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Protein

Histone RNA hairpin-binding protein

Gene

Slbp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.By similarity2 Publications

GO - Molecular functioni

  • histone pre-mRNA stem-loop binding Source: UniProtKB
  • mRNA binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:108402. Slbp.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • 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.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • nucleus Source: UniProtKB
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001003571 – 275Histone RNA hairpin-binding proteinAdd BLAST275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20PhosphoserineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei59PhosphoserineBy similarity1
Modified residuei61Phosphothreonine; by CK2By similarity1
Modified residuei62Phosphothreonine; by CDK1By similarity1
Modified residuei171PhosphothreonineBy similarity1
Modified residuei182PhosphoserineBy similarity1

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP97440.
PaxDbiP97440.
PeptideAtlasiP97440.
PRIDEiP97440.

PTM databases

iPTMnetiP97440.
PhosphoSitePlusiP97440.

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

BgeeiENSMUSG00000004642.
CleanExiMM_SLBP.
ExpressionAtlasiP97440. baseline and differential.
GenevisibleiP97440. MM.

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.By similarity1 Publication

Protein-protein interaction databases

IntActiP97440. 1 interactor.
MINTiMINT-8372793.
STRINGi10090.ENSMUSP00000062930.

Structurei

3D structure databases

ProteinModelPortaliP97440.
SMRiP97440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 198RNA-bindingBy similarityAdd BLAST70

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi31 – 34Nuclear localization signal NLS1By similarity4
Motifi96 – 99Nuclear localization signal NLS2By similarity4

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).By similarity

Sequence similaritiesi

Belongs to the SLBP family.Curated

Phylogenomic databases

eggNOGiKOG3934. Eukaryota.
ENOG41122ZE. LUCA.
GeneTreeiENSGT00390000008738.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiP97440.
KOiK18710.
OMAiRLWKVAL.
OrthoDBiEOG091G0LT8.
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

« Hide

        10         20         30         40         50
MACRPRSPPG YGSRRDGGAS PRSPARWSLG RKRRADGRDR KPEDSEEGEL
60 70 80 90 100
QTADHRPESF TTPEGHKPRS RCSDWASAVE EDEMRTRVNK EIARYKRKLL
110 120 130 140 150
INDFGRERKS SSGSSDSKES MSSVPADVET DESVLMRRQK QINYGKNTIA
160 170 180 190 200
YDRYIKEVPR HLRQPGIHPR TPNKFKKYSR RSWDQQIKLW KVALHFWDPP
210 220 230 240 250
AEEGCDLQEI QPVDLGEMET EFTESSSESQ TSSQDNFDVY AGTPTKVRHV
260 270
DCQVEDEFDL EACLTEPLKD FSAMS
Length:275
Mass (Da):31,603
Last modified:May 1, 1997 - v1
Checksum:i538459F001C59AF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75680 mRNA. Translation: AAC53530.1.
CCDSiCCDS19205.1.
RefSeqiNP_033219.1. NM_009193.2.
UniGeneiMm.4172.

3D structure databases

ProteinModelPortaliP97440.
SMRiP97440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97440. 1 interactor.
MINTiMINT-8372793.
STRINGi10090.ENSMUSP00000062930.

PTM databases

iPTMnetiP97440.
PhosphoSitePlusiP97440.

Proteomic databases

EPDiP97440.
PaxDbiP97440.
PeptideAtlasiP97440.
PRIDEiP97440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642.
GeneIDi20492.
KEGGimmu:20492.
UCSCiuc008xaw.2. mouse.

Organism-specific databases

CTDi7884.
MGIiMGI:108402. Slbp.

Phylogenomic databases

eggNOGiKOG3934. Eukaryota.
ENOG41122ZE. LUCA.
GeneTreeiENSGT00390000008738.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiP97440.
KOiK18710.
OMAiRLWKVAL.
OrthoDBiEOG091G0LT8.
PhylomeDBiP97440.
TreeFamiTF316521.

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Miscellaneous databases

PROiP97440.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004642.
CleanExiMM_SLBP.
ExpressionAtlasiP97440. baseline and differential.
GenevisibleiP97440. MM.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.