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Histone lysine demethylase PHF8 (EC 1.14.11.27) (PHD finger protein 8)

 PHF8_HUMAN              Reviewed;        1060 AA.
Q9UPP1; B3KMV4; B7Z911; Q5H9U5; Q5JPR9; Q5JPS0; Q5JPS2; Q5JPS3;
Q5VUJ4; Q7Z6D4; Q9HAH2;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 3.
25-OCT-2017, entry version 150.
RecName: Full=Histone lysine demethylase PHF8;
EC=1.14.11.27 {ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20023638};
AltName: Full=PHD finger protein 8;
Name=PHF8; Synonyms=KIAA1111, ZNF422;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 34-927 (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 515-1060 (ISOFORM 1).
TISSUE=Embryo, Teratocarcinoma, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Endometrial tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
TISSUE=Brain, and Cervix;
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).
[7]
INVOLVEMENT IN MRXSSD.
PubMed=16199551; DOI=10.1136/jmg.2004.029439;
Laumonnier F., Holbert S., Ronce N., Faravelli F., Lenzner S.,
Schwartz C.E., Lespinasse J., Van Esch H., Lacombe D., Goizet C.,
Phan-Dinh Tuy F., van Bokhoven H., Fryns J.-P., Chelly J.,
Ropers H.-H., Moraine C., Hamel B.C.J., Briault S.;
"Mutations in PHF8 are associated with X linked mental retardation and
cleft lip/cleft palate.";
J. Med. Genet. 42:780-786(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-705; THR-706; SER-854;
SER-857 AND SER-880, 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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; THR-705; THR-706;
SER-854 AND SER-857, 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).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-283.
PubMed=20531378; DOI=10.1038/cr.2010.75;
Zhu Z., Wang Y., Li X., Wang Y., Xu L., Wang X., Sun T., Dong X.,
Chen L., Mao H., Yu Y., Li J., Chen P.A., Chen C.D.;
"PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis.";
Cell Res. 20:794-801(2010).
[13]
FUNCTION, AND CHARACTERIZATION OF VARIANT MRXSSD SER-315.
PubMed=20548336; DOI=10.1038/cr.2010.81;
Qiu J., Shi G., Jia Y., Li J., Wu M., Li J., Dong S., Wong J.;
"The X-linked mental retardation gene PHF8 is a histone demethylase
involved in neuronal differentiation.";
Cell Res. 20:908-918(2010).
[14]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=19843542; DOI=10.1093/hmg/ddp480;
Loenarz C., Ge W., Coleman M.L., Rose N.R., Cooper C.D.O., Klose R.J.,
Ratcliffe P.J., Schofield C.J.;
"PHF8, a gene associated with cleft lip/palate and mental retardation,
encodes for an Nepsilon-dimethyl lysine demethylase.";
Hum. Mol. Genet. 19:217-222(2010).
[15]
FUNCTION, DOMAIN PHD-FINGER, INTERACTION WITH ZNF711, CHARACTERIZATION
OF VARIANT MRXSSD SER-315, AND MUTAGENESIS OF HIS-283.
PubMed=20346720; DOI=10.1016/j.molcel.2010.03.002;
Kleine-Kohlbrecher D., Christensen J., Vandamme J., Abarrategui I.,
Bak M., Tommerup N., Shi X., Gozani O., Rappsilber J., Salcini A.E.,
Helin K.;
"A functional link between the histone demethylase PHF8 and the
transcription factor ZNF711 in X-linked mental retardation.";
Mol. Cell 38:165-178(2010).
[16]
FUNCTION, DOMAIN PHD-FINGER, AND CHARACTERIZATION OF VARIANT MRXSSD
SER-315.
PubMed=20421419; DOI=10.1128/MCB.01520-09;
Fortschegger K., de Graaf P., Outchkourov N.S., van Schaik F.M.,
Timmers H.T., Shiekhattar R.;
"PHF8 targets histone methylation and RNA polymerase II to activate
transcription.";
Mol. Cell. Biol. 30:3286-3298(2010).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POLR1B AND UBTF,
CHARACTERIZATION OF VARIANT MRXSSD SER-315, AND MUTAGENESIS OF TYR-43
AND 283-HIS--ASP-285.
