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0MIB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMIB2
DescriptionUbiquitin ligase protein mib2 (ec 6.3.2.-) (mind bomb homolog 2) (zinc finger zz type with ankyrin repeat domain protein 1) (skeletrophin) (novelzin) (novel zinc finger protein) (putative nf-kappa-b-activating protein 002n).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004871 signal transducer activity (IMP)
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:
Mib is a RING ubiquitin ligase in the Notch pathway. Mib interacts with the intracellular domain of Delta to promote its ubiquitylation and internalisation. Cell transplantation studies suggest that mib function is essential in the signalling cell for efficient activation of Notch in neighbouring cells. This domain has been named mib/herc2 domain in and usually the protein also contains an E3 ligase domain (either Ring or Hect).
  IPR010606:Mib_herc2
Skeletal muscle dystrophin is a 427 kDa protein thought to act as a link between the actin cytoskeleton and the extracellular matrix. Perturbations of the dystrophin-associated complex.or example.etween dystrophin and the transmembrane glycoprotein beta-dystroglycan.ay lead to muscular dystrophy. Previously.he cysteine-rich region and first half of the carboxy-terminal domain of dystrophin were shown to interact with beta-dystroglycan through a stretch of fifteen amino acids at the carboxy-terminus of beta-dystroglycan. This region of dystrophin implicated in binding beta-dystroglycan contains four modular protein domains: a WW domain.wo putative Ca2+-binding EF-hand motifs.nd a putative zinc finger ZZ domain .
  IPR000433:Zinc finger, ZZ-type
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
The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers . The repeat has been found in proteins of diverse function such as transcriptional initiators.ell-cycle regulators.ytoskeletal.on transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures . Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure .
  IPR002110:Ankyrin
IPR010606:MIB_HERC2 
Evalue:-43.6020584106445 
Location:70-138IPR010606:MIB_HERC2 
Evalue:-29.6989707946777 
Location:218-285IPR002110:Ank 
Evalue:-8.82390880584717 
Location:691-724IPR000433:ZnF_ZZ 
Evalue:-7.31875876262441 
Location:143-188IPR002110:Ank 
Evalue:-7.25963735580444 
Location:588-620IPR002110:Ank 
Evalue:-6.45593214035034 
Location:555-587IPR002110:Ank 
Evalue:-6.15490198135376 
Location:522-554IPR002110:Ank 
Evalue:-5.27572393417358 
Location:725-757IPR001841:RING 
Evalue:-1.76955107862173 
Location:969-1001IPR002110:Ank 
Evalue:-1.58502662181854 
Location:657-678IPR002110:Ank 
Evalue:-1.53760194778442 
Location:758-826IPR002110:Ank 
Evalue:-1.14266753196716 
Location:621-656IPR001841:RING 
Evalue:-0.721246399047171 
Location:890-924IPR001841:ZF_RING_1 
Evalue:0 
Location:0-0IPR002110:Ank 
Evalue:1.67209780216217 
Location:827-837
SequencesProtein: MIB2_HUMAN (1013 aa)
mRNA: AB076693 NM_080875
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)
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 44 residues, 1540746-1540876Exon2: 37 residues, 1541750-1541857Exon3: 105 residues, 1548631-1548942Exon4: 59 residues, 1549016-1549188Exon5: 37 residues, 1550037-1550144Exon6: 67 residues, 1550233-1550428Exon7: 49 residues, 1550528-1550671Exon8: 38 residues, 1550788-1550896Exon9: 37 residues, 1551892-1551997Exon10: 56 residues, 1552079-1552242Exon11: 46 residues, 1552316-1552450Exon12: 51 residues, 1552538-1552687Exon13: 54 residues, 1552915-1553072Exon14: 55 residues, 1553261-1553422Exon15: 44 residues, 1553515-1553642Exon16: 80 residues, 1553731-1553965Exon17: 61 residues, 1554375-1554554Exon18: 62 residues, 1554627-1554809Exon19: 24 residues, 1554881-1554947Exon20: 106 residues, 1555534-1555847Exon21: 2 residues, -Jump to MIB2_HUMANExon1: 44 residues, 1540746-1540876Exon2: 37 residues, 1541750-1541857Exon3: 105 residues, 1548631-1548942Exon4: 59 residues, 1549016-1549188Exon5: 37 residues, 1550037-1550144Exon6: 67 residues, 1550233-1550428Exon7: 49 residues, 1550528-1550671Exon8: 34 residues, 1550800-1550896Exon9: 37 residues, 1551892-1551997Exon10: 56 residues, 1552079-1552242Exon11: 46 residues, 1552316-1552450Exon12: 51 residues, 1552538-1552687Exon13: 54 residues, 1552915-1553072Exon14: 55 residues, 1553261-1553422Exon15: 44 residues, 1553515-1553642Exon16: 80 residues, 1553731-1553965Exon17: 61 residues, 1554375-1554554Exon18: 62 residues, 1554627-1554809Exon19: 24 residues, 1554881-1554947Exon20: 106 residues, 1555534-1555847Exon21: 2 residues, -Jump to MIB2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2469 938741-939776 ~-1K 23(G1P2)(+)Loci: 2470 945365-981355 ~-36K 24(AGRN)(+)Loci: 2471 1207438-1217272 ~-10K 59(SCNN1D)(+)Loci: 2472 1540746-1555847 ~-15K 98(MIB2)(+)Loci: 2473 1940702-1952050 ~-11K 141(GABRD)(+)Loci: 2474 1971768-2106692 ~-135K 142(PRKCZ)(+)Loci: 2468 885829-890958 ~-5K 15(KLHL17)(+)Link out to UCSC