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Lysine-specific demethylase 5C (EC 1.14.11.-) (Histone demethylase JARID1C) (Jumonji/ARID domain-containing protein 1C) (Protein SmcX) (Protein Xe169)

 KDM5C_MOUSE             Reviewed;        1554 AA.
P41230; O54995; Q3TYU8; Q3U1X6; Q3U282; Q6ZQF8; Q80XQ9; Q9CVI4;
Q9D0C3; Q9QVR8; Q9R039;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 4.
28-MAR-2018, entry version 155.
RecName: Full=Lysine-specific demethylase 5C;
EC=1.14.11.-;
AltName: Full=Histone demethylase JARID1C;
AltName: Full=Jumonji/ARID domain-containing protein 1C;
AltName: Full=Protein SmcX;
AltName: Full=Protein Xe169;
Name=Kdm5c; Synonyms=Jarid1c, Kiaa0234, Smcx, Xe169;
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 [MRNA] (ISOFORM 2).
STRAIN=129/SvJ;
PubMed=10441747; DOI=10.1007/s003359901116;
Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.;
"Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx.";
Mamm. Genome 10:926-929(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and NOD;
TISSUE=Dendritic cell, Embryo, Inner ear, and Small intestine;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-1068.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=7951230; DOI=10.1093/hmg/3.6.879;
Agulnik A.I., Mitchell M.J., Mattei M.-G., Borsani G., Avner P.A.,
Lerner J.L., Bishop C.E.;
"A novel X gene with a widely transcribed Y-linked homologue escapes
X-inactivation in mouse and human.";
Hum. Mol. Genet. 3:879-884(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-1554 (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. 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. 10:167-180(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1206-1385 (ISOFORM 1).
PubMed=7951318; DOI=10.1038/ng0894-491;
Wu J., Salido E., Yen P., Mohandas T., Shapiro L.J.;
"The murine Xe169 gene escapes X-inactivation like its human
homologue.";
Nat. Genet. 7:491-496(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
PubMed=9723615; DOI=10.1038/29522;
Jegalian K.G., Page D.C.;
"A proposed path by which genes common to mammalian X and Y
chromosomes evolve to become X inactivated.";
Nature 394:776-780(1998).
[8]
FUNCTION.
STRAIN=C3H/HeJ;
PubMed=7544442; DOI=10.1038/376695a0;
Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I.,
Simpson E., Mitchell M.J.;
"Identification of a mouse male-specific transplantation antigen, H-
Y.";
Nature 376:695-698(1995).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-893, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, 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).
[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'. Demethylates trimethylated and
dimethylated but not monomethylated H3 'Lys-4'. Participates in
transcriptional repression of neuronal genes by recruiting histone
deacetylases and REST at neuron-restrictive silencer elements (By
similarity). Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated
transcriptional activation of the core clock component PER2.
{ECO:0000250|UniProtKB:P41229, ECO:0000269|PubMed:21960634}.
-!- COFACTOR:
Name=2-oxoglutarate; Xref=ChEBI:CHEBI:16810;
Evidence={ECO:0000250|UniProtKB:P41229};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000250|UniProtKB:P41229};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000250|UniProtKB:P41229};
-!- SUBUNIT: Part of two distinct complexes, one containing E2F6, and
the other containing REST. {ECO:0000250|UniProtKB:P41229}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P41230-1; Sequence=Displayed;
Name=2;
IsoId=P41230-2; Sequence=VSP_000316;
Name=3;
IsoId=P41230-3; Sequence=VSP_026411, VSP_000316;
-!- DOMAIN: The first PHD-type zinc finger domain recognizes and binds
H3-K9Me3. {ECO:0000250}.
-!- DOMAIN: Both the JmjC domain and the JmjN domain are required for
enzymatic activity. {ECO:0000250}.
-!- MISCELLANEOUS: Escapes X-inactivation.
-!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
{ECO:0000305}.
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EMBL; AF127245; AAD53049.1; -; mRNA.
EMBL; AK008105; BAB25462.1; -; mRNA.
EMBL; AK155279; BAE33161.1; -; mRNA.
