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Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]

 KMT2A_MOUSE             Reviewed;        3966 AA.
P55200; E9QNE7; Q3UEU1; Q3USE7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
30-AUG-2017, entry version 160.
RecName: Full=Histone-lysine N-methyltransferase 2A;
Short=Lysine N-methyltransferase 2A;
EC=2.1.1.43;
AltName: Full=ALL-1;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 1;
AltName: Full=Zinc finger protein HRX;
Contains:
RecName: Full=MLL cleavage product N320;
AltName: Full=N-terminal cleavage product of 320 kDa;
Short=p320;
Contains:
RecName: Full=MLL cleavage product C180;
AltName: Full=C-terminal cleavage product of 180 kDa;
Short=p180;
Name=Kmt2a; Synonyms=All1, Hrx, Mll, Mll1;
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 GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-3966 (ISOFORMS 1 AND 2).
STRAIN=C57BL/6 X CBA, and C57BL/6J; TISSUE=Lung, and Spleen;
PubMed=8327517; DOI=10.1073/pnas.90.13.6350;
Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T.,
Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M.;
"Analysis of the murine All-1 gene reveals conserved domains with
human ALL-1 and identifies a motif shared with DNA
methyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Retina;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-1053; SER-1839;
THR-1847; SER-2100 AND SER-2560, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, 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).
[5]
FUNCTION, AND INTERACTION WITH CLOCK AND ARNTL.
PubMed=21113167; DOI=10.1038/nsmb.1961;
Katada S., Sassone-Corsi P.;
"The histone methyltransferase MLL1 permits the oscillation of
circadian gene expression.";
Nat. Struct. Mol. Biol. 17:1414-1421(2010).
[6]
IDENTIFICATION IN MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30;
KMT2D; RRBP5 AND WDR5.
PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
"Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
methylation within bivalent domains.";
Cell 144:513-525(2011).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237; LYS-371; LYS-2954 AND
LYS-3459, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Histone methyltransferase that plays an essential role
in early development and hematopoiesis. Catalytic subunit of the
MLL1/MLL complex, a multiprotein complex that mediates both
methylation of 'Lys-4' of histone H3 (H3K4me) complex and
acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL
complex, it specifically mediates H3K4me, a specific tag for
epigenetic transcriptional activation. Has weak methyltransferase
activity by itself, and requires other component of the MLL1/MLL
complex to obtain full methyltransferase activity. Has no activity
toward histone H3 phosphorylated on 'Thr-3', less activity toward
H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher
activity toward H3 acetylated on 'Lys-9'. Required for
transcriptional activation of HOXA9. Promotes PPP1R15A-induced
apoptosis (By similarity). Plays a critical role in the control of
circadian gene expression and is essential for the transcriptional
activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer.
Establishes a permissive chromatin state for circadian
transcription by mediating a rhythmic methylation of 'Lys-4' of
histone H3 (H3K4me) and this histone modification directs the
circadian acetylation at H3K9 and H3K14 allowing the recruitment
of CLOCK-ARNTL/BMAL1 to chromatin (PubMed:21113167).
{ECO:0000250|UniProtKB:Q03164, ECO:0000269|PubMed:21113167}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL
cleavage product C180 (via SET and FYRC domains). Interacts with
WDR5; the interaction is direct. Interacts with KAT8/MOF; the
interaction is direct. Interacts with SBF1 and PPP1R15A (By
similarity). Interacts with ZNF335 (By similarity). Component of
some MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCF1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as
well as the facultative components BAP18, CHD8, E2F6, HSP70,
INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1,
PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1,
TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CLOCK and
ARNTL/BMAL1 in a circadian manner. {ECO:0000250|UniProtKB:Q03164,
ECO:0000269|PubMed:21113167, ECO:0000269|PubMed:21335234}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03164}.
-!- SUBCELLULAR LOCATION: MLL cleavage product N320: Nucleus
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: MLL cleavage product C180: Nucleus
{ECO:0000250}. Note=Localizes to a diffuse nuclear pattern when
not associated with MLL cleavage product N320.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P55200-1; Sequence=Displayed;
Name=2;
IsoId=P55200-2; Sequence=VSP_006667;
-!- DOMAIN: The SET domain structure is atypical and is not in an
optimal position to have methyltransferase activity. It requires
other components of the MLL1/MLL complex, such as ASH2L or RBBP5,
to order the active site and obtain optimal histone
methyltransferase activity. {ECO:0000250|UniProtKB:Q03164}.
