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0HRX_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMLL
DescriptionZinc finger protein hrx (all-1) (trithorax-like protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (IDA)
0042803 protein homodimerization activity (IDA)
0003702 RNA polymerase II transcription factor acti... (TAS)
0003700 transcription factor activity (NAS)
0035162 embryonic hemopoiesis (TAS)
0006461 protein complex assembly (IDA)
0006366 transcription from RNA polymerase II promoter (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The SET domain appears generally as one part of a larger multidomain protein.nd recently there were described three structures of very different proteins with distinct domain compositions: Neurospora crassa DIM-5. member of the Su(var) family of HKMTs which methylate histone H3 on lysine 9.uman SET7 (also called SET9).hich methylates H3 on lysine 4 and garden pea Rubisco LSMT.n enzyme that does not modify histones.ut instead methylates lysine 14 in the flexible tail of the large subunit of the enzyme Rubisco. The SET domain itself turned out to be an uncommon structure. Although in all three studies.lectron density maps revealed the location of the AdoMet or AdoHcy cofactor.he SET domain bears no similarity at all to the canonical/AdoMet-dependent methyltransferase fold. Strictly conserved in the C-terminal motif of the SET domain tyrosine could be involved in abstracting a proton from the protonated amino group of the substrate lysine.romoting its nucleophilic attack on the sulphonium methyl group of the AdoMet cofactor. In contrast to the AdoMet-dependent protein methyltranferases of the classical type.hich tend to bind their polypeptide substrates on top of the cofactor.t is noted from the Rubisco LSMT structure that the AdoMet seems to bind in a separate cleft.uggesting how a polypeptide substrate could be subjected to multiple rounds of methylation without having to be released from the enzyme. In contrast.ET7/9 is able to add only a single methyl group to its substrate. It has been demonstrated that association of SET domain and myotubularin-related proteins modulates growth control . The SET domain-containing Drosophila melanogaster (Fruit fly) protein.nhancer of zeste.as a function in segment determination and the mammalian homologue may be involved in the regulation of gene transcription and chromatin structure.Histone lysine methylation is part of the histone code that regulated chromatin function and epigenetic control of gene function. Histone lysine methyltransferases (HMTase) differ both in their substrate specificity for the various acceptor lysines as well as in their product specificity for the number of methyl groups (one.wo.r three) they transfer. With just one exception .he HMTases belong to SET family that can be classified according to the sequences surrounding the SET domain . Structural studies on the human SET7/9. mono-methylase.ave revealed the molecular basis for the specificity of the enzyme for the histone-target and the roles of the invariant residues in the SET domain in determining the methylation specificities . The pre-SET domain.s found in the SUV39 SET family.ontains nine invariant cysteine residues that are grouped into two segments separated by a region of variable length. These 9 cysteines coordinate 3 zinc ions to form to form a triangular cluster.here each of the zinc ions is coordinated by 4 four cysteines to give a tetrahedral configuration. The function of this domain is structural.olding together 2 long segments of random coils.The C-terminal region including the post-SET domain is disordered when not interacting with a histone tail and in the absence of zinc. The three conserved cysteines in the post-SET domain form a zinc-binding site when coupled to a fourth conserved cysteine in the knot-like structure close to the SET domain active site . The structured post-SET region brings in the C-terminal residues that participate in S-adenosylmethine-binding and histone tail interactions. The three conserved cysteine residues are essential for HMTase activity.s replacement with serine abolishes HMTase activity .
  IPR001214:SET
The "FY-rich" domain C-terminal region is sometimes closely juxtaposed with the N-terminal region ().ut sometimes is far distant. It is of unknown function.ut occurs frequently in chromatin-associated proteins like trithorax and its homologues.
  IPR003889:FY-rich, C-terminal
Zinc finger domains .re nucleic acid-binding protein structures first identified in the Xenopus laevis transcription factor TFIIIA. These domains have since been found in numerous nucleic acid-binding proteins. A zinc finger domain is composed of 25 to 30 amino-acid residues including 2 conserved Cys and 2 conserved His residues in a C-2-C-12-H-3-H type motif. The 12 residues separating the second Cys and the first His are mainly polar and basic.mplicating this region in particular in nucleic acid binding. The zinc finger motif is an unusually small.elf-folding domain in which Zn is a crucial component of its tertiary structure. All bind 1 atom of Zn in a tetrahedral array to yield a finger-like projection.hich interacts with nucleotides in the major groove of the nucleic acid. The Zn binds to the conserved Cys and His residues. Fingers have been found to bind to about 5 base pairs of nucleic acid containing short runs of guanine residues. They have the ability to bind to both RNA and DNA.nd it has been suggested that the zinc finger may thus represent the original nucleic acid binding protein. It has also been suggested that a Zn-centred domain could be used in a protein interaction..g. in protein kinase C. Many classes of zinc fingers are characterized according to the number and positions of the histidine and cysteine residues involved in the zinc atom coordination. In the first class to be characterized.alled C2H2.he first pair of zinc coordinating residues are cysteines.hile the second pair are histidines.This domain contains eight conserved cysteine residuesthat bind to zinc. The CXXC domain is found in proteinsthat methylate cytosine.roteins that bind to methylcytosine and HRX related proteins.
