Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
ASH1 like histone lysine methyltransferase [Source:HGNC Symbol;Acc:HGNC:19088]
Entrez Summary
#!usr/local/bin/perl
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microRNAs (miRNAs) are short (20-24 nt) non-coding RNAs that are
involved in post-transcriptional regulation of gene expression in
multicellular organisms by affecting both the stability and translation of
mRNAs. miRNAs are transcribed by RNA polymerase II as part of capped and
polyadenylated primary transcripts (pri-miRNAs) that can be either
protein-coding or non-coding. The primary transcript is cleaved by the Drosha
ribonuclease III enzyme to produce an approximately 70-nt stem-loop precursor
miRNA (pre-miRNA), which is further cleaved by the cytoplasmic Dicer
ribonuclease to generate the mature miRNA and antisense miRNA star (miRNA*)
products. The mature miRNA is incorporated into a RNA-induced silencing
complex (RISC), which recognizes target mRNAs through imperfect base pairing
with the miRNA and most commonly results in translational inhibition or
destabilization of the target mRNA. The RefSeq represents the predicted
microRNA stem-loop. [provided by RefSeq, Sep 2009]
Ensembl ID:
ENSG00000116539
External Link:
CisBP
Interpro
IPR001025 ; IPR001214 ; IPR001487 ; IPR001965 ; IPR003616 ; IPR006560 ; IPR011011 ; IPR017956 ; IPR019786 ; IPR019787 ;
Protein Domain:
ENSP00000357330
Protein Domain:
ENSP00000376204
Protein Domain:
ENSP00000449283
Domain:
Protein: ENSP00000357330DBD: AT hookOther: BAH, Bromodomain, PHD, SETProtein: ENSP00000376204DBD: AT hookOther: BAH, Bromodomain, PHD, SETProtein: ENSP00000449283DBD: AT hookOther:
Previous Annotations
Source
Annotation
TF-CAT classification
No PMIDS:
Vaquerizas 2009 TF classification
"a " Has direct evidence of TF function;
"b " Has evidence for an orthologous TF;
"c " contains likely DBDs, but has no functional evidence;
"x " is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription;
"other " category contains proteins without clear DBDs they curated from external sources.
a
CisBP considers it as a TF?
No
TFclass considers it as a TF?
No
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
No
GO-Info
Initial Assessment
1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding;
1a2 There is high confidence data for a close ortholog (as defined in CisBP);
2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model;
2a2 There is lower confidence evidence for an close ortholog;
3a There is decent circumstantial evidence for its role as a TF or not;
4a Two or more datasets predict it as a TF;
5a One of the source datasets predicts is as a TF
5a, one of the source datasets predicts is as a TF
TF has conditional DNA-binding requirements
Chromatin_Modifier_etc
DNA-Binding
Published Motif Data
Structure
Experimental History
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{"regions": [{"startStyle": "straight", "end": 2256, "endStyle": "straight", "aliStart": 2151, "text": "SET", "colour": "#9999ff", "aliEnd": 2256, "start": 2151, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 2256, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2]. A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3]. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 2151, "scoreName": "E-value", "accession": "PF00856.26", "start": 2151, "score": 1.3e-21, "identifier": "SET domain", "type": "DBD", "aliEnd": 2256}}, {"startStyle": "straight", "end": 2793, "endStyle": "straight", "aliStart": 2658, "text": "BAH", "colour": "#9999ff", "aliEnd": 2791, "start": 2656, "href": "http://pfam.xfam.org/family/PF01426.16", "type": "pfama", "display": "true", "metadata": {"end": 2793, "description": "This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction [3].", "database": "PfamA", "aliStart": 2658, "scoreName": "E-value", "accession": "PF01426.16", "start": 2656, "score": 7e-20, "identifier": "BAH domain", "type": "DBD", "aliEnd": 2791}}, {"startStyle": "straight", "end": 2533, "endStyle": "straight", "aliStart": 2456, "text": "Bromodomain", "colour": "#9999ff", "aliEnd": 2531, "start": 2448, "href": "http://pfam.xfam.org/family/PF00439.23", "type": "pfama", "display": "true", "metadata": {"end": 2533, "description": "Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine [3].", "database": "PfamA", "aliStart": 2456, "scoreName": "E-value", "accession": "PF00439.23", "start": 2448, "score": 1.7e-15, "identifier": "Bromodomain", "type": "DBD", "aliEnd": 2531}}, {"startStyle": "straight", "end": 2626, "endStyle": "straight", "aliStart": 2582, "text": "PHD", "colour": "#9999ff", "aliEnd": 2625, "start": 2582, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 2626, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 2582, "scoreName": "E-value", "accession": "PF00628.27", "start": 2582, "score": 2.1000000000000002e-06, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 2625}}], "length": 2965}