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Q9UBL3 (ASH2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Set1/Ash2 histone methyltransferase complex subunit ASH2
Alternative name(s):
ASH2-like protein
Gene names
Name:ASH2L
Synonyms:ASH2L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.15

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Nucleus Probable Ref.11.

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. Ref.2

Post-translational modification

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. Ref.18

Sequence similarities

Contains 1 B30.2/SPRY domain.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from direct assay Ref.12. Source: MGI

hemopoiesis

Non-traceable author statement Ref.1. Source: UniProtKB

histone H3-K4 methylation

Inferred from direct assay Ref.11Ref.15. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 18245475. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

response to estrogen

Inferred from direct assay PubMed 16603732. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentSet1C/COMPASS complex

Inferred from direct assay Ref.13Ref.14. Source: UniProtKB

histone methyltransferase complex

Inferred from direct assay Ref.11Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8PubMed 18245475. Source: UniProtKB

   Molecular_functionDNA binding

Inferred by curator Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.6Ref.13PubMed 19187761Ref.15. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 16603732. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBL3-1)

Also known as: ASH2L1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UBL3-2)

Also known as: ASH2L2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
     541-573: Missing.
Isoform 3 (identifier: Q9UBL3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 628628Set1/Ash2 histone methyltransferase complex subunit ASH2
PRO_0000064697

Regions

Domain360 – 583224B30.2/SPRY
Zinc finger1 – 6666PHD-type; atypical
Zinc finger117 – 15034C4-type
Region67 – 177111DNA-binding

Amino acid modifications

Modified residue1011Phosphoserine Ref.16
Modified residue2961Asymmetric dimethylarginine; by PRMT1 and PRMT5 Ref.18

Natural variations

Alternative sequence1 – 9494Missing in isoform 2 and isoform 3.
VSP_007577
Alternative sequence541 – 57333Missing in isoform 2.
VSP_007578
Natural variant4781S → F.
Corresponds to variant rs34167006 [ dbSNP | Ensembl ].
VAR_050679

Experimental info

Mutagenesis2961R → K: Abolishes methylation. Ref.18
Mutagenesis3001R → K: Slightly decreased methylation. Ref.18
Sequence conflict2121Q → H in AAC13564. Ref.1
Sequence conflict2171M → T in AAC13564. Ref.1
Sequence conflict2921S → T in AAC13563. Ref.1
Sequence conflict3511H → Q in AAC13564. Ref.1
Sequence conflict3601L → I in AAC13564. Ref.1
Sequence conflict3691P → S in AAC13564. Ref.1

Secondary structure

........................................................................ 628
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ASH2L1) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8F5F007430D4B863

FASTA62868,723
        10         20         30         40         50         60 
MAAAGAGPGQ EAGAGPGPGA VANATGAEEG EMKPVAAGAA APPGEGISAA PTVEPSSGEA 

        70         80         90        100        110        120 
EGGEANLVDV SGGLETESSN GKDTLEGAGD TSEVMDTQAG SVDEENGRQL GEVELQCGIC 

       130        140        150        160        170        180 
TKWFTADTFG IDTSSCLPFM TNYSFHCNVC HHSGNTYFLR KQANLKEMCL SALANLTWQS 

       190        200        210        220        230        240 
RTQDEHPKTM FSKDKDIIPF IDKYWECMTT RQRPGKMTWP NNIVKTMSKE RDVFLVKEHP 

       250        260        270        280        290        300 
DPGSKDPEED YPKFGLLDQD LSNIGPAYDN QKQSSAVSTS GNLNGGIAAG SSGKGRGAKR 

       310        320        330        340        350        360 
KQQDGGTTGT TKKARSDPLF SAQRLPPHGY PLEHPFNKDG YRYILAEPDP HAPDPEKLEL 

       370        380        390        400        410        420 
DCWAGKPIPG DLYRACLYER VLLALHDRAP QLKISDDRLT VVGEKGYSMV RASHGVRKGA 

       430        440        450        460        470        480 
WYFEITVDEM PPDTAARLGW SQPLGNLQAP LGYDKFSYSW RSKKGTKFHQ SIGKHYSSGY 

       490        500        510        520        530        540 
GQGDVLGFYI NLPEDTETAK SLPDTYKDKA LIKFKSYLYF EEKDFVDKAE KSLKQTPHSE 

       550        560        570        580        590        600 
IIFYKNGVNQ GVAYKDIFEG VYFPAISLYK SCTVSINFGP CFKYPPKDLT YRPMSDMGWG 

       610        620 
AVVEHTLADV LYHVETEVDG RRSPPWEP 

« Hide

Isoform 2 (ASH2L2) [UniParc].

Checksum: BD76059C4DE39703
Show »

FASTA50156,477
Isoform 3 [UniParc].

