UniProt Accession

 ASH2L_HUMAN; Q9UBL3; A8K7C3; D3DSW9; O60659; O60660; Q96B62 

Genbank Protein ID

 AF056718; AF056717; AB022785; AB020982; AK291938; CH471080; CH471080; CH471080; BC015936 

Genbank Nucleotide ID

 AAC13564.1; AAC13563.1; BAA74520.1; BAA35127.1; BAF84627.1; EAW63337.1; EAW63336.1; EAW63340.1; AAH15936.1 

Protein Name

 Set1/Ash2 histone methyltransferase complex subunit ASH2 

Protein Synonyms/Alias

 ASH2-like protein 

Gene Name

 ASH2L 

Gene Synonyms/Alias

 ASH2L1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
338	PLEHPFNKDGYRYIL	ubiquitination	[1, 2, 3]
393	HDRAPQLKISDDRLT	ubiquitination	[2]
405	RLTVVGEKGYSMVRA	ubiquitination	[2]
507	KSLPDTYKDKALIKF	ubiquitination	[2]
509	LPDTYKDKALIKFKS	ubiquitination	[2]
531	DFVDKAEKSLKQTPH	ubiquitination	[2]
534	DKAEKSLKQTPHSEI	ubiquitination	[2]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 360 583 B30.2/SPRY.
 ZN_FING 1 66 PHD-type; atypical.
 ZN_FING 117 150 C4-type.
 REGION 67 177 DNA-binding.
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 296 296 Asymmetric dimethylarginine; by PRMT1 and  

Keyword

 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; DNA-binding; Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 628 AA 

Protein Sequence

Gene Ontology

 GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0030097; P:hemopoiesis; NAS:UniProtKB.
 GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
 GO:0043627; P:response to estrogen stimulus; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 

Interpro

 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt. 

Pfam

 PF00622; SPRY 

SMART

 SM00449; SPRY 

PROSITE

 PS50188; B302_SPRY
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 

PRINTS