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Histone RNA hairpin-binding protein (Histone stem-loop-binding protein)

 SLBP_HUMAN              Reviewed;         270 AA.
Q14493; B3KRJ5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 168.
RecName: Full=Histone RNA hairpin-binding protein;
AltName: Full=Histone stem-loop-binding protein;
Name=SLBP; Synonyms=HBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1338771; DOI=10.1038/ng0892-348;
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., Kerlavage A.R., Fields C.,
Venter J.C.;
"Expressed genes, Alu repeats and polymorphisms in cosmids sequenced
from chromosome 4p16.3.";
Nat. Genet. 1:348-353(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cervix adenocarcinoma;
PubMed=8957003; DOI=10.1101/gad.10.23.3028;
Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z.,
Marzluff W.F.;
"The protein that binds the 3' end of histone mRNA: a novel RNA-
binding protein required for histone pre-mRNA processing.";
Genes Dev. 10:3028-3040(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphocyte;
PubMed=9049306; DOI=10.1093/emboj/16.4.769;
Martin F., Schaller A., Eglite S., Schuemperli D., Mueller B.;
"The gene for histone RNA hairpin binding protein is located on human
chromosome 4 and encodes a novel type of RNA binding protein.";
EMBO J. 16:769-778(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
MUTAGENESIS OF 230-ASP--SER-270, AND INTERACTION WITH ZNF473.
PubMed=11782445; DOI=10.1101/gad.932302;
Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.;
"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.";
Genes Dev. 16:58-71(2002).
[9]
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, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=12588979; DOI=10.1128/MCB.23.5.1590-1601.2003;
Zheng L., Dominski Z., Yang X.-C., Elms P., Raska C.S., Borchers C.H.,
Marzluff W.F.;
"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.";
Mol. Cell. Biol. 23:1590-1601(2003).
[10]
INTERACTION WITH TNPO3 AND THE IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 31-ARG--ARG-34;
96-LYS--LYS-99; ARG-137; ARG-138 AND 241-LYS--HIS-244.
PubMed=15829567; DOI=10.1091/mbc.E04-11-1023;
Erkmann J.A., Wagner E.J., Dong J., Zhang Y., Kutay U., Marzluff W.F.;
"Nuclear import of the stem-loop binding protein and localization
during the cell cycle.";
Mol. Biol. Cell 16:2960-2971(2005).
[11]
INTERACTION WITH UPF1.
PubMed=16086026; DOI=10.1038/nsmb972;
Kaygun H., Marzluff W.F.;
"Regulated degradation of replication-dependent histone mRNAs requires
both ATR and Upf1.";
Nat. Struct. Mol. Biol. 12:794-800(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
IDENTIFICATION IN A TERNARY COMPLEX, AND RNA-BINDING.
PubMed=16912046; DOI=10.1074/jbc.M602947200;
Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.;
"Characterization of 3'hExo, a 3' exonuclease specifically interacting
with the 3' end of histone mRNA.";
J. Biol. Chem. 281:30447-30454(2006).
[14]
INTERACTION WITH LSM1.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[15]
INTERACTION WITH MIF4GD.
PubMed=18025107; DOI=10.1128/MCB.01500-07;
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
"SLIP1, a factor required for activation of histone mRNA translation
by the stem-loop binding protein.";
Mol. Cell. Biol. 28:1182-1194(2008).
[16]
PHOSPHORYLATION AT THR-61 AND THR-62, MUTAGENESIS OF THR-61; THR-62;
59-SER--PRO-63 AND 96-LYS--LEU-99, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18490441; DOI=10.1128/MCB.01416-07;
Koseoglu M.M., Graves L.M., Marzluff W.F.;
"Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation
of stem-loop binding protein at the end of S phase.";
Mol. Cell. Biol. 28:4469-4479(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
FUNCTION IN HISTONE MRNA EXPORT.
PubMed=19155325; DOI=10.1261/rna.1205409;
Sullivan K.D., Mullen T.E., Marzluff W.F., Wagner E.J.;
"Knockdown of SLBP results in nuclear retention of histone mRNA.";
RNA 15:459-472(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-59;
THR-62 AND THR-171, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-98, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
STRUCTURE BY NMR OF 129-158, AND PHOSPHORYLATION AT THR-171.
