Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
F-box and leucine rich repeat protein 19 [Source:HGNC Symbol;Acc:HGNC:25300]
Entrez Summary
TBA
Ensembl ID:
ENSG00000099364
External Link:
Interpro
IPR001611 ; IPR001810 ; IPR001965 ; IPR002857 ; IPR006553 ; IPR011011 ; IPR019786 ; IPR019787 ;
Protein Domain:
Protein: ENSP00000397913DBD: CxxCOther: F-box, F-box-like, LRR_4, LRR_6, LRR_8, PHD, PHD_4Protein: ENSP00000369666DBD: CxxCOther: F-box, F-box-like, LRR_4, LRR_6, LRR_8, PHD, PHD_4Protein: ENSP00000458033DBD: CxxCOther: F-box, F-box-like, LRR_1, LRR_4, LRR_6, LRR_8Protein: ENSP00000455529DBD: CxxCOther: F-box, F-box-like, LRR_4, LRR_6, LRR_8, PHD, PHD_4Protein: ENSP00000457199DBD: CxxCOther:
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.
No
CisBP considers it as a TF?
Yes
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
DNA-Binding
Published Motif Data
Structure
Experimental History
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These units form elongated non-globular structures. 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{"regions": [{"startStyle": "curved", "end": 57, "endStyle": "curved", "aliStart": 13, "text": "zfCXXC", "colour": "#009900", "aliEnd": 57, "start": 11, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 57, "description": "This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterised by two repeats [3], and shows a peculiar internal duplication in which the second unit is inserted into the first one [4]. Each of these units is characterised by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR [3]. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins [4]. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases [4].", "database": "PfamA", "aliStart": 13, "scoreName": "E-value", "accession": "PF02008.18", "start": 11, "score": 9.4e-14, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 57}}, {"startStyle": "straight", "end": 129, "endStyle": "straight", "aliStart": 62, "text": "PHD_4", "colour": "#9999ff", "aliEnd": 129, "start": 62, "href": "http://pfam.xfam.org/family/PF16866.3", "type": "pfama", "display": "true", "metadata": {"end": 129, "description": NaN, "database": "PfamA", "aliStart": 62, "scoreName": "E-value", "accession": "PF16866.3", "start": 62, "score": 1.3e-25, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 129}}, {"startStyle": "jagged", "end": 446, "endStyle": "straight", "aliStart": 404, "text": "F-box", "colour": "#9999ff", "aliEnd": 443, "start": 403, "href": "http://pfam.xfam.org/family/PF00646.31", "type": "pfama", "display": "true", "metadata": {"end": 446, "description": "This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; Pfam:PF00560 and Pfam:PF07723) and the WD repeat (Pfam:PF00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression [3].", "database": "PfamA", "aliStart": 404, "scoreName": "E-value", "accession": "PF00646.31", "start": 403, "score": 1.8e-09, "identifier": "F-box domain", "type": "DBD", "aliEnd": 443}}, {"startStyle": "straight", "end": 447, "endStyle": "straight", "aliStart": 404, "text": "F-box-like", "colour": "#9999ff", "aliEnd": 446, "start": 402, "href": "http://pfam.xfam.org/family/PF12937.5", "type": "pfama", "display": "true", "metadata": {"end": 447, "description": "This is an F-box-like family.", "database": "PfamA", "aliStart": 404, "scoreName": "E-value", "accession": "PF12937.5", "start": 402, "score": 3.2e-06, "identifier": "F-box-like", "type": "DBD", "aliEnd": 446}}, {"startStyle": "straight", "end": 532, "endStyle": "jagged", "aliStart": 489, "text": "LRR_4", "colour": "#9999ff", "aliEnd": 524, "start": 488, "href": "http://pfam.xfam.org/family/PF12799.5", "type": "pfama", "display": "true", "metadata": {"end": 532, "description": "Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.", "database": "PfamA", "aliStart": 489, "scoreName": "E-value", "accession": "PF12799.5", "start": 488, "score": 4e-05, "identifier": "Leucine Rich repeats (2 copies)", "type": "DBD", "aliEnd": 524}}, {"startStyle": "straight", "end": 648, "endStyle": "jagged", "aliStart": 609, "text": "LRR_4", "colour": "#9999ff", "aliEnd": 645, "start": 607, "href": "http://pfam.xfam.org/family/PF12799.5", "type": "pfama", "display": "true", "metadata": {"end": 648, "description": "Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.", "database": "PfamA", "aliStart": 609, "scoreName": "E-value", "accession": "PF12799.5", "start": 607, "score": 4e-05, "identifier": "Leucine Rich repeats (2 copies)", "type": "DBD", "aliEnd": 645}}, {"startStyle": "jagged", "end": 598, "endStyle": "jagged", "aliStart": 578, "text": "LRR_6", "colour": "#9999ff", "aliEnd": 594, "start": 575, "href": "http://pfam.xfam.org/family/PF13516.4", "type": "pfama", "display": "true", "metadata": {"end": 598, "description": NaN, "database": "PfamA", "aliStart": 578, "scoreName": "E-value", "accession": "PF13516.4", "start": 575, "score": 5e-05, "identifier": "Leucine Rich repeat", "type": "DBD", "aliEnd": 594}}, {"startStyle": "straight", "end": 654, "endStyle": "jagged", "aliStart": 631, "text": "LRR_6", "colour": "#9999ff", "aliEnd": 648, "start": 630, "href": "http://pfam.xfam.org/family/PF13516.4", "type": "pfama", "display": "true", "metadata": {"end": 654, "description": NaN, "database": "PfamA", "aliStart": 631, "scoreName": "E-value", "accession": "PF13516.4", "start": 630, "score": 5e-05, "identifier": "Leucine Rich repeat", "type": "DBD", "aliEnd": 648}}, {"startStyle": "straight", "end": 131, "endStyle": "straight", "aliStart": 68, "text": "PHD", "colour": "#9999ff", "aliEnd": 130, "start": 67, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 131, "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": 68, "scoreName": "E-value", "accession": "PF00628.27", "start": 67, "score": 0.0014, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 130}}, {"startStyle": "jagged", "end": 521, "endStyle": "straight", "aliStart": 485, "text": "LRR_8", "colour": "#9999ff", "aliEnd": 520, "start": 481, "href": "http://pfam.xfam.org/family/PF13855.4", "type": "pfama", "display": "true", "metadata": {"end": 521, "description": NaN, "database": "PfamA", "aliStart": 485, "scoreName": "E-value", "accession": "PF13855.4", "start": 481, "score": 0.0025, "identifier": "Leucine rich repeat", "type": "DBD", "aliEnd": 520}}, {"startStyle": "straight", "end": 655, "endStyle": "jagged", "aliStart": 608, "text": "LRR_8", "colour": "#9999ff", "aliEnd": 654, "start": 607, "href": "http://pfam.xfam.org/family/PF13855.4", "type": "pfama", "display": "true", "metadata": {"end": 655, "description": NaN, "database": "PfamA", "aliStart": 608, "scoreName": "E-value", "accession": "PF13855.4", "start": 607, "score": 0.0025, "identifier": "Leucine rich repeat", "type": "DBD", "aliEnd": 654}}], "length": 675}