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Q8NHM5

- KDM2B_HUMAN

UniProt

Q8NHM5 - KDM2B_HUMAN

Protein

Lysine-specific demethylase 2B

Gene

KDM2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.2 Publications

    Catalytic activityi

    Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
    Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei239 – 2391SubstrateBy similarity
    Metal bindingi242 – 2421Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi244 – 2441Iron; catalyticPROSITE-ProRule annotation
    Binding sitei259 – 2591SubstrateBy similarity
    Metal bindingi314 – 3141Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri606 – 65247CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri659 – 72567PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. histone demethylase activity Source: BHF-UCL
    3. histone demethylase activity (H3-K36 specific) Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. rRNA binding Source: UniProtKB-KW
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. embryonic camera-type eye morphogenesis Source: BHF-UCL
    2. forebrain development Source: BHF-UCL
    3. fourth ventricle development Source: BHF-UCL
    4. hindbrain development Source: BHF-UCL
    5. histone demethylation Source: GOC
    6. histone H2A monoubiquitination Source: UniProtKB
    7. initiation of neural tube closure Source: BHF-UCL
    8. lateral ventricle development Source: BHF-UCL
    9. midbrain development Source: BHF-UCL
    10. midbrain-hindbrain boundary morphogenesis Source: BHF-UCL
    11. negative regulation of neural precursor cell proliferation Source: BHF-UCL
    12. negative regulation of neuron apoptotic process Source: BHF-UCL
    13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. spermatogenesis Source: BHF-UCL
    15. third ventricle development Source: BHF-UCL
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Iron, Metal-binding, RNA-binding, rRNA-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ8NHM5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 2B (EC:1.14.11.27)
    Alternative name(s):
    CXXC-type zinc finger protein 2
    F-box and leucine-rich repeat protein 10
    F-box protein FBL10
    F-box/LRR-repeat protein 10
    JmjC domain-containing histone demethylation protein 1B
    Jumonji domain-containing EMSY-interactor methyltransferase motif protein
    Short name:
    Protein JEMMA
    Protein-containing CXXC domain 2
    [Histone-H3]-lysine-36 demethylase 1B
    Gene namesi
    Name:KDM2B
    Synonyms:CXXC2, FBL10, FBXL10, JHDM1B, PCCX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13610. KDM2B.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164721242.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13361336Lysine-specific demethylase 2BPRO_0000119853Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei474 – 4741Phosphoserine1 Publication
    Modified residuei477 – 4771Phosphoserine1 Publication
    Modified residuei493 – 4931Phosphothreonine2 Publications
    Modified residuei497 – 4971Phosphoserine1 Publication
    Modified residuei975 – 9751Phosphoserine1 Publication
    Modified residuei979 – 9791Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8NHM5.
    PaxDbiQ8NHM5.
    PRIDEiQ8NHM5.

    PTM databases

    PhosphoSiteiQ8NHM5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8NHM5.
    BgeeiQ8NHM5.
    CleanExiHS_FBXL10.
    GenevestigatoriQ8NHM5.

    Interactioni

    Subunit structurei

    Directly interacts with SKP1 and CUL1.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCORQ6W2J92EBI-3955564,EBI-950027

    Protein-protein interaction databases

    BioGridi124197. 19 interactions.
    IntActiQ8NHM5. 3 interactions.
    STRINGi9606.ENSP00000366271.

    Structurei

    Secondary structure

    1
    1336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi617 – 6204
    Helixi628 – 6325
    Helixi634 – 6363
    Helixi647 – 6493
    Turni663 – 6653
    Helixi671 – 6733
    Helixi677 – 6826
    Beta strandi686 – 6883
    Turni689 – 6913
    Helixi697 – 6993
    Beta strandi711 – 7133
    Beta strandi716 – 7183
    Turni720 – 7223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4O64X-ray2.13A/B/C607-723[»]
    ProteinModelPortaliQ8NHM5.
    SMRiQ8NHM5. Positions 66-392, 508-573, 609-722, 1068-1333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 346169JmjCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1059 – 110547F-boxAdd
    BLAST
    Repeati1093 – 112028LRR 1Add
    BLAST
    Repeati1133 – 115422LRR 2Add
    BLAST
    Repeati1156 – 118227LRR 3Add
    BLAST
    Repeati1222 – 124726LRR 4Add
    BLAST
    Repeati1248 – 127730LRR 5Add
    BLAST
    Repeati1278 – 130225LRR 6Add
    BLAST
    Repeati1303 – 133634LRR 7Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili943 – 97129Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi409 – 43022Glu-richAdd
    BLAST
    Compositional biasi1014 – 105643Pro-richAdd
    BLAST

