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Q9UGL1

- KDM5B_HUMAN

UniProt

Q9UGL1 - KDM5B_HUMAN

Protein

Lysine-specific demethylase 5B

Gene

KDM5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      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. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.4 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: GDB
    2. histone demethylase activity (H3-dimethyl-K4 specific) Source: UniProtKB
    3. histone demethylase activity (H3-trimethyl-K4 specific) Source: UniProtKB
    4. 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
    5. protein binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. transcription corepressor activity Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3-K4 demethylation Source: UniProtKB
    2. histone H3-K4 demethylation, trimethyl-H3-K4-specific Source: GOC
    3. negative regulation of transcription, DNA-templated Source: GDB
    4. 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):
    Cancer/testis antigen 31
    Short name:
    CT31
    Histone demethylase JARID1B
    Jumonji/ARID domain-containing protein 1B
    PLU-1
    Retinoblastoma-binding protein 2 homolog 1
    Short name:
    RBP2-H1
    Gene namesi
    Name:KDM5B
    Synonyms:JARID1B, PLU1, RBBP2H1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18039. KDM5B.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: GDB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi335 – 3351H → A: Slightly impairs transcription repression ability. 1 Publication
    Mutagenesisi499 – 4991H → Y: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi1200 – 12001H → A: Impairs transcription repression ability and interaction with HDAC4. 1 Publication

    Organism-specific databases

    PharmGKBiPA164721626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15441544Lysine-specific demethylase 5BPRO_0000292412Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei832 – 8321N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UGL1.
    PaxDbiQ9UGL1.
    PRIDEiQ9UGL1.

    PTM databases

    PhosphoSiteiQ9UGL1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level).5 Publications

    Gene expression databases

    ArrayExpressiQ9UGL1.
    BgeeiQ9UGL1.
    CleanExiHS_JARID1B.
    GenevestigatoriQ9UGL1.

    Organism-specific databases

    HPAiHPA027179.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi115984. 64 interactions.
    DIPiDIP-53652N.
    IntActiQ9UGL1. 2 interactions.
    STRINGi9606.ENSP00000356234.

    Structurei

    Secondary structure

    1
    1544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1495 – 15006
    Beta strandi1502 – 15054
    Turni1506 – 15094
    Beta strandi1511 – 15144
    Helixi1515 – 15184
    Helixi1522 – 15265
    Helixi1533 – 15375

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MA5NMR-A1487-1544[»]
    DisProtiDP00712.
    ProteinModelPortaliQ9UGL1.
    SMRiQ9UGL1. Positions 31-208, 310-601, 1176-1227, 1486-1544.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1434 – 14396Poly-Lys

    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.

    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.
    HOGENOMiHOG000290719.
    InParanoidiQ9UGL1.
    KOiK11446.
    OMAiELMMEAQ.
    OrthoDBiEOG7D85VK.
    PhylomeDBiQ9UGL1.
    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: Q9UGL1-1) [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

    MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH     50
    KIRPIAEQTG ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK 100
    LNFLDQIAKY WELQGSTLKI PHVERKILDL FQLNKLVAEE GGFAVVCKDR 150
    KWTKIATKMG FAPGKAVGSH IRGHYERILN PYNLFLSGDS LRCLQKPNLT 200
    TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN IKIEPEETTE 250
    ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS 300
    KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD 350
    WRCPKCLAQE CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM 400
    VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKLSPE 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 QCVKCKTTCF 700
    MSAISCSCKP GLLVCLHHVK ELCSCPPYKY KLRYRYTLDD LYPMMNALKL 750
    RAESYNEWAL NVNEALEAKI NKKKSLVSFK ALIEESEMKK FPDNDLLRHL 800
    RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN ELRQFVTQLY 850
    ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF 900
    DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP 950
    YSAVEKAMAR LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI 1000
    PAYLPNGAAL KDSVQRARDW LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP 1050
    VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE NSPYSLLEVL CPRCDIGLLG 1100
    LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS AMATLGEARL 1150
    REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH 1200
    TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD 1250
    ALRYMIERTV NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD 1300
    TNKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGRSCIPLH GVSPEVNELL 1350
    MEAQLLQVSL PEIQELYQTL LAKPSPAQQT DRSSPVRPSS EKNDCCRGKR 1400
    DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL SHPKDMNNFK 1450
    LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 1500
    DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK 1544
    Length:1,544
    Mass (Da):175,658
    Last modified:May 18, 2010 - v3
    Checksum:i70A0738D9A709F61
    GO
    Isoform 2 (identifier: Q9UGL1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         237-237: E → ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASASQ

    Show »
    Length:1,580
    Mass (Da):179,409
    Checksum:i61B03B8A7EE16B3C
    GO

    Sequence cautioni

    The sequence CAB63108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781V → G in CAB63108. (PubMed:10878660)Curated
    Sequence conflicti585 – 5895AYHSG → VPQW in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti708 – 7081C → W in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti759 – 7591A → P in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti771 – 7711N → T in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti771 – 7711N → T in CAB63108. (PubMed:10878660)Curated
    Sequence conflicti1182 – 11821Q → R in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti1293 – 12931A → P in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti1307 – 13071P → L in AAD16061. (PubMed:10616211)Curated
    Sequence conflicti1331 – 13311S → ST in AAD16061. (PubMed:10616211)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei237 – 2371E → ERQSLAVLPRLECSGAILAH CNLRLLDSSNSSASASQ in isoform 2. 1 PublicationVSP_026408

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132440 mRNA. Translation: CAB43532.1.
    AF087481 mRNA. Translation: AAD16061.1.
    AJ243706 mRNA. Translation: CAB63108.1. Different initiation.
    AC098934 Genomic DNA. No translation available.
    AC104463 Genomic DNA. No translation available.
    CCDSiCCDS30974.1. [Q9UGL1-1]
    RefSeqiNP_006609.3. NM_006618.3. [Q9UGL1-1]
    UniGeneiHs.443650.

