Details for: KDM5B

Gene ID: 10765

Symbol: KDM5B

Ensembl ID: ENSG00000117139

Description: lysine demethylase 5B

Associated with

Other Information

Genular Protein ID: 4222444990

Symbol: KDM5B_HUMAN

Name: Lysine-specific demethylase 5B

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10336460

Title: A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer.

PubMed ID: 10336460

DOI: 10.1074/jbc.274.22.15633

PubMed ID: 10616211

Title: Deficiency of a novel retinoblastoma binding protein 2-homolog is a consistent feature of sporadic human melanoma skin cancer.

PubMed ID: 10616211

PubMed ID: 10878660

Title: Isolation and chromosomal localization of a new human retinoblastoma binding protein 2 homologue 1a (RBBP2H1A).

PubMed ID: 10878660

DOI: 10.1038/sj.ejhg.5200474

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 12237901

Title: PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?

PubMed ID: 12237901

DOI: 10.1002/ijc.10644

PubMed ID: 12657635

Title: Human PLU-1 has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9.

PubMed ID: 12657635

DOI: 10.1074/jbc.m301994200

PubMed ID: 15803180

Title: Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas.

PubMed ID: 15803180

DOI: 10.1038/modpathol.3800413

PubMed ID: 16645588

Title: Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells.

PubMed ID: 16645588

DOI: 10.1038/sj.jid.5700324

PubMed ID: 17320161

Title: RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3.

PubMed ID: 17320161

DOI: 10.1016/j.cell.2007.02.003

PubMed ID: 17311883

Title: The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth.

PubMed ID: 17311883

DOI: 10.1101/gad.1523007

PubMed ID: 17373667

Title: Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases.

PubMed ID: 17373667

DOI: 10.1002/ijc.22673

PubMed ID: 17363312

Title: PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation.

PubMed ID: 17363312

DOI: 10.1016/j.molcel.2007.03.001

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 26645689

Title: Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of Histone H3 Lysine 4 Demethylases.

PubMed ID: 26645689

DOI: 10.1074/jbc.m115.698449

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29276005

Title: Histone lysine methylases and demethylases in the landscape of human developmental disorders.

PubMed ID: 29276005

DOI: 10.1016/j.ajhg.2017.11.013

PubMed ID: 30409806

Title: Quantifying the contribution of recessive coding variation to developmental disorders.

PubMed ID: 30409806

DOI: 10.1126/science.aar6731

PubMed ID: 24952722

Title: The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B.

PubMed ID: 24952722

DOI: 10.1007/s13238-014-0078-4

PubMed ID: 26741168

Title: 8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent, Cell Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine Demethylase Inhibitors.

PubMed ID: 26741168

DOI: 10.1021/acs.jmedchem.5b01635

PubMed ID: 27214403

Title: Structural analysis of human KDM5B guides histone demethylase inhibitor development.

PubMed ID: 27214403

DOI: 10.1038/nchembio.2087

PubMed ID: 28262558

Title: Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma Cells.

PubMed ID: 28262558

DOI: 10.1016/j.chembiol.2017.02.006

Sequence Information:

  • Length: 1544
  • Mass: 175658
  • Checksum: 70A0738D9A709F61
  • Sequence:
  • MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 
    ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 
    PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 
    PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN 
    IKIEPEETTE ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS 
    KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD WRCPKCLAQE 
    CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED 
    VTVEYGADIA SKEFGSGFPV RDGKIKLSPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC 
    GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE 
    LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV 
    NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE 
    DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF MSAISCSCKP GLLVCLHHVK 
    ELCSCPPYKY KLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK 
    ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN 
    ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF 
    DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP YSAVEKAMAR 
    LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI PAYLPNGAAL KDSVQRARDW 
    LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE 
    NSPYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS 
    AMATLGEARL REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH 
    TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV 
    NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD TNKVSQPPGT TSFSLPDDWD 
    NRTSYLHSPF STGRSCIPLH GVSPEVNELL MEAQLLQVSL PEIQELYQTL LAKPSPAQQT 
    DRSSPVRPSS EKNDCCRGKR DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL 
    SHPKDMNNFK LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 
    DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK

Genular Protein ID: 3939173459

Symbol: A0A3B3ITA8_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.O114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 1499
  • Mass: 170426
  • Checksum: 921292E99B1C1C23
  • Sequence:
  • MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 
    ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 
    PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 
    PYNLFLSGDS LRAMNIKIEP EETTEARTHN LRRRMGCPTP KCENEKEMKS SIKQEPIERK 
    DYIVENEKEK PKSRSKKATN AVDLYVCLLC GSGNDEDRLL LCDGCDDSYH TFCLIPPLHD 
    VPKGDWRCPK CLAQECSKPQ EAFGFEQAAR DYTLRTFGEM ADAFKSDYFN MPVHMVPTEL 
    VEKEFWRLVS TIEEDVTVEY GADIASKEFG SGFPVRDGKI KLSPEEEEYL DSGWNLNNMP 
    VMEQSVLAHI TADICGMKLP WLYVGMCFSS FCWHIEDHWS YSINYLHWGE PKTWYGVPGY 
    AAEQLENVMK KLAPELFVSQ PDLLHQLVTI MNPNTLMTHE VPVYRTNQCA GEFVITFPRA 
    YHSGFNQGFN FAEAVNFCTV DWLPLGRQCV EHYRLLHRYC VFSHDEMICK MASKADVLDV 
    VVASTVQKDM AIMIEDEKAL RETVRKLGVI DSERMDFELL PDDERQCVKC KTTCFMSAIS 
    CSCKPGLLVC LHHVKELCSC PPYKYKLRYR YTLDDLYPMM NALKLRAESY NEWALNVNEA 
    LEAKINKKKS LVSFKALIEE SEMKKFPDND LLRHLRLVTQ DAEKCASVAQ QLLNGKRQTR 
    YRSGGGKSQN QLTVNELRQF VTQLYALPCV LSQTPLLKDL LNRVEDFQQH SQKLLSEETP 
    SAAELQDLLD VSFEFDVELP QLAEMRIRLE QARWLEEVQQ ACLDPSSLTL DDMRRLIDLG 
    VGLAPYSAVE KAMARLQELL TVSEHWDDKA KSLLKARPRH SLNSLATAVK EIEEIPAYLP 
    NGAALKDSVQ RARDWLQDVE GLQAGGRVPV LDTLIELVTR GRSIPVHLNS LPRLETLVAE 
    VQAWKECAVN TFLTENSPYS LLEVLCPRCD IGLLGLKRKQ RKLKEPLPNG KKKSTKLESL 
    SDLERALTES KETASAMATL GEARLREMEA LQSLRLANEG KLLSPLQDVD IKICLCQKAP 
    AAPMIQCELC RDAFHTSCVA VPSISQGLRI WLCPHCRRSE KPPLEKILPL LASLQRIRVR 
    LPEGDALRYM IERTVNWQHR AQQLLSSGNL KFVQDRVGSG LLYSRWQASA GQVSDTNKVS 
    QPPGTTSFSL PDDWDNRTSY LHSPFSTGRS CIPLHGVSPE VNELLMEAQL LQVSLPEIQE 
    LYQTLLAKPS PAQQTDRSSP VRPSSEKNDC CRGKRDGINS LERKLKRRLE REGLSSERWE 
    RVKKMRTPKK KKIKLSHPKD MNNFKLERER SYELVRSAET HSLPSDTSYS EQEDSEDEDA 
    ICPAVSCLQP EGDEVDWVQC DGSCNQWFHQ VCVGVSPEMA EKEDYICVRC TVKDAPSRK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.