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0MIB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMIB1
DescriptionUbiquitin ligase protein mib1 (ec 6.3.2.-) (mind bomb homolog 1) (dapk-interacting protein 1) (dip-1) (zinc finger zz type with ankyrin repeat domain protein 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
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:-37.7695503234863 
Location:154-221IPR010606:MIB_HERC2 
Evalue:-34 
Location:15-74IPR000433:ZnF_ZZ 
Evalue:-10 
Location:79-124IPR002110:Ank 
Evalue:-9.82390880584717 
Location:665-697IPR002110:Ank 
Evalue:-9.17392539978027 
Location:631-664IPR002110:Ank 
Evalue:-7.85387182235718 
Location:529-561IPR002110:Ank 
Evalue:-7.14874172210693 
Location:562-594IPR002110:Ank 
Evalue:-5.88605642318726 
Location:463-495IPR002110:Ank 
Evalue:-4.53760194778442 
Location:595-627IPR001841:zf-C3HC4 
Evalue:-4.03151702880859 
Location:963-995IPR002110:Ank 
Evalue:-3.92081880569458 
Location:698-771IPR002110:Ank 
Evalue:-2.45593190193176 
Location:496-528IPR001841:RING 
Evalue:-0.744727494896694 
Location:866-900IPR001841:RING 
Evalue:-0.744727494896694 
Location:819-853IPR001841:ZF_RING_1 
Evalue:0 
Location:0-0IPR002110:ANK 
Evalue:3.20411998265592 
Location:430-460
SequencesProtein: MIB1_HUMAN (1006 aa)
mRNA: AY147849 NM_020774
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentK01932
  Level 3 annotation:
    
  Level 2 annotation:
    Tryptophan metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 162 residues, 17575287-17575771Exon2: 59 residues, 17599730-17599902Exon3: 45 residues, 17602581-17602711Exon4: 37 residues, 17607582-17607687Exon5: 24 residues, 17612061-17612128Exon6: 70 residues, 17613439-17613644Exon7: 63 residues, 17625332-17625516Exon8: 50 residues, 17632042-17632187Exon9: 46 residues, 17633799-17633933Exon10: 38 residues, 17637865-17637973Exon11: 68 residues, 17649574-17649772Exon12: 52 residues, 17653453-17653605Exon13: 46 residues, 17672323-17672456Exon14: 31 residues, 17677089-17677176Exon15: 56 residues, 17678050-17678212Exon16: 62 residues, 17680902-17681084Exon17: 66 residues, 17683154-17683347Exon18: 28 residues, 17687098-17687177Exon19: 40 residues, 17691088-17691202Exon20: 35 residues, 17692504-17692605Exon21: 1432 residues, 17698484-17702776Exon22: 2 residues, -Jump to MIB1_HUMANExon1: 77 residues, 17575542-17575771Exon2: 59 residues, 17599730-17599902Exon3: 45 residues, 17602581-17602711Exon4: 37 residues, 17607582-17607687Exon5: 24 residues, 17612061-17612128Exon6: 70 residues, 17613439-17613644Exon7: 63 residues, 17625332-17625516Exon8: 50 residues, 17632042-17632187Exon9: 46 residues, 17633799-17633933Exon10: 38 residues, 17637865-17637973Exon11: 68 residues, 17649574-17649772Exon12: 52 residues, 17653453-17653605Exon13: 46 residues, 17672323-17672456Exon14: 31 residues, 17677089-17677176Exon15: 56 residues, 17678050-17678212Exon16: 62 residues, 17680902-17681084Exon17: 66 residues, 17683154-17683347Exon18: 28 residues, 17687098-17687177Exon19: 40 residues, 17691088-17691202Exon20: 35 residues, 17692504-17692605Exon21: 2143 residues, 17698484-17704908Exon22: 2 residues, -Jump to MIB1_HUMAN  
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