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0KIF1A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameKIF1A
DescriptionKinesin-like protein kif1a (axonal transporter of synaptic vesicles).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003774 motor activity (TAS)
0008089 anterograde axon cargo transport (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 pleckstrin homology (PH) domain is a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton .The function of this domain is not clear.everal putative functions have been suggested:binding to the beta/gamma subunit of heterotrimeric G proteins.inding to lipids..g. phosphatidylinositol-4.-bisphosphate.inding to phosphorylated Ser/Thr residues.ttachment to membranes by an unknown mechanism.It is possible that different PH domains have totally different ligand requirements.The 3D structure of several PH domains has been determined . All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets.ollowed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length.aking the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin.he protein where this domain was first detected.s the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family.he beta-adrenergic receptor kinases.he mu isoform of PKC and the trypanosomal NrkA family.Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains).uanine nucleotide exchange proteins like vav.bl.oS and Saccharomyces cerevisiae CDC24.TPase activating proteins like rasGAP and BEM2/IPL2.nd the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ).aenorhabditis elegans kinesin-like protein unc-104 (see ).pectrin beta-chain.yntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains.he second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP.. cerevisiae OSH1 and YHR073w.Mouse protein citron. putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2.EM3.UD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1.06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w.
  IPR001849:Pleckstrin-like
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
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
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
IPR001752:Kinesin 
Evalue:-181.920822143555 
Location:11-355IPR001849:PH 
Evalue:-20.7212467193604 
Location:1576-1673IPR000253:FHA 
Evalue:-10.1426677703857 
Location:516-587
SequencesProtein: KIF1A_HUMAN (1690 aa)
mRNA: NM_004321
Local Annotation
Synapse Ontology
The directed movement of substances, either within a vesicle or in the vesicle membrane, into, out of or within a cell.
sdb:0057 axon transport  (Evidence:keywords)
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)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
interaction between synaptic vesicle and the scaffold.
sdb:0106 transport of synaptic vesicle in the presynaptic axon  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1214 residues, 241301857-241305496Exon2: 41 residues, 241306139-241306258Exon3: 66 residues, 241307095-241307288Exon4: 53 residues, 241307863-241308016Exon5: 43 residues, 241309003-241309128Exon6: 28 residues, 241309896-241309974Exon7: 69 residues, 241310545-241310746Exon8: 50 residues, 241311502-241311648Exon9: 22 residues, 241312064-241312126Exon10: 46 residues, 241313360-241313494Exon11: 40 residues, 241314915-241315030Exon12: 37 residues, 241325152-241325258Exon13: 30 residues, 241328147-241328232Exon14: 24 residues, 241328387-241328454Exon15: 38 residues, 241329358-241329467Exon16: 20 residues, 241331018-241331074Exon17: 41 residues, 241332031-241332150Exon18: 32 residues, 241333516-241333607Exon19: 59 residues, 241333827-241333999Exon20: 48 residues, 241334128-241334267Exon21: 30 residues, 241335325-241335411Exon22: 41 residues, 241338518-241338637Exon23: 48 residues, 241346449-241346587Exon24: 61 residues, 241348754-241348933Exon25: 51 residues, 241349318-241349467Exon26: 33 residues, 241350808-241350902Exon27: 26 residues, 241351108-241351181Exon28: 62 residues, 241351255-241351436Exon29: 30 residues, 241353799-241353883Exon30: 37 residues, 241355004-241355111Exon31: 28 residues, 241355355-241355435Exon32: 27 residues, 241357222-241357298Exon33: 28 residues, 241357716-241357796Exon34: 46 residues, 241359060-241359194Exon35: 49 residues, 241361203-241361346Exon36: 28 residues, 241362272-241362351Exon37: 27 residues, 241363940-241364016Exon38: 8 residues, 241370679-241370697Exon39: 24 residues, 241371133-241371199Exon40: 28 residues, 241371828-241371906Exon41: 39 residues, 241373078-241373190Exon42: 61 residues, 241374424-241374603Exon43: 24 residues, 241375340-241375406Exon44: 62 residues, 241376140-241376320Exon45: 27 residues, 241377325-241377402Exon46: 57 residues, 241385736-241385902Exon47: 30 residues, 241408211-241408297Exon48: 2 residues, -Jump to KIF1A_HUMAN  
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