Q14684 · RRP1B_HUMAN
- ProteinRibosomal RNA processing protein 1 homolog B
- GeneRRP1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids758 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599).
Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688).
Involved in regulation of mRNA splicing (By similarity).
Inhibits SIPA1 GTPase activity (By similarity).
Involved in regulating expression of extracellular matrix genes (By similarity).
Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015).
Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688).
Involved in regulation of mRNA splicing (By similarity).
Inhibits SIPA1 GTPase activity (By similarity).
Involved in regulating expression of extracellular matrix genes (By similarity).
Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015).
(Microbial infection) Following influenza A virus (IAV) infection, promotes viral mRNA transcription by facilitating the binding of IAV RNA-directed RNA polymerase to capped mRNA.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytosol | |
Cellular Component | euchromatin | |
Cellular Component | granular component | |
Cellular Component | heterochromatin | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | preribosome, small subunit precursor | |
Molecular Function | RNA binding | |
Molecular Function | transcription coactivator activity | |
Biological Process | apoptotic process | |
Biological Process | cellular response to virus | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of GTPase activity | |
Biological Process | positive regulation by host of viral transcription | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of RNA splicing | |
Biological Process | RNA splicing | |
Biological Process | rRNA processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibosomal RNA processing protein 1 homolog B
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14684
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly located in the nucleolus with a small amount found in the nucleoplasm (PubMed:20926688).
Associates with the perichromatin region during metaphase and with cytoplasmic foci during telophase before reaccumulation in the nucleolus during G2 (PubMed:20926688).
Associates with heterochromatin and euchromatin (PubMed:19710015).
Associates with the perichromatin region during metaphase and with cytoplasmic foci during telophase before reaccumulation in the nucleolus during G2 (PubMed:20926688).
Associates with heterochromatin and euchromatin (PubMed:19710015).
Note: (Microbial infection) Following infection by influenza A virus, partially translocates from the nucleolus to the nucleoplasm.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_079135 | 436 | in dbSNP:rs9306160 | |||
Sequence: L → P | ||||||
Mutagenesis | 684 | Abolishes interaction with protein phosphatase PP1 subunits PPP1CB and PPP1CC; when associated with A-686. | ||||
Sequence: V → A | ||||||
Mutagenesis | 686 | Abolishes interaction with protein phosphatase PP1 subunits PPP1CB and PPP1CC; when associated with A-684. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 774 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_0000050729 | 1-758 | UniProt | Ribosomal RNA processing protein 1 homolog B | |||
Sequence: MAPAMQPAEIQFAQRLASSEKGIRDRAVKKLRQYISVKTQRETGGFSQEELLKIWKGLFYCMWVQDEPLLQEELANTIAQLVHAVNNSAAQHLFIQTFWQTMNREWKGIDRLRLDKYYMLIRLVLRQSFEVLKRNGWEESRIKVFLDVLMKEVLCPESQSPNGVRFHFIDIYLDELSKVGGKELLADQNLKFIDPFCKIAAKTKDHTLVQTIARGVFEAIVDQSPFVPEETMEEQKTKVGDGDLSAEEIPENEVSLRRAVSKKKTALGKNHSRKDGLSDERGRDDCGTFEDTGPLLQFDYKAVADRLLEMTSRKNTPHFNRKRLSKLIKKFQDLSEGSSISQLSFAEDISADEDDQILSQGKHKKKGNKLLEKTNLEKEKGSRVFCVEEEDSESSLQKRRRKKKKKHHLQPENPGPGGAAPSLEQNRGREPEASGLKALKARVAEPGAEATSSTGEESGSEHPPAVPMHNKRKRPRKKSPRAHREMLESAVLPPEDMSQSGPSGSHPQGPRGSPTGGAQLLKRKRKLGVVPVNGSGLSTPAWPPLQQEGPPTGPAEGANSHTTLPQRRRLQKKKAGPGSLELCGLPSQKTASLKKRKKMRVMSNLVEHNGVLESEAGQPQALGSSGTCSSLKKQKLRAESDFVKFDTPFLPKPLFFRRAKSSTATHPPGPAVQLNKTPSSSKKVTFGLNRNMTAEFKKTDKSILVSPTGPSRVAFDPEQKPLHGVLKTPTSSPASSPLVAKKPLTTTPRRRPRAMDFF | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 245 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 350 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 392 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 394 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 394 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 395 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 422 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 452 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 452 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 454 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 458 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 513 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 579 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 579 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 652 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 663 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 677 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 679 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 702 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 702 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 706 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 706 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 712 | UniProt | Citrulline | ||||
Sequence: R | |||||||
Modified residue | 728 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 730 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 732 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 732 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 735 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 735 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 736 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Citrullinated by PADI4.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with the transcriptional activator E2F1 (PubMed:20040599).
Interacts with serine/threonine-protein phosphatase PP1 subunits PPP1CB and PPP1CC but not with PPP1CA (PubMed:20926688).
Interacts with 60S ribosomal proteins RPL5 and RPL27, ribosomal processing protein RRP1/NNP1 and other nucleolar proteins including NOP2/NOL1 and FBL (PubMed:20926688).
Also interacts with nucleolar protein NPM1/B23 (PubMed:19710015, PubMed:20926688).
