{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14493","secondaryAccessions":["B3KRJ5"],"uniProtkbId":"SLBP_HUMAN","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":210,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Histone RNA hairpin-binding protein"}},"alternativeNames":[{"fullName":{"value":"Histone stem-loop-binding protein"}}]},"genes":[{"geneName":{"value":"SLBP"},"synonyms":[{"value":"HBP"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97440"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19155325"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8957003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9049306"}],"value":"RNA-binding protein involved in the histone pre-mRNA processing (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). 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:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression (PubMed:12588979, PubMed:19155325, PubMed:8957003, PubMed:9049306). Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis (By similarity). Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97440"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11782445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16086026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16912046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18025107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18172165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22439849"}],"value":"Monomer (PubMed:22439849). SLBP/pre-mRNA complex interacts with ZNF473 (PubMed:11782445). Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1 (PubMed:15829567, PubMed:16086026, PubMed:18025107). Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase (PubMed:18172165). Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA (PubMed:16912046). Associates with polyribosomes (PubMed:12588979). Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity). Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q14493","intActId":"EBI-2696402"},"interactantTwo":{"uniProtKBAccession":"Q8IV48","geneName":"ERI1","intActId":"EBI-5459222"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14493","intActId":"EBI-2696402"},"interactantTwo":{"uniProtKBAccession":"A9UHW6","geneName":"MIF4GD","intActId":"EBI-373498"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14493","intActId":"EBI-2696402"},"interactantTwo":{"uniProtKBAccession":"Q14493","geneName":"SLBP","intActId":"EBI-2696402"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14493","intActId":"EBI-2696402"},"interactantTwo":{"uniProtKBAccession":"Q92900","geneName":"UPF1","intActId":"EBI-373471"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}],"value":"Polyribosome-associated (PubMed:12588979). Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase (PubMed:12588979). Through the S phase, partially redistributes to the cytoplasm (PubMed:12588979). Binding to histone mRNA is necessary for cytoplasmic localization (PubMed:12588979). Shuttles between the nucleus and the cytoplasm (PubMed:15829567). Imported in the nucleus by the Importin alpha/Importin beta receptor (PubMed:15829567)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}],"value":"Nucleus","id":"SL-0191"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q14493-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q14493-2"],"sequenceIds":["VSP_042164"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9049306"}],"value":"Widely expressed"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"value":"Regulated during the cell cycle: protein levels increase 10 to 20 fold in the late G1 and decrease at the S/G2 border"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}],"value":"Amino acids 31-34, 96-99 and 241-244 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 241-244 are necessary for nuclear localization"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18490441"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22439849"}],"value":"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 by the proteasome 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"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28118078"}],"value":"Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C) complexes, leading to its degradation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the SLBP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Histone RNA hairpin-binding protein","featureId":"PRO_0000100356"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"RNA-binding","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8957003"}]},{"type":"Region","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Nuclear localization signal NLS1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}]},{"type":"Motif","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Nuclear localization signal NLS2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}]},{"type":"Compositional bias","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"17081983"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"17081983"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Phosphothreonine; 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Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-96; A-97; A-98 and A-99 or with A-241; A-242; A-243 and A-244.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15829567"}],"alternativeSequence":{"originalSequence":"RKRR","alternativeSequences":["AAAA"]}},{"type":"Mutagenesis","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Does not increase its stability at the end of the S phase and through G2 and mitosis.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18490441"}],"alternativeSequence":{"originalSequence":"SFTTP","alternativeSequences":["AAAA"]}},{"type":"Mutagenesis","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Does not increase its stability at the end of the S phase and through G2 and mitosis.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12588979"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Increases its stability at the end of the S phase and through G2 and mitosis. 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Inhibits phosphorylation of T-62. Localizes in the nucleus. Reduces interaction with the importin alpha/importin beta receptor. 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