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

Set1/Ash2 histone methyltransferase complex subunit ASH2 (ASH2-like protein)

 ASH2L_HUMAN             Reviewed;         628 AA.
Q9UBL3; A8K7C3; D3DSW9; O60659; O60660; Q96B62;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Set1/Ash2 histone methyltransferase complex subunit ASH2;
AltName: Full=ASH2-like protein;
Name=ASH2L; Synonyms=ASH2L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fetal brain;
PubMed=11466562; DOI=10.1007/s001090100222;
Wang J., Zhou Y., Yin B., Du G., Huang X., Li G., Shen Y., Yuan J.,
Qiang B.;
"ASH2L: alternative splicing and downregulation during induced
megakaryocytic differentiation of multipotential leukemia cell
lines.";
J. Mol. Med. 79:399-405(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=10393421;
Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.;
"Cloning and characterization of ASH2L and ash2l, human and mouse
homologs of the Drosophila ash2 gene.";
Cytogenet. Cell Genet. 84:167-172(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Skin;
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).
[6]
FUNCTION, AND INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[7]
IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE
COMPLEX.
PubMed=14992727; DOI=10.1016/S1097-2765(04)00081-4;
Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D.,
Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A.,
Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
"Menin associates with a trithorax family histone methyltransferase
complex and with the hoxc8 locus.";
Mol. Cell 13:587-597(2004).
[8]
IDENTIFICATION IN THE MLL-LIKE COMPLEX.
PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
Kitabayashi I., Herr W., Cleary M.L.;
"Leukemia proto-oncoprotein MLL forms a SET1-like histone
methyltransferase complex with menin to regulate Hox gene
expression.";
Mol. Cell. Biol. 24:5639-5649(2004).
[9]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[10]
IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=16253997; DOI=10.1074/jbc.M508312200;
Lee J.-H., Skalnik D.G.;
"CpG-binding protein (CXXC finger protein 1) is a component of the
mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue
of the yeast Set1/COMPASS complex.";
J. Biol. Chem. 280:41725-41731(2005).
[11]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
PubMed=17355966; DOI=10.1074/jbc.M609809200;
Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
"Identification and characterization of the human Set1B histone H3-
Lys4 methyltransferase complex.";
J. Biol. Chem. 282:13419-13428(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
COMPLEX.
PubMed=17500065; DOI=10.1074/jbc.M701574200;
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
methyltransferase complex.";
J. Biol. Chem. 282:20395-20406(2007).
[13]
IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A AND
SETD1B.
PubMed=17998332; DOI=10.1128/MCB.01356-07;
Lee J.H., Skalnik D.G.;
"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
Histone H3-Lys4 methyltransferase complex to transcription start sites
of transcribed human genes.";
Mol. Cell. Biol. 28:609-618(2008).
[14]
IDENTIFICATION IN SET1 COMPLEX.
PubMed=18838538; DOI=10.1128/MCB.00976-08;
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
Shilatifard A.;
"Molecular regulation of H3K4 trimethylation by Wdr82, a component of
human Set1/COMPASS.";
Mol. Cell. Biol. 28:7337-7344(2008).
[15]
FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, AND INTERACTION
WITH DPY30 AND RBBP5.
PubMed=19556245; DOI=10.1074/jbc.M109.014498;
Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
"On the mechanism of multiple lysine methylation by the human mixed
lineage leukemia protein-1 (MLL1) core complex.";
