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Protein Page:
SLBP (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SLBP 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. 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. Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs. Widely expressed. Belongs to the SLBP family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: RNA binding protein
Cellular Component: nucleoplasm; cytoplasm; cytosol; nucleus; ribonucleoprotein complex
Molecular Function: mRNA binding; protein binding
Biological Process: transcription from RNA polymerase II promoter; mRNA export from nucleus; mRNA transport; histone mRNA metabolic process; DNA replication during S phase; gene expression; histone mRNA 3'-end processing; mRNA 3'-end processing; termination of RNA polymerase II transcription
Reference #:  Q14493 (UniProtKB)
Alt. Names/Synonyms: hairpin binding protein, histone; HBP; histone binding protein; Histone RNA hairpin-binding protein; histone stem-loop binding protein; Histone stem-loop-binding protein; SLBP; stem-loop (histone) binding protein; stem-loop binding protein
Gene Symbols: SLBP
Molecular weight: 31,286 Da
Basal Isoelectric point: 7.06  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SLBP

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: T171‑p
phosphorylation: T62‑p
protein degradation: T61‑p, T62‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 10 S7-p _MACRPRsPPRHQsR
0 1 S13-p RsPPRHQsRCDGDAs
1 40 S20-p sRCDGDAsPPsPARW
1 44 S23-p DGDAsPPsPARWsLG
0 3 S28-p PPsPARWsLGRKRRA
0 7 S59-p GAERRPEsFttPEGP
3 10 T61-p ERRPEsFttPEGPKP
3 10 T62-p RRPEsFttPEGPKPR
0 1 S77-p SRCSDWAsAVEEDEM
0 33 S110-p DFGRERKsssGssDs
0 71 S111-p FGRERKsssGssDsK
0 5 S112-p GRERKsssGssDsKE
0 3 S114-p ERKsssGssDsKEsM
0 6 S115-p RKsssGssDsKEsMs
0 2 S117-p sssGssDsKEsMstV
0 1 S120-p GssDsKEsMstVPAD
0 1 S122-p sDsKEsMstVPADFE
0 1 T123-p DsKEsMstVPADFET
0 1 R137-m1 TDESVLMrRQKQINY
3 27 T171-p QPGIHPKtPNKFKKy
0 1 Y178-p tPNKFKKySRRsWDQ
0 12 S182-p FKKySRRsWDQQIKL
0 1 S220-p VDLESAEsssEPQts
1 1 S221-p DLESAEsssEPQtss
1 1 S222-p LESAEsssEPQtssQ
1 1 T226-p EsssEPQtssQDDFD
0 1 S227-p sssEPQtssQDDFDV
0 2 S228-p ssEPQtssQDDFDVy
0 3 Y235-p sQDDFDVysGtPTKV
0 1 S236-p QDDFDVysGtPTKVR
0 1 T238-p DFDVysGtPTKVRHM
0 1 S247-p TKVRHMDsQVEDEFD
  mouse

 
S7-p _MACRPRsPPGYGSR
S13 RsPPGYGSRRDGGAs
S20-p SRRDGGAsPRsPARW
S23-p DGGAsPRsPARWSLG
S28 PRsPARWSLGRKRRA
S59 TADHRPESFTtPEGH
T61 DHRPESFTtPEGHKP
T62-p HRPESFTtPEGHKPR
S77 SRCSDWASAVEEDEM
S110-p DFGRERKsssGSsDs
S111-p FGRERKsssGSsDsK
S112-p GRERKsssGSsDsKE
S114 ERKsssGSsDsKEsM
S115-p RKsssGSsDsKEsMS
S117-p sssGSsDsKEsMSSV
S120-p GSsDsKEsMSSVPAD
S122 sDsKEsMSSVPADVE
S123 DsKEsMSSVPADVET
R137 TDESVLMRRQKQINY
T171-p QPGIHPRtPNKFKKY
Y178 tPNKFKKYSRRsWDQ
S182-p FKKYSRRsWDQQIKL
S225 METEFTESSSESQTS
S226 ETEFTESSSESQTSS
S227 TEFTESSSESQTSSQ
T231 ESSSESQTSSQDNFD
S232 SSSESQTSSQDNFDV
S233 SSESQTSSQDNFDVY
Y240 SQDNFDVYAGTPTKV
A241 QDNFDVYAGTPTKVR
T243 NFDVYAGTPTKVRHV
C252 TKVRHVDCQVEDEFD
  rat

 
S7 _MACRPRSPPRYGSR
S13 RSPPRYGSRRDGGAS
S20 SRRDGGASPRSPARW
S23 DGGASPRSPARWSLG
S28 PRSPARWSLGRKRRA
S59 TADHRPESFTTPEGH
T61 DHRPESFTTPEGHKP
T62 HRPESFTTPEGHKPR
S77 SRCSDWASAVEEDEM
S110-p DFGRERKsSSGSSDS
S111 FGRERKsSSGSSDSK
S112 GRERKsSSGSSDSKE
S114 ERKsSSGSSDSKESV
S115 RKsSSGSSDSKESVS
S117 sSSGSSDSKESVSSV
S120 GSSDSKESVSSVPAD
S122 SDSKESVSSVPADVE
S123 DSKESVSSVPADVET
R137 TDESVLMRRQKQINY
T171 QPGIHPRTPNKFKKY
Y178 TPNKFKKYSRRSWDQ
S182 FKKYSRRSWDQQIKL
S225 METEFTESSSESQTS
S226 ETEFTESSSESQTSS
S227 TEFTESSSESQTSSQ
T231 ESSSESQTSSQDNFD
S232 SSSESQTSSQDNFDV
S233 SSESQTSSQDNFDVY
Y240 SQDNFDVYAGTPTKV
A241 QDNFDVYAGTPTKVR
T243 NFDVYAGTPTKVRHV
C252 TKVRHVDCQVEDEFD
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