Interacts with splicing factor SRSF1 and with LUC7L3/CROP (PubMed:23604122).
Interacts with GTPase activator SIPA1 (By similarity).
Interacts with CBX5/HP1alpha, H1-10, NCL, PARP1, TRIM28 and YBX3 (PubMed:19710015).
Interacts with serine/threonine-protein phosphatase PP1 subunits PPP1CB and PPP1CC but not with PPP1CA (PubMed:20926688).
Interacts with 60S ribosomal proteins RPL5 and RPL27, ribosomal processing protein RRP1/NNP1 and other nucleolar proteins including NOP2/NOL1 and FBL (PubMed:20926688).
Also interacts with nucleolar protein NPM1/B23 (PubMed:19710015, PubMed:20926688).
Interacts with splicing factor SRSF1 and with LUC7L3/CROP (PubMed:23604122).
Interacts with GTPase activator SIPA1 (By similarity).
Interacts with CBX5/HP1alpha, H1-10, NCL, PARP1, TRIM28 and YBX3 (PubMed:19710015).
(Microbial infection) Interacts with influenza A virus nucleoprotein NP and with RNA-directed RNA polymerase subunits PB1 and PB2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q14684 | E2F1 Q01094 | 10 | EBI-372051, EBI-448924 | |
BINARY | Q14684 | FBL P22087 | 4 | EBI-372051, EBI-358318 | |
BINARY | Q14684 | PPP1CA P62136 | 3 | EBI-372051, EBI-357253 | |
BINARY | Q14684 | PPP1CB P62140 | 3 | EBI-372051, EBI-352350 | |
BINARY | Q14684 | PPP1CC P36873 | 12 | EBI-372051, EBI-356283 | |
BINARY | Q14684 | RPL27 P61353 | 3 | EBI-372051, EBI-352760 | |
BINARY | Q14684 | RPL5 P46777 | 3 | EBI-372051, EBI-358018 | |
BINARY | Q14684 | RRP1 P56182 | 2 | EBI-372051, EBI-2880285 | |
BINARY | Q14684 | SRSF1 Q07955 | 6 | EBI-372051, EBI-398920 | |
BINARY | Q14684-1 | H4C9 P62805 | 3 | EBI-5280110, EBI-302023 | |
BINARY | Q14684-1 | PARP1 P09874 | 4 | EBI-5280110, EBI-355676 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 259-285 | Disordered | ||||
Sequence: AVSKKKTALGKNHSRKDGLSDERGRDD | ||||||
Compositional bias | 270-285 | Basic and acidic residues | ||||
Sequence: NHSRKDGLSDERGRDD | ||||||
Compositional bias | 381-397 | Basic and acidic residues | ||||
Sequence: GSRVFCVEEEDSESSLQ | ||||||
Region | 381-598 | Disordered | ||||
Sequence: GSRVFCVEEEDSESSLQKRRRKKKKKHHLQPENPGPGGAAPSLEQNRGREPEASGLKALKARVAEPGAEATSSTGEESGSEHPPAVPMHNKRKRPRKKSPRAHREMLESAVLPPEDMSQSGPSGSHPQGPRGSPTGGAQLLKRKRKLGVVPVNGSGLSTPAWPPLQQEGPPTGPAEGANSHTTLPQRRRLQKKKAGPGSLELCGLPSQKTASLKKRKK | ||||||
Compositional bias | 496-512 | Polar residues | ||||
Sequence: DMSQSGPSGSHPQGPRG | ||||||
Region | 660-681 | Disordered | ||||
Sequence: KSSTATHPPGPAVQLNKTPSSS | ||||||
Compositional bias | 666-681 | Polar residues | ||||
Sequence: HPPGPAVQLNKTPSSS | ||||||
Region | 707-758 | Disordered | ||||
Sequence: PTGPSRVAFDPEQKPLHGVLKTPTSSPASSPLVAKKPLTTTPRRRPRAMDFF | ||||||
Compositional bias | 725-742 | Polar residues | ||||
Sequence: VLKTPTSSPASSPLVAKK |
Sequence similarities
Belongs to the RRP1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q14684-1
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
- Length758
- Mass (Da)84,428
- Last updated2010-05-18 v3
- Checksum738117A7062054F2
Q14684-2
- Name2
- Differences from canonical
- 51-68: Missing
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007801 | 51-68 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 270-285 | Basic and acidic residues | ||||
Sequence: NHSRKDGLSDERGRDD | ||||||
Compositional bias | 381-397 | Basic and acidic residues | ||||
Sequence: GSRVFCVEEEDSESSLQ | ||||||
Compositional bias | 496-512 | Polar residues | ||||
Sequence: DMSQSGPSGSHPQGPRG | ||||||
Compositional bias | 666-681 | Polar residues | ||||
Sequence: HPPGPAVQLNKTPSSS | ||||||
Compositional bias | 725-742 | Polar residues | ||||
Sequence: VLKTPTSSPASSPLVAKK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D80001 EMBL· GenBank· DDBJ | BAA11496.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AP001052 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC028386 EMBL· GenBank· DDBJ | AAH28386.1 EMBL· GenBank· DDBJ | mRNA |