Q9NQG5 · RPR1B_HUMAN
- ProteinRegulation of nuclear pre-mRNA domain-containing protein 1B
- GeneRPRD1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids326 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation.
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 | |
Cellular Component | transcription preinitiation complex | |
Molecular Function | identical protein binding | |
Molecular Function | RNA polymerase II C-terminal domain binding | |
Molecular Function | RNA polymerase II complex binding | |
Biological Process | mRNA 3'-end processing | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of cell cycle process | |
Biological Process | RNA polymerase II promoter clearance |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulation of nuclear pre-mRNA domain-containing protein 1B
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NQG5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114 | Complete loss of binding to POLR2ACTD in vivo. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 251 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000079441 | 2-326 | UniProt | Regulation of nuclear pre-mRNA domain-containing protein 1B | |||
Sequence: SSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSKSPPPKATEEKKSLKRTFQQIQEEEDDDYPGSYSPQDPSAGPLLTEELIKALQDLENAASGDATVRQKIASLPQEVQDVSLLEKITDKEAAERLSKTVDEACLLLAEYNGRLAAELEDRRQLARMLVEYTQNQKDVLSEKEKKLEEYKQKLARVTQVRKELKSHIQSLPDLSLLPNVTGGLAPLPSAGDLFSTD | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 132 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 134 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 161 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 166 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Preferentially expressed in a range of tumor tissues including colon, lung, liver, breast, prostate, stomach, uterine endometrium and cervical cancers with higher levels in tumors than in adjacent non-tumor tissue (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (PubMed:24997600).
May form a heterodimer with RPRD1A (PubMed:24997600).
Associates with RPAP2 (PubMed:24997600).
Associates with the RNA polymerase II complex (PubMed:22231121, PubMed:24399136, PubMed:24997600).
May form a heterodimer with RPRD1A (PubMed:24997600).
Associates with RPAP2 (PubMed:24997600).
Associates with the RNA polymerase II complex (PubMed:22231121, PubMed:24399136, PubMed:24997600).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-133 | CID | ||||
Sequence: SSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSK | ||||||
Region | 127-149 | Disordered | ||||
Sequence: LSMEDSKSPPPKATEEKKSLKRT | ||||||
Compositional bias | 135-149 | Basic and acidic residues | ||||
Sequence: PPPKATEEKKSLKRT |
Sequence similarities
Belongs to the UPF0400 (RTT103) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length326
- Mass (Da)36,900
- Last updated2000-10-01 v1
- Checksum9057EEF6F3D18215
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PQF3 | E9PQF3_HUMAN | RPRD1B | 60 | ||
E9PIQ9 | E9PIQ9_HUMAN | RPRD1B | 113 | ||
A2A2M0 | A2A2M0_HUMAN | RPRD1B | 197 | ||
A0A087X2D2 | A0A087X2D2_HUMAN | RPRD1B | 63 | ||
A0A087WUK3 | A0A087WUK3_HUMAN | RPRD1B | 34 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 21 | in Ref. 5; AAH33629 | ||||
Sequence: Q → H | ||||||
Compositional bias | 135-149 | Basic and acidic residues | ||||
Sequence: PPPKATEEKKSLKRT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ372938 EMBL· GenBank· DDBJ | ABD34791.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312468 EMBL· GenBank· DDBJ | BAG35375.1 EMBL· GenBank· DDBJ | mRNA | ||
AL109823 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW76045.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001696 EMBL· GenBank· DDBJ | AAH01696.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC033629 EMBL· GenBank· DDBJ | AAH33629.1 EMBL· GenBank· DDBJ | mRNA |