SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0SNX23_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameC20orf23
DescriptionKinesin-like motor protein c20orf23 (sorting nexin 23).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The forkhead-associated (FHA) domain is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich.hich sometimes contain small helical insertions between the loops connecting the strands . To date.enes encoding FHA-containing proteins have been identified in eubacterial and eukaryotic but not archaeal genomes. The domain is present in a diverse range of proteins.uch as kinases.hosphatases.inesins.ranscription factors.NA-binding proteins and metabolic enzymes which partake in many different cellular processes - DNA repair.ignal transduction.esicular transport and protein degradation are just a few examples.
  IPR000253:Forkhead-associated
The PX (phox) domain occurs in a variety of eukaryotic proteins and have been implicated in highly diverse functions such as cell signalling.esicular trafficking.rotein sorting and lipid modification . PX domains are important phosphoinositide-binding modules that have varying lipid-binding specificities .The PX domain is approximately 120 residues long .nd folds into a three-stranded beta-sheet followed by three -helices and a proline-rich region that immediately preceeds a membrane-interaction loop and spans approximately eight hydrophobic and polar residues. The PX domain of p47phox binds to the SH3 domain in the same protein. Phosphorylation of p47(phox). cytoplasmic activator of the microbicidal phagocyte oxidase (phox).licits interaction of p47(phox) with phoinositides. The protein phosphorylation-driven conformational change of p47(phox) enables its PX domain to bind to phosphoinositides.he interaction of which plays a crucial role in recruitment of p47(phox) from the cytoplasm to membranes and subsequent activation of the phagocyte oxidase. The lipid-binding activity of this protein is normally suppressed by intramolecular interaction of the PX domain with the C-terminal Src homology 3 (SH3) domain .The PX domain is conserved from yeast to human. A recent multiple alignment of representative PX domain sequences can be found in .lthough showing relatively little sequence conservation.heir structure appears to be highly conserved. Although phosphatidylinositol-3-phosphate (PtdIns(3)P) is the primary target of PX domains.inding to phosphatidic acid.hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-3.-bisphosphate (PtdIns(3.)P2).hosphatidylinositol-4.-bisphosphate (PtdIns(4.)P2).nd phosphatidylinositol-3..-trisphosphate (PtdIns(3..)P3) has been reported as well. The PX-domain is also a protein-protein interaction domain .
  IPR001683:Phox-like
Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubules plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyze ATP.o bind and move on microtubules). central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains).esicles and membranous organelles.A number of proteins have been recently found that contain a domain similar to that of the kinesin motor domain .Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis.n females.nd in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubules minus end.Homo sapiens CENP-E . CENP-E is a protein that associates with kinetochores during chromosome congression.elocates to the spindle midzone at anaphase.nd is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.H.sapiens mitotic kinesin-like protein-1 (MKLP-1). motor protein whose activity is directed toward the microtubules plus end.Saccharomyces cerevisiae KAR3 protein.hich is essential for S. cerevisiae nuclear fusion during mating. KAR3 may mediate microtubule sliding during nuclear fusion and possibly mitosis.S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce an outwardly directed force acting upon the poles.Emericella nidulans bimC.hich plays an important role in nuclear division.E. nidulans klpA.Caenorhabditis elegans unc-104.hich may be required for the transport of substances needed for neuronal cell differentiation.C. elegans osm-3.Xenopus laevis Eg5.hich may be involved in mitosis.Arabidopsis thaliana KatA.atB and katC.Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.C. elegans hypothetical protein T09A5.2.The kinesin motor domain is located in the N-terminal part of most of the above proteins.ith the exception of KAR3.lpA.nd ncd where it is located in the C-terminal section.The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90.he C-terminal half of the domain is involved in microtubule-binding.
  IPR001752:Kinesin, motor region
FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven beta strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids.hereas the full-length domain is closer to about 150 amino acids. FHA domains are found in transcription factors.inesin motors.nd in a variety of other signalling molecules in organisms ranging from eubacteria to humans. FHA domains are protein-protein interaction domains that are specific for phosphoproteins. FHA-containing proteins function in maintaining cell-cycle checkpoints.NA repair and transcriptional regulation. FHA domain proteins include the Chk2/Rad53/Cds1 family of proteins that contain one or more FHA domains.s well as a Ser/Thr kinase domain . SMAD domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA.nd is separated by a short linker region from the C-terminal MH2 domain.he later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs).ncluding SMAD1.2.3.5.nd -8.ach of which is involved in a ligand-specific signalling pathway ; the comediator SMADs (co-SMADs).ncluding SMAD4.hich interact with R-SMADs to participate in signalling ; and the inhibitory SMADs (I-SMADs).ncluding SMAD6 and -7.hich block the activation of R-SMADs and Co-SMADs.hereby negatively regulating signalling pathways . The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008984:SMAD/FHA
IPR001752:KISc 
Evalue:-173.008773924307 
Location:1-366IPR000253:FHA 
Evalue:-9.30980396270752 
Location:478-544IPR001683:PX 
Evalue:-8.33724212646484 
Location:1182-1286IPR001220:LECTIN_LEGUME_BETA 
Evalue:0 
Location:445-451IPR000253:FHA_DOMAIN 
Evalue:0 
Location:0-0
SequencesProtein: SNX23_HUMAN (1317 aa)
mRNA: NM_024704
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 437 residues, 16200748-16202056Exon2: 30 residues, 16240979-16241063Exon3: 32 residues, 16264570-16264660Exon4: 43 residues, 16284974-16285097Exon5: 19 residues, 16299230-16299281Exon6: 34 residues, 16300309-16300406Exon7: 53 residues, 16302901-16303054Exon8: 455 residues, 16307449-16308808Exon9: 20 residues, 16310338-16310392Exon10: 31 residues, 16333457-16333546Exon11: 29 residues, 16335018-16335101Exon12: 48 residues, 16355748-16355886Exon13: 19 residues, 16357597-16357649Exon14: 42 residues, 16358507-16358627Exon15: 22 residues, 16422935-16422995Exon16: 24 residues, 16426257-16426323Exon17: 60 residues, 16433016-16433192Exon18: 46 residues, 16434366-16434498Exon19: 58 residues, 16434666-16434835Exon20: 49 residues, 16436602-16436745Exon21: 38 residues, 16440062-16440172Exon22: 34 residues, 16441470-16441568Exon23: 41 residues, 16444192-16444309Exon24: 40 residues, 16454736-16454850Exon25: 25 residues, 16457015-16457085Exon26: 70 residues, 16501873-16502078Exon27: 2 residues, -Jump to SNX23_HUMAN  
Tune and view alternative isoforms