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Lysine-specific demethylase 5B (EC 1.14.11.-) (Cancer/testis antigen 31) (CT31) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) (Retinoblastoma-binding protein 2 homolog 1) (RBP2-H1)

 KDM5B_HUMAN             Reviewed;        1544 AA.
Q9UGL1; O95811; Q15752; Q9Y3Q5;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
23-MAY-2018, entry version 149.
RecName: Full=Lysine-specific demethylase 5B;
EC=1.14.11.-;
AltName: Full=Cancer/testis antigen 31;
Short=CT31;
AltName: Full=Histone demethylase JARID1B;
AltName: Full=Jumonji/ARID domain-containing protein 1B;
AltName: Full=PLU-1;
AltName: Full=Retinoblastoma-binding protein 2 homolog 1;
Short=RBP2-H1;
Name=KDM5B; Synonyms=JARID1B, PLU1, RBBP2H1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Mammary cancer;
PubMed=10336460; DOI=10.1074/jbc.274.22.15633;
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.;
"A novel gene (PLU-1) containing highly conserved putative
DNA/chromatin binding motifs is specifically up-regulated in breast
cancer.";
J. Biol. Chem. 274:15633-15645(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Teratocarcinoma;
PubMed=10616211;
Vogt T., Kroiss M., McClelland M., Gruss C., Becker B.,
Bosserhoff A.K., Rumpler G., Bogenrieder T., Landthaler M., Stolz W.;
"Deficiency of a novel retinoblastoma binding protein 2-homolog is a
consistent feature of sporadic human melanoma skin cancer.";
Lab. Invest. 79:1615-1627(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=10878660; DOI=10.1038/sj.ejhg.5200474;
Kashuba V., Protopopov A., Podowski R., Gizatullin R., Li J.,
Klein G., Wahlestedt C., Zabarovsky E.;
"Isolation and chromosomal localization of a new human retinoblastoma
binding protein 2 homologue 1a (RBBP2H1A).";
Eur. J. Hum. Genet. 8:407-413(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12237901; DOI=10.1002/ijc.10644;
Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G.,
Burchell J., Taylor-Papadimitriou J.;
"PLU-1 nuclear protein, which is upregulated in breast cancer, shows
restricted expression in normal human adult tissues: a new
cancer/testis antigen?";
Int. J. Cancer 101:581-588(2002).
[6]
FUNCTION, AND INTERACTION WITH FOXG1B AND PAX9.
PubMed=12657635; DOI=10.1074/jbc.M301994200;
Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J.,
Freemont P.S.;
"Human PLU-1 has transcriptional repression properties and interacts
with the developmental transcription factors BF-1 and PAX9.";
J. Biol. Chem. 278:20507-20513(2003).
[7]
TISSUE SPECIFICITY, AND INTERACTION WITH RB1.
PubMed=15803180; DOI=10.1038/modpathol.3800413;
Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M.,
Vogt T.;
"Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding
protein downregulated in malignant melanomas.";
Mod. Pathol. 18:1249-1257(2005).
[8]
FUNCTION, AND INTERACTION WITH RB1.
PubMed=16645588; DOI=10.1038/sj.jid.5700324;
Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M.,
Vogt T.;
"Re-expression of the retinoblastoma-binding protein 2-homolog 1
reveals tumor-suppressive functions in highly metastatic melanoma
cells.";
J. Invest. Dermatol. 126:1850-1859(2006).
[9]
FUNCTION.
PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S.,
Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
"RBP2 belongs to a family of demethylases, specific for tri-and
dimethylated lysine 4 on histone 3.";
Cell 128:1063-1076(2007).
[10]
INTERACTION WITH MYC AND MYCN.
PubMed=17311883; DOI=10.1101/gad.1523007;
Secombe J., Li L., Carlos L., Eisenman R.N.;
"The Trithorax group protein Lid is a trimethyl histone H3K4
demethylase required for dMyc-induced cell growth.";
Genes Dev. 21:537-551(2007).