Checksum: 4317F1206E97C897
Show »

FASTA53460,208

References

« Hide 'large scale' references
[1]"ASH2L: alternative splicing and downregulation during induced megakaryocytic differentiation of multipotential leukemia cell lines."
Wang J., Zhou Y., Yin B., Du G., Huang X., Li G., Shen Y., Yuan J., Qiang B.
J. Mol. Med. 79:399-405(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Fetal brain.
[2]"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 [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 3).
Tissue: Skin.
[6]"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HCFC1.
[7]"Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus."
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.
Mol. Cell 13:587-597(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
[8]"Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL-LIKE COMPLEX.
[9]"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
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.
Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[10]"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."
Lee J.-H., Skalnik D.G.
J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
[11]"Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.
J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET1 COMPLEX.
[12]"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
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.
J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
[13]"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."
Lee J.H., Skalnik D.G.
Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A AND SETD1B.
[14]"Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SET1 COMPLEX.
[15]"On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex."
Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.
J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH DPY30 AND RBBP5.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes."
Butler J.S., Zurita-Lopez C.I., Clarke S.G., Bedford M.T., Dent S.Y.
J. Biol. Chem. 286:12234-12244(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-296 BY PRMT1 AND PRMT5, MUTAGENESIS OF ARG-296 AND ARG-300.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding."
Chen Y., Wan B., Wang K.C., Cao F., Yang Y., Protacio A., Dou Y., Chang H.Y., Lei M.
EMBO Rep. 12:797-803(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 96-271, DOMAIN PHD, DNA-BINDING REGION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF056718 mRNA. Translation: AAC13564.1.
AF056717 mRNA. Translation: AAC13563.1.
AB022785 Genomic DNA. Translation: BAA74520.1.
AB020982 mRNA. Translation: BAA35127.1.
AK291938 mRNA. Translation: BAF84627.1.
CH471080 Genomic DNA. Translation: EAW63337.1.
CH471080 Genomic DNA. Translation: EAW63336.1.
CH471080 Genomic DNA. Translation: EAW63340.1.
BC015936 mRNA. Translation: AAH15936.1.
CCDSCCDS47840.1. [Q9UBL3-3]
CCDS59100.1. [Q9UBL3-2]
CCDS6101.1. [Q9UBL3-1]
RefSeqNP_001098684.1. NM_001105214.2. [Q9UBL3-3]
NP_001248761.1. NM_001261832.1. [Q9UBL3-2]
NP_004665.2. NM_004674.4. [Q9UBL3-1]
UniGeneHs.521530.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RSNX-ray2.10A96-271[»]
3S32X-ray2.45A95-280[»]
3TOJX-ray2.07A/B370-496[»]
A/B539-617[»]
ProteinModelPortalQ9UBL3.
SMRQ9UBL3. Positions 105-269, 370-605.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114528. 51 interactions.
DIPDIP-29222N.
IntActQ9UBL3. 40 interactions.
MINTMINT-1194078.
STRING9606.ENSP00000340896.

PTM databases

PhosphoSiteQ9UBL3.

Polymorphism databases

DMDM32141382.

Proteomic databases

MaxQBQ9UBL3.
PaxDbQ9UBL3.
PRIDEQ9UBL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250635; ENSP00000250635; ENSG00000129691. [Q9UBL3-2]
ENST00000343823; ENSP00000340896; ENSG00000129691. [Q9UBL3-1]
ENST00000428278; ENSP00000395310; ENSG00000129691. [Q9UBL3-3]
ENST00000521652; ENSP00000430259; ENSG00000129691. [Q9UBL3-2]
GeneID9070.
KEGGhsa:9070.
UCSCuc003xkt.5. human. [Q9UBL3-1]
uc010lwa.4. human. [Q9UBL3-2]

Organism-specific databases

CTD9070.
GeneCardsGC08P037963.
H-InvDBHIX0007454.
HGNCHGNC:744. ASH2L.
HPAHPA042289.
MIM604782. gene.
neXtProtNX_Q9UBL3.
PharmGKBPA25044.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249281.
HOGENOMHOG000013137.
HOVERGENHBG050592.
InParanoidQ9UBL3.
KOK14964.
OMARQEFDES.
OrthoDBEOG70KGP3.
PhylomeDBQ9UBL3.
TreeFamTF314785.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9UBL3.
BgeeQ9UBL3.
CleanExHS_ASH2L.
GenevestigatorQ9UBL3.

Family and domain databases

InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PfamPF00622. SPRY. 1 hit.
[Graphical view]
SMARTSM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
PROSITEPS50188. B302_SPRY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSASH2L. human.
GeneWikiASH2L.
GenomeRNAi9070.
NextBio33985.
PROQ9UBL3.
SOURCESearch...

Entry information

Entry nameASH2L_HUMAN
AccessionPrimary (citable) accession number: Q9UBL3
Secondary accession number(s): A8K7C3 expand/collapse secondary AC list , D3DSW9, O60659, O60660, Q96B62
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM