Q62377 · U2AFM_MOUSE

  • Protein
    U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
  • Gene
    Zrsr2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleolus
Cellular Componentspliceosomal complex
Cellular ComponentU12-type spliceosomal complex
Cellular ComponentU2AF complex
Molecular Functionmetal ion binding
Molecular Functionpre-mRNA 3'-splice site binding
Biological ProcessmRNA splicing, via spliceosome
Biological Processspliceosomal complex assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
  • Alternative names
    • CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2
    • U2(RNU2) small nuclear RNA auxiliary factor 1-like 2
    • U2AF35-related protein (URP)

Gene names

    • Name
      Zrsr2
    • Synonyms
      U2af1-rs2, U2af1l2, U2af1rs2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q62377

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000820021-462
Cross-link49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue353Phosphoserine
Modified residue389Phosphoserine

Post-translational modification

Phosphorylated in the RS domain by SRPK1.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts with U2AF2/U2AF65 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-22Disordered
Region44-66Disordered
Region115-138Disordered
Zinc finger170-198C3H1-type 1
Domain202-308RRM
Zinc finger310-337C3H1-type 2
Region354-462Disordered
Compositional bias362-405Basic and acidic residues
Compositional bias406-427Basic residues
Compositional bias444-462Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    462
  • Mass (Da)
    55,358
  • Last updated
    1996-11-01 v1
  • Checksum
    0E980C029ACBA196
METAGATADATAGPQKLSRKKYLALRKKERRKRRRQALARLREAELAQKEEEEDPLAEEKRLEEERLLEEERQRLHEEWLLREEKAQEEFRAKKKKEEEARKRKEELERKLKAEWEEQQRKEREEEEQKRQEKREREEAVQKMLDQAENELENGGTWQNPEPPMDIRVLEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKGMFTTFGMEQCRRDDYDPDSSLEFSEEEIYQQFLDFYYDVLPEFKSVGKVIQFKVSCNLEPHLRGNVYVQYQSEEDCQAAFSVFNGRWYAGRQLQCEFCPVTRWKMAICGLFEVQQCPRGKHCNFLHVFRNPNNEYRDANRDLYPSPDWTSSSFGKNSERRERASHYDEYYGRSRRRRRSPSPDFYKRNGESDRKSSSRHRVKKSHRYGMKSRERRSSPSRRRKDHSPGPWEPEQEEPPQQESQSQPQPQPQSDP

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
B1B0F0B1B0F0_MOUSEZrsr2113
B1B0F1B1B0F1_MOUSEZrsr271
B1B0E8B1B0E8_MOUSEZrsr2541
B1B0E9B1B0E9_MOUSEZrsr2144

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias362-405Basic and acidic residues
Compositional bias406-427Basic residues
Compositional bias444-462Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D45205
EMBL· GenBank· DDBJ
BAA08143.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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