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Protein

Histone RNA hairpin-binding protein

Gene

SLBP

Organism
Homo sapiens (Human)
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. 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

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

GO - Biological processi

  • histone mRNA metabolic process Source: Reactome
  • mRNA 3'-end processing by stem-loop binding and cleavage Source: UniProtKB
  • mRNA export from nucleus Source: Reactome
  • mRNA transport Source: UniProtKB
  • nuclear DNA replication Source: UniProtKB
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10904. SLBP.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Polyribosome-associated. 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.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: ProtInc
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 344RKRR → 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. 1 Publication
Mutagenesisi59 – 635SFTTP → AAAA: Does not increase its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi59 – 591S → A: Does not increase its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi61 – 611T → 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. 2 Publications
Mutagenesisi62 – 621T → A: Increases its stability at the end of the S phase and through G2 and mitosis. 2 Publications
Mutagenesisi63 – 631P → A: Increases its stability at the end of the S phase and through G2 and mitosis. 1 Publication
Mutagenesisi96 – 994KRKL → 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. 3 Publications
Mutagenesisi137 – 1371R → A: Inhibits histone RNA-binding and localization to the cytoplasm. 1 Publication
Mutagenesisi138 – 1381R → A: Inhibits histone RNA-binding and localization to the cytoplasm. 1 Publication
Mutagenesisi230 – 27041Missing : Decrease in 3'-end processing efficiency. 1 PublicationAdd
BLAST
Mutagenesisi241 – 2444KVRH → 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. 1 Publication

Organism-specific databases

PharmGKBiPA35804.

Polymorphism and mutation databases

BioMutaiSLBP.
DMDMi9789785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Histone RNA hairpin-binding proteinPRO_0000100356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei61 – 611Phosphothreonine; by CK22 Publications
Modified residuei62 – 621Phosphothreonine; by CDK1Combined sources2 Publications
Modified residuei171 – 1711PhosphothreonineCombined sources1 Publication
Modified residuei182 – 1821PhosphoserineCombined sources

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 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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14493.
MaxQBiQ14493.
PaxDbiQ14493.
PeptideAtlasiQ14493.
PRIDEiQ14493.

PTM databases

iPTMnetiQ14493.
PhosphoSiteiQ14493.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Regulated during the cell cycle: protein levels increase 10 to 20 fold in the late G1 and decrease at the S/G2 border.

Gene expression databases

BgeeiENSG00000163950.
CleanExiHS_SLBP.
ExpressionAtlasiQ14493. baseline and differential.
GenevisibleiQ14493. HS.

Organism-specific databases

HPAiHPA019254.
HPA061670.

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. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity). Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (By similarity).By similarity

Protein-protein interaction databases

BioGridi113627. 10 interactions.
DIPiDIP-57045N.
IntActiQ14493. 4 interactions.
STRINGi9606.ENSP00000417686.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi132 – 14615Combined sources
Helixi149 – 1579Combined sources
Turni165 – 1673Combined sources
Helixi180 – 19415Combined sources
Helixi195 – 1973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJMNMR-A129-158[»]
4L8RX-ray2.60C125-223[»]
4QOZX-ray2.30C125-223[»]
ProteinModelPortaliQ14493.
SMRiQ14493. Positions 127-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14493.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 19870RNA-bindingAdd
BLAST

Motif

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

Domaini

Amino acids 31-34, 96-99 and 241-244 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 241-244 are necessary for nuclear localization.

Sequence similaritiesi

Belongs to the SLBP family.Curated

Phylogenomic databases

eggNOGiKOG3934. Eukaryota.
ENOG41122ZE. LUCA.
GeneTreeiENSGT00390000008738.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiQ14493.
KOiK18710.
PhylomeDBiQ14493.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14493-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MACRPRSPPR HQSRCDGDAS PPSPARWSLG RKRRADGRRW RPEDAEEAEH
60 70 80 90 100
RGAERRPESF TTPEGPKPRS RCSDWASAVE EDEMRTRVNK EMARYKRKLL
110 120 130 140 150
INDFGRERKS SSGSSDSKES MSTVPADFET DESVLMRRQK QINYGKNTIA
160 170 180 190 200
YDRYIKEVPR HLRQPGIHPK TPNKFKKYSR RSWDQQIKLW KVALHFWDPP
210 220 230 240 250
AEEGCDLQEI HPVDLESAES SSEPQTSSQD DFDVYSGTPT KVRHMDSQVE
260 270
DEFDLEACLT EPLRDFSAMS
Length:270
Mass (Da):31,286
Last modified:November 1, 1996 - v1
Checksum:i4E84E502393D1BF7
GO
Isoform 2 (identifier: Q14493-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-58: Missing.