[11]
INTERACTION WITH HDAC1; HDAC4; HDAC5 AND HDAC7, AND MUTAGENESIS OF
HIS-335 AND HIS-1200.
PubMed=17373667; DOI=10.1002/ijc.22673;
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.;
"Breast cancer associated transcriptional repressor PLU-1/JARID1B
interacts directly with histone deacetylases.";
Int. J. Cancer 121:265-275(2007).
[12]
FUNCTION, AND MUTAGENESIS OF HIS-499.
PubMed=17363312; DOI=10.1016/j.molcel.2007.03.001;
Yamane K., Tateishi K., Klose R.J., Fang J., Fabrizio L.A.,
Erdjument-Bromage H., Taylor-Papadimitriou J., Tempst P., Zhang Y.;
"PLU-1 is an H3K4 demethylase involved in transcriptional repression
and breast cancer cell proliferation.";
Mol. Cell 25:801-812(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986; SER-1328 AND
SER-1456, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-242 AND LYS-278, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-242; LYS-278 AND LYS-769,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"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.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[17]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=26645689; DOI=10.1074/jbc.M115.698449;
Horton J.R., Engstrom A., Zoeller E.L., Liu X., Shanks J.R., Zhang X.,
Johns M.A., Vertino P.M., Fu H., Cheng X.;
"Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family
of Histone H3 Lysine 4 Demethylases.";
J. Biol. Chem. 291:2631-2646(2016).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-204; LYS-209;
LYS-242; LYS-274; LYS-278; LYS-769 AND LYS-1450, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
STRUCTURE BY NMR OF 306-360 IN COMPLEX WITH ZINC AND HISTONE H3,
FUNCTION, INTERACTION WITH HISTONE H3, AND MUTAGENESIS OF ASP-308;
LEU-309; TYR-310; VAL-311; GLU-321; ASP-322; LEU-324; LEU-325;
LEU-326; ASP-328; ASP-332; SER-333; TYR-334; ASP-345 AND TRP-351.
PubMed=24952722; DOI=10.1007/s13238-014-0078-4;
Zhang Y., Yang H., Guo X., Rong N., Song Y., Xu Y., Lan W., Zhang X.,
Liu M., Xu Y., Cao C.;
"The PHD1 finger of KDM5B recognizes unmodified H3K4 during the
demethylation of histone H3K4me2/3 by KDM5B.";
Protein Cell 5:837-850(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 26-101 AND 374-772 IN
COMPLEX WITH ZINC; MANGANESE AND AN INHIBITOR, FUNCTION, AND ENZYME
REGULATION.
PubMed=26741168; DOI=10.1021/ACS.JMEDCHEM.5B01635;
Bavetsias V., Lanigan R.M., Ruda G.F., Atrash B., McLaughlin M.G.,
Tumber A., Mok N.Y., Le Bihan Y.V., Dempster S., Boxall K.J.,
Jeganathan F., Hatch S.B., Savitsky P., Velupillai S., Krojer T.,
England K.S., Sejberg J., Thai C., Donovan A., Pal A., Scozzafava G.,
Bennett J.M., Kawamura A., Johansson C., Szykowska A., Gileadi C.,
Burgess-Brown N.A., von Delft F., Oppermann U., Walters Z.,
Shipley J., Raynaud F.I., Westaway S.M., Prinjha R.K., Fedorov O.,
Burke R., Schofield C.J., Westwood I.M., Bountra C., Muller S.,
van Montfort R.L., Brennan P.E., Blagg J.;
"8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent,
Cell Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine
Demethylase Inhibitors.";
J. Med. Chem. 59:1388-1409(2016).
[21]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 26-101 AND 374-772 IN
COMPLEX WITH SEVERAL INHIBITORS; ZINC AND MANGANESE, DOMAIN, FUNCTION,
AND ENZYME REGULATION.