PubMed=20208542; DOI=10.1038/nsmb.1778;
Feng W., Yonezawa M., Ye J., Jenuwein T., Grummt I.;
"PHF8 activates transcription of rRNA genes through H3K4me3 binding
and H3K9me1/2 demethylation.";
Nat. Struct. Mol. Biol. 17:445-450(2010).
[18]
FUNCTION, DOMAIN PHD-FINGER, CHARACTERIZATION OF VARIANT MRXSSD
SER-315, AND MUTAGENESIS OF TYR-43; TYR-50 AND TRP-65.
PubMed=20622853; DOI=10.1038/nature09261;
Qi H.H., Sarkissian M., Hu G.Q., Wang Z., Bhattacharjee A.,
Gordon D.B., Gonzales M., Lan F., Ongusaha P.P., Huarte M.,
Yaghi N.K., Lim H., Garcia B.A., Brizuela L., Zhao K., Roberts T.M.,
Shi Y.;
"Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and
craniofacial development.";
Nature 466:503-507(2010).
[19]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN PHD-FINGER, INTERACTION WITH
SETD1A; HCFC1 AND E2F1, CHARACTERIZATION OF VARIANT MRXSSD SER-315,
PHOSPHORYLATION AT SER-69 AND SER-120, AND MUTAGENESIS OF SER-69;
SER-120 AND HIS-283.
PubMed=20622854; DOI=10.1038/nature09272;
Liu W., Tanasa B., Tyurina O.V., Zhou T.Y., Gassmann R., Liu W.T.,
Ohgi K.A., Benner C., Garcia-Bassets I., Aggarwal A.K., Desai A.,
Dorrestein P.C., Glass C.K., Rosenfeld M.G.;
"PHF8 mediates histone H4 lysine 20 demethylation events involved in
cell cycle progression.";
Nature 466:508-512(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804; SER-857 AND
SER-880, 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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854; SER-857 AND
SER-880, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-722; SER-804;
SER-857 AND SER-880, 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).
[24]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 122-483 IN COMPLEX WITH IRON
AND ALPHA-KETOGLUTARATE, FUNCTION, AND CHARACTERIZATION OF VARIANT
MRXSSD SER-315.
PubMed=20101266; DOI=10.1038/cr.2010.8;
Yu L., Wang Y., Huang S., Wang J., Deng Z., Zhang Q., Wu W., Zhang X.,
Liu Z., Gong W., Chen Z.;
"Structural insights into a novel histone demethylase PHF8.";
Cell Res. 20:166-173(2010).
[25]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 115-483.
PubMed=20067792; DOI=10.1016/j.febslet.2009.12.055;
Yue W.W., Hozjan V., Ge W., Loenarz C., Cooper C.D., Schofield C.J.,
Kavanagh K.L., Oppermann U., McDonough M.A.;
"Crystal structure of the PHF8 Jumonji domain, an N(epsilon)-methyl
lysine demethylase.";
FEBS Lett. 584:825-830(2010).
[26]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-447 IN COMPLEX WITH IRON
AND N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND DOMAIN LINKER AND
PHD-FINGER.
PubMed=20023638; DOI=10.1038/nsmb.1753;
Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X.;
"Enzymatic and structural insights for substrate specificity of a
family of jumonji histone lysine demethylases.";
Nat. Struct. Mol. Biol. 17:38-43(2010).
[27]
VARIANT MRXSSD SER-315.
PubMed=17661819; DOI=10.1111/j.1399-0004.2007.00836.x;
Koivisto A.M., Ala-Mello S., Lemmelae S., Komu H.A., Rautio J.,
Jaervelae I.;
"Screening of mutations in the PHF8 gene and identification of a novel
mutation in a Finnish family with XLMR and cleft lip/cleft palate.";
Clin. Genet. 72:145-149(2007).