J. Biol. Chem. 284:24242-24256(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, 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).
[17]
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).
[18]
METHYLATION AT ARG-296 BY PRMT1 AND PRMT5, AND MUTAGENESIS OF ARG-296
AND ARG-300.
PubMed=21285357; DOI=10.1074/jbc.M110.202416;
Butler J.S., Zurita-Lopez C.I., Clarke S.G., Bedford M.T., Dent S.Y.;
"Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a
shared component of mammalian histone H3K4 methyltransferase
complexes.";
J. Biol. Chem. 286:12234-12244(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 2 AND 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 96-271, DOMAIN PHD, AND
DNA-BINDING REGION.
PubMed=21660059; DOI=10.1038/embor.2011.101;
Chen Y., Wan B., Wang K.C., Cao F., Yang Y., Protacio A., Dou Y.,
Chang H.Y., Lei M.;
"Crystal structure of the N-terminal region of human Ash2L shows a
winged-helix motif involved in DNA binding.";
EMBO Rep. 12:797-803(2011).
-!- FUNCTION: Component of the Set1/Ash2 histone methyltransferase
(HMT) complex, a complex that specifically methylates 'Lys-4' of
histone H3, but not if the neighboring 'Lys-9' residue is already
methylated. As part of the MLL1/MLL complex it is involved in
methylation and dimethylation at 'Lys-4' of histone H3. May
function as a transcriptional regulator. May play a role in
hematopoiesis. {ECO:0000269|PubMed:12670868,
ECO:0000269|PubMed:19556245}.
-!- SUBUNIT: Interacts with HCFC1. Core component of several
methyltransferase-containing complexes including MLL1/MLL, MLL2/3
(also named ASCOM complex) and MLL4/WBP7. Each complex is at least
composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific
histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and
KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8,
E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX,
MCRS1, MEN1, MGA, KAT8/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20,
PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with
DPY30 and RBBP5; the interaction is direct. Component of the SET1
complex, at least composed of the catalytic subunit (SETD1A or
SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and
DPY30. Interacts with SETD1A and SETD1B.
{ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:15199122, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:16253997, ECO:0000269|PubMed:17355966,
ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17998332,
ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:19556245}.
-!- INTERACTION:
O43823:AKAP8; NbExp=3; IntAct=EBI-540797, EBI-1237481;
P10275:AR; NbExp=2; IntAct=EBI-540797, EBI-608057;
Q9HCK8:CHD8; NbExp=2; IntAct=EBI-540797, EBI-1169146;
Q9C005:DPY30; NbExp=18; IntAct=EBI-540797, EBI-744973;
Q09472:EP300; NbExp=5; IntAct=EBI-540797, EBI-447295;
P51610:HCFC1; NbExp=5; IntAct=EBI-540797, EBI-396176;
Q03164:KMT2A; NbExp=4; IntAct=EBI-16130425, EBI-591370;
Q9UMN6:KMT2B; NbExp=2; IntAct=EBI-16130425, EBI-765774;
Q8NEZ4:KMT2C; NbExp=5; IntAct=EBI-16130425, EBI-1042997;
O14686:KMT2D; NbExp=2; IntAct=EBI-16130425, EBI-996065;
Q14686:NCOA6; NbExp=13; IntAct=EBI-540797, EBI-78670;
Q6ZW49:PAXIP1; NbExp=11; IntAct=EBI-540797, EBI-743225;
Q15291:RBBP5; NbExp=32; IntAct=EBI-540797, EBI-592823;
O15047:SETD1A; NbExp=2; IntAct=EBI-16130425, EBI-540779;
Q9UPS6-2:SETD1B; NbExp=2; IntAct=EBI-16130425, EBI-16197836;
P04637:TP53; NbExp=7; IntAct=EBI-540797, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17355966}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ASH2L1;
IsoId=Q9UBL3-1; Sequence=Displayed;
Name=2; Synonyms=ASH2L2;
IsoId=Q9UBL3-2; Sequence=VSP_007577, VSP_007578;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
