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0RFP2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRFP2
DescriptionRet finger protein 2 (leukemia associated protein 5) (b-cell chronic lymphocytic leukemia tumor suppressor leu5) (putative tumor suppressor rfp2) (tripartite motif protein 13) (ring finger protein 77).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004871 signal transducer activity (IMP)
0009653 morphogenesis (TAS)
0043123 positive regulation of I-kappaB kinase/NF-k... (IMP)

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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 B-box zinc finger is an around 40 amino acids domain. One or two copies ofthis motif are generally associated with a ring finger and a coiled coil motifto form the so-called tripartite motif. It is found essentially intranscription factors.ibonucleoproteins and protooncoproteins.ut nofunction is clearly assigned to this domain . It has been shown to beessential but not sufficient to localize the PML protein in a punctate patternin interphase nuclei . Among the 7 possible ligands for the zinc atomcontained in a B-box.nly 4 are used and bind one zinc atom in a Cys2-His2tetrahedral arrangement. The NMR analysis reveals that the B-box structurecomprises two beta-strands.wo helical turns and three extended loop regionsdifferent from any other zinc binding motif .
  IPR000315:Zinc finger, B-box
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
IPR000315:zf-B_box 
Evalue:-12.795880317688 
Location:89-131IPR001841:RING 
Evalue:-7.72124639904717 
Location:10-57
SequencesProtein: RFP2_HUMAN (407 aa)
mRNA: NM_001007278 NM_213590
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 71 residues, 49469143-49469353Exon2: 34 residues, 49469803-49469900Exon3: 40 residues, 49473131-49473245Exon4: 2179 residues, 49484071-49490604Exon5: 2 residues, -Jump to RFP2_HUMANExon1: 253 residues, 49469143-49469900Exon2: 2179 residues, 49484071-49490604Exon3: 2 residues, -Jump to RFP2_HUMAN  
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