[28]
VARIANT SER-969 DEL.
PubMed=23092983; DOI=10.1038/tp.2012.102;
Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B.,
Cohen D., Faudet A., Bouteiller D., Gilleron M., Jacquette A.,
Whalen S., Afenjar A., Perisse D., Laurent C., Dupuits C., Gautier C.,
Gerard M., Huguet G., Caillet S., Leheup B., Leboyer M., Gillberg C.,
Delorme R., Bourgeron T., Brice A., Depienne C.;
"Analysis of the chromosome X exome in patients with autism spectrum
disorders identified novel candidate genes, including TMLHE.";
Transl. Psychiatry 2:E179-E179(2012).
-!- FUNCTION: Histone lysine demethylase with selectivity for the
di- and monomethyl states that plays a key role cell cycle
progression, rDNA transcription and brain development.
Demethylates mono- and dimethylated histone H3 'Lys-9' residue
(H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and
monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a
transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1
are epigenetic repressive marks. Involved in cell cycle
progression by being required to control G1-S transition. Acts as
a coactivator of rDNA transcription, by activating polymerase I
(pol I) mediated transcription of rRNA genes. Required for brain
development, probably by regulating expression of neuron-specific
genes. Only has activity toward H4K20Me1 when nucleosome is used
as a substrate and when not histone octamer is used as substrate.
May also have weak activity toward dimethylated H3 'Lys-36'
(H3K36Me2), however, the relevance of this result remains unsure
in vivo. Specifically binds trimethylated 'Lys-4' of histone H3
(H3K4me3), affecting histone demethylase specificity: has weak
activity toward H3K9Me2 in absence of H3K4me3, while it has high
activity toward H3K9me2 when binding H3K4me3.
{ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20023638,
ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542,
ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419,
ECO:0000269|PubMed:20531378, ECO:0000269|PubMed:20548336,
ECO:0000269|PubMed:20622853, ECO:0000269|PubMed:20622854}.
-!- 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:0000269|PubMed:19843542,
ECO:0000269|PubMed:20023638}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000305|PubMed:19843542,
ECO:0000305|PubMed:20023638};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:19843542,
ECO:0000305|PubMed:20023638};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=134 uM for histone H3 H3K9Me2 {ECO:0000269|PubMed:20023638};
KM=8 uM for histone H3 H3K4me3 and H3K9Me2
{ECO:0000269|PubMed:20023638};
-!- SUBUNIT: Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and
ZNF711. {ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20101266,
ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20346720,
ECO:0000269|PubMed:20622854}.
-!- INTERACTION:
P51610-1:HCFC1; NbExp=2; IntAct=EBI-6601215, EBI-396188;
Q15156:PML-RAR; NbExp=6; IntAct=EBI-6601215, EBI-867256;
P10276:RARA; NbExp=2; IntAct=EBI-6601215, EBI-413374;
Q06330:RBPJ; NbExp=2; IntAct=EBI-1560800, EBI-632552;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Note=Recruited
to H3K4me3 sites on chromatin during interphase. Dissociates from
chromatin when cells enter mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q9UPP1-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPP1-2; Sequence=VSP_014964;
Name=3;
IsoId=Q9UPP1-3; Sequence=VSP_014965;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9UPP1-4; Sequence=VSP_014964, VSP_014965, VSP_043640;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9UPP1-5; Sequence=VSP_014964, VSP_054019, VSP_054020,
VSP_054021;
-!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
Binding to H3K4me3 promotes its access to H3K9me2.
-!- DOMAIN: The linker region is a critical determinant of demethylase
specificity. It enables the active site of JmjC to reach the
target H3K9me2 when the PHD-type zinc finger binds to H3K4me3.
-!- PTM: Phosphorylation at Ser-69 and Ser-120 are required for
dissociation from chromatin and accumulation of H4K20Me1 levels
during prophase. {ECO:0000269|PubMed:20622854}.