    Domaini

    The JmjC domain mediates demethylation activity By similarity. It is also required for repression of ribosomal RNA genes.By similarity

    Sequence similaritiesi

    Belongs to the JHDM1 histone demethylase family.Curated
    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 F-box domain.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 7 LRR (leucine-rich) repeats.Curated
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri606 – 65247CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri659 – 72567PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Leucine-rich repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290496.
    HOGENOMiHOG000007396.
    InParanoidiQ8NHM5.
    KOiK10276.
    OMAiNAEDRMA.
    OrthoDBiEOG78SQH0.
    PhylomeDBiQ8NHM5.
    TreeFamiTF106480.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    IPR003347. JmjC_dom.
    IPR002857. Znf_CXXC.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    [Graphical view]
    PfamiPF00646. F-box. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NHM5-1) [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

    MAGPQMGGSA EDHPPRKRHA AEKQKKKTVI YTKCFEFESA TQRPIDRQRY     50
    DENEDLSDVE EIVSVRGFSL EEKLRSQLYQ GDFVHAMEGK DFNYEYVQRE 100
    ALRVPLIFRE KDGLGIKMPD PDFTVRDVKL LVGSRRLVDV MDVNTQKGTE 150
    MSMSQFVRYY ETPEAQRDKL YNVISLEFSH TKLEHLVKRP TVVDLVDWVD 200
    NMWPQHLKEK QTEATNAIAE MKYPKVKKYC LMSVKGCFTD FHIDFGGTSV 250
    WYHVFRGGKI FWLIPPTLHN LALYEEWVLS GKQSDIFLGD RVERCQRIEL 300
    KQGYTFFIPS GWIHAVYTPV DSLVFGGNIL HSFNVPMQLR IYEIEDRTRV 350
    QPKFRYPFYY EMCWYVLERY VYCVTQRSHL TQEYQRESML IDAPRKPSID 400
    GFSSDSWLEM EEEACDQQPQ EEEEKDEEGE GRDRAPKPPT DGSTSPTSTP 450
    SEDQEALGKK PKAPALRFLK RTLSNESEES VKSTTLAVDY PKTPTGSPAT 500
    EVSAKWTHLT EFELKGLKAL VEKLESLPEN KKCVPEGIED PQALLEGVKN 550
    VLKEHADDDP SLAITGVPVV TWPKKTPKNR AVGRPKGKLG PASAVKLAAN 600
    RTTAGARRRR TRCRKCEACL RTECGECHFC KDMKKFGGPG RMKQSCIMRQ 650
    CIAPVLPHTA VCLVCGEAGK EDTVEEEEGK FNLMLMECSI CNEIIHPGCL 700
    KIKESEGVVN DELPNCWECP KCNHAGKTGK QKRGPGFKYA SNLPGSLLKE 750
    QKMNRDNKEG QEPAKRRSEC EEAPRRRSDE HSKKVPPDGL LRRKSDDVHL 800
    RKKRKYEKPQ ELSGRKRASS LQTSPGSSSH LSPRPPLGSS LSPWWRSSLT 850
    YFQQQLKPGK EDKLFRKKRR SWKNAEDRMA LANKPLRRFK QEPEDELPEA 900
    PPKTRESDHS RSSSPTAGPS TEGAEGPEEK KKVKMRRKRR LPNKELSREL 950
    SKELNHEIQR TENSLANENQ QPIKSEPESE GEEPKRPPGI CERPHRFSKG 1000
    LNGTPRELRH QLGPSLRSPP RVISRPPPSV SPPKCIQMER HVIRPPPISP 1050
    PPDSLPLDDG AAHVMHREVW MAVFSYLSHQ DLCVCMRVCR TWNRWCCDKR 1100
    LWTRIDLNHC KSITPLMLSG IIRRQPVSLD LSWTNISKKQ LSWLINRLPG 1150
    LRDLVLSGCS WIAVSALCSS SCPLLRTLDV QWVEGLKDAQ MRDLLSPPTD 1200
    NRPGQMDNRS KLRNIVELRL AGLDITDASL RLIIRHMPLL SKLHLSYCNH 1250
    VTDQSINLLT AVGTTTRDSL TEINLSDCNK VTDQCLSFFK RCGNICHIDL 1300
    RYCKQVTKEG CEQFIAEMSV SVQFGQVEEK LLQKLS 1336
    Length:1,336
    Mass (Da):152,615
    Last modified:October 1, 2002 - v1
    Checksum:i3A1A17B8EA9EA953
    GO
    Isoform 2 (identifier: Q8NHM5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         730-730: K → KAYK
         1277-1336: DCNKVTDQCL...VEEKLLQKLS → ASLLGRVFGLQFWGICEPQARKNAGWA

