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0BRAP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionBrca1-associated protein (ec 6.3.2.-) (brap2) (impedes mitogenic signal propagation) (imp) (ring finger protein 52).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IEP)
0042802 protein self binding (IPI)
0004842 ubiquitin-protein ligase activity (IDA)
0009968 negative regulation of signal transduction (IDA)

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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:
These proteins include BRCA1-associated protein 2 (BRAP2).hich binds nuclear localisation signals (NLSs) in vitro and in yeast two-hybrid screening . These proteins share a region of sequence similarity at their N terminus. They also have at the C terminus.
  IPR011422:BRCA1-associated 2
This domain displays some similarities with the Zn binding domain of the insulinase family. It is found only in a small subfamily of ubiquitinC-terminal hydrolases (deubiquitinases or UBP) All members of thissubfamily are Isopeptidase-T that are known to cleave isopeptide bonds betweenubiquitin moieties.Some of the proteins containing an UBP zinc finger are listed below:Human deubiquitinating enzyme 13 (UBPD)Human deubiquitinating enzyme 5 (UBP5)Dictyostelium discoideum deubiquitinating enzyme A (UBPA)Yeast deubiquitinating enzyme 8 (UBP8)Yeast deubiquitinating enzyme 14 (UBP14)
  IPR001607:Zinc finger, UBP-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
This entry represents nucleotide-binding domains with an alpha-beta plait structure.hich consists of either a ferredoxin-like (beta-alpha-beta)2 fold.uch as that found in RNA-binding domains of various ribonucleoproteins or in viral DNA-binding domains . or a beta-(alpha)-beta-alpha-beta(2) fold.uch as that found in the ribosomal protein L23 .
  IPR012677:Nucleotide-binding, alpha-beta plait
SequencesProtein: BRAP_HUMAN (592 aa)
mRNA: NM_006768
Local Annotation
Synapse Ontology
The Myelin Sheath of a neuron consists of fat-containing cells that insulate the axon from electrical activity. This insulation acts to increase the rate of transmission of signals. A gap exists between each myelin sheath cell along the axon. Since fat inhibits the propagation of electricity, the signals jump from one gap to the next.
sdb:0224 AP propagation through axon process  (Evidence:keywords)
KO assignmentK01932
  Level 3 annotation:
  Level 2 annotation:
    Tryptophan metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 158 residues, 110566278-110566749Exon2: 36 residues, 110572125-110572229Exon3: 32 residues, 110577752-110577842Exon4: 38 residues, 110580922-110581032Exon5: 48 residues, 110581393-110581532Exon6: 27 residues, 110582786-110582862Exon7: 51 residues, 110587825-110587974Exon8: 40 residues, 110594847-110594961Exon9: 65 residues, 110601337-110601527Exon10: 68 residues, 110603823-110604022Exon11: 56 residues, 110605332-110605494Exon12: 77 residues, 110607897-110608122Exon13: 2 residues, -Jump to BRAP_HUMAN  
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Loci Cluster (Details)Loci: 4075 110566278-110608122 ~-42K 9715(BRAP)(-)Loci: 2788 110688728-110732165 ~-43K 9721(ALDH2)(+)Loci: 4074 110374401-110521863 ~-147K 9714(ATXN2)(-)Link out to UCSC