-!- DISEASE: Mental retardation, X-linked, syndromic, Siderius type
(MRXSSD) [MIM:300263]: A syndrome characterized by mild to
borderline mental retardation with or without cleft lip/cleft
palate. {ECO:0000269|PubMed:16199551, ECO:0000269|PubMed:17661819,
ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542,
ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419,
ECO:0000269|PubMed:20548336, ECO:0000269|PubMed:20622853,
ECO:0000269|PubMed:20622854}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
JHDM1D subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA83063.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB13877.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAI45929.1; Type=Erroneous termination; Positions=419; Note=Translated as Arg.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB029034; BAA83063.1; ALT_INIT; mRNA.
EMBL; CR933612; CAI45929.1; ALT_SEQ; mRNA.
EMBL; AK021696; BAB13877.1; ALT_INIT; mRNA.
EMBL; AK022788; BAG51116.1; -; mRNA.
EMBL; AK304272; BAH14147.1; -; mRNA.
EMBL; AL589872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL732374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z98051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC042108; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC053861; AAH53861.1; -; mRNA.
CCDS; CCDS14355.1; -. [Q9UPP1-2]
CCDS; CCDS55418.1; -. [Q9UPP1-4]
CCDS; CCDS55419.1; -. [Q9UPP1-5]
CCDS; CCDS55420.1; -. [Q9UPP1-1]
RefSeq; NP_001171825.1; NM_001184896.1. [Q9UPP1-1]
RefSeq; NP_001171826.1; NM_001184897.1. [Q9UPP1-4]
RefSeq; NP_055922.1; NM_015107.2. [Q9UPP1-2]
RefSeq; XP_016884851.1; XM_017029362.1. [Q9UPP1-2]
UniGene; Hs.133352; -.
PDB; 2WWU; X-ray; 2.15 A; A=115-483.
PDB; 3K3N; X-ray; 2.40 A; A=122-483.
PDB; 3K3O; X-ray; 2.10 A; A=122-483.
PDB; 3KV4; X-ray; 2.19 A; A=37-483.
PDB; 4DO0; X-ray; 2.55 A; A=115-483.
PDBsum; 2WWU; -.
PDBsum; 3K3N; -.
PDBsum; 3K3O; -.
PDBsum; 3KV4; -.
PDBsum; 4DO0; -.
ProteinModelPortal; Q9UPP1; -.
SMR; Q9UPP1; -.
BioGrid; 116751; 78.
DIP; DIP-38913N; -.
IntAct; Q9UPP1; 37.
MINT; MINT-4651164; -.
STRING; 9606.ENSP00000350676; -.
BindingDB; Q9UPP1; -.
ChEMBL; CHEMBL1938212; -.
GuidetoPHARMACOLOGY; 2698; -.
iPTMnet; Q9UPP1; -.
PhosphoSitePlus; Q9UPP1; -.
SwissPalm; Q9UPP1; -.
BioMuta; PHF8; -.
DMDM; 73620986; -.
EPD; Q9UPP1; -.
PaxDb; Q9UPP1; -.
PeptideAtlas; Q9UPP1; -.
PRIDE; Q9UPP1; -.
Ensembl; ENST00000322659; ENSP00000319473; ENSG00000172943. [Q9UPP1-5]
Ensembl; ENST00000338154; ENSP00000338868; ENSG00000172943. [Q9UPP1-2]
Ensembl; ENST00000338946; ENSP00000340051; ENSG00000172943. [Q9UPP1-4]
Ensembl; ENST00000357988; ENSP00000350676; ENSG00000172943. [Q9UPP1-1]
GeneID; 23133; -.
KEGG; hsa:23133; -.
UCSC; uc004dst.4; human. [Q9UPP1-1]
CTD; 23133; -.
DisGeNET; 23133; -.
EuPathDB; HostDB:ENSG00000172943.18; -.
GeneCards; PHF8; -.
HGNC; HGNC:20672; PHF8.
HPA; HPA038779; -.
HPA; HPA062015; -.
MalaCards; PHF8; -.
MIM; 300263; phenotype.
MIM; 300560; gene.
neXtProt; NX_Q9UPP1; -.
