SLBP_MOUSE
ID SLBP_MOUSE Reviewed; 275 AA.
AC P97440;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Histone RNA hairpin-binding protein;
DE AltName: Full=Histone stem-loop-binding protein;
GN Name=Slbp; Synonyms=Hbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=8957003; DOI=10.1101/gad.10.23.3028;
RA Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.;
RT "The protein that binds the 3' end of histone mRNA: a novel RNA-binding
RT protein required for histone pre-mRNA processing.";
RL Genes Dev. 10:3028-3040(1996).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18036581; DOI=10.1016/j.ydbio.2007.10.032;
RA Arnold D.R., Francon P., Zhang J., Martin K., Clarke H.J.;
RT "Stem-loop binding protein expressed in growing oocytes is required for
RT accumulation of mRNAs encoding histones H3 and H4 and for early embryonic
RT development in the mouse.";
RL Dev. Biol. 313:347-358(2008).
RN [3]
RP FUNCTION, IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, RNA-BINDING, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19470752; DOI=10.1128/mcb.00296-09;
RA Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT "Three proteins of the U7-specific Sm ring function as the molecular ruler
RT to determine the site of 3'-end processing in mammalian histone pre-mRNA.";
RL Mol. Cell. Biol. 29:4045-4056(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: RNA-binding protein involved in the histone pre-mRNA
CC processing (PubMed:18036581). Binds the stem-loop structure of
CC replication-dependent histone pre-mRNAs and contributes to efficient
CC 3'-end processing by stabilizing the complex between histone pre-mRNA
CC and U7 small nuclear ribonucleoprotein (snRNP), via the histone
CC downstream element (HDE) (PubMed:18036581). Plays an important role in
CC targeting mature histone mRNA from the nucleus to the cytoplasm and to
CC the translation machinery (By similarity). Stabilizes mature histone
CC mRNA and could be involved in cell-cycle regulation of histone gene
CC expression (By similarity). Involved in the mechanism by which growing
CC oocytes accumulate histone proteins that support early embryogenesis
CC (PubMed:18036581). Binds to the 5' side of the stem-loop structure of
CC histone pre-mRNAs (PubMed:19470752). {ECO:0000250|UniProtKB:Q14493,
CC ECO:0000269|PubMed:18036581, ECO:0000269|PubMed:19470752}.
CC -!- SUBUNIT: Monomer. SLBP/pre-mRNA complex interacts with ZNF473 (By
CC similarity). Interacts with the Importin alpha/Importin beta receptor,
CC LSM1, MIF4GD, TNPO3 and UPF1 (By similarity). Interaction with LSM1
CC occurs when histone mRNA is being rapidly degraded during the S phase
CC (By similarity). Found in a ternary complex with ERI1 and the stem-loop
CC structure of the 3' end of histone mRNA. Associates with polyribosomes
CC (By similarity). Identified in a histone pre-mRNA complex, at least
CC composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1
CC (PubMed:19470752). Binds in a cooperative manner with ERI1 to the
CC mature 3'-end of histone mRNAs (PubMed:19470752).
CC {ECO:0000250|UniProtKB:Q14493, ECO:0000269|PubMed:19470752}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18036581}. Nucleus
CC {ECO:0000269|PubMed:18036581}. Note=Localizes predominantly in the
CC nucleus at the G1/G2 phases and the beginning of S phase. Through the S
CC phase, partially redistributes to the cytoplasm. Binding to histone
CC mRNA is necessary for cytoplasmic localization. Shuttles between the
CC nucleus and the cytoplasm. Imported in the nucleus by the Importin
CC alpha/Importin beta receptor (By similarity). Polyribosome-associated.
CC {ECO:0000250|UniProtKB:Q14493}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in growing primary but
CC not non-growing oocytes, within the primordial follicles. Also detected
CC in fully-grown oocytes in antral follicles (at protein level).
CC {ECO:0000269|PubMed:18036581}.
CC -!- DOMAIN: Amino acids 31-34, 96-99 and 246-249 are necessary for
CC interaction with the Importin alpha/Importin beta receptor. The first
CC 18 amino acids, amino acids 69-76 and 179-182 are necessary for
CC interaction with TNPO3. Amino acids 31-34, 96-99 and 246-249 are
CC necessary for nuclear localization (By similarity).
CC {ECO:0000250|UniProtKB:Q14493}.
CC -!- PTM: Phosphorylated on Thr-61 and Thr-62 in the S-phase.
