Q7TSH6 · SCAF4_MOUSE

  • Protein
    SR-related and CTD-associated factor 4
  • Gene
    Scaf4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Anti-terminator protein required to prevent early mRNA termination during transcription. Together with SCAF8, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins. Mechanistically, associates with the phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit (POLR2A), and subsequently binds nascent RNA upstream of early polyadenylation sites to prevent premature mRNA transcript cleavage and polyadenylation. Independently of SCAF8, also acts as a suppressor of transcriptional readthrough.

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 Componentnucleoplasm
Cellular Componentnucleus
Molecular FunctionRNA binding
Molecular FunctionRNA polymerase II C-terminal domain phosphoserine binding
Biological ProcessmRNA processing
Biological Processnegative regulation of termination of RNA polymerase II transcription, poly(A)-coupled

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    SR-related and CTD-associated factor 4
  • Alternative names
    • CTD-binding SR-like protein RA4
    • Splicing factor, arginine/serine-rich 15

Gene names

    • Name
      Scaf4
    • Synonyms
      Kiaa1172
      , Srsf15

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q7TSH6
  • Secondary accessions
    • A0A338P6Z6
    • Q69ZP8
    • Q6PFF0
    • Q8R1B3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004476311-1183
Modified residue49N6-acetyllysine
Modified residue154Phosphoserine
Modified residue717Phosphoserine
Modified residue1042Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with POLR2A; via C-terminal heptapeptide repeat domain (CTD) phosphorylated at 'Ser-2' and 'Ser-5'.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-139CID
Region299-324Disordered
Region348-561Disordered
Compositional bias365-382Pro residues
Compositional bias398-412Pro residues
Compositional bias428-454Pro residues
Compositional bias455-472Polar residues
Compositional bias496-538Basic residues
Compositional bias539-557Basic and acidic residues
Domain569-643RRM
Region691-722Disordered
Compositional bias800-823Pro residues
Region800-859Disordered
Compositional bias920-956Pro residues
Region920-1183Disordered
Compositional bias977-1003Polar residues
Compositional bias1029-1125Basic and acidic residues

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q7TSH6-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,183
  • Mass (Da)
    129,056
  • Last updated
    2003-10-01 v1
  • Checksum
    525A0CD9AEB7213B
MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPVAENVTNNEGSPPPPVKISSELAQAPTNSMPTVAQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPQPQSPALDSAVMAQVQAITAQLKTAPTQPPEQKTAFDKKLLDRFDYDDEPEAVEDSKKEDAAAISTAALATAAPPAPTAATPAVATAVPVPSATSPPPPQTPFGYPGDGVQQPAYTQHQSMDQFQPRMMPIQQDTMHHQVPLPPNGQMPGFGLLSAPPPFPPMPQPGMPQPGMAQPGLAQPGMAQPTMPQPGMPQPGMPQPGMAQPGLAQPGMAQPGMPQPAMPQPAMPQPGMAQPGVSPAPPVQPTFQSTFQPQNEPHSQKPHQQEMEVEQPCVTEVKRHVPESRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQIKSETASVCSTTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALNKGIKADYKQYWDVELGVTYIPWDKVKAEELESFCEGGMLDSDTLNPDWKGIPKKPDNEVAQNGGAETSHTEPVSPIPKPVPVPVPPIPVPAPITVPPPQVPPHQPGPPVVGALQPPAFTPPLGMPPPGFGPGVPPPPPPPPFLRPGFNPMHLPPGFLPPGPPPPITPPVSIPPPHTPPISIPNLVSGARGNAESGDSAKMYGSAGPPAAPTSLPTPPVTQPVSLLGTQGVAPGPVIGLQAPSTGLLGARPGLIPLQRPPGMPPPHLQRFPMMPPRPMPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGASEDRDGRQQQPQQQPPPQQQQQQQQPQQQPPQQSPSQQPAPAQQQPPQFRNDSRQQFNSGRDQERFGRRSFGSRVENDRERYGSRNDDRDNSNRERREWGRRSPDRDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEENRKEKHEVADRAGGNKAVEPPLSQVGTIDTVSELNKGEAMATVVKPEESPAEVTSPVGPEKDPGSAAEPPR

Q7TSH6-2

Q7TSH6-3

Sequence caution

The sequence AAH24860.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAD32398.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict326in Ref. 1; BAD32398
Compositional bias365-382Pro residues
Compositional bias398-412Pro residues
Compositional bias428-454Pro residues
Compositional bias455-472Polar residues
Alternative sequenceVSP_060218477in isoform 2
Compositional bias496-538Basic residues
Alternative sequenceVSP_060219501in isoform 3
Compositional bias539-557Basic and acidic residues
Compositional bias800-823Pro residues
Alternative sequenceVSP_060220827in isoform 3
Compositional bias920-956Pro residues
Sequence conflict954in Ref. 3; AAH24860
Compositional bias977-1003Polar residues
Sequence conflict999in Ref. 1; BAD32398
Compositional bias1029-1125Basic and acidic residues
Sequence conflict1165in Ref. 1; BAD32398

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK173120
EMBL· GenBank· DDBJ
BAD32398.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AC139573
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC024860
EMBL· GenBank· DDBJ
AAH24860.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC053096
EMBL· GenBank· DDBJ
AAH53096.1
EMBL· GenBank· DDBJ
mRNA
BC057592
EMBL· GenBank· DDBJ
AAH57592.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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