PubMed=27214403; DOI=10.1038/NCHEMBIO.2087;
Johansson C., Velupillai S., Tumber A., Szykowska A., Hookway E.S.,
Nowak R.P., Strain-Damerell C., Gileadi C., Philpott M.,
Burgess-Brown N., Wu N., Kopec J., Nuzzi A., Steuber H., Egner U.,
Badock V., Munro S., LaThangue N.B., Westaway S., Brown J.,
Athanasou N., Prinjha R., Brennan P.E., Oppermann U.;
"Structural analysis of human KDM5B guides histone demethylase
inhibitor development.";
Nat. Chem. Biol. 12:539-545(2016).
[22]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-100 AND 374-772 IN
COMPLEX WITH INHIBITOR KDOAM-25; ZINC AND MANGANESE, FUNCTION, ENZYME
REGULATION, AND MUTAGENESIS OF 499-HIS--GLU-501.
PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S.,
Johansson C., Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N.,
Bountra C., Strain-Damerell C., Burgess-Brown N.A., Ruda G.F.,
Fedorov O., Munro S., England K.S., Nowak R.P., Schofield C.J.,
La Thangue N.B., Pawlyn C., Davies F., Morgan G., Athanasou N.,
Muller S., Oppermann U., Brennan P.E.;
"Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
Cells.";
Cell Chem. Biol. 24:371-380(2017).
-!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone
H3, thereby playing a central role in histone code
(PubMed:24952722, PubMed:27214403, PubMed:28262558). 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 (PubMed:24952722). In
contrast, may act as a tumor suppressor for melanoma. Represses
the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional
activation of the core clock component PER2 (By similarity).
{ECO:0000250|UniProtKB:Q80Y84, ECO:0000269|PubMed:12657635,
ECO:0000269|PubMed:16645588, ECO:0000269|PubMed:17320161,
ECO:0000269|PubMed:17363312, ECO:0000269|PubMed:24952722,
ECO:0000269|PubMed:26645689, ECO:0000269|PubMed:26741168,
ECO:0000269|PubMed:27214403, ECO:0000269|PubMed:28262558}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Several specific inhibitors are being developed
and tested (PubMed:27214403, PubMed:26741168). The inhibitor
KDOAM-25 inhibits its demethylase activity, resulting to cell
cycle arrest in myeloma cells (PubMed:28262558).
{ECO:0000269|PubMed:26741168, ECO:0000269|PubMed:27214403,
ECO:0000269|PubMed:28262558}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9 uM for 2-oxoglutarate {ECO:0000269|PubMed:26645689};
KM=4 uM for histone H3K4me3 {ECO:0000269|PubMed:26645689};
Note=Kcat are 1.9 min(-1) and 2.0 min(-1) for 2-oxoglutarate and
histone H3K4me3, respectively. {ECO:0000269|PubMed:26645689};
-!- SUBUNIT: Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts
with HDAC1, HDAC4, HDAC5 and HDAC7. Interacts (via PHD-type 1 zinc
finger) with histone H3 unmodified at 'Lys-4'; the interaction is
inhibited when histone H3 is methylated at 'Arg-2' or 'Lys-4'
(PubMed:24952722). {ECO:0000269|PubMed:12657635,
ECO:0000269|PubMed:15803180, ECO:0000269|PubMed:16645588,
ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17373667,
ECO:0000269|PubMed:24952722}.
-!- INTERACTION:
P49711:CTCF; NbExp=8; IntAct=EBI-2514978, EBI-932887;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537,
ECO:0000269|PubMed:10336460, ECO:0000269|PubMed:12237901}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UGL1-1; Sequence=Displayed;
Name=2;
IsoId=Q9UGL1-2; Sequence=VSP_026408;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
testis. Down-regulated in melanoma and glioblastoma. Up-regulated
in breast cancer (at protein level). {ECO:0000269|PubMed:10336460,
ECO:0000269|PubMed:10616211, ECO:0000269|PubMed:10878660,
ECO:0000269|PubMed:12237901, ECO:0000269|PubMed:15803180}.
-!- DOMAIN: Both the JmjC domain and the JmjN domain are required for
enzymatic activity. However ARID and PHD-type 1 domain are not
required for activity per se but contributed to recognition of the
H3(1-21)K4me2 substrate peptide. {ECO:0000269|PubMed:27214403}.
