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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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

    • chromatin DNA binding Source: Ensembl
    • core promoter sequence-specific DNA binding Source: CAFA
    • DNA binding Source: GDB
    • histone binding Source: UniProtKB
    • histone demethylase activity Source: Reactome
    • histone demethylase activity (H3-dimethyl-K4 specific) Source: CAFA
    • histone demethylase activity (H3-trimethyl-K4 specific) Source: CAFA
    • methylated histone binding Source: UniProtKB
    • 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: InterPro
    • transcription coactivator activity Source: UniProtKB
    • transcription factor activity, sequence-specific DNA binding Source: CAFA
    • zinc ion binding Source: UniProtKB

    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.

    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.

    PTM databases

    iPTMnetiP29375.
    PhosphoSitePlusiP29375.
    SwissPalmiP29375.

    Expressioni

    Gene expression databases

    BgeeiENSG00000073614.
    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

    GO - Molecular functioni

    • histone binding Source: UniProtKB
    • methylated histone binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi111862. 29 interactors.
    DIPiDIP-472N.
    IntActiP29375. 10 interactors.
    STRINGi9606.ENSP00000382688.

    Chemistry databases

    BindingDBiP29375.

    Structurei

    Secondary structure

    11690
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi28 – 30Combined sources3
    Helixi32 – 43Combined sources12
    Turni44 – 46Combined sources3
    Beta strandi47 – 51Combined sources5
    Turni65 – 67Combined sources3
    Beta strandi73 – 76Combined sources4
    Turni77 – 80Combined sources4
    Helixi81 – 83Combined sources3
    Helixi85 – 100Combined sources16
    Helixi117 – 126Combined sources10
    Helixi130 – 135Combined sources6
    Helixi139 – 145Combined sources7
    Helixi154 – 173Combined sources20
    Beta strandi174 – 176Combined sources3
    Turni350 – 353Combined sources4
    Helixi363 – 378Combined sources16
    Helixi382 – 384Combined sources3
    Helixi387 – 399Combined sources13
    Beta strandi401 – 403Combined sources3
    Beta strandi406 – 414Combined sources9
    Helixi415 – 418Combined sources4
    Beta strandi427 – 429Combined sources3
    Helixi433 – 435Combined sources3
    Helixi436 – 439Combined sources4
    Helixi445 – 447Combined sources3
    Helixi448 – 450Combined sources3
    Helixi455 – 459Combined sources5
    Beta strandi470 – 474Combined sources5
    Beta strandi479 – 483Combined sources5
    Helixi486 – 488Combined sources3
    Beta strandi490 – 499Combined sources10
    Beta strandi501 – 506Combined sources6
    Helixi508 – 510Combined sources3
    Helixi511 – 521Combined sources11
    Helixi524 – 526Combined sources3
    Helixi531 – 534Combined sources4
    Helixi542 – 547Combined sources6
    Beta strandi553 – 557Combined sources5
    Beta strandi562 – 565Combined sources4
    Beta strandi570 – 586Combined sources17
    Helixi589 – 591Combined sources3
    Helixi592 – 604Combined sources13
    Helixi613 – 621Combined sources9
    Helixi629 – 655Combined sources27
    Beta strandi661 – 663Combined sources3
    Helixi666 – 668Combined sources3
    Helixi671 – 673Combined sources3
    Beta strandi685 – 688Combined sources4
    Beta strandi693 – 695Combined sources3
    Helixi703 – 705Combined sources3
    Beta strandi711 – 713Combined sources3
    Beta strandi716 – 720Combined sources5
    Helixi724 – 743Combined sources20
    Helixi766 – 772Combined sources7
    Helixi779 – 784Combined sources6
    Beta strandi1620 – 1627Combined sources8
    Beta strandi1629 – 1632Combined sources4
    Beta strandi1635 – 1637Combined sources3
    Helixi1639 – 1641Combined sources3
    Helixi1645 – 1650Combined sources6
    Turni1656 – 1658Combined sources3

    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[»]
    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.
    OMAiCHEWYHG.
    PhylomeDBiP29375.
    TreeFamiTF106476.

    Family and domain databases

    Gene3Di3.30.40.10. 3 hits.
    InterProiView protein in InterPro
    IPR001606. ARID_dom.
    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

    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

    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

    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: September 27, 2017
    This is version 178 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. Human chromosome 12
      Human chromosome 12: 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