Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: November 25, 2008
    Last modified: November 7, 2018
    This is version 187 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
      Index of protein domains and families
    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. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again