-!- DOMAIN: The 2 first PHD-type zinc finger domains are required for
transcription repression activity.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB63108.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ132440; CAB43532.1; -; mRNA.
EMBL; AF087481; AAD16061.1; -; mRNA.
EMBL; AJ243706; CAB63108.1; ALT_INIT; mRNA.
EMBL; AC098934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS30974.1; -. [Q9UGL1-1]
CCDS; CCDS81417.1; -. [Q9UGL1-2]
RefSeq; NP_001300971.1; NM_001314042.1. [Q9UGL1-2]
RefSeq; NP_006609.3; NM_006618.4. [Q9UGL1-1]
UniGene; Hs.18891; -.
UniGene; Hs.443650; -.
PDB; 2MA5; NMR; -; A=1487-1544.
PDB; 2MNY; NMR; -; A=306-360.
PDB; 2MNZ; NMR; -; A=306-360.
PDB; 5A1F; X-ray; 2.10 A; A=26-770.
PDB; 5A3N; X-ray; 2.00 A; A=26-101, A=374-772.
PDB; 5A3P; X-ray; 2.01 A; A=26-101, A=374-770.
PDB; 5A3T; X-ray; 1.90 A; A=26-101, A=374-772.
PDB; 5A3W; X-ray; 2.00 A; A=26-101, A=374-772.
PDB; 5FPL; X-ray; 2.35 A; A=26-101, A=374-772.
PDB; 5FPU; X-ray; 2.24 A; A=26-101, A=374-772.
PDB; 5FUN; X-ray; 2.30 A; A=26-101, A=374-772.
PDB; 5FUP; X-ray; 2.15 A; A=26-101, A=374-770.
PDB; 5FV3; X-ray; 2.37 A; A=26-101, A=374-770.
PDB; 5FY4; X-ray; 2.10 A; A=26-101, A=374-770.
PDB; 5FY5; X-ray; 2.47 A; A=26-101, A=374-770.
PDB; 5FY9; X-ray; 2.03 A; A=26-101, A=374-770.
PDB; 5FYB; X-ray; 1.87 A; A=26-101, A=374-770.
PDB; 5FYS; X-ray; 1.89 A; A=26-101, A=374-770.
PDB; 5FYT; X-ray; 1.87 A; A=26-101, A=374-770.
PDB; 5FYU; X-ray; 2.06 A; A=26-101, A=374-770.
PDB; 5FYV; X-ray; 1.87 A; A=26-101, A=374-770.
PDB; 5FYY; X-ray; 2.18 A; A=26-101, A=374-770.
PDB; 5FYZ; X-ray; 1.75 A; A=26-101, A=374-770.
PDB; 5FZ0; X-ray; 2.42 A; A=26-101, A=374-770.
PDB; 5FZ1; X-ray; 2.39 A; A=26-101, A=374-770.
PDB; 5FZ3; X-ray; 2.50 A; A=26-101, A=374-770.
PDB; 5FZ4; X-ray; 2.07 A; A=26-101, A=374-770.
PDB; 5FZ6; X-ray; 2.33 A; A=26-101, A=374-770.
PDB; 5FZ7; X-ray; 2.30 A; A=26-101, A=374-770.
PDB; 5FZ8; X-ray; 1.86 A; A=26-101, A=374-770.
PDB; 5FZ9; X-ray; 2.06 A; A=26-101, A=374-770.
PDB; 5FZA; X-ray; 2.10 A; A=26-101, A=374-770.
PDB; 5FZB; X-ray; 2.18 A; A=26-101, A=374-770.
PDB; 5FZC; X-ray; 2.05 A; A=26-101, A=374-770.
PDB; 5FZD; X-ray; 2.05 A; A=26-101, A=374-770.
PDB; 5FZE; X-ray; 2.02 A; A=26-101, A=374-770.
PDB; 5FZF; X-ray; 1.97 A; A=26-101, A=374-770.
