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Q3UXZ9

- KDM5A_MOUSE

UniProt

Q3UXZ9 - KDM5A_MOUSE

Protein

Lysine-specific demethylase 5A

Gene

Kdm5a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    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'. May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12.2 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi483 – 4831Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi486 – 4861Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi571 – 5711Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1153 – 121058PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1599 – 165355PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding Source: InterPro
    3. 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
    4. protein binding Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW
    3. positive regulation of transcription, DNA-templated Source: Ensembl
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    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:Kdm5a
    Synonyms:Jarid1a, Rbp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:2136980. Kdm5a.

    Subcellular locationi

    Nucleusnucleolus By similarity. Nucleus 1 PublicationPROSITE-ProRule annotation
    Note: Occupies promoters of genes involved in RNA metabolism and mitochondrial function.

    GO - Cellular componenti

    1. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are grossly normal, except that they exhibit behavioral abnormalities when held upside down by the tail, and slight hematological defects.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16901690Lysine-specific demethylase 5APRO_0000292411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1111 – 11111Phosphoserine1 Publication
    Modified residuei1331 – 13311PhosphoserineBy similarity
    Modified residuei1598 – 15981PhosphoserineBy similarity
    Modified residuei1603 – 16031PhosphoserineBy similarity
    Modified residuei1666 – 16661PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ3UXZ9.
    PRIDEiQ3UXZ9.

    PTM databases

    PhosphoSiteiQ3UXZ9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3UXZ9.
    BgeeiQ3UXZ9.
    CleanExiMM_RBP2.
    GenevestigatoriQ3UXZ9.

    Interactioni

    Subunit structurei

    Interacts with RB1, ESR1, MYC, MYCN and LMO2 By similarity. Interacts with SUZ12; the interaction is direct.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Suz12Q80U702EBI-2531441,EBI-2526494

    Protein-protein interaction databases

    BioGridi229572. 1 interaction.
    IntActiQ3UXZ9. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3UXZ9.
    SMRiQ3UXZ9. Positions 18-81, 84-175, 260-585, 1162-1221, 1608-1659.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 6042JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini84 – 17491ARIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini437 – 603167JmjCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1622 – 169069Interaction with LMO2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi419 – 4235GSGFP motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1484 – 157996Lys-richAdd
    BLAST

    Domaini

    The GSGFP motif is required for the interaction with SUZ12.1 Publication

    Sequence similaritiesi

    Belongs to the JARID1 histone demethylase family.Curated
    Contains 1 ARID domain.PROSITE-ProRule annotation
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 JmjN domain.PROSITE-ProRule annotation
    Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1153 – 121058PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1599 – 165355PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327026.
    GeneTreeiENSGT00530000063118.
    HOGENOMiHOG000290719.
    InParanoidiQ3UXZ9.
    KOiK11446.
    OMAiCVAHYRR.
    PhylomeDBiQ3UXZ9.
    TreeFamiTF106476.

    Family and domain databases

    Gene3Di1.10.150.60. 1 hit.
    3.30.40.10. 3 hits.
    InterProiIPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR013637. Lys_sp_deMease_like_dom.
    IPR003349. TF_JmjN.
    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.
    [Graphical view]
    PfamiPF01388. 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.
    [Graphical view]
    SMARTiSM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 3 hits.
    [Graphical view]
    SUPFAMiSSF46774. SSF46774. 1 hit.
    SSF57903. SSF57903. 3 hits.
    PROSITEiPS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3UXZ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK     50
    IRPPKDWQPP FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL 100
    QGSTLKIPVV ERKILDLYAL SKIVASKGGF EIVTKEKKWS KVGSRLGYLP 150
    GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPDLDLKE KVEAEVLSTD 200
    IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ IFGAGPKVVG 250
    LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 300
    RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE 350
    AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS 400
    IEEDVIVEYG ADISSKDFGS GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV 450
    LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP 500
    KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV 550
    PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN 600
    HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR 650
    ESVVQMGVVM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL 700
    YHPTDLCSCP MQNKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL 750
    SASFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCGSVAQL 800
    LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI SQTRQVKNLL 850
    DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 900
    ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT 950
    VSERWEEKAK VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK 1000
    AREWTAKVEA IQSGNNYAYL EQLESLSAKG RPIPVRLDAL PQVESQVAAA 1050
    RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKEIIEKE 1100
    KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA MHSLRAANLA 1150
    KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 1200
    SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT 1250
    ERAMSWQDKA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL 1300
    QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPHQTMDYDD EETDSDEDIR 1350
    ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH 1400
    AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM 1450
    VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD 1500
    SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK 1550
    LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA 1600
    EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN 1650
    EDYICINCAK KQGPDSPGQA PPPPFLMSYK LPMEDLKETS 1690
    Length:1,690
    Mass (Da):192,216
    Last modified:June 26, 2007 - v2
    Checksum:iEFCF56AAAA51F0FC
    GO

