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Q80Y84

- KDM5B_MOUSE

UniProt

Q80Y84 - KDM5B_MOUSE

Protein

Lysine-specific demethylase 5B

Gene

Kdm5b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9.2 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi499 – 4991Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi502 – 5021Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi587 – 5871Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri309 – 35951PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1176 – 122449PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1484 – 153855PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. histone demethylase activity (H3-dimethyl-K4 specific) Source: UniProtKB
    3. histone demethylase activity (H3-K4 specific) Source: MGI
    4. histone demethylase activity (H3-trimethyl-K4 specific) Source: UniProtKB
    5. 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
    6. protein binding Source: IntAct
    7. transcription corepressor activity Source: Ensembl
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3-K4 demethylation Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: Ensembl
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 5B (EC:1.14.11.-)
    Alternative name(s):
    Histone demethylase JARID1B
    Jumonji/ARID domain-containing protein 1B
    PLU-1
    Gene namesi
    Name:Kdm5b
    Synonyms:Jarid1b, Kiaa4034, Plu1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1922855. Kdm5b.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi499 – 4991H → A: Abolishes enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15441544Lysine-specific demethylase 5BPRO_0000292413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei832 – 8321N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ80Y84.
    PaxDbiQ80Y84.
    PRIDEiQ80Y84.

    PTM databases

    PhosphoSiteiQ80Y84.

    Expressioni

    Tissue specificityi

    Present at highest levels in testis, where it is enriched in spermatogonia and pachytene cells (at protein level).3 Publications

    Developmental stagei

    Expressed in developing brain, mammary bud, thymus, teeth, whisker follicle, intervertebral disks, olfactory epithelium, eye, stomach and limbs.1 Publication

    Gene expression databases

    ArrayExpressiQ80Y84.
    BgeeiQ80Y84.
    GenevestigatoriQ80Y84.

    Interactioni

    Subunit structurei

    Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Morf4l1P607624EBI-1249551,EBI-2943018

    Protein-protein interaction databases

    BioGridi217610. 3 interactions.
    IntActiQ80Y84. 4 interactions.

    Structurei

    Secondary structure

    1
    1544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi97 – 11418
    Beta strandi122 – 1276
    Helixi130 – 14011
    Helixi143 – 1486
    Turni149 – 1513
    Helixi152 – 1587
    Beta strandi163 – 1653
    Helixi166 – 17712
    Helixi179 – 1879

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EQYNMR-A94-208[»]
    DisProtiDP00711.
    ProteinModelPortaliQ80Y84.
    SMRiQ80Y84. Positions 31-208, 310-601, 1177-1227, 1486-1544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ80Y84.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 7342JmjNPROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 18791ARIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 619167JmjCPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Both the JmjC domain and the JmjN domain are required for enzymatic activity.
    The 2 first PHD-type zinc finger domains are required for transcription repression activity.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 fingeri309 – 35951PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1176 – 122449PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1484 – 153855PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327026.
    GeneTreeiENSGT00530000063118.
    HOGENOMiHOG000290719.
    InParanoidiQ80Y84.
    KOiK11446.
    OMAiPHSSVER.
    OrthoDBiEOG7D85VK.
    PhylomeDBiQ80Y84.
    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. 3 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: Q80Y84-1) [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

    MEPATTLPPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH     50
    KIRPIAEQTG ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK 100
    LNFLDQIAKY WELQGSTLKI PHVERKILDL FQLNKLVAEE GGFAVVCKDR 150
    KWTKIATKMG FAPGKAVGSH IRGHYERILN PYNLFLSGDS LRCLQKPNLT 200
    SDTKDKEYKP HDIPQRQSVQ PAETCPPARR AKRMRAEAMN IKIEPEEATE 250
    ARTHNLRRRM GCTTPKWENE KEMKSTIKQE PTEKKDCELE SEKEKPKSRA 300
    KKTATAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLV PPLHDVPKGD 350
    WRCPKCLAQE CNKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM 400
    VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKISPE 450
    EEEYLDSGWN LNNMPVMEQS VLAHITADIC GMKLPWLYVG MCFSSFCWHI 500
    EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE LFVSQPDLLH 550
    QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV 600
    NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST 650
    VQKDMAIMIE DEKALRETVR KLGVIDSERM DFELLPDDER QCIKCKTTCF 700
    MSAISCSCKP GLLVCLHHVK ELCSCPPYKY NLRYRYTLDD LYPMMNALKL 750
    RAESYNEWAL NVNEALEAKI NKKKSLVSFK ALIEESEMKK FPDNDLLRHL 800
    RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN ELRQFVTQLY 850
    ALPCVLSQTP LLKDLLNRVE DFQQQSQKLL SEEMPSAAEL QELLDVSFEF 900
    DVELPQLTEM RIRLEQARWL EEVQQACLDS SSLSLDDMRR LIDLGVGLAP 950
    YSAVEKAMAR LQELLTVSEH WDDKAKSLLR ARPRHSLSSL ATAVKEMEEI 1000
    PAYLPNGTVL KDSVQRARDW VQDVDALQAG GRVPVLETLI ELVARGRSIP 1050
    VHLNSLPRLE MLVAEVHAWK ECAAKTFLPE NSTYSLLEVL CPRCDIGLLG 1100
    LKRKQRKLKE PLPSGKKRST KLESLSDLER ALMESKETAA AMATLGEARL 1150
    REMEALQSLR FANEEKLLSP VQDLEMKVCL CQKTPATPMI QCELCRDAFH 1200
    TSCVAAPSIS QSSRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD 1250
    ALRYMIERTV NWQHRAQQLL SSGNLKLVQD QVGSGLLSSR WPASAGQASA 1300
    TDKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGQSCLPLH GLSPEVNELL 1350
    MEAQLLQVSL PEIQELYQTL LTKPSSVQQA DRSSPVRSSS EKNDCLRGKR 1400
    DAINSPERKL KRRPEREGLP SERWDRVKHM RTPQKKKIKL SHPKDMDSFK 1450
    LERERSYDLV RNAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 1500
    DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTGKDA PSRK 1544
    Length:1,544
    Mass (Da):175,555
    Last modified:June 1, 2003 - v1
    Checksum:iD83E2691C65DCB31
    GO
    Isoform 2 (identifier: Q80Y84-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1501-1544: DWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAPSRK → SEVWAIEDALSPNSETL

    Note: No experimental confirmation available.

    Show »
    Length:1,517
    Mass (Da):172,410
    Checksum:i37772163EC76CDB2
    GO

    Sequence cautioni

    The sequence BAD90482.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281P → S in BAD90482. 1 PublicationCurated
    Sequence conflicti139 – 1391E → Q in BAC30898. (PubMed:16141072)Curated
    Sequence conflicti761 – 7611N → Y in AAL92848. (PubMed:14516692)Curated
    Sequence conflicti761 – 7611N → Y in AAL92849. (PubMed:14516692)Curated
    Sequence conflicti1428 – 14281K → R in AAL92848. (PubMed:14516692)Curated
    Sequence conflicti1428 – 14281K → R in AAL92849. (PubMed:14516692)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1501 – 154444DWVQC…APSRK → SEVWAIEDALSPNSETL in isoform 2. 1 PublicationVSP_026409Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY082429 mRNA. Translation: AAL92848.1.
    AY082430 mRNA. Translation: AAL92849.1.
    AK220451 mRNA. Translation: BAD90482.1. Different initiation.
    BC048180 mRNA. Translation: AAH48180.1.
    BC057318 mRNA. Translation: AAH57318.1.
    AK041304 mRNA. Translation: BAC30898.1.
    CCDSiCCDS35716.1. [Q80Y84-1]
    RefSeqiNP_690855.2. NM_152895.2. [Q80Y84-1]
    UniGeneiMm.28995.
    Mm.391994.