PubMed=22439849; DOI=10.1021/bi2018255;
Zhang M., Lam T.T., Tonelli M., Marzluff W.F., Thapar R.;
"Interaction of the histone mRNA hairpin with stem-loop binding
protein (SLBP) and regulation of the SLBP-RNA complex by
phosphorylation and proline isomerization.";
Biochemistry 51:3215-3231(2012).
-!- 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.
{ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:19155325}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Q8IV48:ERI1; NbExp=2; IntAct=EBI-2696402, EBI-5459222;
Q92900:UPF1; NbExp=3; IntAct=EBI-2696402, EBI-373471;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14493-1; Sequence=Displayed;
Name=2;
IsoId=Q14493-2; Sequence=VSP_042164;
-!- 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.
-!- 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}.
-!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
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EMBL; M63544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U75679; AAB97091.1; -; mRNA.
EMBL; Z71188; CAA94918.1; -; mRNA.
EMBL; AK091735; BAG52407.1; -; mRNA.
EMBL; AC016773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471131; EAW82579.1; -; Genomic_DNA.
EMBL; BC014908; AAH14908.1; -; mRNA.
EMBL; BC015703; AAH15703.1; -; mRNA.
CCDS; CCDS3350.1; -. [Q14493-1]
CCDS; CCDS82903.1; -. [Q14493-2]
RefSeq; NP_001293003.1; NM_001306074.1.
RefSeq; NP_001293004.1; NM_001306075.1. [Q14493-2]
RefSeq; NP_006518.1; NM_006527.3. [Q14493-1]
UniGene; Hs.298345; -.
PDB; 2KJM; NMR; -; A=129-158.
PDB; 4L8R; X-ray; 2.60 A; C=125-223.
PDB; 4QOZ; X-ray; 2.30 A; C=125-223.
PDBsum; 2KJM; -.
PDBsum; 4L8R; -.
PDBsum; 4QOZ; -.
ProteinModelPortal; Q14493; -.
SMR; Q14493; -.
BioGrid; 113627; 32.
DIP; DIP-57045N; -.
IntAct; Q14493; 9.
STRING; 9606.ENSP00000417686; -.
iPTMnet; Q14493; -.
PhosphoSitePlus; Q14493; -.
BioMuta; SLBP; -.
DMDM; 9789785; -.
EPD; Q14493; -.
PaxDb; Q14493; -.
PeptideAtlas; Q14493; -.
PRIDE; Q14493; -.
ProteomicsDB; 60001; -.
ProteomicsDB; 60002; -. [Q14493-2]
DNASU; 7884; -.
Ensembl; ENST00000429429; ENSP00000406322; ENSG00000163950. [Q14493-2]
Ensembl; ENST00000489418; ENSP00000417686; ENSG00000163950. [Q14493-1]
GeneID; 7884; -.
KEGG; hsa:7884; -.
UCSC; uc003gdk.2; human. [Q14493-1]
CTD; 7884; -.
DisGeNET; 7884; -.
EuPathDB; HostDB:ENSG00000163950.12; -.
GeneCards; SLBP; -.
HGNC; HGNC:10904; SLBP.
HPA; HPA019254; -.
HPA; HPA061670; -.
MIM; 602422; gene.
neXtProt; NX_Q14493; -.
OpenTargets; ENSG00000163950; -.
PharmGKB; PA35804; -.
eggNOG; KOG3934; Eukaryota.
eggNOG; ENOG41122ZE; LUCA.
GeneTree; ENSGT00390000008738; -.
HOGENOM; HOG000065710; -.
HOVERGEN; HBG017805; -.
InParanoid; Q14493; -.
KO; K18710; -.
PhylomeDB; Q14493; -.
TreeFam; TF316521; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
ChiTaRS; SLBP; human.
EvolutionaryTrace; Q14493; -.
GeneWiki; SLBP; -.
GenomeRNAi; 7884; -.
PRO; PR:Q14493; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163950; Expressed in 226 organ(s), highest expression level in oocyte.
