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0RBX2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRNF7
DescriptionRing-box protein 2 (rbx2) (ring finger protein 7) (regulator of cullins 2) (ckii beta-binding protein 1) (ckbbp1) (sensitive to apoptosis gene protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (NAS)
0005634 nucleus (NAS)
0005507 copper ion binding (TAS)
0008270 zinc ion binding (TAS)
0006916 anti-apoptosis (TAS)
0008631 induction of apoptosis by oxidative stress (TAS)
0006980 redox signal response (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:-4.88605642318726 
Location:79-102
SequencesProtein: RBX2_HUMAN (113 aa)
mRNA: AF312226 NM_014245
Local Annotation
Synapse Ontology
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 103 residues, 142939740-142940048Exon2: 18 residues, 142945040-142945088Exon3: 416 residues, 142946690-142947932Exon4: 2 residues, -Jump to RBX2_HUMANExon1: 59 residues, 142939873-142940048Exon2: 90 residues, 142944175-142944439Exon3: 18 residues, 142945040-142945088Exon4: 64 residues, 142946690-142946877Exon5: 2 residues, -Jump to RBX2_HUMAN  
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