Name=3;
IsoId=Q9UBL3-3; Sequence=VSP_007577;
Note=No experimental confirmation available. Contains a
N-acetylmethionine at position 1. {ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Predominantly
expressed in adult heart and testis and fetal lung and liver, with
barely detectable expression in adult lung, liver, kidney,
prostate, and peripheral leukocytes.
{ECO:0000269|PubMed:10393421}.
-!- PTM: Both monomethylated and dimethylated on arginine residues in
the C-terminus. Arg-296 is the major site. Methylation is not
required for nuclear localization, nor for MLL complex integrity
or maintenance of global histone H3K4me3 levels.
{ECO:0000269|PubMed:21285357}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ASH2LID44404ch8p11.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF056718; AAC13564.1; -; mRNA.
EMBL; AF056717; AAC13563.1; -; mRNA.
EMBL; AB022785; BAA74520.1; -; Genomic_DNA.
EMBL; AB020982; BAA35127.1; -; mRNA.
EMBL; AK291938; BAF84627.1; -; mRNA.
EMBL; CH471080; EAW63337.1; -; Genomic_DNA.
EMBL; CH471080; EAW63336.1; -; Genomic_DNA.
EMBL; CH471080; EAW63340.1; -; Genomic_DNA.
EMBL; BC015936; AAH15936.1; -; mRNA.
CCDS; CCDS47840.1; -. [Q9UBL3-3]
CCDS; CCDS59100.1; -. [Q9UBL3-2]
CCDS; CCDS6101.1; -. [Q9UBL3-1]
RefSeq; NP_001098684.1; NM_001105214.2. [Q9UBL3-3]
RefSeq; NP_001248761.1; NM_001261832.1. [Q9UBL3-2]
RefSeq; NP_004665.2; NM_004674.4. [Q9UBL3-1]
UniGene; Hs.521530; -.
PDB; 3RSN; X-ray; 2.10 A; A=96-271.
PDB; 3S32; X-ray; 2.45 A; A=95-280.
PDB; 3TOJ; X-ray; 2.07 A; A/B=370-496, A/B=539-617.
PDB; 4RIQ; X-ray; 2.23 A; C/F/I/L/O/R/U/X=603-618.
PDB; 4X8N; X-ray; 2.10 A; A=380-495, A=539-598.
PDB; 4X8P; X-ray; 2.20 A; A=380-495, A=539-598.
PDB; 5F6K; X-ray; 2.41 A; A/B=380-496, A/B=539-598.
PDB; 5F6L; X-ray; 1.90 A; B=380-496, B=539-598.
PDBsum; 3RSN; -.
PDBsum; 3S32; -.
PDBsum; 3TOJ; -.
PDBsum; 4RIQ; -.
PDBsum; 4X8N; -.
PDBsum; 4X8P; -.
PDBsum; 5F6K; -.
PDBsum; 5F6L; -.
ProteinModelPortal; Q9UBL3; -.
SMR; Q9UBL3; -.
BioGrid; 114528; 67.
CORUM; Q9UBL3; -.
DIP; DIP-29222N; -.
IntAct; Q9UBL3; 64.
MINT; MINT-1194078; -.
STRING; 9606.ENSP00000340896; -.
BindingDB; Q9UBL3; -.
ChEMBL; CHEMBL3137282; -.
iPTMnet; Q9UBL3; -.
PhosphoSitePlus; Q9UBL3; -.
BioMuta; ASH2L; -.
DMDM; 32141382; -.
EPD; Q9UBL3; -.
MaxQB; Q9UBL3; -.
PaxDb; Q9UBL3; -.
PeptideAtlas; Q9UBL3; -.
PRIDE; Q9UBL3; -.
Ensembl; ENST00000343823; ENSP00000340896; ENSG00000129691. [Q9UBL3-1]
Ensembl; ENST00000428278; ENSP00000395310; ENSG00000129691. [Q9UBL3-3]
Ensembl; ENST00000521652; ENSP00000430259; ENSG00000129691. [Q9UBL3-2]
GeneID; 9070; -.
KEGG; hsa:9070; -.
UCSC; uc003xkt.6; human. [Q9UBL3-1]
CTD; 9070; -.
DisGeNET; 9070; -.
EuPathDB; HostDB:ENSG00000129691.15; -.
GeneCards; ASH2L; -.
H-InvDB; HIX0007454; -.
HGNC; HGNC:744; ASH2L.
HPA; HPA042289; -.
MIM; 604782; gene.
neXtProt; NX_Q9UBL3; -.
OpenTargets; ENSG00000129691; -.
PharmGKB; PA25044; -.
eggNOG; KOG2626; Eukaryota.
eggNOG; ENOG410Y5GC; LUCA.
GeneTree; ENSGT00390000010474; -.
HOGENOM; HOG000013137; -.
HOVERGEN; HBG050592; -.
InParanoid; Q9UBL3; -.
KO; K14964; -.
OMA; NYVFVCK; -.
OrthoDB; EOG091G069C; -.
PhylomeDB; Q9UBL3; -.
TreeFam; TF314785; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SIGNOR; Q9UBL3; -.
ChiTaRS; ASH2L; human.
GeneWiki; ASH2L; -.
GenomeRNAi; 9070; -.
PRO; PR:Q9UBL3; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000129691; -.
CleanEx; HS_ASH2L; -.
ExpressionAtlas; Q9UBL3; baseline and differential.
Genevisible; Q9UBL3; HS.
GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
GO; GO:0071339; C:MLL1 complex; IEA:Ensembl.
GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IC:UniProtKB.
GO; GO:1990188; F:euchromatin binding; IEA:Ensembl.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR003877; SPRY_dom.