EMBL; AK155427; BAE33260.1; -; mRNA.
EMBL; AK155651; BAE33367.1; -; mRNA.
EMBL; AK158340; BAE34464.1; -; mRNA.
EMBL; AK011577; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC043096; AAH43096.1; -; mRNA.
EMBL; BC054550; AAH54550.1; -; mRNA.
EMBL; Z29651; CAA82759.1; -; mRNA.
EMBL; AK129096; BAC97906.1; -; mRNA.
EMBL; L29563; AAA62384.1; -; mRNA.
EMBL; AF039894; AAB96762.1; -; mRNA.
CCDS; CCDS41178.1; -. [P41230-2]
PIR; I48775; I48775.
PIR; I84689; I84689.
RefSeq; NP_038696.2; NM_013668.4. [P41230-2]
RefSeq; XP_006528832.1; XM_006528769.3. [P41230-1]
RefSeq; XP_006528835.1; XM_006528772.3. [P41230-3]
UniGene; Mm.142655; -.
UniGene; Mm.482277; -.
ProteinModelPortal; P41230; -.
SMR; P41230; -.
BioGrid; 203341; 2.
STRING; 10090.ENSMUSP00000108207; -.
iPTMnet; P41230; -.
PhosphoSitePlus; P41230; -.
MaxQB; P41230; -.
PaxDb; P41230; -.
PeptideAtlas; P41230; -.
PRIDE; P41230; -.
Ensembl; ENSMUST00000082177; ENSMUSP00000080814; ENSMUSG00000025332. [P41230-3]
Ensembl; ENSMUST00000112584; ENSMUSP00000108203; ENSMUSG00000025332. [P41230-1]
Ensembl; ENSMUST00000112588; ENSMUSP00000108207; ENSMUSG00000025332. [P41230-2]
GeneID; 20591; -.
KEGG; mmu:20591; -.
UCSC; uc009uqc.3; mouse. [P41230-2]
UCSC; uc009uqd.3; mouse. [P41230-3]
UCSC; uc009uqe.3; mouse. [P41230-1]
CTD; 8242; -.
MGI; MGI:99781; Kdm5c.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00530000063118; -.
InParanoid; P41230; -.
KO; K11446; -.
OMA; HLCLEAR; -.
OrthoDB; EOG091G0RFR; -.
PhylomeDB; P41230; -.
TreeFam; TF106476; -.
Reactome; R-MMU-3214842; HDMs demethylate histones.
ChiTaRS; Kdm5c; mouse.
PRO; PR:P41230; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000025332; -.
ExpressionAtlas; P41230; baseline and differential.
Genevisible; P41230; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0034720; P:histone H3-K4 demethylation; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; NAS:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 3.30.40.10; -; 1.
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; 1.
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; 2.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS51011; ARID; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51183; JMJN; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
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 1554 Lysine-specific demethylase 5C.
/FTId=PRO_0000200587.
DOMAIN 14 55 JmjN. {ECO:0000255|PROSITE-
ProRule:PRU00537}.
DOMAIN 79 169 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
DOMAIN 468 634 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 326 372 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1187 1248 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
METAL 514 514 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 517 517 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 602 602 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:P41229}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:P41229}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 897 897 Phosphoserine.
{ECO:0000250|UniProtKB:P41229}.
MOD_RES 1353 1353 Phosphoserine.
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 205 205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 295 295 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
CROSSLNK 1127 1127 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41229}.
VAR_SEQ 77 117 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026411.
VAR_SEQ 1364 1366 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10441747,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_000316.
CONFLICT 3 3 L -> M (in Ref. 7; AAB96762).
{ECO:0000305}.
CONFLICT 26 26 D -> G (in Ref. 7; AAB96762).
{ECO:0000305}.
CONFLICT 123 123 G -> S (in Ref. 2; BAE33161/BAE33260).
{ECO:0000305}.
CONFLICT 249 249 G -> D (in Ref. 2; BAE34464).
{ECO:0000305}.
CONFLICT 726 726 D -> N (in Ref. 5; BAC97906).
{ECO:0000305}.