CC Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by
CC CK2. Phosphorylation of Thr-62 is required for its degradation at the
CC end of the S phase. Its degradation is not required for histone mRNA
CC degradation at the end of the S phase. All the phosphorylated forms
CC detected are present in the cytoplasm. Both unphosphorylated and
CC phosphorylated forms bind the stem-loop structure of histone mRNAs.
CC Phosphorylation at Thr-171 increases affinity for histone mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:Q14493}.
CC -!- PTM: Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C)
CC complexes, leading to its degradation. {ECO:0000250|UniProtKB:Q14493}.
CC -!- DISRUPTION PHENOTYPE: Females show no impaired oogenesis but display a
CC defect in the formation of primordial follicles leading to infertility.
CC Most embryos arrested at the 2-cell stage and fail to complete the
CC second round of DNA replication due to an insufficient supply of
CC histone H3 and H4. Accumulation of histone H2A and H2B is not affected.
CC {ECO:0000269|PubMed:18036581}.
CC -!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
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DR EMBL; U75680; AAC53530.1; -; mRNA.
DR CCDS; CCDS19205.1; -.
DR RefSeq; NP_033219.1; NM_009193.2.
DR AlphaFoldDB; P97440; -.
DR BMRB; P97440; -.
DR SMR; P97440; -.
DR ComplexPortal; CPX-1312; SLBP-SLIP1 complex.
DR IntAct; P97440; 1.
DR MINT; P97440; -.
DR STRING; 10090.ENSMUSP00000062930; -.
DR iPTMnet; P97440; -.
DR PhosphoSitePlus; P97440; -.
DR EPD; P97440; -.
DR PaxDb; P97440; -.
DR PeptideAtlas; P97440; -.
DR PRIDE; P97440; -.
DR ProteomicsDB; 261419; -.
DR Antibodypedia; 8450; 84 antibodies from 23 providers.
DR DNASU; 20492; -.
DR Ensembl; ENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642.
DR GeneID; 20492; -.
DR KEGG; mmu:20492; -.
DR UCSC; uc008xaw.2; mouse.
DR CTD; 7884; -.
DR MGI; MGI:108402; Slbp.
DR VEuPathDB; HostDB:ENSMUSG00000004642; -.
DR eggNOG; KOG3934; Eukaryota.
DR GeneTree; ENSGT00390000008738; -.
DR HOGENOM; CLU_093199_0_0_1; -.
DR InParanoid; P97440; -.
DR OMA; HCRKRGV; -.
DR OrthoDB; 1284291at2759; -.
DR PhylomeDB; P97440; -.
DR TreeFam; TF316521; -.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR BioGRID-ORCS; 20492; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Slbp; mouse.
DR PRO; PR:P97440; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97440; protein.
DR Bgee; ENSMUSG00000004642; Expressed in animal zygote and 144 other tissues.
DR ExpressionAtlas; P97440; baseline and differential.
DR Genevisible; P97440; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0062073; C:histone mRNA stem-loop binding complex; ISO:MGI.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0071207; F:histone pre-mRNA stem-loop binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0002191; P:cap-dependent translational initiation; ISO:MGI.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR Gene3D; 1.10.8.1120; -; 1.
DR InterPro; IPR026502; SLBP1/SLBP2.
DR InterPro; IPR029344; SLBP_RNA_bind.
DR InterPro; IPR038294; SLBP_RNA_bind_sf.
DR PANTHER; PTHR17408; PTHR17408; 1.
DR Pfam; PF15247; SLBP_RNA_bind; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..275
FT /note="Histone RNA hairpin-binding protein"
FT /id="PRO_0000100357"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..198
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..34
FT /note="Nuclear localization signal NLS1"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOTIF 96..99
FT /note="Nuclear localization signal NLS2"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT COMPBIAS 29..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 61
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 62
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14493"
SQ SEQUENCE 275 AA; 31603 MW; 538459F001C59AF4 CRC64;
MACRPRSPPG YGSRRDGGAS PRSPARWSLG RKRRADGRDR KPEDSEEGEL QTADHRPESF
TTPEGHKPRS RCSDWASAVE EDEMRTRVNK EIARYKRKLL INDFGRERKS SSGSSDSKES
MSSVPADVET DESVLMRRQK QINYGKNTIA YDRYIKEVPR HLRQPGIHPR TPNKFKKYSR
RSWDQQIKLW KVALHFWDPP AEEGCDLQEI QPVDLGEMET EFTESSSESQ TSSQDNFDVY
AGTPTKVRHV DCQVEDEFDL EACLTEPLKD FSAMS