    Show »
    Length:1,306
    Mass (Da):149,034
    Checksum:i3329D5375AD25930
    GO
    Isoform 3 (identifier: Q8NHM5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         856-868: LKPGKEDKLFRKK → Q
         1204-1204: G → GPG

    Note: No experimental confirmation available.

    Show »
    Length:1,326
    Mass (Da):151,328
    Checksum:iBCBDAE3F675E017C
    GO
    Isoform 4 (identifier: Q8NHM5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ → MEAEKDSGRRL
         818-855: Missing.
         1320-1336: VSVQFGQVEEKLLQKLS → SFQGRSCSTTRLGDE

    Note: No experimental confirmation available.

    Show »
    Length:1,265
    Mass (Da):144,769
    Checksum:i69C8C16EFDE3541C
    GO

    Sequence cautioni

    The sequence AAH08735.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55112.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55301.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC11159.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti864 – 8641L → F in BAC11159. 1 PublicationCurated
    Sequence conflicti1226 – 12261T → R in BAC11159. 1 PublicationCurated
    Sequence conflicti1295 – 12951I → T in BAC11159. 1 PublicationCurated
    Sequence conflicti1334 – 13341K → R in BAC11159. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242MAGPQ…ESATQ → MEAEKDSGRRL in isoform 4. 1 PublicationVSP_043146Add
    BLAST
    Alternative sequencei730 – 7301K → KAYK in isoform 2. 1 PublicationVSP_011340
    Alternative sequencei818 – 85538Missing in isoform 4. 1 PublicationVSP_043147Add
    BLAST
    Alternative sequencei856 – 86813LKPGK…LFRKK → Q in isoform 3. 1 PublicationVSP_017475Add
    BLAST
    Alternative sequencei1204 – 12041G → GPG in isoform 3. 1 PublicationVSP_017476
    Alternative sequencei1277 – 133660DCNKV…LQKLS → ASLLGRVFGLQFWGICEPQA RKNAGWA in isoform 2. 1 PublicationVSP_011341Add
    BLAST
    Alternative sequencei1320 – 133617VSVQF…LQKLS → SFQGRSCSTTRLGDE in isoform 4. 1 PublicationVSP_043148Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ459424 mRNA. Translation: CAD30700.1.
    AK027440 mRNA. Translation: BAB55112.1. Different initiation.
    AK027692 mRNA. Translation: BAB55301.1. Different initiation.
    AK074718 mRNA. Translation: BAC11159.1. Different initiation.
    AK127328 mRNA. Translation: BAG54483.1.
    AC048337 Genomic DNA. No translation available.
    AC073650 Genomic DNA. No translation available.
    AC145422 Genomic DNA. No translation available.
    AL133572 mRNA. Translation: CAB63721.2.
    AB031230 mRNA. Translation: BAA97672.1.
    BC008735 mRNA. Translation: AAH08735.2. Different initiation.
    CCDSiCCDS41849.1. [Q8NHM5-4]
    CCDS41850.1. [Q8NHM5-1]
    PIRiT43477.
    RefSeqiNP_001005366.1. NM_001005366.1. [Q8NHM5-4]
    NP_115979.3. NM_032590.4. [Q8NHM5-1]
    UniGeneiHs.524800.

