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0ALS2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAlsin (amyotrophic lateral sclerosis protein 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005829 cytosol (IDA)
0005769 early endosome (IDA)
0042598 vesicular fraction (IDA)
0017112 Rab guanyl-nucleotide exchange factor activity (IDA)
0005087 Ran guanyl-nucleotide exchange factor activity (NAS)
0005089 Rho guanyl-nucleotide exchange factor activity (NAS)
0007032 endosome organization and biogenesis (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:
This domain is present in yeast vacuolar sorting protein 9 and other proteins.
  IPR003123:Vacuolar sorting protein 9
The MORN (Membrane Occupation and Recognition Nexus) motif is found in multiple copies in several proteins including junctophilins (). The function of this motif is unknown.
  IPR003409:MORN motif
The Rho family GTPases and CDC42 regulate a diverse array of cellularprocesses. Like all members of the Ras superfamily.he Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states.Activation of Rho proteins through release of bound GDP and subsequentbinding of GTP.s catalyzed by guanine nucleotide exchange factors (GEFs) inthe Dbl family. The proteins encoded by members of the Dbl family share acommon domain.resented in this entry.f about 200 residues (designated the Dbl homology or DH domain)that has been shown to encode a GEF activity specific for a number of Rhofamily members. In addition.ll family members possess a second.hareddomain designated the pleckstrin homology (PH) domain (). Trioand its homolog UNC-73 are unique within the Dbl family insomuch as theyencode two distinct DH/PH domain modules. The PH domain is invariably locatedimmediately C-terminal to the DH domain and this invariant topography suggestsa functional interdependence between these two structural modules. Biochemicaldata have established the role of the conserved DH domain in Rho GTPaseinteraction and activation.nd the role of the tandem PH domain inintracellular targeting and/or regulation of DH domain function. The DH domainof Dbl has been shown to mediate oligomerization that is mostly homophilic innature. In addition to the tandem DH/PH domains Dbl family GEFs containdiverse structural motifs like serine/threonine kinase.BD.DZ.GS.Q.EM.dc25RasGEF.H.H2.H3.F.pectrin or Ig.The DH domain is composed of three structurally conserved regions separated bymore variable regions. It does not share significant sequence homology withother subtypes of small G-protein GEF motifs such as the Cdc25 domain and theSec7 domain.hich specifically interact with Ras and ARFfamily small GTPases.espectively.or with other Rho protein interactivemotifs.ndicating that the Dbl family proteins are evolutionarily unique. TheDH domain is composed of 11 alpha helices that are folded into a flattened.longated alpha-helix bundle in which two of the three conserved regions.onserved region 1 (CR1) and conserved region 3 (CR3).re exposed near thecenter of one surface. CR1 and CR3.ogether with a part of alpha-6 and theDH/PH junction site.onstitute the Rho GTPase interacting pocket.
The regulator of chromosome condensation (RCC1) is a eukaryotic proteinwhich binds to chromatin and interacts with ran. nuclear GTP-bindingprotein .o promote the loss of bound GDP and the uptake offresh GTP.hus acting as a guanine-nucleotide dissociation stimulator (GDS).The interaction of RCC1 with ran probably plays an important role in theregulation of gene expression.RCC1.nown as PRP20 or SRM1 in yeast.im1 in fission yeast and BJ1 inDrosophila.s a protein that contains seven tandem repeats of a domain ofabout 50 to 60 amino acids. As shown in the following schematicrepresentation.he repeats make up the major part of the length of theprotein. Outside the repeat is just a small N-terminal domain ofabout 40 to 50 residues and.n the Drosophila protein only. C-terminaldomain of about 130 residues.The RCC1-type of repeat is also found in the X-linked retinitis pigmentosaGTPase regulator . The RCC repeats form a beta-propellerstructure.
  IPR000408:Regulator of chromosome condensation, RCC1
The beta-lactamase-inhibitor protein II (BLIP-II) is a secreted protein produced by the soil bacteria Streptomyces exfoliates SMF19. BLIP-II acts as a potent inhibitor of beta-lactamases such as TEM-1.hich is the most widespread resistance enzyme to penicillin antibiotics. BLIP-II binds competitively to TEM-1.ut no direct contacts are made with TEM-1 active site residues. BLIP-II shows no sequence similarity with BLIP.ven though both bind to and inhibit TEM-1. However.LIP-II does share significant sequence identity with the regulator of chromosome condensation (RCC1) family of proteins. These two families are clearly related.oth having a seven-bladed beta-propeller structure.lthough they differ in the number of strands per blade.LIP-II having three antiparallel beta-strands per blade.hile RCC1 has four-stranded blades . RCC1 is a eukaryotic nuclear protein that acts as a guanine nucleotide exchange factor for Ran. member of the Ras GTPase family. RCC1 mediates a Ran-GTP gradient necessary for the regulation of spindle formation and nuclear assembly during mitosis.s well as for the transport of macromolecules across the nuclear membrane during interphase.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009091:Regulator of chromosome condensation/beta-lactamase-inhibitor protein II
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling 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 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
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 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.
SequencesProtein: ALS2_HUMAN (1657 aa)
mRNA: NM_020919
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)
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
KO assignmentK04575
  Level 3 annotation:
    amyotrophic lateral sclerosis 2 (juvenile)
  Level 2 annotation:
    Amyotrophic lateral sclerosis (ALS)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 446 residues, 202273521-202274857Exon2: 34 residues, 202277089-202277186Exon3: 52 residues, 202277421-202277571Exon4: 22 residues, 202278106-202278168Exon5: 17 residues, 202278383-202278429Exon6: 61 residues, 202279813-202279990Exon7: 43 residues, 202280836-202280959Exon8: 54 residues, 202282848-202283006Exon9: 41 residues, 202283958-202284076Exon10: 58 residues, 202288639-202288807Exon11: 46 residues, 202291044-202291178Exon12: 28 residues, 202296010-202296088Exon13: 39 residues, 202296297-202296409Exon14: 57 residues, 202297262-202297427Exon15: 35 residues, 202298323-202298422Exon16: 24 residues, 202299451-202299517Exon17: 69 residues, 202299631-202299834Exon18: 24 residues, 202300179-202300246Exon19: 25 residues, 202300672-202300743Exon20: 45 residues, 202301479-202301608Exon21: 46 residues, 202302019-202302151Exon22: 56 residues, 202306243-202306406Exon23: 24 residues, 202311637-202311703Exon24: 62 residues, 202314641-202314822Exon25: 59 residues, 202317225-202317397Exon26: 63 residues, 202319533-202319716Exon27: 28 residues, 202322679-202322757Exon28: 34 residues, 202326113-202326210Exon29: 58 residues, 202327470-202327639Exon30: 121 residues, 202330369-202330727Exon31: 314 residues, 202333848-202334786Exon32: 53 residues, 202340196-202340351Exon33: 28 residues, 202341833-202341913Exon34: 48 residues, 202353844-202353983Exon35: 2 residues, -Jump to ALS2_HUMAN  
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Loci Cluster (Details)Loci: 4489 202273521-202353983 ~-80K 21886(ALS2)(-)Loci: 4488 201950175-202024499 ~-74K 21876(ALS2CR3)(-)Link out to UCSC