PDB; 5FZG; X-ray; 1.96 A; A=26-101, A=374-770.
PDB; 5FZH; X-ray; 2.09 A; A=26-101, A=374-442, A=444-770.
PDB; 5FZI; X-ray; 1.95 A; A=26-101, A=374-770.
PDB; 5FZK; X-ray; 2.05 A; A=26-101, A=374-770.
PDB; 5FZL; X-ray; 2.55 A; A=26-101, A=374-770.
PDB; 5FZM; X-ray; 2.49 A; A=26-101, A=376-770.
PDB; 5LW9; X-ray; 2.30 A; A=26-99, A=374-772.
PDB; 5LWB; X-ray; 2.39 A; A=26-101, A=374-772.
PDB; 6EK6; X-ray; 2.05 A; A=347-754.
PDBsum; 2MA5; -.
PDBsum; 2MNY; -.
PDBsum; 2MNZ; -.
PDBsum; 5A1F; -.
PDBsum; 5A3N; -.
PDBsum; 5A3P; -.
PDBsum; 5A3T; -.
PDBsum; 5A3W; -.
PDBsum; 5FPL; -.
PDBsum; 5FPU; -.
PDBsum; 5FUN; -.
PDBsum; 5FUP; -.
PDBsum; 5FV3; -.
PDBsum; 5FY4; -.
PDBsum; 5FY5; -.
PDBsum; 5FY9; -.
PDBsum; 5FYB; -.
PDBsum; 5FYS; -.
PDBsum; 5FYT; -.
PDBsum; 5FYU; -.
PDBsum; 5FYV; -.
PDBsum; 5FYY; -.
PDBsum; 5FYZ; -.
PDBsum; 5FZ0; -.
PDBsum; 5FZ1; -.
PDBsum; 5FZ3; -.
PDBsum; 5FZ4; -.
PDBsum; 5FZ6; -.
PDBsum; 5FZ7; -.
PDBsum; 5FZ8; -.
PDBsum; 5FZ9; -.
PDBsum; 5FZA; -.
PDBsum; 5FZB; -.
PDBsum; 5FZC; -.
PDBsum; 5FZD; -.
PDBsum; 5FZE; -.
PDBsum; 5FZF; -.
PDBsum; 5FZG; -.
PDBsum; 5FZH; -.
PDBsum; 5FZI; -.
PDBsum; 5FZK; -.
PDBsum; 5FZL; -.
PDBsum; 5FZM; -.
PDBsum; 5LW9; -.
PDBsum; 5LWB; -.
PDBsum; 6EK6; -.
DisProt; DP00712; -.
ProteinModelPortal; Q9UGL1; -.
SMR; Q9UGL1; -.
BioGrid; 115984; 64.
CORUM; Q9UGL1; -.
DIP; DIP-53652N; -.
IntAct; Q9UGL1; 4.
STRING; 9606.ENSP00000356234; -.
BindingDB; Q9UGL1; -.
ChEMBL; CHEMBL3774295; -.
GuidetoPHARMACOLOGY; 2681; -.
iPTMnet; Q9UGL1; -.
PhosphoSitePlus; Q9UGL1; -.
BioMuta; KDM5B; -.
DMDM; 296439317; -.
EPD; Q9UGL1; -.
PaxDb; Q9UGL1; -.
PeptideAtlas; Q9UGL1; -.
PRIDE; Q9UGL1; -.
Ensembl; ENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
Ensembl; ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
GeneID; 10765; -.
KEGG; hsa:10765; -.
UCSC; uc001gyf.4; human. [Q9UGL1-1]
CTD; 10765; -.
DisGeNET; 10765; -.
EuPathDB; HostDB:ENSG00000117139.16; -.
GeneCards; KDM5B; -.
H-InvDB; HIX0001478; -.
HGNC; HGNC:18039; KDM5B.
HPA; CAB068193; -.
HPA; HPA027179; -.
HPA; HPA053723; -.
MalaCards; KDM5B; -.
