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Lysine-specific demethylase 5A (EC 1.14.11.-) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2)

 KDM5A_HUMAN             Reviewed;        1690 AA.
P29375; A8MV76; Q4LE72; Q86XZ1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
12-SEP-2018, entry version 186.
RecName: Full=Lysine-specific demethylase 5A;
EC=1.14.11.-;
AltName: Full=Histone demethylase JARID1A;
AltName: Full=Jumonji/ARID domain-containing protein 1A;
AltName: Full=Retinoblastoma-binding protein 2;
Short=RBBP-2;
Name=KDM5A {ECO:0000312|HGNC:HGNC:9886};
Synonyms=JARID1A, RBBP2, RBP2 {ECO:0000303|PubMed:18270511};
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 2), AND INTERACTION WITH RB1.
PubMed=8414517;
Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E.,
Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D.,
Jones R.E.;
"Characterization of the retinoblastoma binding proteins RBP1 and
RBP2.";
Oncogene 8:3149-3156(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1099 (ISOFORMS 1/2).
TISSUE=Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1102-1564.
PubMed=1857421; DOI=10.1038/352251a0;
Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A.,
Hanobik M.G., Huber H.E., Oliff A.;
"Cloning of cDNAs for cellular proteins that bind to the
retinoblastoma gene product.";
Nature 352:251-254(1991).
[6]
INTERACTION WITH RB1, AND SUBCELLULAR LOCATION.
PubMed=7935440; DOI=10.1128/MCB.14.11.7256;
Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.;
"Differential specificity for binding of retinoblastoma binding
protein 2 to RB, p107, and TATA-binding protein.";
Mol. Cell. Biol. 14:7256-7264(1994).
[7]
INTERACTION WITH LMO2.
PubMed=9129143; DOI=10.1038/sj.onc.1200988;
Mao S., Neale G.A.M., Goorha R.M.;
"T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding
protein 2.";
Oncogene 14:1531-1539(1997).
[8]
FUNCTION, AND INTERACTION WITH ESR1.
PubMed=11358960; DOI=10.1074/jbc.M100313200;
Chan S.W., Hong W.;
"Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone
receptor-mediated transcription.";
J. Biol. Chem. 276:28402-28412(2001).
[9]
SUBCELLULAR LOCATION, INTERACTION WITH RB1, AND FUNCTION.
PubMed=15949438; DOI=10.1016/j.molcel.2005.05.012;
Benevolenskaya E.V., Murray H.L., Branton P., Young R.A.,
Kaelin W.G. Jr.;
"Binding of pRB to the PHD protein RBP2 promotes cellular
differentiation.";
Mol. Cell 18:623-635(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598 AND SER-1603, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION.
PubMed=17320163; DOI=10.1016/j.cell.2007.02.013;
Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H.,
Tempst P., Gilliland D.G., Zhang Y., Kaelin W.G. Jr.;
"The retinoblastoma binding protein RBP2 is an H3K4 demethylase.";
Cell 128:889-900(2007).
[12]
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).
[13]
FUNCTION.
PubMed=17320160; DOI=10.1016/j.cell.2007.02.017;
Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M.,
Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.;
"The X-linked mental retardation gene SMCX/JARID1C defines a family of
histone H3 lysine 4 demethylases.";
Cell 128:1077-1088(2007).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111 AND SER-1331, AND
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
INTERACTION WITH ARNTL AND CLOCK.
PubMed=21960634; DOI=10.1126/science.1206022;
DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
Panda S.;
"Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and
influences the circadian clock.";
Science 333:1881-1885(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-1330; SER-1438;
SER-1488 AND SER-1666, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191 AND LYS-1007, 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).
[22]
STRUCTURE BY NMR OF 85-175, FUNCTION, DOMAIN, DNA-BINDING, AND
MUTAGENESIS OF ARG-112; LYS-152; SER-156 AND LEU-157.
PubMed=18270511; DOI=10.1038/nsmb.1400;
Tu S., Teng Y.C., Yuan C., Wu Y.T., Chan M.Y., Cheng A.N., Lin P.H.,
Juan L.J., Tsai M.D.;
"The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC
motif.";
Nat. Struct. Mol. Biol. 15:419-421(2008).
