Q7TSH6 · SCAF4_MOUSE
- ProteinSR-related and CTD-associated factor 4
- GeneScaf4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1183 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | RNA binding | |
Molecular Function | RNA polymerase II C-terminal domain phosphoserine binding | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSR-related and CTD-associated factor 4
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TSH6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447631 | 1-1183 | SR-related and CTD-associated factor 4 | |||
Sequence: MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPVAENVTNNEGSPPPPVKISSELAQAPTNSMPTVAQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPQPQSPALDSAVMAQVQAITAQLKTAPTQPPEQKTAFDKKLLDRFDYDDEPEAVEDSKKEDAAAISTAALATAAPPAPTAATPAVATAVPVPSATSPPPPQTPFGYPGDGVQQPAYTQHQSMDQFQPRMMPIQQDTMHHQVPLPPNGQMPGFGLLSAPPPFPPMPQPGMPQPGMAQPGLAQPGMAQPTMPQPGMPQPGMPQPGMAQPGLAQPGMAQPGMPQPAMPQPAMPQPGMAQPGVSPAPPVQPTFQSTFQPQNEPHSQKPHQQEMEVEQPCVTEVKRHVPESRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQIKSETASVCSTTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALNKGIKADYKQYWDVELGVTYIPWDKVKAEELESFCEGGMLDSDTLNPDWKGIPKKPDNEVAQNGGAETSHTEPVSPIPKPVPVPVPPIPVPAPITVPPPQVPPHQPGPPVVGALQPPAFTPPLGMPPPGFGPGVPPPPPPPPFLRPGFNPMHLPPGFLPPGPPPPITPPVSIPPPHTPPISIPNLVSGARGNAESGDSAKMYGSAGPPAAPTSLPTPPVTQPVSLLGTQGVAPGPVIGLQAPSTGLLGARPGLIPLQRPPGMPPPHLQRFPMMPPRPMPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGASEDRDGRQQQPQQQPPPQQQQQQQQPQQQPPQQSPSQQPAPAQQQPPQFRNDSRQQFNSGRDQERFGRRSFGSRVENDRERYGSRNDDRDNSNRERREWGRRSPDRDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEENRKEKHEVADRAGGNKAVEPPLSQVGTIDTVSELNKGEAMATVVKPEESPAEVTSPVGPEKDPGSAAEPPR | ||||||
Modified residue | 49 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 154 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 717 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1042 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-139 | CID | ||||
Sequence: MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTS | ||||||
Region | 299-324 | Disordered | ||||
Sequence: VPVPSATSPPPPQTPFGYPGDGVQQP | ||||||
Region | 348-561 | Disordered | ||||
Sequence: HHQVPLPPNGQMPGFGLLSAPPPFPPMPQPGMPQPGMAQPGLAQPGMAQPTMPQPGMPQPGMPQPGMAQPGLAQPGMAQPGMPQPAMPQPAMPQPGMAQPGVSPAPPVQPTFQSTFQPQNEPHSQKPHQQEMEVEQPCVTEVKRHVPESRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQIKS | ||||||
Compositional bias | 365-382 | Pro residues | ||||
Sequence: LSAPPPFPPMPQPGMPQP | ||||||
Compositional bias | 398-412 | Pro residues | ||||
Sequence: TMPQPGMPQPGMPQP | ||||||
Compositional bias | 428-454 | Pro residues | ||||
Sequence: GMPQPAMPQPAMPQPGMAQPGVSPAPP | ||||||
Compositional bias | 455-472 | Polar residues | ||||
Sequence: VQPTFQSTFQPQNEPHSQ | ||||||
Compositional bias | 496-538 | Basic residues | ||||
Sequence: SRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSR | ||||||
Compositional bias | 539-557 | Basic and acidic residues | ||||
Sequence: SQERRDREKERERRQKGLP | ||||||
Domain | 569-643 | RRM | ||||
Sequence: TTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALN | ||||||