-!- DOMAIN: The CXXC-type zinc finger binds bind to nonmethyl-CpG
dinucleotides. {ECO:0000250|UniProtKB:Q03164}.
-!- PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product
N320 and MLL cleavage product C180, which reassemble through a
non-covalent association. 2 cleavage sites exist, cleavage site 1
(CS1) and cleavage site 2 (CS2), to generate MLL cleavage products
N320 and C180. CS2 is the major site.
{ECO:0000250|UniProtKB:Q03164}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=BAE24386.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AC061963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC142113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L17069; AAA62593.1; -; mRNA.
EMBL; AK140439; BAE24386.1; ALT_INIT; mRNA.
EMBL; AK149341; BAE28820.1; -; mRNA.
CCDS; CCDS40603.1; -. [P55200-2]
RefSeq; NP_001074518.1; NM_001081049.1. [P55200-2]
UniGene; Mm.2389; -.
ProteinModelPortal; P55200; -.
SMR; P55200; -.
BioGrid; 229502; 6.
DIP; DIP-58597N; -.
IntAct; P55200; 1.
MINT; MINT-4084570; -.
STRING; 10090.ENSMUSP00000002095; -.
iPTMnet; P55200; -.
PhosphoSitePlus; P55200; -.
MaxQB; P55200; -.
PaxDb; P55200; -.
PeptideAtlas; P55200; -.
PRIDE; P55200; -.
Ensembl; ENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028. [P55200-2]
Ensembl; ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028. [P55200-1]
GeneID; 214162; -.
KEGG; mmu:214162; -.
UCSC; uc009pep.1; mouse. [P55200-2]
UCSC; uc009peq.1; mouse. [P55200-1]
CTD; 4297; -.
MGI; MGI:96995; Kmt2a.
eggNOG; KOG1084; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOGENOM; HOG000112954; -.
HOVERGEN; HBG051927; -.
InParanoid; P55200; -.
KO; K09186; -.
OMA; RIMSPMR; -.
OrthoDB; EOG091G001P; -.
TreeFam; TF319820; -.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
PRO; PR:P55200; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000002028; -.
CleanEx; MM_MLL1; -.
ExpressionAtlas; P55200; baseline and differential.
Genevisible; P55200; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0050890; P:cognition; IMP:MGI.
GO; GO:0060216; P:definitive hemopoiesis; IMP:CACAO.
GO; GO:0006306; P:DNA methylation; IMP:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
GO; GO:0035640; P:exploration behavior; IMP:MGI.
GO; GO:0044648; P:histone H3-K4 dimethylation; IMP:MGI.
GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:MGI.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:MGI.
GO; GO:2001040; P:positive regulation of cellular response to drug; ISO:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032411; P:positive regulation of transporter activity; ISO:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0006461; P:protein complex assembly; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0071440; P:regulation of histone H3-K14 acetylation; IMP:UniProtKB.
GO; GO:1901674; P:regulation of histone H3-K27 acetylation; IMP:MGI.
GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
GO; GO:2000615; P:regulation of histone H3-K9 acetylation; IMP:UniProtKB.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0009416; P:response to light stimulus; IMP:MGI.
GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0008542; P:visual learning; IMP:MGI.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR001487; Bromodomain.
InterPro; IPR034732; EPHD.
InterPro; IPR003889; FYrich_C.
InterPro; IPR003888; FYrich_N.
InterPro; IPR016569; MeTrfase_trithorax.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
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; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 2.
Pfam; PF00856; SET; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
SMART; SM00297; BROMO; 1.
SMART; SM00542; FYRC; 1.
SMART; SM00541; FYRN; 1.
SMART; SM00249; PHD; 4.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51805; EPHD; 1.
PROSITE; PS51543; FYRC; 1.
PROSITE; PS51542; FYRN; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS51058; ZF_CXXC; 1.
PROSITE; PS01359; ZF_PHD_1; 3.
PROSITE; PS50016; ZF_PHD_2; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Biological rhythms; Bromodomain;
Chromatin regulator; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 3966 Histone-lysine N-methyltransferase 2A.
/FTId=PRO_0000124877.
CHAIN 1 2714 MLL cleavage product N320. {ECO:0000250}.
/FTId=PRO_0000390951.
CHAIN 2715 3966 MLL cleavage product C180. {ECO:0000250}.
/FTId=PRO_0000390952.
DOMAIN 1705 1750 Bromo; divergent. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 2020 2076 FYR N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00875}.
DOMAIN 3663 3744 FYR C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00876}.
DOMAIN 3826 3942 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 3950 3966 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 167 178 A.T hook 1.