  IPR002857:Zinc finger, CXXC-type
The "FY-rich" domain N-terminal region is sometimes closely juxtaposed with the C-terminal region ().ut sometimes is far distant. It is of unknown function.ut occurs frequently in chromatin-associated proteins like trithorax and its homologues.
  IPR003888:FY-rich, N-terminal
Bromodomains are found in a variety of mammalian.nvertebrate and yeast DNA-binding proteins . Bromodomains can interact withacetylated lysine .In some proteins.he classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g..ammalian protein HRX.aenorhabditis elegans hypothetical protein ZK783.4.east protein YTA7). The bromodomain may occur as a single copy.r in duplicate. The precise function of the domain is unclear.ut it may be involved in protein-protein interactions and may play a role in assembly or activity of multi-component complexes involved in transcriptional activation .
  IPR001487:Bromodomain
The homeodomain (PHD) finger .s a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of.ut distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively.he interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain.he PHD finger is thought to bind two zinc ions.
  IPR001965:Zinc finger, PHD-type
This region is found in a number of histone lysine methyltransferases (HMTase).-terminal to the SET domain; it is generally described as the post-SET domain.Histone lysine methylation is part of the histone code that regulated chromatin function and epigenetic control of gene function. Histone lysine methyltransferases (HMTase) differ both in their substrate specificity for the various acceptor lysines as well as in their product specificity for the number of methyl groups (one.wo.r three) they transfer. With just one exception .he HMTases belong to SET family that can be classified according to the sequences surrounding the SET domain . Structural studies on the human SET7/9. mono-methylase.ave revealed the molecular basis for the specificity of the enzyme for the histone-target and the roles of the invariant residues in the SET domain in determining the methylation specificities . The pre-SET domain.s found in the SUV39 SET family.ontains nine invariant cysteine residues that are grouped into two segments separated by a region of variable length. These 9 cysteines coordinate 3 zinc ions to form to form a triangular cluster.here each of the zinc ions is coordinated by 4 four cysteines to give a tetrahedral configuration. The function of this domain is structural.olding together 2 long segments of random coils.The C-terminal region including the post-SET domain is disordered when not interacting with a histone tail and in the absence of zinc. The three conserved cysteines in the post-SET domain form a zinc-binding site when coupled to a fourth conserved cysteine in the knot-like structure close to the SET domain active site . The structured post-SET region brings in the C-terminal residues that participate in S-adenosylmethine-binding and histone tail interactions. The three conserved cysteine residues are essential for HMTase activity.s replacement with serine abolishes HMTase activity .
  IPR003616:Post-SET zinc-binding region
Cytochrome cd1 (cyt cd1) nitrite reductase is a dimeric enzyme of the bacterial periplasm that plays a key role in denitrification.he respiratory reduction of nitrite to nitric oxide in the nitrogen cycle. Each subunit of the cyt cd1 dimer contains one cytochrome c and one d1 haem group . The active site contains a specialised d1 haem.here the nitrite substrate is bound and reduced. This d1 haem is bound in an 8-bladed beta-propeller.hich is also found in some members of the WD40 repeat-containing proteins ().The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011048:Cytochrome cd1-nitrite reductase-like, C-terminal haem d1
High mobility group (HMG) proteins are a family of relatively low molecular weight non-histone componentsin chromatin. HMG-I and HMG-Y are proteins of about 100 amino acid residues which are produced by thealternative splicing of a single gene. HMG-I proteins bind preferentially to the minor groove of AT-richregions in double-stranded DNA . It is suggested that these proteins could functionin nucleosome phasing and in the 3 end processing of mRNA transcripts. They are also involved in thetranscription regulation of genes containing.r in close proximity to.T-rich regions. DNA-binding of these.nd several related.roteins is effected by an 11-residue domain known as an AT-hook. Within known HMG-Iproteins are found three highly conserved regions.losely related to the consensus sequence TPKRPRGRPKK. Asynthetic oligopeptide with this sequence specifically binds to substrate DNA in a manner reminiscent ofintact HMG-I proteins. Structure predictions suggest that the peptide has a secondary structure similar tothe anti-tumour and anti-viral drugs netropsin and distamycin.nd to the dye Hoechst 33258. These ligands.hich also preferentially bind to AT-rich DNA.ffectively compete with both the synthetic peptide and theHMG-I proteins for DNA binding. The peptide also contains novel structural features such as a predicted Asxbend.r hook.t its N-terminus.nd laterally-projecting cationic Arg/Lys bristles.hich may play arole in the binding of HMG-I proteins. The predicted peptide structure.he AT-hook.s a previouslyundescribed DNA-binding motif .