Pfam; PF00622; SPRY; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS50188; B302_SPRY; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 628 Set1/Ash2 histone methyltransferase
complex subunit ASH2.
/FTId=PRO_0000064697.
DOMAIN 360 583 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 1 66 PHD-type; atypical.
ZN_FING 117 150 C4-type.
REGION 67 177 DNA-binding.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 296 296 Asymmetric dimethylarginine; by PRMT1 and
PRMT5. {ECO:0000269|PubMed:21285357}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 94 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11466562,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007577.
VAR_SEQ 541 573 Missing (in isoform 2).
{ECO:0000303|PubMed:11466562}.
/FTId=VSP_007578.
VARIANT 478 478 S -> F (in dbSNP:rs34167006).
/FTId=VAR_050679.
MUTAGEN 296 296 R->K: Abolishes methylation.
{ECO:0000269|PubMed:21285357}.
MUTAGEN 300 300 R->K: Slightly decreased methylation.
{ECO:0000269|PubMed:21285357}.
CONFLICT 212 212 Q -> H (in Ref. 1; AAC13564).
{ECO:0000305}.
CONFLICT 217 217 M -> T (in Ref. 1; AAC13564).
{ECO:0000305}.
CONFLICT 292 292 S -> T (in Ref. 1; AAC13563).
{ECO:0000305}.
CONFLICT 351 351 H -> Q (in Ref. 1; AAC13564).
{ECO:0000305}.
CONFLICT 360 360 L -> I (in Ref. 1; AAC13564).
{ECO:0000305}.
CONFLICT 369 369 P -> S (in Ref. 1; AAC13564).
{ECO:0000305}.
STRAND 114 116 {ECO:0000244|PDB:3RSN}.
TURN 118 120 {ECO:0000244|PDB:3RSN}.
STRAND 123 125 {ECO:0000244|PDB:3RSN}.
HELIX 126 129 {ECO:0000244|PDB:3RSN}.
STRAND 142 146 {ECO:0000244|PDB:3RSN}.
TURN 148 150 {ECO:0000244|PDB:3RSN}.
STRAND 157 160 {ECO:0000244|PDB:3RSN}.
HELIX 165 183 {ECO:0000244|PDB:3RSN}.
TURN 193 196 {ECO:0000244|PDB:3RSN}.
HELIX 197 203 {ECO:0000244|PDB:3RSN}.
HELIX 205 207 {ECO:0000244|PDB:3RSN}.
HELIX 219 221 {ECO:0000244|PDB:3RSN}.
HELIX 223 228 {ECO:0000244|PDB:3RSN}.
TURN 231 233 {ECO:0000244|PDB:3RSN}.
STRAND 234 239 {ECO:0000244|PDB:3RSN}.
HELIX 248 250 {ECO:0000244|PDB:3RSN}.
STRAND 252 257 {ECO:0000244|PDB:3RSN}.
HELIX 261 263 {ECO:0000244|PDB:3RSN}.
HELIX 371 373 {ECO:0000244|PDB:3TOJ}.
STRAND 376 378 {ECO:0000244|PDB:3TOJ}.
STRAND 383 388 {ECO:0000244|PDB:5F6L}.
STRAND 392 394 {ECO:0000244|PDB:5F6L}.
STRAND 398 402 {ECO:0000244|PDB:5F6L}.
STRAND 408 413 {ECO:0000244|PDB:5F6L}.
STRAND 416 429 {ECO:0000244|PDB:5F6L}.
STRAND 435 441 {ECO:0000244|PDB:5F6L}.
STRAND 457 461 {ECO:0000244|PDB:5F6L}.
TURN 462 465 {ECO:0000244|PDB:5F6L}.
STRAND 467 469 {ECO:0000244|PDB:5F6L}.
STRAND 472 474 {ECO:0000244|PDB:5F6L}.
STRAND 485 492 {ECO:0000244|PDB:5F6L}.
STRAND 511 516 {ECO:0000244|PDB:5F6L}.
STRAND 539 541 {ECO:0000244|PDB:4X8N}.
STRAND 542 550 {ECO:0000244|PDB:5F6L}.
STRAND 556 565 {ECO:0000244|PDB:5F6L}.
STRAND 567 571 {ECO:0000244|PDB:5F6L}.
STRAND 573 575 {ECO:0000244|PDB:3TOJ}.
STRAND 583 585 {ECO:0000244|PDB:4X8P}.
HELIX 588 591 {ECO:0000244|PDB:5F6L}.
STRAND 593 596 {ECO:0000244|PDB:3TOJ}.
HELIX 603 615 {ECO:0000244|PDB:4RIQ}.
SEQUENCE 628 AA; 68723 MW; 8F5F007430D4B863 CRC64;
MAAAGAGPGQ EAGAGPGPGA VANATGAEEG EMKPVAAGAA APPGEGISAA PTVEPSSGEA
EGGEANLVDV SGGLETESSN GKDTLEGAGD TSEVMDTQAG SVDEENGRQL GEVELQCGIC
TKWFTADTFG IDTSSCLPFM TNYSFHCNVC HHSGNTYFLR KQANLKEMCL SALANLTWQS
RTQDEHPKTM FSKDKDIIPF IDKYWECMTT RQRPGKMTWP NNIVKTMSKE RDVFLVKEHP
DPGSKDPEED YPKFGLLDQD LSNIGPAYDN QKQSSAVSTS GNLNGGIAAG SSGKGRGAKR
KQQDGGTTGT TKKARSDPLF SAQRLPPHGY PLEHPFNKDG YRYILAEPDP HAPDPEKLEL
DCWAGKPIPG DLYRACLYER VLLALHDRAP QLKISDDRLT VVGEKGYSMV RASHGVRKGA
WYFEITVDEM PPDTAARLGW SQPLGNLQAP LGYDKFSYSW RSKKGTKFHQ SIGKHYSSGY
GQGDVLGFYI NLPEDTETAK SLPDTYKDKA LIKFKSYLYF EEKDFVDKAE KSLKQTPHSE
IIFYKNGVNQ GVAYKDIFEG VYFPAISLYK SCTVSINFGP CFKYPPKDLT YRPMSDMGWG
AVVEHTLADV LYHVETEVDG RRSPPWEP