[23]
STRUCTURE BY NMR OF 1609-1659 IN COMPLEX WITH ZINC AND HISTONE H3,
STRUCTURE BY X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1609-1659 IN
COMPLEX WITH ZINC AND HISTONE H3, FUNCTION, INTERACTION WITH HISTONE
H3, MUTAGENESIS OF VAL-1609; TRP-1625 AND 1634-GLU-TRP-1635, AND
DOMAIN.
PubMed=19430464; DOI=10.1038/nature08036;
Wang G.G., Song J., Wang Z., Dormann H.L., Casadio F., Li H.,
Luo J.L., Patel D.J., Allis C.D.;
"Haematopoietic malignancies caused by dysregulation of a chromatin-
binding PHD finger.";
Nature 459:847-851(2009).
[24]
X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF 12-797 IN COMPLEX WITH ZINC
AND NICKEL.
PubMed=27499454; DOI=10.1016/j.bmcl.2016.07.070;
Labadie S.S., Dragovich P.S., Cummings R.T., Deshmukh G.,
Gustafson A., Han N., Harmange J.C., Kiefer J.R., Li Y., Liang J.,
Liederer B.M., Liu Y., Manieri W., Mao W., Murray L., Ortwine D.F.,
Trojer P., VanderPorten E., Vinogradova M., Wen L.;
"Design and evaluation of 1,7-naphthyridones as novel KDM5
inhibitors.";
Bioorg. Med. Chem. Lett. 26:4492-4496(2016).
[25]
X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 1-87 AND 348-588 IN COMPLEX
WITH INHIBITORS; MANGANESE AND 2-OXOGLUTARATE, BIOPHYSICOCHEMICAL
PROPERTIES, FUNCTION, AND MUTAGENESIS OF CYS-626 AND CYS-636.
PubMed=27427228; DOI=10.1016/j.chembiol.2016.06.006;
Horton J.R., Liu X., Gale M., Wu L., Shanks J.R., Zhang X.,
Webber P.J., Bell J.S., Kales S.C., Mott B.T., Rai G., Jansen D.J.,
Henderson M.J., Urban D.J., Hall M.D., Simeonov A., Maloney D.J.,
Johns M.A., Fu H., Jadhav A., Vertino P.M., Yan Q., Cheng X.;
"Structural Basis for KDM5A Histone Lysine Demethylase Inhibition by
Diverse Compounds.";
Cell Chem. Biol. 23:769-781(2016).
[26]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1-87 AND 348-588 IN COMPLEX
WITH MANGANESE AND 2-OXOGLUTARATE.
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).
[27]
X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 12-797 IN COMPLEX WITH AN
INHIBITOR ZINC AND NICKEL, AND ACTIVITY REGULATION.
PubMed=27214401; DOI=10.1038/nchembio.2085;
Vinogradova M., Gehling V.S., Gustafson A., Arora S., Tindell C.A.,
Wilson C., Williamson K.E., Guler G.D., Gangurde P., Manieri W.,
Busby J., Flynn E.M., Lan F., Kim H.J., Odate S., Cochran A.G.,
Liu Y., Wongchenko M., Yang Y., Cheung T.K., Maile T.M., Lau T.,
Costa M., Hegde G.V., Jackson E., Pitti R., Arnott D., Bailey C.,
Bellon S., Cummings R.T., Albrecht B.K., Harmange J.C., Kiefer J.R.,
Trojer P., Classon M.;
"An inhibitor of KDM5 demethylases reduces survival of drug-tolerant
cancer cells.";
Nat. Chem. Biol. 12:531-538(2016).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
4' of histone H3, thereby playing a central role in histone code.
Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36',
H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and
dimethylated but not monomethylated H3 'Lys-4'. Regulates specific
gene transcription through DNA-binding on 5'-CCGCCC-3' motif
(PubMed:18270511). May stimulate transcription mediated by nuclear
receptors. Involved in transcriptional regulation of Hox proteins
during cell differentiation (PubMed:19430464). May participate in
transcriptional repression of cytokines such as CXCL12. Plays a
role in the regulation of the circadian rhythm and in maintaining
the normal periodicity of the circadian clock. In a histone
demethylase-independent manner, acts as a coactivator of the
CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2
and other clock-controlled genes and increases histone acetylation
at PER1/2 promoters by inhibiting the activity of HDAC1 (By
similarity). Seems to act as a transcriptional corepressor for
some genes such as MT1F and to favor the proliferation of cancer
cells (PubMed:27427228). {ECO:0000250|UniProtKB:Q3UXZ9,
ECO:0000269|PubMed:11358960, ECO:0000269|PubMed:15949438,
ECO:0000269|PubMed:17320160, ECO:0000269|PubMed:17320161,
ECO:0000269|PubMed:17320163, ECO:0000269|PubMed:18270511,
ECO:0000269|PubMed:19430464, ECO:0000269|PubMed:27427228}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: The inhibitors KDOAM-25, CPI-455 and others
inhibits its demethylase activity, resulting to cell growth arrest
in cancer cells. {ECO:0000269|PubMed:27214401,
ECO:0000269|PubMed:27427228}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9 uM for 2-oxoglutarate {ECO:0000269|PubMed:27427228};
KM=2.9 uM for histone H3K4me3 {ECO:0000269|PubMed:27427228};
Note=Kcat are 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and
histone H3K4me3, respectively. {ECO:0000269|PubMed:27427228};
-!- SUBUNIT: Interacts with SUZ12; the interaction is direct (By
similarity). Interacts with the viral protein-binding domain of
RB1. Interacts with ESR1, MYC, MYCN and LMO2. Interacts with HDAC1
(By similarity). Interacts with ARNTL/BMAL1 and CLOCK. Interacts
(via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4'
and (via PHD-type 3 zinc finger) with histone H3 di- and
trimethylated at 'Lys-4' (PubMed:19430464).
{ECO:0000250|UniProtKB:Q3UXZ9, ECO:0000269|PubMed:11358960,
ECO:0000269|PubMed:15949438, ECO:0000269|PubMed:17311883,
ECO:0000269|PubMed:19430464, ECO:0000269|PubMed:21960634,
ECO:0000269|PubMed:7935440, ECO:0000269|PubMed:8414517,
ECO:0000269|PubMed:9129143}.
-!- INTERACTION:
P06400:RB1; NbExp=2; IntAct=EBI-1560836, EBI-491274;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:15949438, ECO:0000269|PubMed:7935440}. Nucleus
{ECO:0000250|UniProtKB:Q3UXZ9}. Note=Occupies promoters of genes
involved in RNA metabolism and mitochondrial function.
{ECO:0000250|UniProtKB:Q3UXZ9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29375-1; Sequence=Displayed;
Name=2;
IsoId=P29375-2; Sequence=VSP_035746;
-!- DOMAIN: The GSGFP motif is required for the interaction with SUZ12
(By similarity). The ARID domain specifically binds to the CCGCCC
motif and is required for the lysine-specific histone demethylase
activity (PubMed:18270511). The PHD-type 3 zinc finger is required
for the interaction with histone H3 di- and trimethylated at 'Lys-
4' (PubMed:19430464). {ECO:0000250|UniProtKB:Q3UXZ9,
ECO:0000269|PubMed:18270511, ECO:0000269|PubMed:19430464}.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB28544.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAE06081.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JARID1AID41033ch12p13.html";
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EMBL; S66431; AAB28544.1; ALT_FRAME; mRNA.
EMBL; AB209999; BAE06081.1; ALT_INIT; mRNA.
EMBL; AC005844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC048307; AAH48307.1; ALT_TERM; mRNA.
EMBL; BC053893; AAH53893.1; ALT_TERM; mRNA.
EMBL; BC110916; AAI10917.1; ALT_TERM; mRNA.
CCDS; CCDS41736.1; -. [P29375-1]
PIR; I78879; I78879.
RefSeq; NP_001036068.1; NM_001042603.2. [P29375-1]
UniGene; Hs.76272; -.
PDB; 2JXJ; NMR; -; A=85-175.
PDB; 2KGG; NMR; -; A=1609-1659.
PDB; 2KGI; NMR; -; A=1609-1659.
PDB; 3GL6; X-ray; 1.90 A; A=1609-1659.
