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Q14493 (SLBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone RNA hairpin-binding protein
Alternative name(s):
Histone stem-loop-binding protein
Gene names
Name:SLBP
Synonyms:HBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.19

Subunit structure

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. Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Subcellular location

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. Ref.9 Ref.10

Tissue specificity

Widely expressed.

Developmental stage

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

Domain

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.

Post-translational modification

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. Ref.9 Ref.16 Ref.23

Sequence similarities

Belongs to the SLBP family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

histone mRNA 3'-end processing

Inferred from sequence or structural similarity. Source: UniProtKB

histone mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA transport

Inferred from direct assay Ref.19. Source: UniProtKB

nuclear cell cycle DNA replication

Inferred from mutant phenotype Ref.19. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

histone pre-mRNA 3'end processing complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

ribonucleoprotein complex

Traceable author statement PubMed 10825184. Source: ProtInc

   Molecular_functionhistone pre-mRNA DCP binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone pre-mRNA stem-loop binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14493-1)

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.
Isoform 2 (identifier: Q14493-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Histone RNA hairpin-binding protein
PRO_0000100356

Regions

Region129 – 19870RNA-binding
Motif31 – 344Nuclear localization signal NLS1
Motif96 – 994Nuclear localization signal NLS2

Amino acid modifications

Modified residue201Phosphoserine Ref.12
Modified residue231Phosphoserine Ref.12
Modified residue611Phosphothreonine; by CK2 Ref.9 Ref.16
Modified residue621Phosphothreonine; by CDK1 Ref.9 Ref.16
Modified residue1711Phosphothreonine Ref.23
Modified residue1821Phosphoserine Ref.22

Natural variations

Alternative sequence20 – 5839Missing in isoform 2.
VSP_042164

Experimental info

Mutagenesis31 – 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. Ref.10
Mutagenesis59 – 635SFTTP → AAAA: Does not increase its stability at the end of the S phase and through G2 and mitosis. Ref.9 Ref.16
Mutagenesis591S → A: Does not increase its stability at the end of the S phase and through G2 and mitosis. Ref.9
Mutagenesis611T → 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. Ref.9 Ref.16
Mutagenesis621T → A: Increases its stability at the end of the S phase and through G2 and mitosis. Ref.9 Ref.16
Mutagenesis631P → A: Increases its stability at the end of the S phase and through G2 and mitosis. Ref.9
Mutagenesis96 – 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. Ref.9 Ref.10 Ref.16
Mutagenesis1371R → A: Inhibits histone RNA-binding and localization to the cytoplasm. Ref.10
Mutagenesis1381R → A: Inhibits histone RNA-binding and localization to the cytoplasm. Ref.10
Mutagenesis230 – 27041Missing: Decrease in 3'-end processing efficiency. Ref.8
Mutagenesis241 – 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. Ref.10

Secondary structure

........ 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4E84E502393D1BF7

FASTA27031,286
        10         20         30         40         50         60 
MACRPRSPPR HQSRCDGDAS PPSPARWSLG RKRRADGRRW RPEDAEEAEH RGAERRPESF 

        70         80         90        100        110        120 
TTPEGPKPRS RCSDWASAVE EDEMRTRVNK EMARYKRKLL INDFGRERKS SSGSSDSKES 

       130        140        150        160        170        180 
MSTVPADFET DESVLMRRQK QINYGKNTIA YDRYIKEVPR HLRQPGIHPK TPNKFKKYSR 

       190        200        210        220        230        240 
RSWDQQIKLW KVALHFWDPP AEEGCDLQEI HPVDLESAES SSEPQTSSQD DFDVYSGTPT 

       250        260        270 
KVRHMDSQVE DEFDLEACLT EPLRDFSAMS 

« Hide

Isoform 2 [UniParc].

