Q60560 · SMBP2_MESAU

Function

function

5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction (By similarity).
Specific to 5'-phosphorylated single-stranded guanine-rich sequences (By similarity).
May play a role in RNA metabolism, ribosome biogenesis or initiation of translation (By similarity).
May play a role in regulation of transcription (By similarity).
Interacts with tRNA-Tyr (By similarity).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site213-220ATP (UniProtKB | ChEBI)
Binding site402ATP (UniProtKB | ChEBI)
Binding site441ATP (UniProtKB | ChEBI)
Binding site570ATP (UniProtKB | ChEBI)
Binding site891Zn2+ 1 (UniProtKB | ChEBI)
Binding site896Zn2+ 1 (UniProtKB | ChEBI)
Binding site907Zn2+ 2 (UniProtKB | ChEBI)
Binding site910Zn2+ 2 (UniProtKB | ChEBI)
Binding site915Zn2+ 1 (UniProtKB | ChEBI)
Binding site918Zn2+ 1 (UniProtKB | ChEBI)
Binding site924Zn2+ 2 (UniProtKB | ChEBI)
Binding site926Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytoplasm
Cellular Componentnuclear body
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular Function5'-3' DNA helicase activity
Molecular Function5'-3' RNA helicase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent activity, acting on DNA
Molecular FunctionATP-dependent activity, acting on RNA
Molecular Functiondouble-stranded DNA helicase activity
Molecular Functionidentical protein binding
Molecular Functionribosome binding
Molecular FunctionRNA binding
Molecular Functionsingle-stranded DNA binding
Molecular Functionsingle-stranded RNA binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological ProcessDNA duplex unwinding
Biological ProcessRNA secondary structure unwinding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA-binding protein SMUBP-2
  • EC number
  • Alternative names
    • ATP-dependent helicase IGHMBP2
    • Immunoglobulin mu-binding protein 2
    • Insulin II gene enhancer-binding protein
    • RIPE3B-binding complex 3B2 p110 subunit (RIP-1)

Gene names

    • Name
      IGHMBP2
    • Synonyms
      RIP1, SMUBP2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Mesocricetus

Accessions

  • Primary accession
    Q60560

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000807022-989DNA-binding protein SMUBP-2
Modified residue797Phosphoserine
Modified residue800Phosphoserine

Keywords

Expression

Tissue specificity

High expression in brain and testis, moderate in heart, spleen, and kidney, and low in other tissues.

Interaction

Subunit

Homooligomer (By similarity).
Interacts with RUVBL1 (By similarity).
Interacts with RUVBL2 (By similarity).
Interacts with GTF3C1 (By similarity).
Interacts with ABT1 (By similarity).
Interacts with ribosomes (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias, motif, zinc finger.

TypeIDPosition(s)Description
Region637-783SS DNA-binding
Region650-717Disordered
Domain721-784R3H
Compositional bias765-779Basic and acidic residues
Region765-818Disordered
Compositional bias792-806Pro residues
Region833-869Disordered
Motif860-864Nuclear localization signal
Zinc finger885-934AN1-type
Region954-989Disordered

Domain

The R3H domain recognizes phosphorylated 5'-ends of single-stranded nucleic acids which promotes binding of nucleic acids and stimulates ATPase activity.

Sequence similarities

Belongs to the DNA2/NAM7 helicase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    989
  • Mass (Da)
    108,439
  • Last updated
    1997-11-01 v1
  • Checksum
    9489671E46DAD04E
MALSTVESFVAQQLELLELERDAEVEERRSWQEHSSLKELQSRGVCLLKLQVSSQCTGLYGQRLVTFEPRKLGPVVVLPSNSFTSGDIVGLYDANESSQLATGVLTRITQKSVTVAFDESHDFQLNLDRENTYRLLKLANDVTYKRLKKALMTLKKYHSGPASSLIDVLLGGSSPSPTTEIPPFTFYNTALDPSQKEAVSFALAQKEVAIIHGPPGTGKTTTVVEIILQAVKQGLKILCCAPSNVAVDNLVERLALCKKRILRLGHPARLLESAQQHSLDAVLARSDNAQIVADIRKDIDQVFGKNKKTQDKREKSNFRNEIKLLRKELKEREEAAIVQSLTAADVVLATNTGASSDGPLKLLPENHFDVVVVDECAQALEASCWIPLLKAPKCILAGDHRQLPPTTISHKAALAGLSRSLMERLVEKHGAGAVRMLTVQYRMHQAITRWASEAMYHGQLTAHPSVAGHLLKDLPGVADTEETSVPLLLIDTAGCGLLELDEEDSQSKGNPGEVRLVTLHIQALVDAGVHAGDIAVIAPYNLQVDLLRQSLSNKHPELEIKSVDGFQGREKEAVILTFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKTLVDYFTEHGEVRTAFEYLDDIVPENYTHEGSQGHSHAPKPRGPVTSIRKPTNEQENGQEARAAAGQGRRKPNERPPGSQVHSQPSSGARGCDRTGAIDRTEHFRAMIEGFVASKESQLEFPASLSSHDRLLVHQIAEEHGLRHDSTGEGKARHITVSRKSPAGSGGVAPQLPSPPSPAQAEPEPLSQQPLGQPHCSTQLDLKALHLQRLQRQQGSQAQPAKAQPGVGLHPQKTQQKKKKKETKGPALPCEEDFDALVSAVIKADNTCSFAKCTASTTTLGQFCMHCSRRYCLSHHLPEIHGCGEKARAHARQMISREGVLYAGSGTRDRALDPAKRAQLQRRLDKKLGELSSQRTSKRKEKERGT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias765-779Basic and acidic residues
Compositional bias792-806Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L15625
EMBL· GenBank· DDBJ
AAB00104.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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