CleanEx; HS_SLBP; -.
ExpressionAtlas; Q14493; baseline and differential.
Genevisible; Q14493; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; TAS:ProtInc.
GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB.
GO; GO:0071207; F:histone pre-mRNA stem-loop binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB.
GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
GO; GO:0033260; P:nuclear DNA replication; IMP:UniProtKB.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
Gene3D; 1.10.8.1120; -; 1.
InterPro; IPR026502; SLBP1/SLBP2.
InterPro; IPR029344; SLBP_RNA_bind.
InterPro; IPR038294; SLBP_RNA_bind_sf.
PANTHER; PTHR17408; PTHR17408; 1.
Pfam; PF15247; SLBP_RNA_bind; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Isopeptide bond; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation.
CHAIN 1 270 Histone RNA hairpin-binding protein.
/FTId=PRO_0000100356.
REGION 129 198 RNA-binding.
MOTIF 31 34 Nuclear localization signal NLS1.
MOTIF 96 99 Nuclear localization signal NLS2.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 61 61 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:12588979,
ECO:0000269|PubMed:18490441}.
MOD_RES 62 62 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12588979,
ECO:0000269|PubMed:18490441}.
MOD_RES 171 171 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22439849}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 98 98 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 20 58 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042164.
MUTAGEN 31 34 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.
{ECO:0000269|PubMed:15829567}.
MUTAGEN 59 63 SFTTP->AAAA: Does not increase its
stability at the end of the S phase and
through G2 and mitosis.
{ECO:0000269|PubMed:18490441}.
MUTAGEN 59 59 S->A: Does not increase its stability at
the end of the S phase and through G2 and
mitosis. {ECO:0000269|PubMed:12588979}.
MUTAGEN 61 61 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.
{ECO:0000269|PubMed:12588979,
ECO:0000269|PubMed:18490441}.
MUTAGEN 62 62 T->A: Increases its stability at the end
of the S phase and through G2 and
mitosis. {ECO:0000269|PubMed:12588979,
ECO:0000269|PubMed:18490441}.
MUTAGEN 63 63 P->A: Increases its stability at the end
of the S phase and through G2 and
mitosis. {ECO:0000269|PubMed:12588979}.
MUTAGEN 96 99 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.
{ECO:0000269|PubMed:12588979,
ECO:0000269|PubMed:15829567,
ECO:0000269|PubMed:18490441}.
MUTAGEN 137 137 R->A: Inhibits histone RNA-binding and
localization to the cytoplasm.
{ECO:0000269|PubMed:15829567}.
MUTAGEN 138 138 R->A: Inhibits histone RNA-binding and
localization to the cytoplasm.
{ECO:0000269|PubMed:15829567}.
MUTAGEN 230 270 Missing: Decrease in 3'-end processing
efficiency.
{ECO:0000269|PubMed:11782445}.
MUTAGEN 241 244 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.
{ECO:0000269|PubMed:15829567}.
HELIX 132 146 {ECO:0000244|PDB:4QOZ}.
HELIX 149 157 {ECO:0000244|PDB:4QOZ}.
TURN 165 167 {ECO:0000244|PDB:4QOZ}.
HELIX 180 194 {ECO:0000244|PDB:4QOZ}.
HELIX 195 197 {ECO:0000244|PDB:4QOZ}.
SEQUENCE 270 AA; 31286 MW; 4E84E502393D1BF7 CRC64;
MACRPRSPPR HQSRCDGDAS PPSPARWSLG RKRRADGRRW RPEDAEEAEH RGAERRPESF
TTPEGPKPRS RCSDWASAVE EDEMRTRVNK EMARYKRKLL INDFGRERKS SSGSSDSKES
MSTVPADFET DESVLMRRQK QINYGKNTIA YDRYIKEVPR HLRQPGIHPK TPNKFKKYSR
RSWDQQIKLW KVALHFWDPP AEEGCDLQEI HPVDLESAES SSEPQTSSQD DFDVYSGTPT
KVRHMDSQVE DEFDLEACLT EPLRDFSAMS


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