OpenTargets; ENSG00000172943; -.
Orphanet; 85287; X-linked intellectual disability, Siderius type.
PharmGKB; PA134889361; -.
eggNOG; KOG1633; Eukaryota.
eggNOG; ENOG410XQXU; LUCA.
GeneTree; ENSGT00550000074396; -.
HOGENOM; HOG000231232; -.
HOVERGEN; HBG045631; -.
InParanoid; Q9UPP1; -.
KO; K19415; -.
OMA; PKFPRKL; -.
OrthoDB; EOG091G09DB; -.
PhylomeDB; Q9UPP1; -.
TreeFam; TF106480; -.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-3214842; HDMs demethylate histones.
ChiTaRS; PHF8; human.
EvolutionaryTrace; Q9UPP1; -.
GeneWiki; PHF8; -.
GenomeRNAi; 23133; -.
PRO; PR:Q9UPP1; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000172943; -.
CleanEx; HS_PHF8; -.
ExpressionAtlas; Q9UPP1; baseline and differential.
Genevisible; Q9UPP1; HS.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0032452; F:histone demethylase activity; IDA:UniProtKB.
GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IDA:UniProtKB.
GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IDA:UniProtKB.
GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0035575; F:histone demethylase activity (H4-K20 specific); IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007420; P:brain development; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0071557; P:histone H3-K27 demethylation; IDA:UniProtKB.
GO; GO:0070544; P:histone H3-K36 demethylation; IDA:UniProtKB.
GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
GO; GO:0035574; P:histone H4-K20 demethylation; IDA:UniProtKB.
GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; IDA:UniProtKB.
GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF02373; JmjC; 1.
Pfam; PF00628; PHD; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell cycle;
Chromatin regulator; Complete proteome; Dioxygenase; Disease mutation;
Iron; Mental retardation; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1060 Histone lysine demethylase PHF8.
/FTId=PRO_0000059295.
DOMAIN 231 387 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
ZN_FING 41 92 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 101 115 Linker.
COMPBIAS 769 807 Ser-rich.
METAL 283 283 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000269|PubMed:20023638,
ECO:0000269|PubMed:20101266}.
METAL 285 285 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000269|PubMed:20023638,
ECO:0000269|PubMed:20101266}.
METAL 355 355 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538,
ECO:0000269|PubMed:20023638,
ECO:0000269|PubMed:20101266}.
BINDING 280 280 Substrate.
BINDING 300 300 Substrate.
MOD_RES 69 69 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:20622854}.
MOD_RES 120 120 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:20622854}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 704 704 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q80TJ7}.
MOD_RES 705 705 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 706 706 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 722 722 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 804 804 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TJ7}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000250|UniProtKB:Q80TJ7}.
MOD_RES 854 854 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 880 880 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 36 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_014964.
VAR_SEQ 478 578 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014965.
VAR_SEQ 717 746 KLGNGSGAGGILDLLKASRQVGGPDYAALT -> YQTATPA
PAQGAS (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054019.
VAR_SEQ 920 931 ELQKAQKKKYIK -> VKKMKLSLTDSG (in isoform
5). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_054020.
VAR_SEQ 932 1060 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054021.
VAR_SEQ 1060 1060 L -> LRQVIVQAECRQAIHEPKLKRRDAHP (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043640.
VARIANT 315 315 F -> S (in MRXSSD; abolishes histone
methyltransferase activity;
dbSNP:rs121918524).
{ECO:0000269|PubMed:17661819,
ECO:0000269|PubMed:20101266,
ECO:0000269|PubMed:20208542,
ECO:0000269|PubMed:20346720,
ECO:0000269|PubMed:20421419,
ECO:0000269|PubMed:20548336,
ECO:0000269|PubMed:20622853,
ECO:0000269|PubMed:20622854}.
/FTId=VAR_062250.
VARIANT 969 969 Missing (found in patients with autism
spectrum disorders; unknown pathological
significance).
{ECO:0000269|PubMed:23092983}.
/FTId=VAR_076254.