PDB; 5C11; X-ray; 2.80 A; A=1609-1659.
PDB; 5CEH; X-ray; 3.14 A; A=12-797.
PDB; 5E6H; X-ray; 2.24 A; A=1-87, A=348-588.
PDB; 5ISL; X-ray; 1.69 A; A=1-87, A=348-588.
PDB; 5IVB; X-ray; 1.39 A; A=1-87, A=348-588.
PDB; 5IVC; X-ray; 1.57 A; A=1-87, A=348-588.
PDB; 5IVE; X-ray; 1.78 A; A=1-87, A=348-588.
PDB; 5IVF; X-ray; 1.68 A; A=1-87, A=348-588.
PDB; 5IVJ; X-ray; 1.57 A; A=1-87, A=348-588.
PDB; 5IVV; X-ray; 1.85 A; A=1-87, A=348-588.
PDB; 5IVY; X-ray; 1.45 A; A=1-87, A=348-588.
PDB; 5IW0; X-ray; 1.63 A; A=1-87, A=348-588.
PDB; 5IWF; X-ray; 2.29 A; A=1-87, A=348-588.
PDB; 5K4L; X-ray; 3.18 A; A/B=12-797.
PDB; 5V9P; X-ray; 3.00 A; A=12-797.
PDB; 5V9T; X-ray; 3.05 A; A/B=12-797.
PDB; 6BGU; X-ray; 1.68 A; A=1-588.
PDB; 6BGV; X-ray; 1.59 A; A=1-588.
PDB; 6BGW; X-ray; 1.64 A; A=1-588.
PDB; 6BGX; X-ray; 1.88 A; A=1-588.
PDB; 6BGY; X-ray; 1.22 A; A=1-588.
PDB; 6BGZ; X-ray; 1.69 A; A=1-588.
PDB; 6BH0; X-ray; 1.99 A; A=1-588.
PDB; 6BH1; X-ray; 1.93 A; A=1-588.
PDB; 6BH2; X-ray; 1.45 A; A=1-588.
PDB; 6BH3; X-ray; 1.70 A; A=1-588.
PDB; 6BH4; X-ray; 2.05 A; A=1-588.
PDB; 6BH5; X-ray; 1.65 A; A=1-588.
PDBsum; 2JXJ; -.
PDBsum; 2KGG; -.
PDBsum; 2KGI; -.
PDBsum; 3GL6; -.
PDBsum; 5C11; -.
PDBsum; 5CEH; -.
PDBsum; 5E6H; -.
PDBsum; 5ISL; -.
PDBsum; 5IVB; -.
PDBsum; 5IVC; -.
PDBsum; 5IVE; -.
PDBsum; 5IVF; -.
PDBsum; 5IVJ; -.
PDBsum; 5IVV; -.
PDBsum; 5IVY; -.
PDBsum; 5IW0; -.
PDBsum; 5IWF; -.
PDBsum; 5K4L; -.
PDBsum; 5V9P; -.
PDBsum; 5V9T; -.
PDBsum; 6BGU; -.
PDBsum; 6BGV; -.
PDBsum; 6BGW; -.
PDBsum; 6BGX; -.
PDBsum; 6BGY; -.
PDBsum; 6BGZ; -.
PDBsum; 6BH0; -.
PDBsum; 6BH1; -.
PDBsum; 6BH2; -.
PDBsum; 6BH3; -.
PDBsum; 6BH4; -.
PDBsum; 6BH5; -.
ProteinModelPortal; P29375; -.
SMR; P29375; -.
BioGrid; 111862; 30.
DIP; DIP-472N; -.
IntAct; P29375; 11.
MINT; P29375; -.
STRING; 9606.ENSP00000382688; -.
BindingDB; P29375; -.
ChEMBL; CHEMBL2424504; -.
GuidetoPHARMACOLOGY; 2680; -.
iPTMnet; P29375; -.
PhosphoSitePlus; P29375; -.
SwissPalm; P29375; -.
BioMuta; KDM5A; -.
DMDM; 215274124; -.
EPD; P29375; -.
MaxQB; P29375; -.
PaxDb; P29375; -.
PeptideAtlas; P29375; -.
PRIDE; P29375; -.
ProteomicsDB; 54559; -.