MIM; 605393; gene.
neXtProt; NX_Q9UGL1; -.
OpenTargets; ENSG00000117139; -.
PharmGKB; PA164721626; -.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00530000063118; -.
HOGENOM; HOG000290719; -.
InParanoid; Q9UGL1; -.
KO; K11446; -.
OMA; CKTTCFM; -.
OrthoDB; EOG091G0RFR; -.
PhylomeDB; Q9UGL1; -.
TreeFam; TF106476; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
SIGNOR; Q9UGL1; -.
ChiTaRS; KDM5B; human.
GeneWiki; JARID1B; -.
GenomeRNAi; 10765; -.
PRO; PR:Q9UGL1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117139; -.
CleanEx; HS_JARID1B; -.
ExpressionAtlas; Q9UGL1; baseline and differential.
Genevisible; Q9UGL1; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:GDB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); IDA:UniProtKB.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IDA:CACAO.
GO; GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IMP:CAFA.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:GDB.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:2000864; P:regulation of estradiol secretion; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007338; P:single fertilization; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR003349; JmjN.
InterPro; IPR013637; Lys_sp_deMease-like_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR004198; Znf_C5HC2.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01388; ARID; 1.
Pfam; PF02373; JmjC; 1.
Pfam; PF02375; JmjN; 1.
Pfam; PF00628; PHD; 3.
Pfam; PF08429; PLU-1; 1.
Pfam; PF02928; zf-C5HC2; 1.
SMART; SM00501; BRIGHT; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00545; JmjN; 1.
SMART; SM00249; PHD; 3.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF57903; SSF57903; 3.
PROSITE; PS51011; ARID; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51183; JMJN; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Chromatin regulator; Complete proteome; Dioxygenase; Iron;
Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1544 Lysine-specific demethylase 5B.
/FTId=PRO_0000292412.
DOMAIN 32 73 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 97 187 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 453 619 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 309 359 PHD-type 1. {ECO:0000244|PDB:2MNY,
ECO:0000269|PubMed:24952722}.
ZN_FING 692 744 C5HC2. {ECO:0000269|PubMed:26741168,
ECO:0000269|PubMed:27214403,
ECO:0000269|PubMed:28262558}.
ZN_FING 1176 1224 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1484 1538 PHD-type 3. {ECO:0000244|PDB:2MA5}.
COMPBIAS 1434 1439 Poly-Lys.
METAL 499 499 Iron; catalytic.
{ECO:0000305|PubMed:26741168,
ECO:0000305|PubMed:27214403,
ECO:0000305|PubMed:28262558}.
METAL 501 501 Iron; catalytic.
{ECO:0000305|PubMed:26741168,
ECO:0000305|PubMed:27214403,
ECO:0000305|PubMed:28262558}.
METAL 587 587 Iron; catalytic.
{ECO:0000305|PubMed:26741168,
ECO:0000305|PubMed:27214403,
ECO:0000305|PubMed:28262558}.
BINDING 425 425 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 507 507 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 509 509 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
BINDING 517 517 2-oxoglutarate.
{ECO:0000250|UniProtKB:P29375}.
MOD_RES 832 832 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q80Y84}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1456 1456 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 148 148 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 204 204 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 209 209 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 242 242 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 769 769 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1450 1450 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 237 237 E -> ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASAS
Q (in isoform 2).
{ECO:0000303|PubMed:10616211}.
/FTId=VSP_026408.
MUTAGEN 308 308 D->A: Slightly decreases interaction with
histone H3. Decreases by 21% demethylase
activity and repression of tumor
suppressor genes expression.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 309 309 L->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 310 310 Y->A: Slightly decreases interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 310 310 Y->F: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 311 311 V->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 321 321 E->A: Decreases interaction with histone
H3. {ECO:0000269|PubMed:24952722}.
MUTAGEN 322 322 D->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 324 324 L->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 325 325 L->A: Abolishes interaction with histone
H3. Decreases by 44% demethylase activity
and repression of tumor suppressor genes
expression; when associated with A-328.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 326 326 L->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 328 328 D->A: Almost abolishes interaction with
histone H3. Decreases by 44% demethylase
activity and repression of tumor
suppressor genes expression; when
associated with A-325.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 332 332 D->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 333 333 S->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 334 334 Y->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 335 335 H->A: Slightly impairs transcription
repression ability.
{ECO:0000269|PubMed:17373667}.
MUTAGEN 345 345 D->A: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 351 351 W->A: Abolishes interaction with histone
H3. Decreases by 28% demethylase activity
and repression of tumor suppressor genes
expression.
{ECO:0000269|PubMed:24952722}.
MUTAGEN 499 501 HIE->AIA: Abolishes lysine-specific
histone demethylase activity.
{ECO:0000269|PubMed:28262558}.
MUTAGEN 499 499 H->Y: Abolishes lysine-specific histone
demethylase activity.
{ECO:0000269|PubMed:17363312}.
MUTAGEN 1200 1200 H->A: Impairs transcription repression
ability and interaction with HDAC4.
{ECO:0000269|PubMed:17373667}.
CONFLICT 78 78 V -> G (in Ref. 3; CAB63108).
{ECO:0000305}.
CONFLICT 585 589 AYHSG -> VPQW (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 708 708 C -> W (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 759 759 A -> P (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 771 771 N -> T (in Ref. 2; AAD16061 and 3;
CAB63108). {ECO:0000305}.
CONFLICT 1182 1182 Q -> R (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 1293 1293 A -> P (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 1307 1307 P -> L (in Ref. 2; AAD16061).
{ECO:0000305}.
CONFLICT 1331 1331 S -> ST (in Ref. 2; AAD16061).
{ECO:0000305}.
HELIX 39 42 {ECO:0000244|PDB:5FYZ}.
HELIX 45 56 {ECO:0000244|PDB:5FYZ}.
TURN 57 59 {ECO:0000244|PDB:5FYZ}.
STRAND 60 64 {ECO:0000244|PDB:5FYZ}.
TURN 78 80 {ECO:0000244|PDB:5FYZ}.
STRAND 86 89 {ECO:0000244|PDB:5FYZ}.
STRAND 96 98 {ECO:0000244|PDB:5FYS}.
STRAND 308 310 {ECO:0000244|PDB:2MNY}.
STRAND 313 315 {ECO:0000244|PDB:2MNZ}.
HELIX 319 323 {ECO:0000244|PDB:2MNY}.
STRAND 324 326 {ECO:0000244|PDB:2MNY}.
STRAND 328 331 {ECO:0000244|PDB:2MNY}.
STRAND 333 335 {ECO:0000244|PDB:2MNY}.
TURN 336 339 {ECO:0000244|PDB:2MNY}.
TURN 358 360 {ECO:0000244|PDB:6EK6}.
STRAND 363 366 {ECO:0000244|PDB:6EK6}.
HELIX 379 394 {ECO:0000244|PDB:5FYZ}.
HELIX 398 400 {ECO:0000244|PDB:5FYZ}.
HELIX 403 415 {ECO:0000244|PDB:5FYZ}.
STRAND 422 429 {ECO:0000244|PDB:5FYZ}.
STRAND 432 434 {ECO:0000244|PDB:5FYT}.
STRAND 443 445 {ECO:0000244|PDB:5A3N}.
HELIX 449 454 {ECO:0000244|PDB:5FYZ}.
STRAND 458 460 {ECO:0000244|PDB:5FZ7}.
TURN 461 466 {ECO:0000244|PDB:5FYZ}.
STRAND 467 469 {ECO:0000244|PDB:5A3P}.
HELIX 472 474 {ECO:0000244|PDB:5FYZ}.
HELIX 480 483 {ECO:0000244|PDB:5FYZ}.
STRAND 486 490 {ECO:0000244|PDB:5FYZ}.
STRAND 495 499 {ECO:0000244|PDB:5FYZ}.
HELIX 502 504 {ECO:0000244|PDB:5FYZ}.
