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Protein

Set1/Ash2 histone methyltransferase complex subunit ASH2

Gene

Ash2l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 6262PHD-type; atypicalBy similarityAdd
BLAST
Zinc fingeri112 – 14534C4-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Set1/Ash2 histone methyltransferase complex subunit ASH2
Alternative name(s):
ASH2-like protein
Gene namesi
Name:Ash2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1344416. Ash2l.

Subcellular locationi

GO - Cellular componenti

  • histone methyltransferase complex Source: UniProtKB
  • MLL1 complex Source: UniProtKB
  • MLL3/4 complex Source: MGI
  • nuclear euchromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Set1/Ash2 histone methyltransferase complex subunit ASH2PRO_0000064698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei291 – 2911Asymmetric dimethylarginine; by PRMT1 and PRMT5By similarity

Post-translational modificationi

Both monomethylated and dimethylated on arginine residues in the C-terminus. Arg-291 is the major site. Methylation is not required for nuclear localization, nor for MLL complex integrity or maintenance of global histone H3K4me3 levels (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ91X20.
MaxQBiQ91X20.
PaxDbiQ91X20.
PRIDEiQ91X20.

PTM databases

iPTMnetiQ91X20.
PhosphoSiteiQ91X20.

Expressioni

Tissue specificityi

Ubiquitously expressed, with abundant expression in the heart, skeletal muscle and kidney. Low expression is seen in spleen, lung and testis.1 Publication

Gene expression databases

BgeeiQ91X20.
ExpressionAtlasiQ91X20. baseline and differential.
GenevisibleiQ91X20. MM.

Interactioni

Subunit structurei

Interacts with HCFC1 (By similarity). 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 (By similarity). Interacts with SETD1A and SETD1B (By similarity). 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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Rbbp5Q8BX097EBI-1556554,EBI-1556543

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204728. 14 interactions.
DIPiDIP-39161N.
IntActiQ91X20. 9 interactions.
MINTiMINT-4088443.
STRINGi10090.ENSMUSP00000070957.

Structurei

3D structure databases

ProteinModelPortaliQ91X20.
SMRiQ91X20. Positions 100-264, 365-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 578224B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 172110DNA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1 – 6262PHD-type; atypicalBy similarityAdd
BLAST
Zinc fingeri112 – 14534C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2626. Eukaryota.
ENOG410Y5GC. LUCA.
GeneTreeiENSGT00390000010474.
HOGENOMiHOG000013137.
HOVERGENiHBG050592.
InParanoidiQ91X20.
KOiK14964.
OMAiCATCSRW.
OrthoDBiEOG70KGP3.
PhylomeDBiQ91X20.
TreeFamiTF314785.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00622. SPRY. 2 hits.
[Graphical view]
SMARTiSM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91X20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGAGPGP GVSAGPGPGA AASATTAEDR ETEPVAAGAG EGPSAAPGAE
60 70 80 90 100
PSSGEAESGD ANLVDVSGLE TESSNGKDTL EGTGDTSEVM DTQAGSVDEE
110 120 130 140 150
NGRQLGEVEL QCGICTKWFT ADTFGIDTSS CLPFMTNYSF HCNVCHHSGN
160 170 180 190 200
TYFLRKQANL KEMCLSALAN LTWQSRTQDE HPKTMFSKDK DIIPFIDKYW
210 220 230 240 250
ECMTTRQRPG KMTWPNNIVK TMSKERDVFL VKEHPDPGSK DPEEDYPKFG
260 270 280 290 300
LLDQDLSNIG PAYDNQKQSS AVSASGNLNG GIAAGSSGKG RGAKRKQQDG
310 320 330 340 350
GTTGTTKKAR SDPLFSAQRL PPHGYPLEHP FNKDGYRYIL AEPDPHAPDP
360 370 380 390 400
EKLELDCWAG KPIPGDLYRA CLYERVLLAL HDRAPQLKIS DDRLTVVGEK
410 420 430 440 450
GYSMVRASHG VRKGAWYFEI TVDEMPPDTA ARLGWSQPLG NLQAPLGYDK
460 470 480 490 500
FSYSWRSKKG TKFHQSIGKH YSSGYGQGDV LGFYINLPED TETAKSLPDT
510 520 530 540 550
YKDKALIKFK SYLYFEEKDF VDKAEKSLKQ TPHSEIIFYK NGVNQGVAYR
560 570 580 590 600
DIFEGVYFPA ISLYKSCTVS INFGPSFKYP PKDLTYHPMS DMGWGAVVEH
610 620
TLADVLYHVE TEVDGRRSPP WEP
Length:623
Mass (Da):68,250
Last modified:December 1, 2001 - v1
Checksum:iBEB2A46B7F3E8BA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391L → V in BAA35128 (PubMed:10393421).Curated
Sequence conflicti455 – 4584WRSK → LAAS in BAA35128 (PubMed:10393421).Curated
Sequence conflicti619 – 6235PPWEP → HPGNPNQSLLLVTL in BAA35128 (PubMed:10393421).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020983 mRNA. Translation: BAA35128.1.
BC012957 mRNA. Translation: AAH12957.1.
AK087934 mRNA. Translation: BAC40047.1.
AK146938 mRNA. Translation: BAE27547.1.
CCDSiCCDS40307.1.
RefSeqiNP_035921.2. NM_011791.3.
UniGeneiMm.27706.