ProteomicsDB; 54560; -. [P29375-2]
Ensembl; ENST00000399788; ENSP00000382688; ENSG00000073614. [P29375-1]
GeneID; 5927; -.
KEGG; hsa:5927; -.
UCSC; uc001qif.3; human. [P29375-1]
CTD; 5927; -.
DisGeNET; 5927; -.
EuPathDB; HostDB:ENSG00000073614.11; -.
GeneCards; KDM5A; -.
H-InvDB; HIX0010308; -.
HGNC; HGNC:9886; KDM5A.
HPA; HPA006201; -.
MIM; 180202; gene.
neXtProt; NX_P29375; -.
OpenTargets; ENSG00000073614; -.
PharmGKB; PA34250; -.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00530000063118; -.
HOGENOM; HOG000290719; -.
InParanoid; P29375; -.
KO; K11446; -.
OMA; CHEWYHG; -.
PhylomeDB; P29375; -.
TreeFam; TF106476; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
SIGNOR; P29375; -.
ChiTaRS; KDM5A; human.
EvolutionaryTrace; P29375; -.
GeneWiki; JARID1A; -.
GenomeRNAi; 5927; -.
PRO; PR:P29375; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000073614; Expressed in 244 organ(s), highest expression level in peritoneum.
CleanEx; HS_JARID1A; -.
CleanEx; HS_RBP2; -.
ExpressionAtlas; P29375; baseline and differential.
Genevisible; P29375; HS.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP: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; IMP:CAFA.
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:CAFA.
GO; GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); IDA:CAFA.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0034720; P:histone H3-K4 demethylation; IDA:CAFA.
GO; GO:0033169; P:histone H3-K9 demethylation; IEA:GOC.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:1901726; P:negative regulation of histone deacetylase activity; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:CAFA.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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; 2.
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; Activator; Alternative splicing; Biological rhythms;
Chromatin regulator; Complete proteome; Developmental protein;
Dioxygenase; Iron; Isopeptide bond; Metal-binding; Nucleus;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transcription; Transcription regulation; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 1690 Lysine-specific demethylase 5A.
/FTId=PRO_0000200584.
DOMAIN 19 60 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 84 174 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 437 603 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 293 343 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 676 728 C5HC2. {ECO:0000244|PDB:5CEH,
ECO:0000269|PubMed:27214401,
ECO:0000269|PubMed:27499454}.
ZN_FING 1161 1218 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1607 1661 PHD-type 3.
{ECO:0000269|PubMed:19430464}.
REGION 1623 1690 Interaction with LMO2.
{ECO:0000269|PubMed:9129143}.
MOTIF 419 423 GSGFP motif.
{ECO:0000250|UniProtKB:Q3UXZ9}.
COMPBIAS 1492 1587 Lys-rich.
METAL 483 483 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000305|PubMed:26645689,
ECO:0000305|PubMed:27214401,
ECO:0000305|PubMed:27427228,
ECO:0000305|PubMed:27499454}.
METAL 485 485 Iron; catalytic.
{ECO:0000305|PubMed:26645689,
ECO:0000305|PubMed:27214401,
ECO:0000305|PubMed:27427228,
ECO:0000305|PubMed:27499454}.
METAL 571 571 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000305|PubMed:26645689,
ECO:0000305|PubMed:27214401,
ECO:0000305|PubMed:27427228,
ECO:0000305|PubMed:27499454}.
BINDING 409 409 2-oxoglutarate.
{ECO:0000269|PubMed:26645689,
ECO:0000269|PubMed:27427228}.
BINDING 491 491 2-oxoglutarate.
{ECO:0000269|PubMed:26645689,
ECO:0000269|PubMed:27427228}.
BINDING 493 493 2-oxoglutarate.
{ECO:0000269|PubMed:26645689,
ECO:0000269|PubMed:27427228}.
BINDING 501 501 2-oxoglutarate.
{ECO:0000269|PubMed:26645689,
ECO:0000269|PubMed:27427228}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1111 1111 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1331 1331 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1343 1343 Phosphothreonine.
{ECO:0000250|UniProtKB:Q3UXZ9}.
MOD_RES 1345 1345 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UXZ9}.
