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P29375

- KDM5A_HUMAN

UniProt

P29375 - KDM5A_HUMAN

Protein

Lysine-specific demethylase 5A

Gene

KDM5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      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. May be involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12.5 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 fingeri1161 – 121858PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1607 – 166155PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. DNA binding Source: GDB
    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. sequence-specific DNA binding transcription factor activity Source: ProtInc
    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: UniProtKB
    4. transcription from RNA polymerase II promoter Source: ProtInc

    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, RBBP2, RBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9886. KDM5A.

    Subcellular locationi

    Nucleusnucleolus 2 Publications
    Note: Occupies promoters of genes involved in RNA metabolism and mitochondrial function.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34250.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16901690Lysine-specific demethylase 5APRO_0000200584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1111 – 11111Phosphoserine3 Publications
    Modified residuei1331 – 13311Phosphoserine1 Publication
    Modified residuei1598 – 15981Phosphoserine1 Publication
    Modified residuei1603 – 16031Phosphoserine1 Publication
    Modified residuei1666 – 16661Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29375.
    PaxDbiP29375.
    PRIDEiP29375.

    PTM databases

    PhosphoSiteiP29375.

    Expressioni

    Gene expression databases

    ArrayExpressiP29375.
    BgeeiP29375.
    CleanExiHS_JARID1A.
    HS_RBP2.
    GenevestigatoriP29375.

    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.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi111862. 21 interactions.
    DIPiDIP-472N.
    IntActiP29375. 3 interactions.
    STRINGi9606.ENSP00000382688.

    Structurei

    Secondary structure

    1
    1690
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 10117
    Helixi118 – 12811
    Helixi131 – 1366
    Helixi139 – 1468
    Helixi154 – 1629
    Turni163 – 1664
    Helixi167 – 1737
    Beta strandi1620 – 16278
    Beta strandi1629 – 16324
    Beta strandi1635 – 16373
    Helixi1639 – 16413
    Helixi1645 – 16506
    Turni1656 – 16583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JXJNMR-A85-175[»]
    2KGGNMR-A1609-1659[»]
    2KGINMR-A1609-1659[»]
    3GL6X-ray1.90A1609-1659[»]
    DisProtiDP00713.
    ProteinModelPortaliP29375.
    SMRiP29375. Positions 18-81, 84-175, 260-585, 1162-1221, 1608-1659.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29375.

    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
    Regioni1623 – 169068Interaction with LMO2Add
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1492 – 158796Lys-richAdd
    BLAST

    Domaini

    The GSGFP motif is required for the interaction with SUZ12.By similarity

    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 fingeri1161 – 121858PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1607 – 166155PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327026.
    HOGENOMiHOG000290719.
    KOiK11446.
    OMAiCVAHYRR.
    OrthoDBiEOG7D85VK.
    PhylomeDBiP29375.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK     50
    IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL 100
    QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP 150
    GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD 200
    TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG 250
    LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG 300
    RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE 350
    AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS 400
    IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL 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
    ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL 700
    YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL 750
    SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL 800
    LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL 850
    DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ 900
    ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT 950
    VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK 1000
    AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA 1050
    RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE 1100
    KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA 1150
    KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG 1200
    SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT 1250
    ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL 1300
    QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR 1350
    ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH 1400
    AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM 1450
    VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD 1500
    SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK 1550
    LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA 1600
    EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN 1650
    EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS 1690
    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 AAB28544.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAE06081.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1411 – 14111Q → QVFFGK in AAB28544. (PubMed:8414517)Curated
    Sequence conflicti1547 – 15471E → K in AAB28544. (PubMed:8414517)Curated
    Sequence conflicti1612 – 16143AQN → EPD in AAB28544. (PubMed:8414517)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti865 – 8651M → T.
    Corresponds to variant rs11062385 [ dbSNP | Ensembl ].
    VAR_032984
    Natural varianti1190 – 11901P → A.
    Corresponds to variant rs2229353 [ dbSNP | Ensembl ].
    VAR_032985

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1623 – 169068VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationVSP_035746Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.1. human. [P29375-1]

    Polymorphism databases

    DMDMi215274124.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS41736.1. [P29375-1 ]
    PIRi I78879.
    RefSeqi NP_001036068.1. NM_001042603.2. [P29375-1 ]
    UniGenei Hs.76272.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JXJ NMR - A 85-175 [» ]
    2KGG NMR - A 1609-1659 [» ]
    2KGI NMR - A 1609-1659 [» ]
    3GL6 X-ray 1.90 A 1609-1659 [» ]
    DisProti DP00713.
    ProteinModelPortali P29375.
    SMRi P29375. Positions 18-81, 84-175, 260-585, 1162-1221, 1608-1659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111862. 21 interactions.
    DIPi DIP-472N.
    IntActi P29375. 3 interactions.
    STRINGi 9606.ENSP00000382688.

    Chemistry

    ChEMBLi CHEMBL2424504.
    GuidetoPHARMACOLOGYi 2680.

    PTM databases

    PhosphoSitei P29375.

    Polymorphism databases

    DMDMi 215274124.

    Proteomic databases

    MaxQBi P29375.
    PaxDbi P29375.
    PRIDEi P29375.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399788 ; ENSP00000382688 ; ENSG00000073614 . [P29375-1 ]
    GeneIDi 5927.
    KEGGi hsa:5927.
    UCSCi uc001qif.1. human. [P29375-1 ]

    Organism-specific databases

    CTDi 5927.
    GeneCardsi GC12M000389.
    H-InvDB HIX0010308.
    HGNCi HGNC:9886. KDM5A.
    HPAi HPA006201.
    MIMi 180202. gene.
    neXtProti NX_P29375.
    PharmGKBi PA34250.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327026.
    HOGENOMi HOG000290719.
    KOi K11446.
    OMAi CVAHYRR.
    OrthoDBi EOG7D85VK.
    PhylomeDBi P29375.
    TreeFami TF106476.

    Miscellaneous databases

    ChiTaRSi KDM5A. human.
    EvolutionaryTracei P29375.
    GeneWikii JARID1A.
    GenomeRNAii 5927.
    NextBioi 23088.
    PROi P29375.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29375.
    Bgeei P29375.
    CleanExi HS_JARID1A.
    HS_RBP2.
    Genevestigatori P29375.

    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. "Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
      Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
      Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RB1.
    2. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 (ISOFORMS 1/2).
      Tissue: Eye and Testis.
    5. "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product."
      Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A., Hanobik M.G., Huber H.E., Oliff A.
      Nature 352:251-254(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1564.
    6. "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein."
      Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.
      Mol. Cell. Biol. 14:7256-7264(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1, SUBCELLULAR LOCATION.
    7. "T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2."
      Mao S., Neale G.A.M., Goorha R.M.
      Oncogene 14:1531-1539(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LMO2.
    8. "Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription."
      Chan S.W., Hong W.
      J. Biol. Chem. 276:28402-28412(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1.
    9. "Binding of pRB to the PHD protein RBP2 promotes cellular differentiation."
      Benevolenskaya E.V., Murray H.L., Branton P., Young R.A., Kaelin W.G. Jr.
      Mol. Cell 18:623-635(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RB1, FUNCTION.
    10. "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-1598 AND SER-1603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: FUNCTION.
    12. "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.
    13. "The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases."
      Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.
      Cell 128:1077-1088(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth."
      Secombe J., Li L., Carlos L., Eisenman R.N.
      Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYC AND MYCN.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111 AND SER-1331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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-1666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKDM5A_HUMAN
    AccessioniPrimary (citable) accession number: P29375
    Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 147 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 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

    External Data

    Dasty 3