Q9BY42 · RTF2_HUMAN
- ProteinReplication termination factor 2
- GeneRTF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids306 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Replication termination factor which is a component of the elongating replisome (Probable). Required for ATR pathway signaling upon DNA damage and has a positive activity during DNA replication. Might function to facilitate fork pausing at replication fork barriers like the rDNA. May be globally required to stimulate ATR signaling after the fork stalls or encounters a lesion (Probable). Interacts with nascent DNA (PubMed:29290612).
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 | nucleus | |
Cellular Component | replication fork | |
Molecular Function | DNA binding | |
Biological Process | cellular response to hydroxyurea | |
Biological Process | DNA replication termination | |
Biological Process | mitotic DNA replication termination | |
Biological Process | regulation of DNA stability |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReplication termination factor 2
- Short namesRTF2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BY42
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at the replication fork.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_028134 | 159 | in dbSNP:rs6024909 | |||
Sequence: T → A | ||||||
Natural variant | VAR_028135 | 171 | in dbSNP:rs1059768 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 347 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000079427 | 1-306 | UniProt | Replication termination factor 2 | |||
Sequence: MGCDGGTIPKRHELVKGPKKVEKVDKDAELVAQWNYCTLSQEILRRPIVACELGRLYNKDAVIEFLLDKSAEKALGKAASHIKSIKNVTELKLSDNPAWEGDKGNTKGDKHDDLQRARFICPVVGLEMNGRHRFCFLRCCGCVFSERALKEIKAEVCHTCGAAFQEDDVIMLNGTKEDVDVLKTRMEERRLRAKLEKKTKKPKAAESVSKPDVSEEAPGPSKVKTGKPEEASLDSREKKTNLAPKSTAMNESSSGKAGKPPCGATKRSIADSEESEAYKSLFTTHSSAKRSKEESAHWVTHTSYCF | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Undergoes proteasomal degradation, via DDI1 and DDI2. Removal from stalled replisomes and degradation are required for genome stability.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with DDI2; probably also interacts with DDI1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BY42 | FLNC Q14315 | 2 | EBI-1045669, EBI-489954 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 193-210 | Basic and acidic residues | ||||
Sequence: AKLEKKTKKPKAAESVSK | ||||||
Region | 193-276 | Disordered | ||||
Sequence: AKLEKKTKKPKAAESVSKPDVSEEAPGPSKVKTGKPEEASLDSREKKTNLAPKSTAMNESSSGKAGKPPCGATKRSIADSEESE | ||||||
Compositional bias | 227-241 | Basic and acidic residues | ||||
Sequence: KPEEASLDSREKKTN |
Sequence similarities
Belongs to the rtf2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length306
- Mass (Da)33,887
- Last updated2010-11-30 v3
- Checksum41EBAB29F7D535BF
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MQR2 | A0A0A0MQR2_HUMAN | RTF2 | 336 | ||
A2A2L5 | A2A2L5_HUMAN | RTF2 | 277 | ||
A2A2L6 | A2A2L6_HUMAN | RTF2 | 230 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 189 | in Ref. 4; BAA91193 | ||||
Sequence: R → G | ||||||
Compositional bias | 193-210 | Basic and acidic residues | ||||
Sequence: AKLEKKTKKPKAAESVSK | ||||||
Sequence conflict | 194 | in Ref. 1; AAF17212 and 3; AAK14929 | ||||
Sequence: K → N | ||||||
Sequence conflict | 195 | in Ref. 1; AAF17212 | ||||
Sequence: L → R | ||||||
Sequence conflict | 195 | in Ref. 3; AAK14929 | ||||
Sequence: L → W | ||||||
Sequence conflict | 199 | in Ref. 2; AAF29128 | ||||
Sequence: T → P | ||||||
Sequence conflict | 208 | in Ref. 2; AAF29128 | ||||
Sequence: V → A | ||||||
Compositional bias | 227-241 | Basic and acidic residues | ||||
Sequence: KPEEASLDSREKKTN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF117231 EMBL· GenBank· DDBJ | AAF17212.1 EMBL· GenBank· DDBJ | mRNA | ||
AF161513 EMBL· GenBank· DDBJ | AAF29128.1 EMBL· GenBank· DDBJ | mRNA | ||
AF161518 EMBL· GenBank· DDBJ | AAF29133.1 EMBL· GenBank· DDBJ | mRNA | ||
AF212244 EMBL· GenBank· DDBJ | AAK14929.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000481 EMBL· GenBank· DDBJ | BAA91193.1 EMBL· GenBank· DDBJ | mRNA | ||
AL109806 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75539.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75540.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003359 EMBL· GenBank· DDBJ | AAH03359.1 EMBL· GenBank· DDBJ | mRNA |