  IPR000637:HMG-I and HMG-Y, DNA-binding
IPR001214:SET 
Evalue:-55 
Location:3823-3951IPR003889:FYRC 
Evalue:-36.6777807052661 
Location:3668-3753IPR002857:zf-CXXC 
Evalue:-23.8860569000244 
Location:1147-1194IPR003888:FYRN 
Evalue:-18.7212463990472 
Location:2030-2073IPR001965:PHD 
Evalue:-11.32790184021 
Location:1568-1627IPR001965:PHD 
Evalue:-9.92081875395237 
Location:1481-1531IPR001487:BROMO 
Evalue:-6.61978875828839 
Location:1633-1767IPR001965:PHD 
Evalue:-3.76955107862173 
Location:1932-1978IPR003616:PostSET 
Evalue:-3.76955107862173 
Location:3953-3969IPR001965:PHD 
Evalue:-2.24412514432751 
Location:1433-1480IPR000637:AT_hook 
Evalue:-0.408935397863388 
Location:300-312IPR002048:EF_HAND_1 
Evalue:0 
Location:2884-2896IPR000637:HMGI_Y 
Evalue:0 
Location:170-181IPR000637:AT_hook 
Evalue:0.380211234092712 
Location:219-230
SequencesProtein: HRX_HUMAN (3969 aa)
mRNA: NM_005933
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 152 residues, 117812414-117812869Exon2: 25 residues, 117844699-117844769Exon3: 886 residues, 117847586-117850240Exon4: 61 residues, 117852729-117852907Exon5: 80 residues, 117853891-117854126Exon6: 23 residues, 117856098-117856163Exon7: 128 residues, 117857639-117858017Exon8: 26 residues, 117858346-117858420Exon9: 46 residues, 117860107-117860239Exon10: 40 residues, 117860786-117860900Exon11: 51 residues, 117864538-117864685Exon12: 34 residues, 117865716-117865812Exon13: 42 residues, 117866053-117866174Exon14: 40 residues, 117867120-117867234Exon15: 63 residues, 117867668-117867853Exon16: 60 residues, 117868981-117869155Exon17: 39 residues, 117870212-117870323Exon18: 26 residues, 117870618-117870692Exon19: 66 residues, 117871624-117871818Exon20: 37 residues, 117872185-117872292Exon21: 48 residues, 117873860-117873998Exon22: 55 residues, 117874294-117874453Exon23: 41 residues, 117875227-117875345Exon24: 28 residues, 117875759-117875838Exon25: 55 residues, 117876911-117877072Exon26: 64 residues, 117877596-117877782Exon27: 1418 residues, 117878322-117882571Exon28: 29 residues, 117883453-117883534Exon29: 23 residues, 117885060-117885125Exon30: 59 residues, 117885872-117886043Exon31: 27 residues, 117887875-117887950Exon32: 60 residues, 117895542-117895717Exon33: 38 residues, 117895881-117895989Exon34: 30 residues, 117896726-117896810Exon35: 45 residues, 117897212-117897342Exon36: 1109 residues, 117897821-117901144Exon37: 2 residues, -Jump to HRX_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3997 117509303-117528745 ~-19K 7842(SCN4B)(-)Loci: 3998 117538729-117552546 ~-14K 7844(SCN2B)(-)Loci: 2710 117720310-117729261 ~-9K 7856(CD3G)(+)Loci: 2711 117812414-117901144 ~-89K 7860(MLL)(+)Loci: 2712 117948320-117978854 ~-31K 7867(ARCN1)(+)Loci: 2713 118394450-118399592 ~-5K 7892(TRAPPC4)(+)Loci: 3999 118794097-118799064 ~-5K 7924(THY1)(-)Loci: 2709 117452975-117494380 ~-41K 7838(TMPRSS4)(+)Link out to UCSC