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0NUIM_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNDUFS8
DescriptionNadh-ubiquinone oxidoreductase 23 kda subunit, mitochondrial precursor (ec 1.6.5.3) (ec 1.6.99.3) (complex i-23kd) (ci-23kd) (tyky subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009055 electron carrier activity (TAS)
0008137 NADH dehydrogenase (ubiquinone) activity (TAS)
0006120 mitochondrial electron transport, NADH to u... (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:
Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s) . One group.riginally found in bacteria.as been termed "bacterial-type".n which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups.ased on their sequence properties. Most contain at least one conserved domain.ncluding four Cys residues that bind to a 4Fe-4S centre. During the evolution of bacterial-type ferredoxins.ntrasequence gene duplication.ransposition and fusion events occured.esulting in the appearance of proteins with multiple iron-sulphur centres: e.g. dicluster- type (2[4Fe-4S]) and polyferredoxins.ron-sulphur subunits of bacterial succinate dehydrogenase/fumarate reductase.ormate hydrogenlyase and formate dehydrogenase complexes.yruvate-flavodoxin oxidoreductase.ADH:ubiquinone reductase and others. In some bacterial ferredoxins.ne of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron-sulphur binding property.r bind to a 3Fe-4S centre instead of a 4Fe-4S centre. 3D structures are now known both for a number of monocluster-type and dicluster-type 4Fe-4S ferredoxins.CAUTION: PRINTS signature in the current entry is known to miss protein matches and should be updated in the near future.
  IPR001450:4Fe-4S ferredoxin, iron-sulfur binding
The alpha-helical ferredoxin domain contains two Fe4-S4 clusters.ypical of bacterial ferredoxin. Iron-sulphur proteins play an important role in electron transfer processes and in various enzymatic reactions. In eukaryotes.he mitochondria are the major site of Fe-S cluster biosynthesis in the cell.sed for the assembly of mitochondrial and non-mitochondrial Fe-S proteins. The alpha-helical ferredoxin domain is present in several proteins involved in redox reactions.ncluding the C-terminal of the respiratory proteins succinate dehydrogenase (SQR) in bacteria/mitochondria.nd fumarate reductase (QFR) in bacteria. SQR is analogous to the mitochondrial respiratory complex II.nd is involved in the electron transport pathway from succinate as a donor to the acceptor ubiquinone . SQR helps prevent the formation of reactive oxygen species and is used during aerobic respiration.hereas QFR does not and.onsequently.s used to catalyse the final step of anaerobic respiration using the acceptor fumarate .The alpha-helical ferredoxin domain is also present in the N-terminal of the cytosolic protein dihydropyrimidine dehydrogenase.DPD) which catalyses the NADPH-dependent.ate-limiting step in pyrimidine degradation.onverting pyrimidines to 5.-dihydro compounds . DPD catalysis involves electron transfer from NADPH to the substrate via the Fe4-S4 centre and FAD. In mammals.his pathway produces the neurotransmitter beta-alanine.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009051:Alpha-helical ferredoxin
This entry represents the I subunit (one of 14 subunits. to N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria.ut may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This family does not contain I subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes.
  IPR010226:NADH-quinone oxidoreductase, chain I
IPR001450:Fer4 
Evalue:-7.67778062820435 
Location:143-166IPR001450:Fer4 
Evalue:-4.85387182235718 
Location:104-127
SequencesProtein: NUIM_HUMAN (210 aa)
mRNA: NM_002496
Local Annotation
Synapse Ontology
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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 31 residues, 67554684-67554776Exon2: 21 residues, 67556194-67556252Exon3: 19 residues, 67556328-67556379Exon4: 32 residues, 67556965-67557055Exon5: 59 residues, 67557153-67557326Exon6: 45 residues, 67560295-67560424Exon7: 64 residues, 67560504-67560690Exon8: 2 residues, -Jump to NUIM_HUMAN  
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Loci Cluster (Details)Loci: 2672 63498654-63500590 ~-2K 6992(COX8A)(+)Loci: 2673 63758841-63762834 ~-4K 7008(VEGFB)(+)Loci: 2674 63775570-63791969 ~-16K 7011(PLCB3)(+)Loci: 2675 63883200-63896262 ~-13K 7031(RPS6KA4)(+)Loci: 3958 64130223-64247236 ~-117K 7042(NRXN2)(-)Loci: 3959 64376783-64402767 ~-26K 7059(EHD1)(-)Loci: 2676 64551485-64564618 ~-13K 7071(SNX15)(+)Loci: 2677 64635935-64640274 ~-4K 7081(TM7SF2)(+)Loci: 2678 64705918-64736052 ~-30K 7088(CAPN1)(+)Loci: 2679 65049159-65062750 ~-14K 7102(+)Loci: 3960 65121802-65138296 ~-16K 7115(MAP3K11)(-)Loci: 3961 65407787-65412586 ~-5K 7136(FIBP)(-)Loci: 3962 65416267-65424573 ~-8K 7139(FOSL1)(-)Loci: 2680 65594399-65768789 ~-174K 7153(PACS1)(+)Loci: 2681 65792680-65801537 ~-9K 7155(RAB1B)(+)Loci: 2682 65815916-65820707 ~-5K 7159(+)Loci: 3963 65856117-65860576 ~-4K 7162(RIN1)(-)Loci: 2683 66140672-66151387 ~-11K 7189(RBM14)(+)Loci: 2684 66162753-66170514 ~-8K 7192(RBM4)(+)Loci: 3964 66209298-66245446 ~-36K 7194(SPTBN2)(-)Loci: 3965 66372572-66478456 ~-106K 7198(PC)(-)Loci: 2685 66547466-66574905 ~-27K 7200(SYT12)(+)Loci: 2686 66580896-66596059 ~-15K 7201(RHOD)(+)Loci: 3966 66922227-66925952 ~-4K 7219(PPP1CA)(-)Loci: 2687 66979393-66983261 ~-4K 7229(CABP4)(+)Loci: 2688 67130982-67136581 ~-6K 7239(NDUFV1)(+)Loci: 2689 67554684-67560690 ~-6K 7248(NDUFS8)(+)Loci: 2690 67836710-67973317 ~-137K 7259(LRP5)(+)Loci: 2671 63412650-63433621 ~-21K 6988(MARK2)(+)Link out to UCSC