    Genome annotation databases

    EnsembliENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
    ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
    GeneIDi10765.
    KEGGihsa:10765.
    UCSCiuc001gyf.3. human. [Q9UGL1-1]
    uc009xag.3. human. [Q9UGL1-2]

    Polymorphism databases

    DMDMi296439317.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132440 mRNA. Translation: CAB43532.1 .
    AF087481 mRNA. Translation: AAD16061.1 .
    AJ243706 mRNA. Translation: CAB63108.1 . Different initiation.
    AC098934 Genomic DNA. No translation available.
    AC104463 Genomic DNA. No translation available.
    CCDSi CCDS30974.1. [Q9UGL1-1 ]
    RefSeqi NP_006609.3. NM_006618.3. [Q9UGL1-1 ]
    UniGenei Hs.443650.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MA5 NMR - A 1487-1544 [» ]
    DisProti DP00712.
    ProteinModelPortali Q9UGL1.
    SMRi Q9UGL1. Positions 31-208, 310-601, 1176-1227, 1486-1544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115984. 64 interactions.
    DIPi DIP-53652N.
    IntActi Q9UGL1. 2 interactions.
    STRINGi 9606.ENSP00000356234.

    Chemistry

    GuidetoPHARMACOLOGYi 2681.

    PTM databases

    PhosphoSitei Q9UGL1.

    Polymorphism databases

    DMDMi 296439317.

    Proteomic databases

    MaxQBi Q9UGL1.
    PaxDbi Q9UGL1.
    PRIDEi Q9UGL1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367264 ; ENSP00000356233 ; ENSG00000117139 . [Q9UGL1-2 ]
    ENST00000367265 ; ENSP00000356234 ; ENSG00000117139 . [Q9UGL1-1 ]
    GeneIDi 10765.
    KEGGi hsa:10765.
    UCSCi uc001gyf.3. human. [Q9UGL1-1 ]
    uc009xag.3. human. [Q9UGL1-2 ]

    Organism-specific databases

    CTDi 10765.
    GeneCardsi GC01M202696.
    H-InvDB HIX0001478.
    HGNCi HGNC:18039. KDM5B.
    HPAi HPA027179.
    MIMi 605393. gene.
    neXtProti NX_Q9UGL1.
    PharmGKBi PA164721626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327026.
    HOGENOMi HOG000290719.
    InParanoidi Q9UGL1.
    KOi K11446.
    OMAi ELMMEAQ.
    OrthoDBi EOG7D85VK.
    PhylomeDBi Q9UGL1.
    TreeFami TF106476.

    Miscellaneous databases

    ChiTaRSi KDM5B. human.
    GeneWikii JARID1B.
    GenomeRNAii 10765.
    NextBioi 40877.
    PROi Q9UGL1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UGL1.
    Bgeei Q9UGL1.
    CleanExi HS_JARID1B.
    Genevestigatori Q9UGL1.

    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. "A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer."
      Lu P.J., Sundquist K., Baeckstrom D., Poulsom R., Hanby A., Meier-Ewert S., Jones T., Mitchell M., Pitha-Rowe P., Freemont P., Taylor-Papadimitriou J.
      J. Biol. Chem. 274:15633-15645(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Mammary cancer.
    2. "Deficiency of a novel retinoblastoma binding protein 2-homolog is a consistent feature of sporadic human melanoma skin cancer."
      Vogt T., Kroiss M., McClelland M., Gruss C., Becker B., Bosserhoff A.K., Rumpler G., Bogenrieder T., Landthaler M., Stolz W.
      Lab. Invest. 79:1615-1627(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Teratocarcinoma.
    3. "Isolation and chromosomal localization of a new human retinoblastoma binding protein 2 homologue 1a (RBBP2H1A)."
      Kashuba V., Protopopov A., Podowski R., Gizatullin R., Li J., Klein G., Wahlestedt C., Zabarovsky E.
      Eur. J. Hum. Genet. 8:407-413(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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, SUBCELLULAR LOCATION.
    6. "Human PLU-1 has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9."
      Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J., Freemont P.S.
      J. Biol. Chem. 278:20507-20513(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FOXG1B AND PAX9.
    7. "Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas."
      Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T.
      Mod. Pathol. 18:1249-1257(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH RB1.
    8. "Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells."
      Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M., Vogt T.
      J. Invest. Dermatol. 126:1850-1859(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RB1.
    9. "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.
    10. "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.
    11. "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
      Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
      Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1; HDAC4; HDAC5 AND HDAC7, MUTAGENESIS OF HIS-335 AND HIS-1200.
    12. "PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation."
      Yamane K., Tateishi K., Klose R.J., Fang J., Fabrizio L.A., Erdjument-Bromage H., Taylor-Papadimitriou J., Tempst P., Zhang Y.
      Mol. Cell 25:801-812(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-499.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiKDM5B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UGL1
    Secondary accession number(s): O95811, Q15752, Q9Y3Q5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 108 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 1
      Human chromosome 1: 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