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0TRI10_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRIM10
DescriptionTripartite motif protein 10 (ring finger protein 9) (b30-ring finger protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (NAS)
0008270 zinc ion binding (NAS)
0030097 hemopoiesis (NAS)

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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 SPRY domain is of unknown function. Distant homologues are domains inbutyrophilin/marenostrin/pyrin .Ca2+-release from the sarcoplasmic or endoplasmic reticulum.he intracellular Ca2+ store.s mediated by the ryanodine receptor (RyR) and/or the inositol trisphosphate receptor (IP3R).
  IPR003877:SPla/RYanodine receptor SPRY
PRY is a domain associated with SPRY domains. The SPRY domain () is of unknown function however distant homologues are domains in butyrophilin/marenostrin/pyrin. Ca2+-release from the sarcoplasmic or endoplasmic reticulum.he intracellular Ca2+ store.s mediated by the ryanodine receptor (RyR) and/or the inositol trisphosphate receptor (IP3R).The proteins identified by the PRY domain.learly fall into 3 sets which can be defined by their combination of signatures:This group contains an immunoglobulin domain N-terminal to the PRY and butyrophilin domains. Butyrophilins are glycoproteins that are expressed on the apical surfaces of secretory cells in lactating mammary tissue and which may function in the secretion of milk-fat droplets.This group contain a RING-finger domain N-terminal to the PRY domain. The RING-finger is a specialized 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 is not found associated with this group of proteins. This set of proteins are described as TRIM (TRIpartite Motif) family members and are involved in cellular compartmentalisation . The TRIM family sequences are defined by a Ring finger domain. B-box type1 (B1) and a B-box type 2 (B2) followed by a coiled-coil (CC) region . Genes belonging to this family are implicated in a variety of processes such as development and cell growth and are involved in human disease. Many of these proteins.f not all of those with the PRY domain have a number of C-terminal signatures.PRY.FP-like (B30.2) and butyrophilin domain. The B30.2-like domain is a well conserved C-terminal domain of 160-170 amino acids which is found in nuclear and cytoplasmic proteins.s well as transmembrane and secreted proteins. The function of the B30.2-like domain is not known.ut the cytoplasmic B30.2-like domain of butyrophilin has been shown to interact with xanthine oxidase .The third set of proteins have the C-terminal signatures but have no N-terminal RING-finger or immunoglobulin domain signatures. These proteins have not been functionally described.
  IPR006574:SPRY-associated
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
Several proteins that contain RING fingers also contain a well-conserved40-residue cysteine-rich domain termed a B-box zinc finger. Often.ne or two copies of the B-box are associated with a coiled coil domain in additionto the ring finger.orming a tripartite motif. The tripartite motif is found in transcription factors.ibonucleoproteins and proto-oncoproteins.ut no function has yet been ascribed to the domain . The solution structure of the B-box motif has been determined by NMR. The protein is a monomer.ith 2 beta-strands. helical turns and 3extended loop regions packed in a novel topology . Of 7 potential zincligands.nly 4 are used.inding a single zinc atom in a C2-H2 tetrahedral arrangement. The B-box structure differs in tertiary fold from allother known zinc-binding motifs.A group of proteins that contain the B-box motif also host a well conserveddomain of unknown function (DUF). Proteins that include this domain are..g.: butyrophilin.he RET finger protein.he 52kDa Ro protein and theXenopus nuclear factor protein. The C-terminal portion of this region hasbeen termed the SPRY domain (after SPla and the RYanodine Receptor) .