Show »
Length:231
Mass (Da):26,695
Checksum:i09C5137F52AC416D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 5839Missing in isoform 2. 1 PublicationVSP_042164Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63544 Genomic DNA. No translation available.
U75679 mRNA. Translation: AAB97091.1.
Z71188 mRNA. Translation: CAA94918.1.
AK091735 mRNA. Translation: BAG52407.1.
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82579.1.
BC014908 mRNA. Translation: AAH14908.1.
BC015703 mRNA. Translation: AAH15703.1.
CCDSiCCDS3350.1. [Q14493-1]
RefSeqiNP_001293003.1. NM_001306074.1.
NP_001293004.1. NM_001306075.1. [Q14493-2]
NP_006518.1. NM_006527.3. [Q14493-1]
UniGeneiHs.298345.

Genome annotation databases

EnsembliENST00000429429; ENSP00000406322; ENSG00000163950. [Q14493-2]
ENST00000489418; ENSP00000417686; ENSG00000163950. [Q14493-1]
GeneIDi7884.
KEGGihsa:7884.
UCSCiuc003gdk.2. human. [Q14493-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63544 Genomic DNA. No translation available.
U75679 mRNA. Translation: AAB97091.1.
Z71188 mRNA. Translation: CAA94918.1.
AK091735 mRNA. Translation: BAG52407.1.
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82579.1.
BC014908 mRNA. Translation: AAH14908.1.
BC015703 mRNA. Translation: AAH15703.1.
CCDSiCCDS3350.1. [Q14493-1]
RefSeqiNP_001293003.1. NM_001306074.1.
NP_001293004.1. NM_001306075.1. [Q14493-2]
NP_006518.1. NM_006527.3. [Q14493-1]
UniGeneiHs.298345.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJMNMR-A129-158[»]
4L8RX-ray2.60C125-223[»]
4QOZX-ray2.30C125-223[»]
ProteinModelPortaliQ14493.
SMRiQ14493. Positions 127-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113627. 10 interactions.
DIPiDIP-57045N.
IntActiQ14493. 4 interactions.
STRINGi9606.ENSP00000417686.

PTM databases

iPTMnetiQ14493.
PhosphoSiteiQ14493.

Polymorphism and mutation databases

BioMutaiSLBP.
DMDMi9789785.

Proteomic databases

EPDiQ14493.
MaxQBiQ14493.
PaxDbiQ14493.
PeptideAtlasiQ14493.
PRIDEiQ14493.

Protocols and materials databases

DNASUi7884.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000429429; ENSP00000406322; ENSG00000163950. [Q14493-2]
ENST00000489418; ENSP00000417686; ENSG00000163950. [Q14493-1]
GeneIDi7884.
KEGGihsa:7884.
UCSCiuc003gdk.2. human. [Q14493-1]

Organism-specific databases

CTDi7884.
GeneCardsiSLBP.
HGNCiHGNC:10904. SLBP.
HPAiHPA019254.
HPA061670.
MIMi602422. gene.
neXtProtiNX_Q14493.
PharmGKBiPA35804.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3934. Eukaryota.
ENOG41122ZE. LUCA.
GeneTreeiENSGT00390000008738.
HOGENOMiHOG000065710.
HOVERGENiHBG017805.
InParanoidiQ14493.
KOiK18710.
PhylomeDBiQ14493.
TreeFamiTF316521.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Miscellaneous databases

ChiTaRSiSLBP. human.
EvolutionaryTraceiQ14493.
GeneWikiiSLBP.
GenomeRNAii7884.
PROiQ14493.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163950.
CleanExiHS_SLBP.
ExpressionAtlasiQ14493. baseline and differential.
GenevisibleiQ14493. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q14493
Secondary accession number(s): B3KRJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.