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Lysine-specific demethylase 2A (EC 1.14.11.27) (F-box and leucine-rich repeat protein 11) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)

 KDM2A_MOUSE             Reviewed;        1161 AA.
P59997; Q3U1M5; Q3UR56; Q3V3Q1; Q69ZT4;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
22-NOV-2017, entry version 131.
RecName: Full=Lysine-specific demethylase 2A;
EC=1.14.11.27 {ECO:0000250|UniProtKB:Q9Y2K7};
AltName: Full=F-box and leucine-rich repeat protein 11;
AltName: Full=F-box/LRR-repeat protein 11;
AltName: Full=JmjC domain-containing histone demethylation protein 1A;
AltName: Full=[Histone-H3]-lysine-36 demethylase 1A;
Name=Kdm2a; Synonyms=Fbxl11, Jhdm1a, Kiaa1004;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-1161.
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1161.
TISSUE=Thymus;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-444; SER-692;
THR-713; SER-718 AND SER-731, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
36' of histone H3, thereby playing a central role in histone code.
Preferentially demethylates dimethylated H3 'Lys-36' residue while
it has weak or no activity for mono- and tri-methylated H3 'Lys-
36'. May also recognize and bind to some phosphorylated proteins
and promote their ubiquitination and degradation. Required to
maintain the heterochromatic state. Associates with centromeres
and represses transcription of small non-coding RNAs that are
encoded by the clusters of satellite repeats at the centromere.
Required to sustain centromeric integrity and genomic stability,
particularly during mitosis. {ECO:0000250|UniProtKB:Q9Y2K7}.
-!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2 2-
oxoglutarate + 2 O(2) = protein L-lysine + 2 succinate + 2
formaldehyde + 2 CO(2). {ECO:0000250|UniProtKB:Q9Y2K7}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
Interacts with CBX5/HP1A; the interaction promotes CBX5
localization to chromatin (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
Note=Punctate expression throughout the nucleoplasm and enriched
in the perinucleolar region. Specifically nucleates at CpG islands
where it's presence results in chromatin depleted in H3K36me2 (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P59997-1; Sequence=Displayed;
Name=2;
IsoId=P59997-2; Sequence=VSP_017473, VSP_017474;
Note=No experimental confirmation available.;
Name=3;
IsoId=P59997-3; Sequence=VSP_017471, VSP_017472;
Note=No experimental confirmation available.;
-!- DOMAIN: The JmjC domain mediates demethylation activity and is
required for satellite silencing. {ECO:0000250}.
-!- DOMAIN: The CXXC zinc finger preferentially recognizes
nonmethylated CpG DNA, and binding is blocked when the CpG DNA is
methylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BC076576; Type=Frameshift; Positions=834; Evidence={ECO:0000305};
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EMBL; AK037157; BAE20506.1; -; mRNA.
EMBL; AK141779; BAE24832.1; -; mRNA.
EMBL; AK155866; BAE33470.1; -; mRNA.
EMBL; BC057051; AAH57051.1; -; mRNA.
EMBL; BC076576; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK173084; BAD32362.1; -; mRNA.
CCDS; CCDS37886.1; -. [P59997-1]
RefSeq; NP_001001984.2; NM_001001984.2.
UniGene; Mm.31941; -.
PDB; 4QWN; X-ray; 2.10 A; A/C=36-364, B/D=450-517.
PDB; 4QX7; X-ray; 2.34 A; A/C=36-364, B/D=450-517.
PDB; 4QX8; X-ray; 1.65 A; A/C=36-364, B/D=450-517.
PDB; 4QXB; X-ray; 1.60 A; A/C=36-364, B/D=450-517.
PDB; 4QXC; X-ray; 1.75 A; A/C=36-364, B/D=450-517.
PDB; 4QXH; X-ray; 2.20 A; A/C=36-364, B/D=450-517.
PDB; 4TN7; X-ray; 2.20 A; A/C=36-364, B/D=450-517.
PDBsum; 4QWN; -.
PDBsum; 4QX7; -.
PDBsum; 4QX8; -.
PDBsum; 4QXB; -.
PDBsum; 4QXC; -.
PDBsum; 4QXH; -.
PDBsum; 4TN7; -.
ProteinModelPortal; P59997; -.
SMR; P59997; -.
DIP; DIP-46352N; -.
IntAct; P59997; 1.
STRING; 10090.ENSMUSP00000047683; -.
iPTMnet; P59997; -.
PhosphoSitePlus; P59997; -.
EPD; P59997; -.
MaxQB; P59997; -.
PaxDb; P59997; -.
PeptideAtlas; P59997; -.
PRIDE; P59997; -.
GeneID; 225876; -.
KEGG; mmu:225876; -.
CTD; 22992; -.
MGI; MGI:1354736; Kdm2a.
eggNOG; KOG1633; Eukaryota.
eggNOG; KOG1947; Eukaryota.
eggNOG; ENOG410XQXU; LUCA.
HOGENOM; HOG000007396; -.
InParanoid; P59997; -.
KO; K10276; -.
PhylomeDB; P59997; -.
ChiTaRS; Kdm2a; mouse.
PRO; PR:P59997; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FBXL11; -.
GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); ISO:MGI.
GO; GO:0045322; F:unmethylated CpG binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
GO; GO:0001947; P:heart looping; IMP:MGI.
GO; GO:0070544; P:histone H3-K36 demethylation; ISO:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0033184; P:positive regulation of histone ubiquitination; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR001810; F-box_dom.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR002857; Znf_CXXC.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00646; F-box; 1.
Pfam; PF02373; JmjC; 1.
Pfam; PF16866; PHD_4; 1.
Pfam; PF02008; zf-CXXC; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00367; LRR_CC; 3.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51058; ZF_CXXC; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Dioxygenase; DNA-binding; Iron; Isopeptide bond;
Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 1161 Lysine-specific demethylase 2A.
/FTId=PRO_0000119856.
DOMAIN 148 316 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
DOMAIN 888 935 F-box.
REPEAT 960 981 LRR 1.
REPEAT 983 1009 LRR 2.
REPEAT 1047 1072 LRR 3.
REPEAT 1073 1102 LRR 4.
REPEAT 1103 1127 LRR 5.
REPEAT 1128 1155 LRR 6.
ZN_FING 564 610 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 617 678 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
METAL 212 212 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 214 214 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 284 284 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
BINDING 209 209 Substrate. {ECO:0000250}.
BINDING 229 229 Substrate. {ECO:0000250}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 550 550 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
MOD_RES 632 632 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 713 713 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
MOD_RES 868 868 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2K7}.
CROSSLNK 505 505 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y2K7}.
VAR_SEQ 321 338 PNKFRYPFYYEMCWYVLE -> SNVTIICVDVSPFKADVR
(in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017471.
VAR_SEQ 339 1161 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017472.
VAR_SEQ 494 494 I -> S (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017473.
VAR_SEQ 495 1161 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017474.
CONFLICT 159 159 W -> R (in Ref. 1; BAE20506 and 2;
BC076576). {ECO:0000305}.
CONFLICT 202 202 I -> M (in Ref. 1; BAE20506 and 2;
BC076576). {ECO:0000305}.
CONFLICT 913 913 M -> I (in Ref. 2; AAH57051).
{ECO:0000305}.
HELIX 40 45 {ECO:0000244|PDB:4QXB}.
HELIX 59 61 {ECO:0000244|PDB:4QXB}.
HELIX 64 70 {ECO:0000244|PDB:4QXB}.
STRAND 76 80 {ECO:0000244|PDB:4QXB}.
TURN 82 84 {ECO:0000244|PDB:4TN7}.
HELIX 95 102 {ECO:0000244|PDB:4QXB}.
STRAND 107 112 {ECO:0000244|PDB:4QXB}.
TURN 113 116 {ECO:0000244|PDB:4QXB}.
STRAND 117 122 {ECO:0000244|PDB:4QXB}.
HELIX 123 131 {ECO:0000244|PDB:4QXB}.
HELIX 134 136 {ECO:0000244|PDB:4QXB}.
STRAND 141 147 {ECO:0000244|PDB:4QXB}.
HELIX 154 156 {ECO:0000244|PDB:4QXB}.
HELIX 161 166 {ECO:0000244|PDB:4QXB}.