MOD_RES 1438 1438 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1488 1488 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1595 1595 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q3UXZ9}.
MOD_RES 1598 1598 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1603 1603 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1666 1666 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1007 1007 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1623 1690 VDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCAKKQG
PVSPGPAPPPSFIMSYKLPMEDLKETS -> GVVFVTEEER
DKKY (in isoform 2).
{ECO:0000303|PubMed:8414517}.
/FTId=VSP_035746.
VARIANT 865 865 M -> T (in dbSNP:rs11062385).
/FTId=VAR_032984.
VARIANT 1190 1190 P -> A (in dbSNP:rs2229353).
/FTId=VAR_032985.
MUTAGEN 112 112 R->E: Decreases DNA-binding.
{ECO:0000269|PubMed:18270511}.
MUTAGEN 152 152 K->E: Abolishes DNA-binding.
{ECO:0000269|PubMed:18270511}.
MUTAGEN 156 156 S->D: Decreases DNA-binding.
{ECO:0000269|PubMed:18270511}.
MUTAGEN 157 157 L->E: Decreases DNA-binding.
{ECO:0000269|PubMed:18270511}.
MUTAGEN 626 626 C->S: No effect on lysine-specific
histone demethylase activity; when
associated with S-636.
{ECO:0000269|PubMed:27427228}.
MUTAGEN 636 636 C->S: No effect on lysine-specific
histone demethylase activity; when
associated with S-626.
{ECO:0000269|PubMed:27427228}.
MUTAGEN 1609 1609 V->G: No effect on interaction with
histone H3 di- and trimethylated at 'Lys-
4'. {ECO:0000269|PubMed:19430464}.
MUTAGEN 1625 1625 W->A: Abolishes interaction with histone
H3 di- and trimethylated at 'Lys-4'.
{ECO:0000269|PubMed:19430464}.
MUTAGEN 1634 1635 EW->AA: Abolishes interaction with
histone H3 di- and trimethylated at 'Lys-
4'. {ECO:0000269|PubMed:19430464}.
CONFLICT 1411 1411 Q -> QVFFGK (in Ref. 1; AAB28544).
{ECO:0000305}.
CONFLICT 1547 1547 E -> K (in Ref. 1; AAB28544).
{ECO:0000305}.
CONFLICT 1612 1614 AQN -> EPD (in Ref. 1; AAB28544).
{ECO:0000305}.
HELIX 28 30 {ECO:0000244|PDB:6BGY}.
HELIX 32 43 {ECO:0000244|PDB:6BGY}.
TURN 44 46 {ECO:0000244|PDB:6BGY}.
STRAND 47 51 {ECO:0000244|PDB:6BGY}.
TURN 65 67 {ECO:0000244|PDB:6BGY}.
STRAND 73 76 {ECO:0000244|PDB:6BGY}.
TURN 77 82 {ECO:0000244|PDB:6BGY}.
HELIX 85 100 {ECO:0000244|PDB:5V9P}.
HELIX 117 126 {ECO:0000244|PDB:5V9P}.
HELIX 130 136 {ECO:0000244|PDB:5V9P}.
HELIX 139 145 {ECO:0000244|PDB:5V9P}.
HELIX 154 173 {ECO:0000244|PDB:5V9P}.
STRAND 174 176 {ECO:0000244|PDB:5V9P}.
HELIX 198 201 {ECO:0000244|PDB:5V9T}.
TURN 350 353 {ECO:0000244|PDB:5IVC}.
HELIX 363 378 {ECO:0000244|PDB:6BGY}.
HELIX 382 384 {ECO:0000244|PDB:6BGY}.
HELIX 387 399 {ECO:0000244|PDB:6BGY}.
STRAND 401 403 {ECO:0000244|PDB:5E6H}.
STRAND 406 414 {ECO:0000244|PDB:6BGY}.
HELIX 415 418 {ECO:0000244|PDB:6BGY}.
STRAND 426 429 {ECO:0000244|PDB:6BGY}.
HELIX 433 435 {ECO:0000244|PDB:6BGY}.
HELIX 436 440 {ECO:0000244|PDB:6BGY}.
HELIX 445 447 {ECO:0000244|PDB:6BGY}.