MUTAGEN 43 43 Y->A: Abolishes binding to H3K4me3; when
associated with A-50.
{ECO:0000269|PubMed:20208542,
ECO:0000269|PubMed:20622853}.
MUTAGEN 50 50 Y->A: Abolishes binding to H3K4me3; when
associated with A-43. Abolishes binding
to H3K4me3; when associated with A-65.
{ECO:0000269|PubMed:20622853}.
MUTAGEN 65 65 W->A: Abolishes binding to H3K4me3; when
associated with A-50.
{ECO:0000269|PubMed:20622853}.
MUTAGEN 69 69 S->A: Impairs phosphorylation by CDK1 and
dissociation from chromatin when cells
enter mitosis; when associated with A-
120. {ECO:0000269|PubMed:20622854}.
MUTAGEN 120 120 S->A: Impairs phosphorylation by CDK1 and
dissociation from chromatin when cells
enter mitosis; when associated with A-69.
{ECO:0000269|PubMed:20622854}.
MUTAGEN 283 285 HID->AAA: Abolishes histone
methyltransferase activity.
{ECO:0000269|PubMed:20208542}.
MUTAGEN 283 283 H->A: Abolishes histone methyltransferase
activity. {ECO:0000269|PubMed:20346720,
ECO:0000269|PubMed:20531378,
ECO:0000269|PubMed:20622854}.
CONFLICT 232 232 S -> P (in Ref. 2; BAB13877).
{ECO:0000305}.
TURN 44 47 {ECO:0000244|PDB:3KV4}.
STRAND 56 58 {ECO:0000244|PDB:3KV4}.
TURN 60 62 {ECO:0000244|PDB:3KV4}.
STRAND 65 67 {ECO:0000244|PDB:3KV4}.
HELIX 68 71 {ECO:0000244|PDB:3KV4}.
HELIX 75 78 {ECO:0000244|PDB:3KV4}.
STRAND 81 83 {ECO:0000244|PDB:3KV4}.
HELIX 87 93 {ECO:0000244|PDB:3KV4}.
HELIX 121 129 {ECO:0000244|PDB:2WWU}.
TURN 136 138 {ECO:0000244|PDB:3K3O}.
TURN 144 146 {ECO:0000244|PDB:3K3O}.
HELIX 149 155 {ECO:0000244|PDB:3K3O}.
STRAND 161 165 {ECO:0000244|PDB:3K3O}.
TURN 167 170 {ECO:0000244|PDB:4DO0}.
HELIX 180 187 {ECO:0000244|PDB:3K3O}.
STRAND 192 197 {ECO:0000244|PDB:3K3O}.
TURN 198 201 {ECO:0000244|PDB:3K3O}.
STRAND 202 207 {ECO:0000244|PDB:3K3O}.
HELIX 208 215 {ECO:0000244|PDB:3K3O}.
STRAND 224 230 {ECO:0000244|PDB:3K3O}.
HELIX 235 238 {ECO:0000244|PDB:3K3O}.
HELIX 244 249 {ECO:0000244|PDB:3K3O}.
HELIX 251 255 {ECO:0000244|PDB:3K3O}.
STRAND 270 274 {ECO:0000244|PDB:3K3O}.
STRAND 278 283 {ECO:0000244|PDB:3K3O}.
HELIX 286 288 {ECO:0000244|PDB:3K3O}.
STRAND 290 305 {ECO:0000244|PDB:3K3O}.
HELIX 309 319 {ECO:0000244|PDB:3K3O}.
HELIX 324 326 {ECO:0000244|PDB:3K3O}.
HELIX 329 331 {ECO:0000244|PDB:3K3O}.
STRAND 332 334 {ECO:0000244|PDB:3K3N}.
STRAND 337 342 {ECO:0000244|PDB:3K3O}.
STRAND 346 349 {ECO:0000244|PDB:3K3O}.
STRAND 354 370 {ECO:0000244|PDB:3K3O}.
STRAND 373 375 {ECO:0000244|PDB:3K3N}.