    Genome annotation databases

    EnsembliENSMUST00000047714; ENSMUSP00000038138; ENSMUSG00000042207. [Q80Y84-1]
    ENSMUST00000112198; ENSMUSP00000107817; ENSMUSG00000042207. [Q80Y84-2]
    GeneIDi75605.
    KEGGimmu:75605.
    UCSCiuc007csg.2. mouse. [Q80Y84-2]
    uc011wsg.1. mouse. [Q80Y84-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY082429 mRNA. Translation: AAL92848.1 .
    AY082430 mRNA. Translation: AAL92849.1 .
    AK220451 mRNA. Translation: BAD90482.1 . Different initiation.
    BC048180 mRNA. Translation: AAH48180.1 .
    BC057318 mRNA. Translation: AAH57318.1 .
    AK041304 mRNA. Translation: BAC30898.1 .
    CCDSi CCDS35716.1. [Q80Y84-1 ]
    RefSeqi NP_690855.2. NM_152895.2. [Q80Y84-1 ]
    UniGenei Mm.28995.
    Mm.391994.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EQY NMR - A 94-208 [» ]
    DisProti DP00711.
    ProteinModelPortali Q80Y84.
    SMRi Q80Y84. Positions 31-208, 310-601, 1177-1227, 1486-1544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 217610. 3 interactions.
    IntActi Q80Y84. 4 interactions.

    PTM databases

    PhosphoSitei Q80Y84.

    Proteomic databases

    MaxQBi Q80Y84.
    PaxDbi Q80Y84.
    PRIDEi Q80Y84.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047714 ; ENSMUSP00000038138 ; ENSMUSG00000042207 . [Q80Y84-1 ]
    ENSMUST00000112198 ; ENSMUSP00000107817 ; ENSMUSG00000042207 . [Q80Y84-2 ]
    GeneIDi 75605.
    KEGGi mmu:75605.
    UCSCi uc007csg.2. mouse. [Q80Y84-2 ]
    uc011wsg.1. mouse. [Q80Y84-1 ]

    Organism-specific databases

    CTDi 10765.
    MGIi MGI:1922855. Kdm5b.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG327026.
    GeneTreei ENSGT00530000063118.
    HOGENOMi HOG000290719.
    InParanoidi Q80Y84.
    KOi K11446.
    OMAi PHSSVER.
    OrthoDBi EOG7D85VK.
    PhylomeDBi Q80Y84.
    TreeFami TF106476.

    Miscellaneous databases

    EvolutionaryTracei Q80Y84.
    NextBioi 343484.
    PROi Q80Y84.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80Y84.
    Bgeei Q80Y84.
    Genevestigatori Q80Y84.

    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. 3 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. "Characterisation and developmental expression of mouse Plu-1, a homologue of a human nuclear protein (PLU-1) which is specifically up-regulated in breast cancer."
      Madsen B., Spencer-Dene B., Poulsom R., Hall D., Lu P.J., Scott K., Shaw A.T., Burchell J.M., Freemont P., Taylor-Papadimitriou J.
      Mech. Dev. 119:S239-S246(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: BALB/c.
      Tissue: Testis.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "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 1-1433.
      Strain: C57BL/6J.
      Tissue: Aorta.
    5. "PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?"
      Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G., Burchell J., Taylor-Papadimitriou J.
      Int. J. Cancer 101:581-588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "PLU-1, a transcriptional repressor and putative testis-cancer antigen, has a specific expression and localisation pattern during meiosis."
      Madsen B., Tarsounas M., Burchell J.M., Hall D., Poulsom R., Taylor-Papadimitriou J.
      Chromosoma 112:124-132(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. "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.
    8. "Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins."
      Seward D.J., Cubberley G., Kim S., Schonewald M., Zhang L., Tripet B., Bentley D.L.
      Nat. Struct. Mol. Biol. 14:240-242(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-499.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKDM5B_MOUSE
    AccessioniPrimary (citable) accession number: Q80Y84
    Secondary accession number(s): Q5DTR9, Q8BLU1, Q8JZL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3