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0RANB9_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRANBP9
DescriptionRan-binding protein 9 (ranbp9) (ranbp7) (ran-binding protein m) (ranbpm) (bpm90) (bpm-l).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (IDA)
0005515 protein binding (IPI)
0007020 microtubule nucleation (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
The CR.r CT11-RanBPM.omain is a protein-protein interaction domain present in crown eukaryotes (plants.nimals.ungi).
  IPR013144:CT11-RanBPM
The 33-residue LIS1 homology (LisH) motif () is found in eukaryotic intracellularproteins involved in microtubule dynamics.ell migration.ucleokinesis andchromosome segregation. The LisH motif is likely to possess a conservedprotein-binding function and it has been proposed that LisH motifs contributeto the regulation of microtubule dynamics.ither by mediating dimerization.r else by binding cytoplasmic dynein heavy chain or microtubules directly.The LisH motif is found associated to other domains.uch as WD-40 (see).PRY.elch.AA ATPase.asGEF.r HEAT (see ) .The secondary structure of the LisH domain is predicted to be two alpha-helices .Some proteins known to contain a LisH motif are listed below: Animal LIS1. It regulates cytoplasmic dynein function. In human.hildren with defects in LIS1 suffer from Miller-Dieker lissencephaly. brain malformation that results in severe retardation.pilepsy and an early death. Emericella nidulans nuclear migration protein nudF.he orthologue of LIS1. Eukaryotic RanBPM. Ran binding protein involved in microtubule nucleation. Eukaryotic Nopp140. nucleolar phosphoprotein. Mammalian treacle. nucleolar protein. In human.efects in treacle are the cause of Treacher Collins syndrome (TCS).n autosomal dominant disorder of craniofacial development. Animal muskelin. It acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component thrombospondin 1. Animal transducin beta-like 1 protein (TBL1). Plant tonneau. Arabidopsis thaliana LEUNIG. putative transcriptional corepressor that regulates AGAMOUS expression during flower development. Fungal aimless RasGEF. Leishmania major katanin-like protein.The C-terminal to LisH (CTLH) motif is a predicted alpha-helical sequence ofunknown function that is found adjacent to the LisH motif in a number of theseproteins but is absent in other (e.g. LIS1) . The CTLH domain can alsobe found in the absence of the LisH motif.ike in: Arabidopsis thaliana hypothetical protein MUD21.5. Yeast protein RMD5.
  IPR006595:CTLH, C-terminal to LisH motif
A sequence motif.isH.as been identified in the products of genes mutated in Miller-Dieker lissencephaly.reacher Collins.ral-facial-digital type 1 and contiguous syndrome ocular albinism with late onset sensorineural deafness syndromes. An additional homologous motif was detected in a gene product fused to the fibroblast growth factor receptor type 1 in patients with an atypical stem cell myeloproliferative disorder. In total.ver 100 eukaryotic intracellular proteins are shown to possess a LIS1 homology (LisH) motif.ncluding several katanin p60 subunits.uskelin.onneau.EUNIG.opp140.imless and numerous WD repeat-containing beta-propeller proteins . It is suggested that LisH motifs contribute to the regulation of microtubule dynamics.ither by mediating dimerization.r else by binding cytoplasmic dynein heavy chain or microtubules directly. The predicted secondary structure of LisH motifs.nd their occurrence in homologues of Gbeta beta-propeller subunits.uggests that they are analogues of Ggamma subunits.nd might associate with the periphery of beta-propeller domains.
  IPR006594:Lissencephaly type-1-like homology motif
The LisH (lis homology) domain mediates protein dimerisation and tetramerisation. The LisH domain is found in Sif2. component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex .
  IPR013720:LisH
IPR003877:SPRY 
Evalue:-42.7695510786217 
Location:212-333IPR013144:CRA 
Evalue:-23.4948501586914 
Location:615-717IPR006595:CTLH 
Evalue:-14.0222763947112 
Location:403-460IPR006594:LisH 
Evalue:-4.18045606445813 
Location:365-397
SequencesProtein: RANB9_HUMAN (729 aa)
mRNA: NM_005493
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 332 residues, 13729709-13730703Exon2: 39 residues, 13733863-13733975Exon3: 52 residues, 13740580-13740732Exon4: 42 residues, 13742641-13742763Exon5: 51 residues, 13746018-13746166Exon6: 65 residues, 13747773-13747964Exon7: 38 residues, 13749409-13749518Exon8: 39 residues, 13750689-13750802Exon9: 63 residues, 13752755-13752940Exon10: 9 residues, 13760869-13760892Exon11: 58 residues, 13765319-13765487Exon12: 19 residues, 13766990-13767043Exon13: 39 residues, 13804995-13805107Exon14: 212 residues, 13819145-13819775Exon15: 2 residues, -Jump to RANB9_HUMAN  
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