    Genome annotation databases

    EnsembliENST00000377069; ENSP00000366269; ENSG00000089094. [Q8NHM5-4]
    ENST00000377071; ENSP00000366271; ENSG00000089094. [Q8NHM5-1]
    ENST00000542973; ENSP00000437821; ENSG00000089094.
    GeneIDi84678.
    KEGGihsa:84678.
    UCSCiuc001uaq.3. human. [Q8NHM5-1]
    uc001uas.3. human. [Q8NHM5-4]

    Polymorphism databases

    DMDMi51316032.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ459424 mRNA. Translation: CAD30700.1 .
    AK027440 mRNA. Translation: BAB55112.1 . Different initiation.
    AK027692 mRNA. Translation: BAB55301.1 . Different initiation.
    AK074718 mRNA. Translation: BAC11159.1 . Different initiation.
    AK127328 mRNA. Translation: BAG54483.1 .
    AC048337 Genomic DNA. No translation available.
    AC073650 Genomic DNA. No translation available.
    AC145422 Genomic DNA. No translation available.
    AL133572 mRNA. Translation: CAB63721.2 .
    AB031230 mRNA. Translation: BAA97672.1 .
    BC008735 mRNA. Translation: AAH08735.2 . Different initiation.
    CCDSi CCDS41849.1. [Q8NHM5-4 ]
    CCDS41850.1. [Q8NHM5-1 ]
    PIRi T43477.
    RefSeqi NP_001005366.1. NM_001005366.1. [Q8NHM5-4 ]
    NP_115979.3. NM_032590.4. [Q8NHM5-1 ]
    UniGenei Hs.524800.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4O64 X-ray 2.13 A/B/C 607-723 [» ]
    ProteinModelPortali Q8NHM5.
    SMRi Q8NHM5. Positions 66-392, 508-573, 609-722, 1068-1333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124197. 19 interactions.
    IntActi Q8NHM5. 3 interactions.
    STRINGi 9606.ENSP00000366271.

    PTM databases

    PhosphoSitei Q8NHM5.

    Polymorphism databases

    DMDMi 51316032.

    Proteomic databases

    MaxQBi Q8NHM5.
    PaxDbi Q8NHM5.
    PRIDEi Q8NHM5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377069 ; ENSP00000366269 ; ENSG00000089094 . [Q8NHM5-4 ]
    ENST00000377071 ; ENSP00000366271 ; ENSG00000089094 . [Q8NHM5-1 ]
    ENST00000542973 ; ENSP00000437821 ; ENSG00000089094 .
    GeneIDi 84678.
    KEGGi hsa:84678.
    UCSCi uc001uaq.3. human. [Q8NHM5-1 ]
    uc001uas.3. human. [Q8NHM5-4 ]

    Organism-specific databases

    CTDi 84678.
    GeneCardsi GC12M121866.
    HGNCi HGNC:13610. KDM2B.
    MIMi 609078. gene.
    neXtProti NX_Q8NHM5.
    PharmGKBi PA164721242.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290496.
    HOGENOMi HOG000007396.
    InParanoidi Q8NHM5.
    KOi K10276.
    OMAi NAEDRMA.
    OrthoDBi EOG78SQH0.
    PhylomeDBi Q8NHM5.
    TreeFami TF106480.

    Enzyme and pathway databases

    SignaLinki Q8NHM5.

    Miscellaneous databases

    ChiTaRSi KDM2B. human.
    GenomeRNAii 84678.
    NextBioi 74711.
    PROi Q8NHM5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NHM5.
    Bgeei Q8NHM5.
    CleanExi HS_FBXL10.
    Genevestigatori Q8NHM5.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    IPR003347. JmjC_dom.
    IPR002857. Znf_CXXC.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    [Graphical view ]
    Pfami PF00646. F-box. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS51058. ZF_CXXC. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "JEMMA (Jumonji domain, EMSY-interactor, methyltransferase motif) is a novel protein which interacts with EMSY."
      Hughes-Davies L.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
      Tissue: Hippocampus.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
      Tissue: Testis.
    5. Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 480-1336 (ISOFORM 2).
      Tissue: Fibroblast.
    6. "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 710-1336 (ISOFORM 1).
      Tissue: Brain.
    7. "Histone demethylation by a family of JmjC domain-containing proteins."
      Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
      Nature 439:811-816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY.
    8. "JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes."
      Frescas D., Guardavaccaro D., Bassermann F., Koyama-Nasu R., Pagano M.
      Nature 450:309-313(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 THR-493; SER-975 AND SER-979, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-474; SER-477; THR-493 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKDM2B_HUMAN
    AccessioniPrimary (citable) accession number: Q8NHM5
    Secondary accession number(s): A8MRS1
    , Q8NCI2, Q96HC7, Q96SL0, Q96T03, Q9NS96, Q9UF75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3