HELIX 448 450 {ECO:0000244|PDB:5V9P}.
HELIX 455 459 {ECO:0000244|PDB:6BGY}.
STRAND 465 468 {ECO:0000244|PDB:5V9T}.
STRAND 470 474 {ECO:0000244|PDB:6BGY}.
STRAND 479 483 {ECO:0000244|PDB:6BGY}.
HELIX 486 488 {ECO:0000244|PDB:6BGY}.
STRAND 490 499 {ECO:0000244|PDB:6BGY}.
STRAND 501 506 {ECO:0000244|PDB:6BGY}.
HELIX 508 510 {ECO:0000244|PDB:6BGY}.
HELIX 511 521 {ECO:0000244|PDB:6BGY}.
HELIX 524 526 {ECO:0000244|PDB:6BGY}.
HELIX 531 534 {ECO:0000244|PDB:6BGY}.
TURN 535 537 {ECO:0000244|PDB:6BGV}.
HELIX 542 547 {ECO:0000244|PDB:6BGY}.
STRAND 553 557 {ECO:0000244|PDB:6BGY}.
STRAND 562 565 {ECO:0000244|PDB:6BGY}.
STRAND 570 586 {ECO:0000244|PDB:6BGY}.
HELIX 589 591 {ECO:0000244|PDB:5V9P}.
HELIX 592 604 {ECO:0000244|PDB:5V9P}.
HELIX 613 621 {ECO:0000244|PDB:5V9P}.
HELIX 629 655 {ECO:0000244|PDB:5V9P}.
STRAND 661 663 {ECO:0000244|PDB:5K4L}.
HELIX 666 668 {ECO:0000244|PDB:5V9P}.
HELIX 671 673 {ECO:0000244|PDB:5V9P}.
STRAND 674 676 {ECO:0000244|PDB:5V9T}.
STRAND 685 688 {ECO:0000244|PDB:5V9P}.
STRAND 691 693 {ECO:0000244|PDB:5V9P}.
HELIX 703 705 {ECO:0000244|PDB:5CEH}.
STRAND 711 713 {ECO:0000244|PDB:5CEH}.
STRAND 716 720 {ECO:0000244|PDB:5V9P}.
HELIX 724 743 {ECO:0000244|PDB:5V9P}.
HELIX 766 772 {ECO:0000244|PDB:5V9P}.
TURN 780 784 {ECO:0000244|PDB:5V9P}.
STRAND 1620 1627 {ECO:0000244|PDB:3GL6}.
STRAND 1629 1632 {ECO:0000244|PDB:3GL6}.
STRAND 1635 1637 {ECO:0000244|PDB:3GL6}.
HELIX 1639 1641 {ECO:0000244|PDB:3GL6}.
HELIX 1645 1650 {ECO:0000244|PDB:3GL6}.
TURN 1656 1658 {ECO:0000244|PDB:3GL6}.
SEQUENCE 1690 AA; 192095 MW; FCF6DC22DEF001DF CRC64;
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK IRPPKDWQPP
FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL
SKIVASKGGF EMVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG
VQMPNLDLKE KVEPEVLSTD TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ
IFGAGPKVVG LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE AFGFEQAVRE
YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS
GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF
CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM
NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVLM
SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCPCP MQKKCLRYRY
PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL SANFNHKKDL IELRVMLEDA EDRKYPENDL
FRKLRDAVKE AETCASVAQL LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI
SQARQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK
VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGSNYAYL
EQLESLSAKG RPIPVRLEAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI
GVYGSGKNRR KKVKELIEKE KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA
MHSLRAANLA KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDRA
RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA
FNRVVSSVSS SPRQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP
IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG
AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK LAKKLAKEEE
RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK
DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN EDYICINCAK KQGPVSPGPA PPPSFIMSYK
LPMEDLKETS


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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
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
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
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
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
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
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 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
EIAAB33918 B5T-overexpressed gene protein,BOG,Homo sapiens,Human,Protein BOG,Putative hydrolase RBBP9,RBBP10,RBBP-10,RBBP9,RBBP-9,Retinoblastoma-binding protein 10,Retinoblastoma-binding protein 9


 

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