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0ARD1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRIM23
DescriptionGtp-binding protein ard-1 (adp-ribosylation factor domain protein 1) (tripartite motif protein 23) (ring finger protein 46).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008047 enzyme activator activity (TAS)
0003924 GTPase activity (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:
The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic . They are the founding members of a growing family that includes Arl (Arf-like).rp(Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterized by conformational changes at the so-called switch 1 and switch 2 regions.hich bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes.hey depart from other small GTP-binding proteins in that they use an additional.nique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. In GDP-boundArf1 and Arf6.he interswitch is retracted and forms a pocket to which the N-terminal helix binds.he latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins.he interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up.estoring an active conformation that can bind GTP. In this conformation.he interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.
  IPR006689:ARF/SAR superfamily
The small ADP ribosylation factor (Arf) GTP-binding proteins are major regulators of vesicle biogenesis in intracellular traffic . They are the founding members of a growing family that includes Arl (Arf-like).rp (Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterized by conformational changes at the so-called switch 1 and switch 2 regions.hich bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes.hey depart from other small GTP-binding proteins in that they use an additional.nique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2-beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus. In GDP-bound Arf1 and Arf6.he interswitch is retracted and forms a pocket to which the N-terminal helix binds.he latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins.he interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up.estoring an active conformation that can bind GTP. In this conformation.he interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket. ADP-ribosylation factors (ARF) are 20 kDa GTP-binding proteins involved in protein trafficking. They may modulate vesicle budding and uncoating within the Golgi apparatus. ARFs also act as allosteric activators of cholera toxin ADP-ribosyltransferase activity. They are evolutionary conserved and present in all eukaryotes. At least six forms of ARF are present in mammals and three in budding yeast. The ARF family also includes proteins highly related to ARFs but which lack the cholera toxin cofactor activity.hey are collectively known as ARLs (ARF-like). The ARFs are N-terminally myristoylated (the ARLs have not yet been shown to be modified in such a fashion).
  IPR006688:ADP-ribosylation factor
The B-box C-terminal domain is a coiled coil region C-terminal to (some) B-Box domains. It is found in transcription intermediary factor 1-alpha.hich associates with DNA-bound estrogen receptors; ring finger protein. putative transcriptional regulator; and the GTP-binding protein Ard-1.
  IPR003649:B-box, C-terminal
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
Many members of the Ras superfamily of GTPases have been implicated in the regulation of hematopoietic cells.ith roles in growth.urvival.ifferentiation.ytokine production.hemotaxis.esicle-trafficking.nd phagocytosis. The Ras superfamily of proteins now includes over 150 small GTPases (distinguished from the large.eterotrimeric GTPases.he G-proteins). It comprises six subfamilies.he Ras.ho.an.ab.rf.nd Kir/Rem/Rad subfamilies . They exhibit remarkable overall amino acid identities.specially in the regions interacting with the guanine nucleotide exchange factors that catalyze their activation .
  IPR001806:Ras GTPase
Proteins with a small GTP-binding domain include Ras.hoA.ab11.ranslation elongation factor G.ranslation initiation factor IF-2.etratcycline resistance protein TetM.DC42.ra.DP-ribosylation factors.dhF.nd many others . In some proteins the domain occurs more than once. Among them there is a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.
  IPR005225:Small GTP-binding protein domain
IPR006689:Arf 
Evalue:-116.091514587402 
Location:390-565IPR003649:BBC 
Evalue:-41.7695510786217 
Location:226-370IPR000315:zf-B_box 
Evalue:-6.95860719680786 
Location:122-168IPR000315:BBOX 
Evalue:-6.2518119729938 
Location:173-219IPR001841:zf-C3HC4 
Evalue:-4.76955127716064 
Location:31-74
SequencesProtein: ARD1_HUMAN (574 aa)
mRNA: NM_001656
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentK07963
  Level 3 annotation:
    tripartite motif-containing 2
  Level 2 annotation:
    GTP-binding proteins
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 756 residues, 64921264-64923531Exon2: 43 residues, 64926103-64926228Exon3: 39 residues, 64928003-64928114Exon4: 45 residues, 64928633-64928763Exon5: 47 residues, 64936493-64936628Exon6: 74 residues, 64940825-64941041Exon7: 63 residues, 64942443-64942626Exon8: 95 residues, 64943185-64943464Exon9: 42 residues, 64945680-64945802Exon10: 56 residues, 64949675-64949838Exon11: 57 residues, 64955776-64955943Exon12: 2 residues, -Jump to ARD1_HUMAN  
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Loci Cluster (Details)Loci: 3457 65053840-65155143 ~-101K 28898(NLN)(+)Loci: 3458 65258139-65412606 ~-154K 28902(ERBB2IP)(+)Loci: 3459 65489710-65512393 ~-23K 28906(SFRS12)(+)Loci: 4715 64921264-64955943 ~-35K 28891(TRIM23)(-)Link out to UCSC