HELIX 168 172 {ECO:0000244|PDB:4QXB}.
HELIX 175 180 {ECO:0000244|PDB:4QXB}.
HELIX 188 190 {ECO:0000244|PDB:4QXB}.
STRAND 199 203 {ECO:0000244|PDB:4QXB}.
STRAND 208 212 {ECO:0000244|PDB:4QXB}.
HELIX 215 217 {ECO:0000244|PDB:4QXB}.
STRAND 219 227 {ECO:0000244|PDB:4QXB}.
STRAND 229 234 {ECO:0000244|PDB:4QXB}.
HELIX 238 250 {ECO:0000244|PDB:4QXB}.
TURN 253 255 {ECO:0000244|PDB:4QXB}.
HELIX 258 260 {ECO:0000244|PDB:4QXB}.
STRAND 261 263 {ECO:0000244|PDB:4QXB}.
STRAND 266 270 {ECO:0000244|PDB:4QXB}.
STRAND 275 278 {ECO:0000244|PDB:4QXB}.
STRAND 283 287 {ECO:0000244|PDB:4QXB}.
STRAND 292 299 {ECO:0000244|PDB:4QXB}.
HELIX 305 317 {ECO:0000244|PDB:4QXB}.
HELIX 322 324 {ECO:0000244|PDB:4QXB}.
HELIX 329 345 {ECO:0000244|PDB:4QXB}.
HELIX 352 362 {ECO:0000244|PDB:4QXB}.
HELIX 455 469 {ECO:0000244|PDB:4QXB}.
HELIX 473 476 {ECO:0000244|PDB:4QXB}.
HELIX 485 499 {ECO:0000244|PDB:4QXB}.
TURN 504 507 {ECO:0000244|PDB:4QXB}.
SEQUENCE 1161 AA; 132680 MW; 210BD9F65BED0AE4 CRC64;
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLQTNKYN ANFVTFMEGK
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQWP STVDFIDWVD NMWPRHLKES
QTESTNAILE MQYPKVQKYC LISVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL
HSFNIPMQLK IYSIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKDFQKESLS
MDMELNELES GNGDEEGVDR EARRMNNKRS VLTSPVANGV NLDYDGLGKA CRSLPSLKKT
LSGDSSSDST RGSHNGQVWD PQCSPKKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT
GIEDEDALIA DVKILLEELA SSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG
LLNEELPNCW ECPKCYQEDS SDKAQKRKIE ESDEEAVQAK VLRPLRSCEE PLTPPPHSPT
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR PNPRVLMQHC
PARNPQHGDE EGLGGEEEEE EEEEEDDSAE EGGAARLNGR GSWAQDGDES WMQREVWMSV
FRYLSRKELC ECMRVCKTWY KWCCDKRLWT KIDLSRCKAI VPQALSGIIK RQPVSLDLSW
TNISKKQLTW LVNRLPGLKD LLLAGCSWSA VSALSTSSCP LLRTLDLRWA VGIKDPQIRD
LLTPPTDKPG QDNRSKLRNM TDFRLAGLDI TDATLRLIIR HMPLLSRLDL SHCSHLTDQS
SNLLTAVGSS TRYSLTELNM AGCNKLTDQT LFFLRRIANV TLIDLRGCKQ ITRKACEHFI
SDLSINSLYC LSDEKLIQKI S


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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
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 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
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
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
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
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
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
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 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 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
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
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
ARP40101_P050 JMJD3(jumonji domain containing 3, histone lysine demethylase) 50 µg
PC-543 Antibodies: LSD1 (IN), (Lysine-specific histone demethylase) Clone: Polyclonal 100 ug
129-10424 Rabbit Anti-Lysine-specific Histone Demethylase, N-terminus 100
CSB-EL001856HU Human Lysine-specific histone demethylase 1B(AOF1) ELISA kit 96T
EIAAB11717 DOT1L,DOT1-like protein,H3-K79-HMTase,Histone H3-K79 methyltransferase,Histone-lysine N-methyltransferase, H3 lysine-79 specific,Homo sapiens,Human,KIAA1814,KMT4,Lysine N-methyltransferase 4
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


 

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