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0TRI45_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRIM45
DescriptionTripartite motif protein 45 (ring finger protein 99).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
The many different actin cross-linking proteins share a common architecture.onsisting of a globular actin-binding domain and an extended rod. Whereas their actin-binding domains consist of two calponin homology domains (see ).heir rods fall into three families.The rod domain of the family including the Dictyostelium discoideum gelation factor (ABP120) and human filamin (ABP280) is constructed from tandem repeats of a 100-residue motif that is glycine and proline rich . The gelation factors rod contains 6 copies of the repeat.hereas filamin has a rod constructed from 24 repeats. The resolution of the 3D structure of rod repeats from the gelation factor has shown that they consist of a beta-sandwich.ormed by two beta-sheets arranged in an immunoglobulin-like fold . Because conserved residues that form the core of the repeats are preserved in filamin.he repeat structure should be common to the members of the gelation factor/filamin family.The head to tail homodimerisation is crucial to the function of the ABP120 and ABP280 proteins. This interaction involves a small portion at the distal end of the rod domains. For the gelation factor it has been shown that the carboxy-terminal repeat 6 dimerises through a double edge-to-edge extension of the beta-sheet and that repeat 5 contributes to dimerisation to some extent .
  IPR001298:Filamin/ABP280 repeat
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
This family represents ferritin and related proteins. Ferritin is a major non-haem iron storage protein in animal.lants and microorganisms . Iron is required by most organisms.ut is potentially toxic due to its reactivity.hich is counteracted by sequestering it into ferritin. Ferritin consists of a 4-helical bundle core.nd contains a bimetal-ion centre in the middle of the bundle. Other proteins with this structure include: haem-containing bacteriferritins; rubrerythrin.hich appears to have a role in anaerobic detoxification pathway for reactive oxygen species ; Dps (DNA-binding proteins from starved cells) used in bacteria for iron storage-detoxification; and CRD1 (AcsF).hich is required for the maintenance of photosystem I .
  IPR012347:Ferritin-related
IPR001298:IG_FLMN 
Evalue:-34.6382721639824 
Location:398-500IPR001841:RING 
Evalue:-6.74472749489669 
Location:29-97IPR000315:zf-B_box 
Evalue:-4.82390880584717 
Location:186-227IPR000315:zf-B_box 
Evalue:-3.18708658218384 
Location:130-176IPR012347:Ferritin_rel 
Evalue:0 
Location:237-315
SequencesProtein: TRI45_HUMAN (580 aa)
mRNA: NM_025188
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 463 residues, 117455212-117456598Exon2: 44 residues, 117457503-117457630Exon3: 40 residues, 117459719-117459834Exon4: 45 residues, 117460760-117460890Exon5: 246 residues, 117462178-117462912Exon6: 360 residues, 117464858-117465934Exon7: 2 residues, -Jump to TRI45_HUMAN  
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