Checksum: 09C5137F52AC416D
Show »

FASTA23126,695

References

« Hide 'large scale' references
[1]"Expressed genes, Alu repeats and polymorphisms in cosmids sequenced from chromosome 4p16.3."
McCombie W.R., Martin-Gallardo A., Gocayne J.D., FitzGerald M., Dubnick M., Kelley J.M., Castilla L., Liu L.I., Wallace S., Trapp S., Tagle D., Whaley W.L., Cheng S., Gusella J., Frischauf A.-M., Poustka A., Lehrach H., Collins F.S. expand/collapse author list , Kerlavage A.R., Fields C., Venter J.C.
Nat. Genet. 1:348-353(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing."
Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.
Genes Dev. 10:3028-3040(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix adenocarcinoma.
[3]"The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein."
Martin F., Schaller A., Eglite S., Schuemperli D., Mueller B.
EMBO J. 16:769-778(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lymphocyte.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Heart.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[8]"A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end processing."
Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.
Genes Dev. 16:58-71(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 230-ASP--SER-270, INTERACTION WITH ZNF473.
[9]"Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase."
Zheng L., Dominski Z., Yang X.-C., Elms P., Raska C.S., Borchers C.H., Marzluff W.F.
Mol. Cell. Biol. 23:1590-1601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH POLYRIBOSOMES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-61 AND THR-62, RNA-BINDING, MUTAGENESIS OF SER-59; THR-61; THR-62; PRO-63 AND 96-LYS--LEU-99, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Nuclear import of the stem-loop binding protein and localization during the cell cycle."
Erkmann J.A., Wagner E.J., Dong J., Zhang Y., Kutay U., Marzluff W.F.
Mol. Biol. Cell 16:2960-2971(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNPO3 AND THE IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF 31-ARG--ARG-34; 96-LYS--LYS-99; ARG-137; ARG-138 AND 241-LYS--HIS-244.
[11]"Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1."
Kaygun H., Marzluff W.F.
Nat. Struct. Mol. Biol. 12:794-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UPF1.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA."
Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.
J. Biol. Chem. 281:30447-30454(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A TERNARY COMPLEX, RNA-BINDING.
[14]"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
Mullen T.E., Marzluff W.F.
Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LSM1.
[15]"SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIF4GD.
[16]"Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase."
Koseoglu M.M., Graves L.M., Marzluff W.F.
Mol. Cell. Biol. 28:4469-4479(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-61 AND THR-62, MUTAGENESIS OF THR-61; THR-62; 59-SER--PRO-63 AND 96-LYS--LEU-99, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Knockdown of SLBP results in nuclear retention of histone mRNA."
Sullivan K.D., Mullen T.E., Marzluff W.F., Wagner E.J.
RNA 15:459-472(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE MRNA EXPORT.
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization."
Zhang M., Lam T.T., Tonelli M., Marzluff W.F., Thapar R.
Biochemistry 51:3215-3231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 129-158, PHOSPHORYLATION AT THR-171.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006518.1. NM_006527.2.
UniGeneHs.298345.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KJMNMR-A129-158[»]
4L8RX-ray2.60C125-223[»]
ProteinModelPortalQ14493.
SMRQ14493. Positions 127-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113627. 5 interactions.
DIPDIP-57045N.
IntActQ14493. 3 interactions.
STRING9606.ENSP00000417686.

PTM databases

PhosphoSiteQ14493.

Polymorphism databases

DMDM9789785.

Proteomic databases

PaxDbQ14493.
PeptideAtlasQ14493.
PRIDEQ14493.

Protocols and materials databases

DNASU7884.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000429429; ENSP00000406322; ENSG00000163950. [Q14493-2]
ENST00000489418; ENSP00000417686; ENSG00000163950. [Q14493-1]
GeneID7884.
KEGGhsa:7884.
UCSCuc003gdi.1. human. [Q14493-1]
uc003gdk.1. human. [Q14493-2]

Organism-specific databases

CTD7884.
GeneCardsGC04M001694.
HGNCHGNC:10904. SLBP.
HPAHPA019254.
MIM602422. gene.
neXtProtNX_Q14493.
PharmGKBPA35804.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278381.
HOGENOMHOG000065710.
HOVERGENHBG017805.
InParanoidQ14493.
OrthoDBEOG789CF1.
PhylomeDBQ14493.
TreeFamTF316521.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ14493.
BgeeQ14493.
CleanExHS_SLBP.
GenevestigatorQ14493.

Family and domain databases

InterProIPR026502. SLBP1/SLBP2.
[Graphical view]
PANTHERPTHR17408. PTHR17408. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14493.
GeneWikiSLBP.
GenomeRNAi7884.
NextBio30350.
PROQ14493.
SOURCESearch...

Entry information

Entry nameSLBP_HUMAN
AccessionPrimary (citable) accession number: Q14493
Secondary accession number(s): B3KRJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM