Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lysine-specific demethylase lid (EC 1.14.11.-) (Histone demethylase lid) (Jumonji/ARID domain-containing protein lid) (Protein little imaginal disks) (Retinoblastoma-binding protein 2 homolog)

 KDM5_DROME              Reviewed;        1838 AA.
Q9VMJ7;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 148.
RecName: Full=Lysine-specific demethylase lid;
EC=1.14.11.-;
AltName: Full=Histone demethylase lid;
AltName: Full=Jumonji/ARID domain-containing protein lid;
AltName: Full=Protein little imaginal disks;
AltName: Full=Retinoblastoma-binding protein 2 homolog;
Name=lid; ORFNames=CG9088;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
IDENTIFICATION, AND FUNCTION.
PubMed=11014813;
Gildea J.J., Lopez R., Shearn A.;
"A screen for new trithorax group genes identified little imaginal
discs, the Drosophila melanogaster homologue of human retinoblastoma
binding protein 2.";
Genetics 156:645-663(2000).
[5]
FUNCTION, ACTIVITY REGULATION, INTERACTION WITH MYC, IDENTIFICATION IN
COMPLEX WITH MYC AND ASH2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
HIS-637 AND GLU-639.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1474, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[7]
FUNCTION.
PubMed=17351631; DOI=10.1038/nsmb1216;
Lee N., Zhang J., Klose R.J., Erdjument-Bromage H., Tempst P.,
Jones R.S., Zhang Y.;
"The trithorax-group protein Lid is a histone H3 trimethyl-Lys4
demethylase.";
Nat. Struct. Mol. Biol. 14:341-343(2007).
[8]
FUNCTION.
PubMed=17351630; DOI=10.1038/nsmb1217;
Eissenberg J.C., Lee M.G., Schneider J., Ilvarsonn A., Shiekhattar R.,
Shilatifard A.;
"The trithorax-group gene in Drosophila little imaginal discs encodes
a trimethylated histone H3 Lys4 demethylase.";
Nat. Struct. Mol. Biol. 14:344-346(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323; SER-1422; SER-1433;
SER-1635 AND SER-1640, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[10]
FUNCTION.
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).
-!- 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'. Specifically demethylates
trimethylated H3 'Lys-4'. Required for the correct regulation of
homeotic genes during development. Plays a role in the regulation
of the circadian rhythm and in maintaining the normal periodicity
of the circadian clock. Regulates the expression of clock-
controlled genes including tim, per and cry.
{ECO:0000269|PubMed:11014813, ECO:0000269|PubMed:17311883,
ECO:0000269|PubMed:17351630, ECO:0000269|PubMed:17351631,
ECO:0000269|PubMed:21960634}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Inhibited by Myc.
{ECO:0000269|PubMed:17311883}.
-!- SUBUNIT: Interacts with Myc. Part of a complex containing Lid, Myc
and Ash2. {ECO:0000269|PubMed:17311883}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537,
ECO:0000269|PubMed:17311883}.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE014134; AAF52319.1; -; Genomic_DNA.
EMBL; AY095051; AAM11379.1; -; mRNA.
EMBL; AE014134; AAN10569.1; -; Genomic_DNA.
RefSeq; NP_001245908.1; NM_001258979.2.
RefSeq; NP_001245909.1; NM_001258980.1.
RefSeq; NP_001245910.1; NM_001258981.2.
RefSeq; NP_001285649.1; NM_001298720.1.
RefSeq; NP_523486.1; NM_078762.6.
RefSeq; NP_723140.1; NM_164671.1.
UniGene; Dm.2779; -.
PDB; 2LM1; NMR; -; A=214-320.
PDB; 2MIQ; NMR; -; A=414-504.
PDBsum; 2LM1; -.
PDBsum; 2MIQ; -.
ProteinModelPortal; Q9VMJ7; -.
SMR; Q9VMJ7; -.
BioGrid; 60002; 35.
DIP; DIP-29330N; -.
IntAct; Q9VMJ7; 6.
MINT; Q9VMJ7; -.
STRING; 7227.FBpp0297914; -.
iPTMnet; Q9VMJ7; -.
PaxDb; Q9VMJ7; -.
PRIDE; Q9VMJ7; -.
EnsemblMetazoa; FBtr0079231; FBpp0078862; FBgn0031759.
EnsemblMetazoa; FBtr0079232; FBpp0078863; FBgn0031759.
EnsemblMetazoa; FBtr0307069; FBpp0297912; FBgn0031759.
EnsemblMetazoa; FBtr0307070; FBpp0297913; FBgn0031759.