    Sequence cautioni

    The sequence BAE22414.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101A → S in BAE38548. (PubMed:16141072)Curated
    Sequence conflicti14 – 141V → R in BAE38548. (PubMed:16141072)Curated
    Sequence conflicti17 – 171P → A in BAE38548. (PubMed:16141072)Curated
    Sequence conflicti24 – 241P → A in BAE38548. (PubMed:16141072)Curated
    Sequence conflicti544 – 5441V → A in BAE38548. (PubMed:16141072)Curated
    Sequence conflicti1272 – 12721A → P in BAE22414. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC155720 Genomic DNA. No translation available.
    AC078896 Genomic DNA. No translation available.
    AK135085 mRNA. Translation: BAE22414.1. Different initiation.
    AK144877 mRNA. Translation: BAE26113.1.
    AK166055 mRNA. Translation: BAE38548.1.
    BC080691 mRNA. Translation: AAH80691.1. Different termination.
    CCDSiCCDS51889.1.
    RefSeqiNP_666109.2. NM_145997.2.
    UniGeneiMm.404761.
    Mm.463658.

    Genome annotation databases

    EnsembliENSMUST00000100996; ENSMUSP00000098558; ENSMUSG00000030180.
    GeneIDi214899.
    KEGGimmu:214899.
    UCSCiuc009dne.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC155720 Genomic DNA. No translation available.
    AC078896 Genomic DNA. No translation available.
    AK135085 mRNA. Translation: BAE22414.1 . Different initiation.
    AK144877 mRNA. Translation: BAE26113.1 .
    AK166055 mRNA. Translation: BAE38548.1 .
    BC080691 mRNA. Translation: AAH80691.1 . Different termination.
    CCDSi CCDS51889.1.
    RefSeqi NP_666109.2. NM_145997.2.
    UniGenei Mm.404761.
    Mm.463658.

    3D structure databases

    ProteinModelPortali Q3UXZ9.
    SMRi Q3UXZ9. Positions 18-81, 84-175, 260-585, 1162-1221, 1608-1659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229572. 1 interaction.
    IntActi Q3UXZ9. 1 interaction.

    PTM databases

    PhosphoSitei Q3UXZ9.

    Proteomic databases

    PaxDbi Q3UXZ9.
    PRIDEi Q3UXZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100996 ; ENSMUSP00000098558 ; ENSMUSG00000030180 .
    GeneIDi 214899.
    KEGGi mmu:214899.
    UCSCi uc009dne.2. mouse.

    Organism-specific databases

    CTDi 5927.
    MGIi MGI:2136980. Kdm5a.

    Phylogenomic databases

    eggNOGi NOG327026.
    GeneTreei ENSGT00530000063118.
    HOGENOMi HOG000290719.
    InParanoidi Q3UXZ9.
    KOi K11446.
    OMAi CVAHYRR.
    PhylomeDBi Q3UXZ9.
    TreeFami TF106476.

    Miscellaneous databases

    ChiTaRSi KDM5A. mouse.
    NextBioi 374501.
    PROi Q3UXZ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3UXZ9.
    Bgeei Q3UXZ9.
    CleanExi MM_RBP2.
    Genevestigatori Q3UXZ9.

    Family and domain databases

    Gene3Di 1.10.150.60. 1 hit.
    3.30.40.10. 3 hits.
    InterProi IPR001606. ARID/BRIGHT_DNA-bd.
    IPR003347. JmjC_dom.
    IPR013637. Lys_sp_deMease_like_dom.
    IPR003349. TF_JmjN.
    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.
    [Graphical view ]
    Pfami 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.
    [Graphical view ]
    SMARTi SM00501. BRIGHT. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00545. JmjN. 1 hit.
    SM00249. PHD. 3 hits.
    [Graphical view ]
    SUPFAMi SSF46774. SSF46774. 1 hit.
    SSF57903. SSF57903. 3 hits.
    PROSITEi PS51011. ARID. 1 hit.
    PS51184. JMJC. 1 hit.
    PS51183. JMJN. 1 hit.
    PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1552.
      Strain: C57BL/6J.
      Tissue: Lung and Olfactory bulb.
    3. "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] OF 1-1099.
      Strain: C57BL/6J.
      Tissue: Germ cell.
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1538-1546, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3."
      Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.
      Cell 128:1063-1076(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells."
      Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., Wysocka J.
      Cell 139:1290-1302(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, INTERACTION WITH SUZ12.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKDM5A_MOUSE
    AccessioniPrimary (citable) accession number: Q3UXZ9
    Secondary accession number(s): Q3TM94, Q3UMI5, Q66JZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3