  IPR003879:Butyrophylin-like
IPR003877:SPRY 
Evalue:-26 
Location:362-481IPR006574:PRY 
Evalue:-23.8538719643218 
Location:309-361IPR000315:zf-B_box 
Evalue:-17.1739253997803 
Location:94-135IPR001841:zf-C3HC4 
Evalue:-10.5850267410278 
Location:16-60
SequencesProtein: TRI10_HUMAN (481 aa)
mRNA: AF220122 NM_006778
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 334 residues, 30229242-30230242Exon2: 13 residues, 30231482-30231515Exon3: 40 residues, 30232694-30232810Exon4: 9 residues, 30233124-30233147Exon5: 79 residues, 30234154-30234385Exon6: 34 residues, 30234905-30235001Exon7: 170 residues, 30236185-30236690Exon8: 2 residues, -Jump to TRI10_HUMANLoci index, Chromosomal location, Length, Possible relational loci clusterExon1: 334 residues, 1368158-1369158Exon2: 13 residues, 1370398-1370431Exon3: 40 residues, 1371610-1371726Exon4: 9 residues, 1372040-1372063Exon5: 79 residues, 1373069-1373300Exon6: 34 residues, 1373820-1373916Exon7: 170 residues, 1375100-1375605Exon8: 2 residues, -Jump to TRI10_HUMANLoci index, Chromosomal location, Length, Possible relational loci clusterExon1: 334 residues, 1569907-1570907Exon2: 13 residues, 1572147-1572180Exon3: 40 residues, 1573359-1573475Exon4: 9 residues, 1573789-1573812Exon5: 79 residues, 1574817-1575048Exon6: 34 residues, 1575568-1575664Exon7: 170 residues, 1576848-1577353Exon8: 2 residues, -Jump to TRI10_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3524 30403018-30419484 ~-16K 30623(+)Loci: 4778 30775563-30790934 ~-15K 30651(MDC1)(-)Loci: 3525 30796135-30801172 ~-5K 30654(TUBB2)(+)Loci: 3526 30960305-30975910 ~-16K 30660(DDR1)(+)Loci: 4779 31240107-31246432 ~-6K 30683(POU5F1)(-)Loci: 3527 31651328-31654089 ~-3K 30704(TNF)(+)Loci: 3528 31696575-31713516 ~-17K 30718(BAT2)(+)Loci: 4780 31762714-31779067 ~-16K 30732(BAT5)(-)Loci: 4781 31806338-31812320 ~-6K 30744(CLIC1)(-)Loci: 4782 31934931-31938662 ~-4K 30760(NEU1)(-)Loci: 4783 32027843-32034843 ~-7K 30774(RDBP)(-)Loci: 4784 32116910-32185131 ~-68K 30791(TNXB)(-)Loci: 4785 32191022-32204008 ~-13K 30793(CREBL1)(-)Loci: 4786 32270598-32299822 ~-29K 30822(NOTCH4)(-)Loci: 4777 30229242-30236690 ~-7K 30617(TRIM10)(-)Link out to UCSC  
Loci: 3576 882132-897414 ~-15K 32584(MOG)(+)Loci: 4860 1368158-1375605 ~-7K 32610(TRIM10)(-)Loci: 3577 1541880-1558353 ~-16K 32616(+)Loci: 4861 1914463-1929833 ~-15K 32644(MDC1)(-)Loci: 3578 1935034-1940072 ~-5K 32647(TUBB2)(+)Loci: 3579 2099260-2114867 ~-16K 32653(DDR1)(+)Loci: 4862 2381927-2388269 ~-6K 32673(POU5F1)(-)Loci: 3580 2744366-2745636 ~-1K 32685(MCCD1)(+)Loci: 3581 2790934-2793697 ~-3K 32694(TNF)(+)Loci: 3582 2836184-2853121 ~-17K 32708(BAT2)(+)Loci: 4863 2902325-2918686 ~-16K 32722(BAT5)(-)Loci: 4864 2945936-2951926 ~-6K 32734(CLIC1)(-)Loci: 4865 3074690-3078421 ~-4K 32743(NEU1)(-)Loci: 4866 3167604-3174600 ~-7K 32757(RDBP)(-)Loci: 4867 3377585-3406812 ~-29K 32798(NOTCH4)(-)Loci: 4859 827283-858139 ~-31K 32580(GABBR1)(-)Link out to UCSC  
Loci: 3568 1080116-1095456 ~-15K 32266(MOG)(+)Loci: 4846 1569907-1577353 ~-7K 32295(TRIM10)(-)Loci: 3569 1743552-1760022 ~-16K 32299(+)Loci: 4847 2116160-2131531 ~-15K 32327(MDC1)(-)Loci: 3570 2136731-2141768 ~-5K 32330(TUBB2)(+)Loci: 3571 2300931-2316538 ~-16K 32336(DDR1)(+)Loci: 4848 2583391-2589717 ~-6K 32358(POU5F1)(-)Loci: 3572 2942907-2944177 ~-1K 32370(MCCD1)(+)Loci: 3573 2989472-2992233 ~-3K 32379(TNF)(+)Loci: 3574 3034720-3051660 ~-17K 32394(BAT2)(+)Loci: 4849 3100861-3117213 ~-16K 32408(BAT5)(-)Loci: 4850 3144482-3150469 ~-6K 32420(CLIC1)(-)Loci: 4851 3273206-3276937 ~-4K 32436(NEU1)(-)Loci: 4852 3366127-3373127 ~-7K 32450(RDBP)(-)Loci: 4853 3416089-3484322 ~-68K 32465(TNXB)(-)Loci: 4854 3490215-3503197 ~-13K 32467(CREBL1)(-)Loci: 4855 3569805-3599027 ~-29K 32497(NOTCH4)(-)Loci: 4845 1025321-1056177 ~-31K 32256(GABBR1)(-)Link out to UCSC