Region | 691-722 | Disordered | ||||
Sequence: WKGIPKKPDNEVAQNGGAETSHTEPVSPIPKP | ||||||
Compositional bias | 800-823 | Pro residues | ||||
Sequence: LPPGPPPPITPPVSIPPPHTPPIS | ||||||
Region | 800-859 | Disordered | ||||
Sequence: LPPGPPPPITPPVSIPPPHTPPISIPNLVSGARGNAESGDSAKMYGSAGPPAAPTSLPTP | ||||||
Compositional bias | 920-956 | Pro residues | ||||
Sequence: MPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVR | ||||||
Region | 920-1183 | Disordered | ||||
Sequence: MPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGASEDRDGRQQQPQQQPPPQQQQQQQQPQQQPPQQSPSQQPAPAQQQPPQFRNDSRQQFNSGRDQERFGRRSFGSRVENDRERYGSRNDDRDNSNRERREWGRRSPDRDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEENRKEKHEVADRAGGNKAVEPPLSQVGTIDTVSELNKGEAMATVVKPEESPAEVTSPVGPEKDPGSAAEPPR | ||||||
Compositional bias | 977-1003 | Polar residues | ||||
Sequence: DGRQQQPQQQPPPQQQQQQQQPQQQPP | ||||||
Compositional bias | 1029-1125 | Basic and acidic residues | ||||
Sequence: FNSGRDQERFGRRSFGSRVENDRERYGSRNDDRDNSNRERREWGRRSPDRDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEENRKEKHEVADRAG |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length1,183
- Mass (Da)129,056
- Last updated2003-10-01 v1
- Checksum525A0CD9AEB7213B
Q7TSH6-2
- Name2
- Differences from canonical
- 477-477: Q → QV
Q7TSH6-3
- Name3
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 326 | in Ref. 1; BAD32398 | ||||
Sequence: Y → C | ||||||
Compositional bias | 365-382 | Pro residues | ||||
Sequence: LSAPPPFPPMPQPGMPQP | ||||||
Compositional bias | 398-412 | Pro residues | ||||
Sequence: TMPQPGMPQPGMPQP | ||||||
Compositional bias | 428-454 | Pro residues | ||||
Sequence: GMPQPAMPQPAMPQPGMAQPGVSPAPP | ||||||
Compositional bias | 455-472 | Polar residues | ||||
Sequence: VQPTFQSTFQPQNEPHSQ | ||||||
Alternative sequence | VSP_060218 | 477 | in isoform 2 | |||
Sequence: Q → QV | ||||||
Compositional bias | 496-538 | Basic residues | ||||
Sequence: SRKSRSRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSR | ||||||
Alternative sequence | VSP_060219 | 501 | in isoform 3 | |||
Sequence: S → SRSAS | ||||||
Compositional bias | 539-557 | Basic and acidic residues | ||||
Sequence: SQERRDREKERERRQKGLP | ||||||
Compositional bias | 800-823 | Pro residues | ||||
Sequence: LPPGPPPPITPPVSIPPPHTPPIS | ||||||
Alternative sequence | VSP_060220 | 827 | in isoform 3 | |||
Sequence: L → STIAGINEDTTKDLSIGNPIPTV | ||||||
Compositional bias | 920-956 | Pro residues | ||||
Sequence: MPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVR | ||||||
Sequence conflict | 954 | in Ref. 3; AAH24860 | ||||
Sequence: F → L | ||||||
Compositional bias | 977-1003 | Polar residues | ||||
Sequence: DGRQQQPQQQPPPQQQQQQQQPQQQPP | ||||||
Sequence conflict | 999 | in Ref. 1; BAD32398 | ||||
Sequence: Missing | ||||||
Compositional bias | 1029-1125 | Basic and acidic residues | ||||
Sequence: FNSGRDQERFGRRSFGSRVENDRERYGSRNDDRDNSNRERREWGRRSPDRDRHRDLEERSRRSSGHRDRDRDSRDRESRREKEENRKEKHEVADRAG | ||||||
Sequence conflict | 1165 | in Ref. 1; BAD32398 | ||||
Sequence: V → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |