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0SMC3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCSPG6
DescriptionStructural maintenance of chromosome 3 (chondroitin sulfate proteoglycan 6) (chromosome-associated polypeptide) (hcap) (bamacan) (basement membrane-associated chondroitin proteoglycan).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005604 basement membrane (TAS)
0008278 cohesin complex (NAS)
0005737 cytoplasm (IDA)
0016363 nuclear matrix (IDA)
0000922 spindle pole (IDA)
0045502 dynein binding (IDA)
0003777 microtubule motor activity (NAS)
0046982 protein heterodimerization activity (IPI)
0007001 chromosome organization and biogenesis (sen... (TAS)
0009294 DNA mediated transformation (TAS)
0007126 meiosis (IDA)
0007052 mitotic spindle organization and biogenesis (IEP)
0007165 signal transduction (IDA)
0007062 sister chromatid cohesion (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 SMC (structural maintenance of chromosomes) family of proteins exists in virtually all organisms including both bacteria and archaea. The SMC proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms and form three types of heterodimer (SMC1SMC3.MC2SMC4.MC5SMC6).hich are core components of large multiprotein complexes. The best known complexes are cohesin.hich is responsible for sister-chromatid cohesion.nd condensin.hich is required for full chromosome condensation in mitosis. SMCs are generally present as single proteins in bacteria.nd as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa.nd share a five-domain structure.ith globular N- and C-terminal domains separated by a long (circa 100 nm or 900 residues) coiled coil segment in the centre of which is a globular hinge domain.haracterized by a set of four highly conserved glycine residues that are typical of flexible regions in a protein. The amino-terminal domain contains a Walker A nucleotide-binding domain (GxxGxGKS/T).hich by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a Walker B motif (XXXXD.here X is any hydrophobic residue).nd a LSGG motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases . All SMC proteins appear to form dimers.ither forming homodimers with themselves.s in the case of prokaryotic SMC proteins.r heterodimers between different but related SMC proteins. The dimers are arranged in an antiparallel alignment. This orientation brings the N- and C-terminal globular domains (from either different or identical protamers) together.hich unites an ATP binding site (Walker A motif) within the N-terminal domain with a Walker B motif (DA box) within the C-terminal domain.o form a potentially functional ATPase. Protein interaction and microscopy data suggest that SMC dimers form a ring-like structure which might embrace DNA molecules. Non-SMC subunits associate with the SMC amino- and carboxy-terminal domains. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group.hereas SMC5 and SMC6 show some divergence in both of these sequences. SMCs share not only sequence similarity but also structural similarity with ABC proteins. SMC proteins function together with other proteins in a range of chromosomal transactions.ncluding chromosome condensation.ister-chromatid cohesion.ecombination.NA repair and epigenetic silencing of gene expression .This domain is found at the N terminus of SMC proteins.
  IPR003395:SMC protein, N-terminal
This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction .
  IPR010935:SMCs flexible hinge
ATP-binding cassette (ABC) transporters are multidomain membrane proteins.esponsible for the controlled efflux and influx of substances (allocrites) across cellular membranes. They are minimally composed of four domains.ith two transmembrane domains (TMDs) responsible for allocrite binding and transport and two nucleotide-binding domains (NBDs) responsible for coupling the energy of ATP hydrolysis to conformational changes in the TMDs. Both NBDs are capable of ATP hydrolysis.nd inhibition of hydrolysis at one NBD effectively abrogates hydrolysis at the other. Hydrolysis at the two NBDs may occur in an alternative fashion although they appear substantially functionally symmetrical in terms of their binding to diverse nucleotides .On the basis of sequence similarities a family of related ATP-binding proteins has been characterized . The proteins belonging to this family also contain one or two copies of the A consensus sequence or the P-loop (see ).
  IPR003439:ABC transporter related
IPR003395:SMC_N 
Evalue:-116.055519104004 
Location:2-1197
SequencesProtein: SMC3_HUMAN (1217 aa)
mRNA: NM_005445
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)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentK06669
  Level 3 annotation:
    structural maintenance of chromosome 3 (chondroitin sulfate proteoglycan 6)
  Level 2 annotation:
    Proteoglycans
    Cell cycle
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 48 residues, 112317438-112317579Exon2: 27 residues, 112318685-112318761Exon3: 15 residues, 112323454-112323493Exon4: 24 residues, 112325083-112325151Exon5: 26 residues, 112327168-112327240Exon6: 28 residues, 112327582-112327662Exon7: 28 residues, 112328375-112328454Exon8: 41 residues, 112330651-112330769Exon9: 60 residues, 112331670-112331846Exon10: 29 residues, 112332309-112332390Exon11: 57 residues, 112333131-112333296Exon12: 42 residues, 112333588-112333710Exon13: 73 residues, 112333930-112334144Exon14: 36 residues, 112339352-112339456Exon15: 35 residues, 112339639-112339739Exon16: 55 residues, 112340159-112340320Exon17: 49 residues, 112340738-112340880Exon18: 52 residues, 112342820-112342971Exon19: 53 residues, 112346145-112346298Exon20: 52 residues, 112347886-112348038Exon21: 55 residues, 112349401-112349560Exon22: 38 residues, 112350186-112350294Exon23: 38 residues, 112350769-112350878Exon24: 84 residues, 112351384-112351632Exon25: 73 residues, 112351713-112351926Exon26: 66 residues, 112352221-112352413Exon27: 61 residues, 112352572-112352750Exon28: 37 residues, 112352931-112353038Exon29: 136 residues, 112353978-112354380Exon30: 2 residues, -Jump to SMC3_HUMAN  
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