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0CRIM1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCRIM1
DescriptionCysteine-rich motor neuron 1 protein precursor (crim-1) (cysteine-rich repeat-containing protein s52).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (TAS)
0005010 insulin-like growth factor receptor activity (TAS)
0007399 neurogenesis (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 vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands .The domain is named after the von Willebrand factor (VWF) type C repeat which is found in multidomain protein/multifunctional proteins involved in maintaining homeostasis . For the von Willebrand factor the duplicated VWFC domain is thought to participate in oligomerization.ut not in the initial dimerization step . The presence of this region in a number of other complex-forming proteins points to the possible involvment of the VWFC domain in complex formation.
  IPR001007:von Willebrand factor, type C
The insulin-like growth factors (IGF-I and IGF-II) bind to specific binding proteins in extracellular fluids with high affinity . These IGF-bindingproteins (IGFBP) prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cells culture. They seem to alter the interaction of IGFs with their cell surface receptors. There are at least six different IGFBPs and they are structurally related. The following growth-factor inducible proteins are structurally related to IGFBPs and could function as growth-factor binding proteins mouse protein cyr61 and its probable chicken homolog.rotein CEF-10; human connective tissue growth factor (CTGF) and its mouse homolog.rotein FISP-12; and vertebrate protein NOV.
  IPR000867:Insulin-like growth factor-binding protein, IGFBP
Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors.espectively. In many cases they are synthesised as part of a larger precursor protein.ither as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. This group of serine protease inhibitors belong to MEROPS inhibitor family I15.lan IO. They inhibit serine peptidases of the S1 family () and are characterized by a well conserved pattern of cysteine residues. Many of the proteins that belong to this family are anti-coagulants.
  IPR004094:Proteinase inhibitor I15, antistasin
This SSF signature was designed to identify serine proteases inhibitors belonging to the grasshopper PMP inhibitor family .nd to the desert locust SGCI/SGTI family .oth of which belong to MEROPS inhibitor family I19.lan IW. The PMP inhibitors have a conserved array of six cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-4)-Cys-Thr-Xaa(3)-Cys).hich are involved in an identical disulfide bridge pattern (Cys(1)-Cys(4).ys(2)-Cys(6).ys(3)-Cys(5)) . Some of the PMP inhibitors are fucosylated.he function of the fucose moiety being unknown.The signature also matches many proteins which are not known to be proteinase inhibitors.nd which are annotated as mucin.CO-spondin.ollagen alpha 1.agged1.agged2 or von Willebrand factor.ype D and type C.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009041:Proteinase inhibitor, PMP and SGCI
Leeches.uch as the medicinal leech Hirudo medicinalis.roduce a variety of antihaemostatic proteins that act as proteinase inhibitors. These inhibitors are used to aid the leech in feeding upon its host by blocking blood coagulation . Examples of these proteins include hirustasin (inhibitor of tissue kallikrein.rypsin.lpha-chymotrypsin.nd granulocyte cathepsin G) .dellastasin (inhibitor of trypsin.lasmin.nd acrosin) .actor Xa inhibitor antistasin (inhibitor of blood coagulation factor Xa) .irudin (thrombin inhibitor).ecorsin (inhibitor of platelet aggregation) and haemadin (thrombin inhibitor) .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011061:Antihaemostatic protein
IPR001007:VWC 
Evalue:-13.6382722854614 
Location:819-873IPR001007:VWC 
Evalue:-12.0409586076789 
Location:753-808IPR001007:VWC 
Evalue:-11.4436974992327 
Location:336-390IPR001007:VWC 
Evalue:-10.8860566476932 
Location:679-734IPR001007:VWC 
Evalue:-10.5850266520292 
Location:608-662IPR001007:VWC 
Evalue:-10.0604807473814 
Location:403-456IPR004094:Antistasin 
Evalue:-5.0915150642395 
Location:567-592IPR000867:IB 
Evalue:-4.60205999132796 
Location:35-111IPR004094:Antistasin 
Evalue:-1.92081880569458 
Location:505-532IPR004094:Antistasin 
Evalue:-1.61978876590729 
Location:539-564IPR004094:Antistasin 
Evalue:-0.920818746089935 
Location:469-498
SequencesProtein: CRIM1_HUMAN (1036 aa)
mRNA: NM_016441
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 124 residues, 36436900-36437270Exon2: 60 residues, 36477260-36477434Exon3: 83 residues, 36521904-36522147Exon4: 42 residues, 36523261-36523382Exon5: 42 residues, 36545180-36545302Exon6: 63 residues, 36557535-36557718Exon7: 68 residues, 36560143-36560341Exon8: 45 residues, 36579865-36579994Exon9: 54 residues, 36590629-36590786Exon10: 42 residues, 36592919-36593041Exon11: 72 residues, 36594202-36594412Exon12: 74 residues, 36597973-36598189Exon13: 76 residues, 36602738-36602960Exon14: 67 residues, 36617998-36618193Exon15: 43 residues, 36625022-36625145Exon16: 64 residues, 36627630-36627818Exon17: 872 residues, 36629171-36631781Exon18: 2 residues, -Jump to CRIM1_HUMAN  
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Loci Cluster (Details)Loci: 4432 36632909-36678821 ~-46K 20263(FEZ2)(-)Loci: 3158 36436900-36631781 ~-195K 20259(CRIM1)(+)Link out to UCSC