Genome annotation databases

EnsembliENSMUST00000068892; ENSMUSP00000070957; ENSMUSG00000031575.
GeneIDi23808.
KEGGimmu:23808.
UCSCiuc009lhc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020983 mRNA. Translation: BAA35128.1.
BC012957 mRNA. Translation: AAH12957.1.
AK087934 mRNA. Translation: BAC40047.1.
AK146938 mRNA. Translation: BAE27547.1.
CCDSiCCDS40307.1.
RefSeqiNP_035921.2. NM_011791.3.
UniGeneiMm.27706.

3D structure databases

ProteinModelPortaliQ91X20.
SMRiQ91X20. Positions 100-264, 365-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204728. 14 interactions.
DIPiDIP-39161N.
IntActiQ91X20. 9 interactions.
MINTiMINT-4088443.
STRINGi10090.ENSMUSP00000070957.

PTM databases

iPTMnetiQ91X20.
PhosphoSiteiQ91X20.

Proteomic databases

EPDiQ91X20.
MaxQBiQ91X20.
PaxDbiQ91X20.
PRIDEiQ91X20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068892; ENSMUSP00000070957; ENSMUSG00000031575.
GeneIDi23808.
KEGGimmu:23808.
UCSCiuc009lhc.2. mouse.

Organism-specific databases

CTDi9070.
MGIiMGI:1344416. Ash2l.

Phylogenomic databases

eggNOGiKOG2626. Eukaryota.
ENOG410Y5GC. LUCA.
GeneTreeiENSGT00390000010474.
HOGENOMiHOG000013137.
HOVERGENiHBG050592.
InParanoidiQ91X20.
KOiK14964.
OMAiCATCSRW.
OrthoDBiEOG70KGP3.
PhylomeDBiQ91X20.
TreeFamiTF314785.

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

PROiQ91X20.
SOURCEiSearch...

Gene expression databases

BgeeiQ91X20.
ExpressionAtlasiQ91X20. baseline and differential.
GenevisibleiQ91X20. MM.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00622. SPRY. 2 hits.
[Graphical view]
SMARTiSM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of ASH2L and ash2l, human and mouse homologs of the Drosophila ash2 gene."
    Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.
    Cytogenet. Cell Genet. 84:167-172(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Amnion and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Spleen and Testis.
  5. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL COMPLEX, INTERACTION WITH DPY30; KMT2A; KMT2D; RRBP5 AND WDR5.

Entry informationi

Entry nameiASH2L_MOUSE
AccessioniPrimary (citable) accession number: Q91X20
Secondary accession number(s): Q3UIF9, Q9Z2X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.