Related products :

Catalog number Product name Quantity
ASH2L_HUMAN Human ELISA Kit FOR Set1 per Ash2 histone methyltransferase complex subunit ASH2 96T
H0106 Set1 Ash2 histone methyltransferase complex subunit ASH2 (ASH2L), Human, ELISA Kit 96T
H0107 Set1 Ash2 histone methyltransferase complex subunit ASH2 (ASH2L), Mouse, ELISA Kit 96T
ASH2L_MOUSE ELISA Kit FOR Set1 per Ash2 histone methyltransferase complex subunit ASH2; organism: Mouse; gene name: Ash2l 96T
18-003-42495 Set1_Ash2 histone methyltransferase complex subunit ASH2 - ASH2-like protein Polyclonal 0.05 mg Aff Pur
18-003-42495 Set1_Ash2 histone methyltransferase complex subunit ASH2 - ASH2-like protein Polyclonal 0.1 mg Protein A
ARP34203_P100 Anti-Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) Species_Reactivity: Human
ARP34203_P050 Anti-Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) Species_Reactivity: Human
CSB-EL002210HU Human Set1_Ash2 histone methyltransferase complex subunit ASH2(ASH2L) ELISA kit 96T
CSB-EL002210MO Mouse Set1_Ash2 histone methyltransferase complex subunit ASH2(ASH2L) ELISA kit 96T
ARP34203_T200 Anti-Set1_Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) Species_Reactivity: Human
CSB-EL002210MO Mouse Set1_Ash2 histone methyltransferase complex subunit ASH2(ASH2L) ELISA kit SpeciesMouse 96T
CSB-EL002210HU Human Set1_Ash2 histone methyltransferase complex subunit ASH2(ASH2L) ELISA kit SpeciesHuman 96T
20-372-60155 ash2 (absent. small. or homeotic)-like (Drosophila) (ASH2L) - Mouse monoclonal anti-human ASH2L antibody; ASH2-like protein Monoclonal 0.1 mg
3772-100 ASH2 Antibody 100 ug
3772-100 ASH2 Antibody 100 µl
3772-100 ASH2 Antibody 100
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
BP300-107 ASH2 Blocking Peptide 50 ug
BP300-108 ASH2 Blocking Peptide 50 ug
BP300-112 ASH2 Blocking Peptide 50 ug
BP300-489 ASH2 Blocking Peptide 50 ug
Y051218 Anti-ASH2 antibody 250ug
3772-100 ASH2 Polyclonal Antibody100 ul 100 ul
Y051218 Anti-ASH2 Antibody 100μl


 

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

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





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

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

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

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

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

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




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






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






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

GENTAUR Poland Sp. z o.o.


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

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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