EnsemblMetazoa; FBtr0307071; FBpp0297914; FBgn0031759.
EnsemblMetazoa; FBtr0345336; FBpp0311492; FBgn0031759.
GeneID; 33837; -.
KEGG; dme:Dmel_CG9088; -.
CTD; 33837; -.
FlyBase; FBgn0031759; lid.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00940000168915; -.
InParanoid; Q9VMJ7; -.
KO; K11446; -.
OMA; PICDWRV; -.
OrthoDB; EOG091G0RFR; -.
PhylomeDB; Q9VMJ7; -.
BRENDA; 1.14.11.B2; 1994.
Reactome; R-DME-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
GenomeRNAi; 33837; -.
PRO; PR:Q9VMJ7; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0031759; Expressed in 34 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9VMJ7; baseline and differential.
Genevisible; Q9VMJ7; DM.
GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IMP:UniProtKB.
GO; GO:0034647; F:histone demethylase activity (H3-trimethyl-K4 specific); IMP:FlyBase.
GO; GO:0033749; F:histone demethylase activity (H4-R3 specific); IMP:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0016577; P:histone demethylation; IMP:UniProtKB.
GO; GO:0034720; P:histone H3-K4 demethylation; IMP:FlyBase.
GO; GO:0034721; P:histone H3-K4 demethylation, trimethyl-H3-K4-specific; IMP:FlyBase.
GO; GO:0043970; P:histone H3-K9 acetylation; IMP:FlyBase.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:FlyBase.
GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0070193; P:synaptonemal complex organization; IMP:FlyBase.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 3.30.40.10; -; 3.
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; Biological rhythms; Chromatin regulator; Coiled coil;
Complete proteome; Developmental protein; Dioxygenase; Iron;
Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 1838 Lysine-specific demethylase lid.
/FTId=PRO_0000292421.
DOMAIN 161 202 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 226 316 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 591 757 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 448 498 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1293 1354 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1753 1808 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
COILED 960 1049 {ECO:0000255}.
COMPBIAS 16 23 Poly-Gly.
COMPBIAS 1415 1418 Poly-Gln.
COMPBIAS 1454 1462 Poly-Asp.
COMPBIAS 1697 1719 Asn-rich.
METAL 637 637 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 640 640 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 725 725 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOD_RES 323 323 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1422 1422 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1433 1433 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1474 1474 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 1635 1635 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1640 1640 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 637 637 H->A: Abolishes enzymatic activity; when
associated with A-536.
{ECO:0000269|PubMed:17311883}.
MUTAGEN 639 639 E->A: Abolishes enzymatic activity; when
associated with A-534.
{ECO:0000269|PubMed:17311883}.
STRAND 217 219 {ECO:0000244|PDB:2LM1}.
HELIX 227 240 {ECO:0000244|PDB:2LM1}.
TURN 241 243 {ECO:0000244|PDB:2LM1}.
TURN 252 254 {ECO:0000244|PDB:2LM1}.
HELIX 259 269 {ECO:0000244|PDB:2LM1}.
HELIX 272 278 {ECO:0000244|PDB:2LM1}.
HELIX 281 287 {ECO:0000244|PDB:2LM1}.
HELIX 294 315 {ECO:0000244|PDB:2LM1}.
TURN 433 436 {ECO:0000244|PDB:2MIQ}.
STRAND 443 446 {ECO:0000244|PDB:2MIQ}.
TURN 452 455 {ECO:0000244|PDB:2MIQ}.
HELIX 460 462 {ECO:0000244|PDB:2MIQ}.
STRAND 463 465 {ECO:0000244|PDB:2MIQ}.
STRAND 472 474 {ECO:0000244|PDB:2MIQ}.
TURN 475 477 {ECO:0000244|PDB:2MIQ}.
STRAND 478 480 {ECO:0000244|PDB:2MIQ}.
HELIX 493 496 {ECO:0000244|PDB:2MIQ}.