DNA_BIND 215 225 A.T hook 2.
DNA_BIND 299 307 A.T hook 3.
ZN_FING 1144 1192 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 1430 1481 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1478 1532 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1565 1629 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1872 1912 C2HC pre-PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 1933 1980 PHD-type 4. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 3903 3904 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COMPBIAS 14 150 Gly-rich.
COMPBIAS 17 100 Ala/Gly/Ser-rich.
COMPBIAS 80 99 Ser-rich.
COMPBIAS 135 141 Poly-Gly.
COMPBIAS 199 287 Lys-rich.
COMPBIAS 443 491 Ser-rich.
COMPBIAS 559 601 Pro-rich.
COMPBIAS 559 562 Poly-Pro.
COMPBIAS 566 569 Poly-Pro.
COMPBIAS 703 807 Ser-rich.
COMPBIAS 1234 1366 Pro-rich.
COMPBIAS 1819 1867 Pro-rich.
COMPBIAS 2185 2320 Ser-rich.
METAL 3906 3906 Zinc. {ECO:0000250|UniProtKB:Q03164}.
METAL 3954 3954 Zinc. {ECO:0000250|UniProtKB:Q03164}.
METAL 3956 3956 Zinc. {ECO:0000250|UniProtKB:Q03164}.
METAL 3961 3961 Zinc. {ECO:0000250|UniProtKB:Q03164}.
BINDING 3836 3836 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3838 3838 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3880 3880 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 3955 3955 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
SITE 2662 2663 Cleavage; by TASP1, site 1.
{ECO:0000250|UniProtKB:Q03164}.
SITE 2714 2715 Cleavage; by TASP1, site 2.
{ECO:0000250|UniProtKB:Q03164}.
SITE 3762 3762 Important for WDR5-recognition and
binding. {ECO:0000250|UniProtKB:Q03164}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 237 237 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 371 371 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 634 634 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 837 837 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 923 923 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 1053 1053 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1127 1127 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 1232 1232 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 1839 1839 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1847 1847 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1860 1860 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2100 2100 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2148 2148 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2152 2152 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2202 2202 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2560 2560 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2607 2607 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2792 2792 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2951 2951 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 2954 2954 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 3032 3032 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 3369 3369 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 3459 3459 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 3510 3510 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
MOD_RES 3523 3523 Phosphoserine.
{ECO:0000250|UniProtKB:Q03164}.
CROSSLNK 2524 2524 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q03164}.
VAR_SEQ 1603 1605 Missing (in isoform 2).
{ECO:0000303|PubMed:8327517}.
/FTId=VSP_006667.
VARIANT 1597 1597 K -> T.
CONFLICT 372 372 Q -> E (in Ref. 3; BAE28820).
{ECO:0000305}.
CONFLICT 554 554 Q -> K (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 564 564 L -> F (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 797 797 P -> S (in Ref. 3; BAE28820).
{ECO:0000305}.
CONFLICT 806 806 E -> D (in Ref. 2; AAA62593 and 3;
BAE28820). {ECO:0000305}.
CONFLICT 821 821 L -> P (in Ref. 2; AAA62593 and 3;
BAE28820). {ECO:0000305}.
CONFLICT 1069 1069 C -> Y (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 1230 1230 A -> S (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 1349 1349 R -> L (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 1437 1437 A -> S (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 1440 1440 G -> E (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 1632 1632 A -> P (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 2292 2292 S -> L (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 3481 3481 N -> I (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 3493 3493 R -> S (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 3548 3548 G -> V (in Ref. 2; AAA62593).
{ECO:0000305}.
CONFLICT 3769 3769 Q -> K (in Ref. 2; AAA62593).
{ECO:0000305}.
SEQUENCE 3966 AA; 429649 MW; EA9CB2A467AB3545 CRC64;
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV
AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI
GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG
SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA
ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR
RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP
SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII
KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP
SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA
TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA
PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG
FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT
SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI
PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS
QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS
ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK
KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV
ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR
AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE
PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK
ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP
RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK
AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN
PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG
HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK
LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA
YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE
SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI
NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL
DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS
PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL
KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR
DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS
DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS
PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC
RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY
SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG
SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE
LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL
KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP
EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV
TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ
SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED
IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR
EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK
EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY
NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD
SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ
NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI
SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV
QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP
MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL
LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA
PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP
QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT
LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA
SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS
NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ
LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE
CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER
KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL
HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRQS AFDMFNFLAS
KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL
FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR
FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK
CRKFLN


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