HELIX 376 389 {ECO:0000244|PDB:3K3O}.
HELIX 393 395 {ECO:0000244|PDB:3KV4}.
HELIX 400 420 {ECO:0000244|PDB:3K3O}.
HELIX 427 444 {ECO:0000244|PDB:3K3O}.
TURN 446 448 {ECO:0000244|PDB:3K3O}.
HELIX 449 451 {ECO:0000244|PDB:3K3O}.
HELIX 453 455 {ECO:0000244|PDB:3K3O}.
HELIX 462 477 {ECO:0000244|PDB:3K3O}.
SEQUENCE 1060 AA; 117864 MW; 04C83D7C5E9E56B8 CRC64;
MNRSRAIVQR GRVLPPPAPL DTTNLAGRRT LQGRAKMASV PVYCLCRLPY DVTRFMIECD
MCQDWFHGSC VGVEEEKAAD IDLYHCPNCE VLHGPSIMKK RRGSSKGHDT HKGKPVKTGS
PTFVRELRSR TFDSSDEVIL KPTGNQLTVE FLEENSFSVP ILVLKKDGLG MTLPSPSFTV
RDVEHYVGSD KEIDVIDVTR QADCKMKLGD FVKYYYSGKR EKVLNVISLE FSDTRLSNLV
ETPKIVRKLS WVENLWPEEC VFERPNVQKY CLMSVRDSYT DFHIDFGGTS VWYHVLKGEK
IFYLIRPTNA NLTLFECWSS SSNQNEMFFG DQVDKCYKCS VKQGQTLFIP TGWIHAVLTP
VDCLAFGGNF LHSLNIEMQL KAYEIEKRLS TADLFRFPNF ETICWYVGKH ILDIFRGLRE
NRRHPASYLV HGGKALNLAF RAWTRKEALP DHEDEIPETV RTVQLIKDLA REIRLVEDIF
QQNVGKTSNI FGLQRIFPAG SIPLTRPAHS TSVSMSRLSL PSKNGSKKKG LKPKELFKKA
ERKGKESSAL GPAGQLSYNL MDTYSHQALK TGSFQKAKFN ITGACLNDSD DDSPDLDLDG
NESPLALLMS NGSTKRVKSL SKSRRTKIAK KVDKARLMAE QVMEDEFDLD SDDELQIDER
LGKEKATLII RPKFPRKLPR AKPCSDPNRV REPGEVEFDI EEDYTTDEDM VEGVEGKLGN
GSGAGGILDL LKASRQVGGP DYAALTEAPA SPSTQEAIQG MLCMANLQSS SSSPATSSLQ
AWWTGGQDRS SGSSSSGLGT VSNSPASQRT PGKRPIKRPA YWRTESEEEE ENASLDEQDS
LGACFKDAEY IYPSLESDDD DPALKSRPKK KKNSDDAPWS PKARVTPTLP KQDRPVREGT
RVASIETGLA AAAAKLAQQE LQKAQKKKYI KKKPLLKEVE QPRPQDSNLS LTVPAPTVAA
TPQLVTSSSP LPPPEPKQEA LSGSLADHEY TARPNAFGMA QANRSTTPMA PGVFLTQRRP
SVGSQSNQAG QGKRPKKGLA TAKQRLGRIL KIHRNGKLLL


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AHP1630T RABBIT ANTI LYSINE-SPECIFIC HISTONE DEMETHYLASE (N-TERMINAL)-POLYCLONAL ANTIBODY 50 |g
AHP1630 RABBIT ANTI LYSINE-SPECIFIC HISTONE DEMETHYLASE (N-TERMINAL)-POLYCLONAL ANTIBODY 0.1 mg
EIAAB24938 ALL1,ALL-1,CXXC7,CXXC-type zinc finger protein 7,Histone-lysine N-methyltransferase MLL,Homo sapiens,HRX,HTRX,Human,KMT2A,KMT2A,Lysine N-methyltransferase 2A,MLL,MLL1,Trithorax-like protein,TRX1,Zinc


 

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