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0RNF4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRNF4
DescriptionRing finger protein 4.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (TAS)
0050681 androgen receptor binding (NAS)
0003713 transcription coactivator activity (NAS)
0003700 transcription factor activity (TAS)
0008270 zinc ion binding (TAS)
0030521 androgen receptor signaling pathway (NAS)
0045893 positive regulation of transcription, DNA-d... (NAS)
0006357 regulation of transcription from RNA polyme... (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:
Quality control of intracellular proteins is essential for cellular homeostasis. Molecular chaperones recognise and contribute to the refolding of misfolded or unfolded proteins.hereas the ubiquitin-proteasome system mediates the degradation of such abnormal proteins. Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently.owever.-box proteins.hich contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans.ave been identified as a new type of E3 .The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc.nd is probably involved in mediating protein-protein interactions. . There are two different variants.he C3HC4-type and a C3H2C3-type.hich is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as RING-H2 finger. The RING domain is a protein interaction domain which has been implicated in a range of diverse biological processes.E3 ubiquitin-protein ligase activity is intrinsic to the RING domain ofc-Cbl and is likely to be a general function of this domain; Various RINGfingers exhibit binding to E2 ubiquitin-conjugating enzymes (Ubcs) .Several 3D-structures for RING-fingers are known . The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the cross-brace motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion.hilst pairs two and four bind the second.s illustrated in the following schematic representation:Note that in the older literature.ome RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family.lbeit with similar Cys-spacing (see ).
  IPR001841:Zinc finger, RING-type
IPR001841:zf-C3HC4 
Evalue:-8.95860767364502 
Location:132-176
SequencesProtein: RNF4_HUMAN (190 aa)
mRNA: NM_002938
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 60 residues, 2440604-2440783Exon2: 57 residues, 2461861-2462027Exon3: 40 residues, 2468531-2468646Exon4: 28 residues, 2472183-2472263Exon5: 5 residues, 2483480-2483490Exon6: 55 residues, 2483962-2484122Exon7: 18 residues, 2484607-2484656Exon8: 730 residues, 2485194-2487379Exon9: 2 residues, -Jump to RNF4_HUMAN  
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Loci Cluster (Details)Loci: 4661 1784557-1827772 ~-43K 27218(LETM1)(-)Loci: 3399 2031384-2037433 ~-6K 27229(+)Loci: 3400 2440604-2487379 ~-47K 27243(RNF4)(+)Loci: 3398 1765420-1780396 ~-15K 27216(FGFR3)(+)Link out to UCSC