SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0SMBP2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionDna-binding protein smubp-2 (immunoglobulin mu-binding protein 2) (smubp-2) (glial factor 1) (gf-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003678 DNA helicase activity (TAS)
0005515 protein binding (IPI)
0003697 single-stranded DNA binding (TAS)
0006310 DNA recombination (TAS)
0006281 DNA repair (TAS)
0006260 DNA replication (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/ [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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 R3H motif: a domain that binds single-stranded nucleic acids.The most prominent feature of the R3H motif is the presence of an invariant arginine residue and a highly conserved histidine residue that are separated by three residues. The motif also displays a conserved pattern of hydrophobic residues.rolines and glycines. The R3H motif is present in proteins from a diverse range of organisms that includes Eubacteria.reen plants.ungi and various groups of metazoans. Intriguingly.t has not yet been identified in Archaea and Escherichia coli.The sequences that contain the R3H domain.any of which are hypothetical proteins predicted from genome sequencing be grouped into eight families on the basis of similarities outside the R3H region. Three of the families contain ATPase domains either upstream (families II and VII) or downstream of the R3H domain (family VIII). The N-terminal part of members of family VII contains an SF1 helicase domain5. The C-terminal part of family VIII contains an SF2 DEAH helicase domain5. The ATPase domain in the members of family II is similar to the stage-III sporulation protein AA (S3AA_BACSU).he proteasome ATPase.acterial transcription-termination factor r and the mitochondrial F1-ATPase b subunit (the F5 helicase family5). Family VI contains Cys-rich repeats6.s well as a ring-type zinc finger upstream of the R3H domain. JAG bacterial proteins (family I) contain a KH domain N-terminal to the R3H domain. The functions of other domains in R3H proteins support the notion that the R3H domain might be involved in interactions with single-stranded nucleic acids .
  IPR001374:Single-stranded nucleic acid binding R3H
This domain was first identified as a zinc finger at the C-terminus of An1 a ubiquitin-likeprotein in Xenopus laevis .The following pattern describes the zinc finger.where X can be any amino acid.nd numbers in brackets indicate the number of residues. It has now been identified in a number of.s yet uncharacterised proteins from various sources.
  IPR000058:Zinc finger, AN1-type
AAA ATPases form a large.unctionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases.hich exert their activity through the energy-dependent unfolding of macromolecules. AAA ATPases contain a P-loop NTPase domain.hich is the most abundant class of NTP-binding protein fold.nd is found throughout all kingdoms of life . P-loop NTPase domains act to hydrolyse the beta-gamma phosphate bond of bound nucleoside triphosphate. There are two classes of P-loop domains: the KG (kinase-GTPase) division.nd the ASCE division.he latter including the AAA+ group as well as several other ATPases.There are at least six major clades of AAA domains (metalloproteases.eiotic proteins.1 and D2 domains of ATPases with two AAA domains.roteasome subunits.nd BSC1).s well as several minor clades.ome of which consist of hypothetical proteins . The domain organisation of AAA ATPases consists of a non-ATPase N-terminal domain that acts in substrate recognition.ollowed by one or two AAA domains (D1 and D2).ne of which may be degenerate.
  IPR003593:AAA ATPase
This entry is found in DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism.ncluding nuclear mRNA splicing.ibosome biogenesis.ucleocytoplasmic transport.ranslation.NA decay and organellar gene expression.
  IPR014001:DEAD-like helicases, N-terminal
Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterised as helicases.
  IPR004483:Putative DNA helicase
SequencesProtein: SMBP2_HUMAN (993 aa)
mRNA: NM_002180
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)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 46 residues, 68427947-68428082Exon2: 58 residues, 68430112-68430282Exon3: 66 residues, 68432188-68432381Exon4: 34 residues, 68432577-68432675Exon5: 56 residues, 68435483-68435647Exon6: 69 residues, 68438866-68439067Exon7: 51 residues, 68441779-68441927Exon8: 60 residues, 68453226-68453401Exon9: 63 residues, 68457342-68457525Exon10: 41 residues, 68457838-68457957Exon11: 33 residues, 68458507-68458602Exon12: 43 residues, 68459342-68459466Exon13: 287 residues, 68460280-68461135Exon14: 59 residues, 68462225-68462398Exon15: 354 residues, 68463577-68464635Exon16: 2 residues, -Jump to SMBP2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2691 68427947-68464635 ~-37K 7282(IGHMBP2)(+)Loci: 3967 68281144-68365881 ~-85K 7280(CPT1A)(-)Link out to UCSC