Slbp
entrez
20492
canonical
uniprot
P97440
canonical
ensembl
ENSMUSG00000004642
resolver
ensp
ENSMUSP00000062930
resolver
ensp
ENSMUSP00000098906
resolver
ensp
ENSMUSP00000206730
resolver
enst
ENSMUST00000057551
resolver
enst
ENSMUST00000101354
resolver
genesymbol
Slbp
resolver
genesymbol_syn
Hbp
resolver
uniprot
F6V5X7
resolver
uniprot
Q3TSD8
resolver
uniprot
Q3U4T7
resolver
uniprot
Q8K2W7
resolver
uniprot_entry
F6V5X7_MOUSE
resolver
uniprot_entry
Q3TSD8_MOUSE
resolver
uniprot_entry
Q3U4T7_MOUSE
resolver
uniprot_entry
Q8K2W7_MOUSE
resolver
uniprot_entry
SLBP_MOUSE
resolver
amino_acid_sequence
MACRPRSPPGYGSRRDGGASPRSPARWSLGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRVNKEIARYKRKLLINDFGRERKSSSGSSDSKESMSSVPADVETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPRTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIQPVDLGEMETEFTESSSESQTSSQDNFDVYAGTPTKVRHVDCQVEDEFDLEACLTEPLKDFSAMS
uniprot
proteins
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). {ECO:0000250|UniProtKB:Q14493, ECO:0000269|PubMed:18036581, ECO:0000269|PubMed:19470752}.
uniprot
proteins
mass_dalton
31603
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250|UniProtKB:Q14493}.; PTM: Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C) complexes, leading to its degradation. {ECO:0000250|UniProtKB:Q14493}.
uniprot
proteins
protein_family
SLBP family
uniprot
proteins
pubmed
18036581
uniprot
proteins
pubmed
19470752
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8957003
uniprot
proteins
sequence_length
275
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18036581}. Nucleus {ECO:0000269|PubMed:18036581}. 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. {ECO:0000250|UniProtKB:Q14493}.
uniprot
proteins