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P97440

- SLBP_MOUSE

UniProt

P97440 - SLBP_MOUSE

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Protein

Histone RNA hairpin-binding protein

Gene
Slbp, Hbp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

RNA-binding protein involved in the histone pre-mRNA processing. 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). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. 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. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs.2 Publications

GO - Molecular functioni

  1. histone pre-mRNA stem-loop binding Source: UniProtKB
  2. mRNA binding Source: MGI

GO - Biological processi

  1. histone mRNA 3'-end processing Source: UniProtKB
  2. mRNA transport Source: UniProtKB
  3. nuclear cell cycle DNA replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone RNA hairpin-binding protein
Alternative name(s):
Histone stem-loop-binding protein
Gene namesi
Name:Slbp
Synonyms:Hbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:108402. Slbp.

Subcellular locationi

Cytoplasm. Nucleus
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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone pre-mRNA 3'end processing complex Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275Histone RNA hairpin-binding proteinPRO_0000100357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine By similarity
Modified residuei23 – 231Phosphoserine By similarity
Modified residuei61 – 611Phosphothreonine; by CK2 By similarity
Modified residuei62 – 621Phosphothreonine; by CDK1 By similarity
Modified residuei171 – 1711Phosphothreonine By similarity
Modified residuei182 – 1821Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP97440.
PRIDEiP97440.

PTM databases

PhosphoSiteiP97440.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

ArrayExpressiP97440.
BgeeiP97440.
CleanExiMM_SLBP.
GenevestigatoriP97440.

Interactioni

Subunit structurei

Monomer. SLBP/pre-mRNA complex interacts with ZNF473. Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1. Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase. 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. Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs.1 Publication

Protein-protein interaction databases

IntActiP97440. 1 interaction.
MINTiMINT-8372793.

Structurei

3D structure databases

ProteinModelPortaliP97440.
SMRiP97440. Positions 127-199.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 19870RNA-binding By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi31 – 344Nuclear localization signal NLS1 By similarity
Motifi96 – 994Nuclear localization signal NLS2 By similarity

Domaini

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 similaritiesi

Belongs to the SLBP family.

Phylogenomic databases

eggNOGiNOG278381.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiP97440.
OMAiKEVPRCH.
PhylomeDBiP97440.
TreeFamiTF316521.

Family and domain databases

InterProiIPR026502. SLBP1/SLBP2.
IPR029344. SLBP_RNA_bind.
[Graphical view]
PANTHERiPTHR17408. PTHR17408. 1 hit.
PfamiPF15247. SLBP_RNA_bind. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97440-1 [UniParc]FASTAAdd to Basket

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MACRPRSPPG YGSRRDGGAS PRSPARWSLG RKRRADGRDR KPEDSEEGEL    50
QTADHRPESF TTPEGHKPRS RCSDWASAVE EDEMRTRVNK EIARYKRKLL 100
INDFGRERKS SSGSSDSKES MSSVPADVET DESVLMRRQK QINYGKNTIA 150
YDRYIKEVPR HLRQPGIHPR TPNKFKKYSR RSWDQQIKLW KVALHFWDPP 200
AEEGCDLQEI QPVDLGEMET EFTESSSESQ TSSQDNFDVY AGTPTKVRHV 250
DCQVEDEFDL EACLTEPLKD FSAMS 275
Length:275
Mass (Da):31,603
Last modified:May 1, 1997 - v1
Checksum:i538459F001C59AF4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U75680 mRNA. Translation: AAC53530.1.
CCDSiCCDS19205.1.
RefSeqiNP_033219.1. NM_009193.2.
UniGeneiMm.4172.

Genome annotation databases

EnsembliENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642.
GeneIDi20492.
KEGGimmu:20492.
UCSCiuc008xaw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U75680 mRNA. Translation: AAC53530.1 .
CCDSi CCDS19205.1.
RefSeqi NP_033219.1. NM_009193.2.
UniGenei Mm.4172.

3D structure databases

ProteinModelPortali P97440.
SMRi P97440. Positions 127-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97440. 1 interaction.
MINTi MINT-8372793.

PTM databases

PhosphoSitei P97440.

Proteomic databases

PaxDbi P97440.
PRIDEi P97440.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000057551 ; ENSMUSP00000062930 ; ENSMUSG00000004642 .
GeneIDi 20492.
KEGGi mmu:20492.
UCSCi uc008xaw.1. mouse.

Organism-specific databases

CTDi 7884.
MGIi MGI:108402. Slbp.

Phylogenomic databases

eggNOGi NOG278381.
HOGENOMi HOG000065710.
HOVERGENi HBG017805.
InParanoidi P97440.
OMAi KEVPRCH.
PhylomeDBi P97440.
TreeFami TF316521.

Miscellaneous databases

NextBioi 298633.
PROi P97440.
SOURCEi Search...

Gene expression databases

ArrayExpressi P97440.
Bgeei P97440.
CleanExi MM_SLBP.
Genevestigatori P97440.

Family and domain databases

InterProi IPR026502. SLBP1/SLBP2.
IPR029344. SLBP_RNA_bind.
[Graphical view ]
PANTHERi PTHR17408. PTHR17408. 1 hit.
Pfami PF15247. SLBP_RNA_bind. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing."
    Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.
    Genes Dev. 10:3028-3040(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
    Tissue: Embryo.
  2. "Stem-loop binding protein expressed in growing oocytes is required for accumulation of mRNAs encoding histones H3 and H4 and for early embryonic development in the mouse."
    Arnold D.R., Francon P., Zhang J., Martin K., Clarke H.J.
    Dev. Biol. 313:347-358(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA."
    Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.
    Mol. Cell. Biol. 29:4045-4056(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, RNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSLBP_MOUSE
AccessioniPrimary (citable) accession number: P97440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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