CONFLICT 865 865 C -> L (in Ref. 1; AAD53049 and 4;
CAA82759). {ECO:0000305}.
CONFLICT 1068 1068 L -> P (in Ref. 4; CAA82759).
{ECO:0000305}.
CONFLICT 1126 1126 Y -> C (in Ref. 2; BAE33367).
{ECO:0000305}.
SEQUENCE 1554 AA; 175313 MW; 585EA9F890B0D9A0 CRC64;
MELGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVV
EEGGYETICK DRRWARVAQR LNYPPGKNIG SLLRSHYERI VYPYEMYQSG ANLVQCNTRP
FDNEEKDKEY KPHSIPLRQS VQPSKFNSYG RRAKRLQPDP EPTEEDIEKN PELKKLQIYG
AGPKMMGLGL MAKDKTLRKK DKEGPECPPT VVVKEELGGD VKMESTSPKT FLEGKEELSH
SPEPCTKMTM RLRRNHSNAQ FIESYVCRMC SRGDEDDKLL LCDGCDDNYH IFCLLPPLPE
IPKGVWRCPK CVMAECKRPP EAFGFEQATR EYTLQSFGEM ADSFKADYFN MPVHMVPTEL
VEKEFWRLVN SIEEDVTVEY GADIHSKEFG SGFPVSDSKR HLTPEEEEYA TSGWNLNVMP
VLEQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHWGE PKTWYGVPSL
AAEHLEEVMK KLTPELFDSQ PDLLHQLVTL MNPNTLMSHG VPVVRTNQCA GEFVITFPRA
YHSGFNQGYN FAEAVNFCTA DWLPAGRQCI EHYRRLRRYC VFSHEELICK MAACPEKLDL
NLAAAVHKEM FIMVQEERRL RKALLEKGIT EAEREAFELL PDDERQCIKC KTTCFLSALA
CYDCPDGLVC LSHINDLCKC SSSRQYLRYR YTLDELPAML HKLKVRAESF DTWANKVRVA
LEVEDGRKRS LEELRALESE ARERRFPNSE LLQRLKNCLS EAEACVSRAL GLVSGQEAGP
DRVAGLQMTL AELRDFLGQM NNLPCAMHQI GDVKGILEQV EAYQTEAREA LVSQPSSPGL
LQSLLERGQQ LGVEVPEAQQ LQRQVEQARW LDEVKRTLAP SARRGTLAIM RGLLVAGASV
APSPAVDKAQ AELQELLTIA ERWEEKAHLC LEARQKHPPA TLEAIIHEAE NIPVHLPNIQ
SLKEALAKAR AWIADVDEIQ NGDHYPCLDD LEGLVAVGRD LPVGLEELRQ LELQVLTAHS
WREKASKTFL KKNSCYTLLE VLCPCADAGS DSTKRSRWME KELGLYKSDT ELLGLSAQDL
RDPGSVIVAF KEGEQKEKEG ILQLRRTNSA KPSPLALLTT ASSTASICVC GQVPAGVGAL
QCDLCQDWFH GRCVTVPRLL SSQRSSLPSS PLLAWWEWDT KFLCPLCMRS RRPRLETILA
LLVALQRLPV RLPEGEALQC LTERAISWQG RARQVLASEE VTALLGRLAE LRQRLQAESK
PEESLAYPSD GGEGTGNMPK VQGLLENGDS VTSPEKVATE EGSGKRDLEL LSSILPQLSG
PVLELPEATR APLEELMMEG DLLEVTLDEN HSIWQLLQAG QPPDLKRVQT LLELEKAERH
GSRTRGRALE RRRRRKVDRG GEPDDPAREE LEPKRVRSSG PEAEEVQEEE ELEEETGGEV
PPVPFPNSGS PSIQEDQDGL EPVLEAGSDT SAPFSTLTSR LLMSCPQQPS LQQL


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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
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
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
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
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
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
CSB-EL011939HU Human Lysine-specific demethylase 5C(JARID1C) ELISA kit 96T
CSB-EL011939HU Human Lysine-specific demethylase 5C(JARID1C) ELISA kit SpeciesHuman 96T


 

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