SEQUENCE 1838 AA; 203993 MW; E01BDB89027F9F50 CRC64;
MSAKTEADNT TAANSGGGGV GSGTSSGGGA SANGTATPAR RLRTRNSTGN GTNSGSESVK
KSNANDEPST PVTPAGATGS HTHAPPGISP AVMERPMPSV PMNHASSSVS ASKKYHNSCP
HPTPTPAPTG HKKSVHTQPH SSNKFDQGKN EEFHFDTPPE CPVFRPTTEE FKNPLAYISK
IRSIAEKCGI AKILPPATWS PPFAVDVDKL RFVPRVQRLN ELEAKTRVKL NFLDQIAKFW
ELQGSSLKIP MVERKALDLY TLHRIVQEEG GMEQTTKDRK WAKVANRMQY PSSKSVGATL
KAHYERILHP FEVYTSGKVL GPTPTSSGSG STPVKLEDGG GTDYKAHEIP TRQQIAPPNE
TNTRRSKRFG NSNASCGLSG VTPTTKPSAG VFVKTETKEE FKRDLLSSFN AVNSGGSPLA
TGTTANTRGA SQKKGGEPPA LIVDPLMKYI CHICNRGDVE ESMLLCDGCD DSYHTFCLLP
PLTSIPKGEW LCPRCVVEEV SKPQEAFGFE QAEREYTLQQ FGQMADQFKQ EYFRKPVHLV
PTEMVEREFW RIVSSIDEDV TVEYGADLHT MDHGSGFPTK SSLYLLPGDQ EYAESSWNLN
NLPLLEDSIL GHINADISGM NAPWMYVGMC FAAFCWHNED HWSYSINYLH WGEPKTWYGV
PGSCAEQFEE TMKQAAPELF SSQPDLLHQL VTIMNPNILM NNRVPVFRTD QHAGEFVITF
PRAYHAGFNQ GYNFAEAVNF APADWLKMGR ECVNHYSMLR RFCVFSHDEL VCKMALEPAK
LTFGIATACY IDMAEMVDTE KKLRKSLLEW GVTRAERRAF ELVNDDERHC QECNTTCFLS
AVACECNDKL IVCLRHYTVL CGCAPEKHTL IYRYTLDEMP LMLQKLKVKA HSFERWLSRC
RDIVDAHTPT SVTLQELQEL CKEAETKKFP SSLLIDRLNA AAVEAEKCVT VIQQLGINKV
RTRSDHNQEA AQYKLTMEEL ELFVQEIDNL CCIIDEGASV RELLVLGKQF VERSESQLQL
SLESLEESEL ETLINEGSSL RIELQQLDLL QKRLKQCKWY KRSQGLRETS SKLTYQDVKN
LLHIAAADLD PTDPYVDKEM RKLQQIGADI EAWESQAAKY FRRLTQQHEL GEIEQFLKSA
SDINGQVPSH GLLKDALRKA REWLRAVEQL QQNNHVTYCH TLEAMIERGL NIPIQLEELS
RMQGHLNSAH QWKDNTACAF LKKGTFYTLL EVLMPRSDAI NIDSDLKPRF QDDFLKEKNP
AEIVASFKHA EEQELLDMRE LRRQNMNKNP MRDMFCLCKS EFRNLMFNCQ LCRDWFHEDC
VPPPSATNQN GIVNGGSGPG TNRPKWLCPS CVRSKRPRLE TILPLLVQLQ QLPIRLPEDE
ALRCLAERAM NWQDRARKAL SSPDVSAAQE AIMAQQQQKR RSEGGAGVGN ISSPRKPRRR
GSLTKEASGS TESDADDDDD EDECRLRIVE DNFSNDEDEP RTAPATSTVN SDLLKLLSDS
EIENLLDLMM EGDLLEVSLD ETQELWRILE TMPPTLLQAE AMERVVQYMQ RQRQQHTNPL
PTSGAEDSND SLMVQNSPNS NSNSGGATGS ASNSGRNKKR RSNDTGGNSA VPRKKQSTPK
QTPGKKGSAA AARKSDAKAS PAASTTPGAD ADAENKQANG GNTNSSTGSG GGNSATTTPT
PGSTHKKRKR TSTTATNNNN NNNNNSTNNS NSSTNLNSNT TSGQGAATGG NNATGGQKKH
AQRSQQAAQE DDEEECRAEN CHKPTGREVD WVQCDGGCNE WFHMYCVGLN RSQIKPDDDY
ICIRCTKTVA IGTQGSGHSM SVASTTTPGK QRAVQSAR


Related products :

Catalog number Product name Quantity
U1916h CLIA 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,KIAA 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
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
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
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
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
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
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
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
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
ARP40101_P050 JMJD3(jumonji domain containing 3, histone lysine demethylase) 50 µg
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
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
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
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
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
JMJD1C JHDM1D Gene jumonji C domain containing histone demethylase 1 homolog D (S. cerevisiae)
18-003-42333 AT-rich interactive domain-containing protein 4A - ARID domain-containing protein 4A; Retinoblastoma-binding protein 1; RBBP-1 Polyclonal 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur