SLBP
entrez
7884
canonical
uniprot
Q14493
canonical
ensembl
ENSG00000163950
resolver
ensp
ENSP00000406322
resolver
ensp
ENSP00000417686
resolver
ensp
ENSP00000418658
resolver
enst
ENST00000488267
resolver
genesymbol
SLBP
resolver
genesymbol_syn
HBP
resolver
hgnc
HGNC:10904
resolver
uniprot
B3KRJ5
resolver
uniprot
B3KSC5
resolver
uniprot
B3KST9
resolver
uniprot
B4DUW7
resolver
uniprot
D3DVP7
resolver
uniprot
E7EUV9
resolver
uniprot
Q53XR2
resolver
uniprot_entry
B3KSC5_HUMAN
resolver
uniprot_entry
B3KST9_HUMAN
resolver
uniprot_entry
B4DUW7_HUMAN
resolver
uniprot_entry
E7EUV9_HUMAN
resolver
uniprot_entry
Q53XR2_HUMAN
resolver
uniprot_entry
SLBP_HUMAN
resolver
uniprot_sec
B3KRJ5
resolver
uniprot_sec
D3DVP7
resolver
amino_acid_sequence
MACRPRSPPRHQSRCDGDASPPSPARWSLGRKRRADGRRWRPEDAEEAEHRGAERRPESFTTPEGPKPRSRCSDWASAVEEDEMRTRVNKEMARYKRKLLINDFGRERKSSSGSSDSKESMSTVPADFETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPKTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIHPVDLESAESSSEPQTSSQDDFDVYSGTPTKVRHMDSQVEDEFDLEACLTEPLRDFSAMS
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:P97440, ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:19155325, ECO:0000269|PubMed:8957003, ECO:0000269|PubMed:9049306}.
uniprot
proteins
mass_dalton
31286
uniprot
proteins
mutagenesis
MUTAGEN 31..34; /note="RKRR->AAAA: Reduces interaction with the importin alpha/importin beta receptor. 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."; /evidence="ECO:0000269|PubMed:15829567"; MUTAGEN 59..63; /note="SFTTP->AAAA: Does not increase its stability at the end of the S phase and through G2 and mitosis."; /evidence="ECO:0000269|PubMed:18490441"; MUTAGEN 59; /note="S->A: Does not increase its stability at the end of the S phase and through G2 and mitosis."; /evidence="ECO:0000269|PubMed:12588979"; MUTAGEN 61; /note="T->A: Increases its stability at the end of the S phase and through G2 and mitosis. Active in histone pre-mRNA processing during the G2 phase."; /evidence="ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:18490441"; MUTAGEN 62; /note="T->A: Increases its stability at the end of the S phase and through G2 and mitosis."; /evidence="ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:18490441"; MUTAGEN 63; /note="P->A: Increases its stability at the end of the S phase and through G2 and mitosis."; /evidence="ECO:0000269|PubMed:12588979"; MUTAGEN 96..99; /note="KRKL->AAAA: Increases its stability at the end of the S phase and through G2 and mitosis. Inhibits phosphorylation of T-62. Localizes in the nucleus. Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-241; A-242; A-243 and A-244."; /evidence="ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567, ECO:0000269|PubMed:18490441"; MUTAGEN 137; /note="R->A: Inhibits histone RNA-binding and localization to the cytoplasm."; /evidence="ECO:0000269|PubMed:15829567"; MUTAGEN 138; /note="R->A: Inhibits histone RNA-binding and localization to the cytoplasm."; /evidence="ECO:0000269|PubMed:15829567"; MUTAGEN 230..270; /note="Missing: Decrease in 3'-end processing efficiency."; /evidence="ECO:0000269|PubMed:11782445"; MUTAGEN 241..244; /note="KVRH->AAAA: Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-96; A-97; A-98 and A-99."; /evidence="ECO:0000269|PubMed:15829567
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 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. {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:18490441, ECO:0000269|PubMed:22439849}.; PTM: Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C) complexes, leading to its degradation. {ECO:0000269|PubMed:28118078}.
uniprot
proteins
protein_family
SLBP family
uniprot
proteins
pubmed
11782445
uniprot
proteins
pubmed
12588979
uniprot
proteins
pubmed
1338771
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15829567
uniprot
proteins
pubmed
16086026
uniprot
proteins
pubmed
16912046
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18025107
uniprot
proteins
pubmed
18172165
uniprot
proteins
pubmed
18490441
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19155325
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22439849
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28118078
uniprot
proteins
pubmed
8957003
uniprot
proteins
pubmed
9049306
uniprot
proteins
sequence_length
270
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}. Nucleus {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}. Note=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). {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}.
uniprot
proteins