P97440 · SLBP_MOUSE
- ProteinHistone RNA hairpin-binding protein
- GeneSlbp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids275 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
RNA-binding protein involved in the histone pre-mRNA processing (PubMed:18036581).
Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE) (PubMed:18036581).
Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery (By similarity).
Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (By similarity).
Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis (PubMed:18036581).
Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (PubMed:19470752).
Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE) (PubMed:18036581).
Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery (By similarity).
Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (By similarity).
Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis (PubMed:18036581).
Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (PubMed:19470752).
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | histone mRNA stem-loop binding complex | |
Cellular Component | histone pre-mRNA 3'end processing complex | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | histone pre-mRNA stem-loop binding | |
Molecular Function | identical protein binding | |
Molecular Function | mRNA binding | |
Biological Process | cap-dependent translational initiation | |
Biological Process | mRNA 3'-end processing by stem-loop binding and cleavage | |
Biological Process | mRNA transport |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone RNA hairpin-binding protein
- 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 accessionP97440
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase. Through the S phase, partially redistributes to the cytoplasm. Binding to histone mRNA is necessary for cytoplasmic localization. Shuttles between the nucleus and the cytoplasm. Imported in the nucleus by the Importin alpha/Importin beta receptor (By similarity).
Polyribosome-associated
Polyribosome-associated
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Females show no impaired oogenesis but display a defect in the formation of primordial follicles leading to infertility. Most embryos arrested at the 2-cell stage and fail to complete the second round of DNA replication due to an insufficient supply of histone H3 and H4. Accumulation of histone H2A and H2B is not affected.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000100357 | 1-275 | Histone RNA hairpin-binding protein | |||
Sequence: MACRPRSPPGYGSRRDGGASPRSPARWSLGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRVNKEIARYKRKLLINDFGRERKSSSGSSDSKESMSSVPADVETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPRTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIQPVDLGEMETEFTESSSESQTSSQDNFDVYAGTPTKVRHVDCQVEDEFDLEACLTEPLKDFSAMS | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 23 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 59 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 61 | Phosphothreonine; by CK2 | ||||
Sequence: T | ||||||
Modified residue | 62 | Phosphothreonine; by CDK1 | ||||
Sequence: T | ||||||
Cross-link | 98 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 171 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 182 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Thr-61 and Thr-62 in the S-phase. Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2. Phosphorylation of Thr-62 is required for its degradation at the end of the S phase. Its degradation is not required for histone mRNA degradation at the end of the S phase. All the phosphorylated forms detected are present in the cytoplasm. Both unphosphorylated and phosphorylated forms bind the stem-loop structure of histone mRNAs. Phosphorylation at Thr-171 increases affinity for histone mRNAs (By similarity).
Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C) complexes, leading to its degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed in growing primary but not non-growing oocytes, within the primordial follicles. Also detected in fully-grown oocytes in antral follicles (at protein level).
Gene expression databases
Interaction
Subunit
Monomer. SLBP/pre-mRNA complex interacts with ZNF473 (By similarity).
Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1 (By similarity).
Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase (By similarity).
Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA. Associates with polyribosomes (By similarity).
Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (PubMed:19470752).
Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (PubMed:19470752).
Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1 (By similarity).
Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase (By similarity).
Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA. Associates with polyribosomes (By similarity).
Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (PubMed:19470752).
Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (PubMed:19470752).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-88 | Disordered | ||||
Sequence: MACRPRSPPGYGSRRDGGASPRSPARWSLGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRV | ||||||
Compositional bias | 29-88 | Basic and acidic residues | ||||
Sequence: LGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRV | ||||||
Motif | 31-34 | Nuclear localization signal NLS1 | ||||
Sequence: RKRR | ||||||
Motif | 96-99 | Nuclear localization signal NLS2 | ||||
Sequence: KRKL | ||||||
Region | 103-133 | Disordered | ||||
Sequence: DFGRERKSSSGSSDSKESMSSVPADVETDES | ||||||
Region | 129-198 | RNA-binding | ||||
Sequence: ETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPRTPNKFKKYSRRSWDQQIKLWKVALHFWD | ||||||
Region | 219-240 | Disordered | ||||
Sequence: ETEFTESSSESQTSSQDNFDVY | ||||||
Compositional bias | 220-240 | Polar residues | ||||
Sequence: TEFTESSSESQTSSQDNFDVY |
Domain
Amino acids 31-34, 96-99 and 246-249 are necessary for interaction with the Importin alpha/Importin beta receptor. The first 18 amino acids, amino acids 69-76 and 179-182 are necessary for interaction with TNPO3. Amino acids 31-34, 96-99 and 246-249 are necessary for nuclear localization (By similarity).
Sequence similarities
Belongs to the SLBP family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)31,603
- Last updated1997-05-01 v1
- Checksum538459F001C59AF4
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YV40 | A0A0J9YV40_MOUSE | Slbp | 219 | ||
Q8K2W7 | Q8K2W7_MOUSE | Slbp | 255 | ||
D3Z1S0 | D3Z1S0_MOUSE | Slbp | 33 | ||
Q3V2L1 | Q3V2L1_MOUSE | Slbp | 250 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-88 | Basic and acidic residues | ||||
Sequence: LGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRV | ||||||
Compositional bias | 220-240 | Polar residues | ||||
Sequence: TEFTESSSESQTSSQDNFDVY |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U75680 EMBL· GenBank· DDBJ | AAC53530.1 EMBL· GenBank· DDBJ | mRNA |