STRAND 506 515 {ECO:0000244|PDB:5FYZ}.
STRAND 517 521 {ECO:0000244|PDB:5FYZ}.
HELIX 524 526 {ECO:0000244|PDB:5FYZ}.
HELIX 527 537 {ECO:0000244|PDB:5FYZ}.
HELIX 539 542 {ECO:0000244|PDB:5FYZ}.
HELIX 548 550 {ECO:0000244|PDB:5FYZ}.
STRAND 552 554 {ECO:0000244|PDB:5FZG}.
HELIX 558 563 {ECO:0000244|PDB:5FYZ}.
STRAND 569 573 {ECO:0000244|PDB:5FYZ}.
STRAND 578 581 {ECO:0000244|PDB:5FYZ}.
STRAND 587 602 {ECO:0000244|PDB:5FYZ}.
HELIX 605 607 {ECO:0000244|PDB:5FYZ}.
HELIX 608 621 {ECO:0000244|PDB:5FYZ}.
HELIX 629 637 {ECO:0000244|PDB:5FYZ}.
HELIX 638 642 {ECO:0000244|PDB:5FYZ}.
HELIX 645 671 {ECO:0000244|PDB:5FYZ}.
STRAND 676 679 {ECO:0000244|PDB:5FYZ}.
HELIX 682 684 {ECO:0000244|PDB:5FYZ}.
HELIX 687 689 {ECO:0000244|PDB:5FYZ}.
STRAND 690 692 {ECO:0000244|PDB:5FYZ}.
TURN 693 695 {ECO:0000244|PDB:5FYZ}.
STRAND 701 706 {ECO:0000244|PDB:5FYZ}.
HELIX 719 721 {ECO:0000244|PDB:5FYZ}.
HELIX 727 729 {ECO:0000244|PDB:5FYZ}.
STRAND 730 735 {ECO:0000244|PDB:5FYZ}.
HELIX 738 752 {ECO:0000244|PDB:5FYZ}.
STRAND 1495 1500 {ECO:0000244|PDB:2MA5}.
STRAND 1502 1505 {ECO:0000244|PDB:2MA5}.
TURN 1506 1509 {ECO:0000244|PDB:2MA5}.
STRAND 1511 1514 {ECO:0000244|PDB:2MA5}.
HELIX 1515 1518 {ECO:0000244|PDB:2MA5}.
HELIX 1522 1526 {ECO:0000244|PDB:2MA5}.
HELIX 1533 1537 {ECO:0000244|PDB:2MA5}.
SEQUENCE 1544 AA; 175658 MW; 70A0738D9A709F61 CRC64;
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


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E1916b ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,Lysy 96T
U1916h CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6 96T
E1916h ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,KIA 96T
E1916h ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 96T
E1916b ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6 96T
U1916b CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
27-137 JMJD5 is a histone lysine demethylase. Studies of a similar protein in mouse indicate a potential role for this protein as a tumor suppressor.JMJD5 is a putative histone lysine demethylase that contai 0.05 mg
U1916m CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxyl 96T
E1916c ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
U1916c CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,L 96T
E1916m ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxy 96T
U1916b CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,Lysyl 96T
U1916m CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hyd 96T
E1916m ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hy 96T
E1916c ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing prote 96T
U1916c CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protei 96T
JMJD1C JHDM1D Gene jumonji C domain containing histone demethylase 1 homolog D (S. cerevisiae)
E1916r ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD 96T
U1916r CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
E1916r ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
U1916r CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD6 96T
18-003-43413 JmjC domain-containing histone demethylation protein 1A - EC 1.14.11.27; [Histone-H3]-lysine-36 demethylase 1A; F-box_LRR-repeat protein 11; F-box and leucine-rich repeat protein 11; F-box protein FBL 0.05 mg Aff Pur
CSB-EL011946MO Mouse jumonji C domain containing histone demethylase 1 homolog D (S. cerevisiae) (JHDM1D) ELISA kit, Species Mouse, Sample Type serum, plasma 96T


 

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