SLBP_HUMAN
ID SLBP_HUMAN Reviewed; 270 AA.
AC Q14493; B3KRJ5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Histone RNA hairpin-binding protein;
DE AltName: Full=Histone stem-loop-binding protein;
GN Name=SLBP; Synonyms=HBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1338771; DOI=10.1038/ng0892-348;
RA McCombie W.R., Martin-Gallardo A., Gocayne J.D., FitzGerald M., Dubnick M.,
RA Kelley J.M., Castilla L., Liu L.I., Wallace S., Trapp S., Tagle D.,
RA Whaley W.L., Cheng S., Gusella J., Frischauf A.-M., Poustka A., Lehrach H.,
RA Collins F.S., Kerlavage A.R., Fields C., Venter J.C.;
RT "Expressed genes, Alu repeats and polymorphisms in cosmids sequenced from
RT chromosome 4p16.3.";
RL Nat. Genet. 1:348-353(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Cervix adenocarcinoma;
RX PubMed=8957003; DOI=10.1101/gad.10.23.3028;
RA Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.;
RT "The protein that binds the 3' end of histone mRNA: a novel RNA-binding
RT protein required for histone pre-mRNA processing.";
RL Genes Dev. 10:3028-3040(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=9049306; DOI=10.1093/emboj/16.4.769;
RA Martin F., Schaller A., Eglite S., Schuemperli D., Mueller B.;
RT "The gene for histone RNA hairpin binding protein is located on human
RT chromosome 4 and encodes a novel type of RNA binding protein.";
RL EMBO J. 16:769-778(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP MUTAGENESIS OF 230-ASP--SER-270, AND INTERACTION WITH ZNF473.
RX PubMed=11782445; DOI=10.1101/gad.932302;
RA Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F.;
RT "A novel zinc finger protein is associated with U7 snRNP and interacts with
RT the stem-loop binding protein in the histone pre-mRNP to stimulate 3'-end
RT processing.";
RL Genes Dev. 16:58-71(2002).
RN [9]
RP FUNCTION, ASSOCIATION WITH POLYRIBOSOMES, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT THR-61 AND THR-62, RNA-BINDING, MUTAGENESIS OF SER-59;
RP THR-61; THR-62; PRO-63 AND 96-LYS--LEU-99, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12588979; DOI=10.1128/mcb.23.5.1590-1601.2003;
RA Zheng L., Dominski Z., Yang X.-C., Elms P., Raska C.S., Borchers C.H.,
RA Marzluff W.F.;
RT "Phosphorylation of stem-loop binding protein (SLBP) on two threonines
RT triggers degradation of SLBP, the sole cell cycle-regulated factor required
RT for regulation of histone mRNA processing, at the end of S phase.";
RL Mol. Cell. Biol. 23:1590-1601(2003).
RN [10]
RP INTERACTION WITH TNPO3 AND THE IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 31-ARG--ARG-34; 96-LYS--LYS-99;
RP ARG-137; ARG-138 AND 241-LYS--HIS-244.
RX PubMed=15829567; DOI=10.1091/mbc.e04-11-1023;
RA Erkmann J.A., Wagner E.J., Dong J., Zhang Y., Kutay U., Marzluff W.F.;
RT "Nuclear import of the stem-loop binding protein and localization during
RT the cell cycle.";
RL Mol. Biol. Cell 16:2960-2971(2005).
RN [11]
RP INTERACTION WITH UPF1.
RX PubMed=16086026; DOI=10.1038/nsmb972;
RA Kaygun H., Marzluff W.F.;
RT "Regulated degradation of replication-dependent histone mRNAs requires both
RT ATR and Upf1.";
RL Nat. Struct. Mol. Biol. 12:794-800(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-23, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION IN A TERNARY COMPLEX, AND RNA-BINDING.
RX PubMed=16912046; DOI=10.1074/jbc.m602947200;
RA Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.;
RT "Characterization of 3'hExo, a 3' exonuclease specifically interacting with
RT the 3' end of histone mRNA.";
RL J. Biol. Chem. 281:30447-30454(2006).
RN [14]
RP INTERACTION WITH LSM1.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [15]
RP INTERACTION WITH MIF4GD.
RX PubMed=18025107; DOI=10.1128/mcb.01500-07;
RA Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.;
RT "SLIP1, a factor required for activation of histone mRNA translation by the
RT stem-loop binding protein.";
RL Mol. Cell. Biol. 28:1182-1194(2008).
RN [16]
RP PHOSPHORYLATION AT THR-61 AND THR-62, MUTAGENESIS OF THR-61; THR-62;
RP 59-SER--PRO-63 AND 96-LYS--LEU-99, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18490441; DOI=10.1128/mcb.01416-07;
RA Koseoglu M.M., Graves L.M., Marzluff W.F.;
RT "Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of
RT stem-loop binding protein at the end of S phase.";
RL Mol. Cell. Biol. 28:4469-4479(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP FUNCTION IN HISTONE MRNA EXPORT.
RX PubMed=19155325; DOI=10.1261/rna.1205409;
RA Sullivan K.D., Mullen T.E., Marzluff W.F., Wagner E.J.;
RT "Knockdown of SLBP results in nuclear retention of histone mRNA.";
RL RNA 15:459-472(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-59; THR-62
RP AND THR-171, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP UBIQUITINATION.
RX PubMed=28118078; DOI=10.1080/15384101.2017.1284715;
RA Dankert J.F., Pagan J.K., Starostina N.G., Kipreos E.T., Pagano M.;
RT "FEM1 proteins are ancient regulators of SLBP degradation.";
RL Cell Cycle 16:556-564(2017).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-98, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP STRUCTURE BY NMR OF 129-158, AND PHOSPHORYLATION AT THR-171.
RX PubMed=22439849; DOI=10.1021/bi2018255;
RA Zhang M., Lam T.T., Tonelli M., Marzluff W.F., Thapar R.;
RT "Interaction of the histone mRNA hairpin with stem-loop binding protein
RT (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and
RT proline isomerization.";
RL Biochemistry 51:3215-3231(2012).
CC -!- FUNCTION: RNA-binding protein involved in the histone pre-mRNA
CC processing (PubMed:8957003, PubMed:9049306, PubMed:12588979,
CC PubMed:19155325). Binds the stem-loop structure of replication-
CC dependent histone pre-mRNAs and contributes to efficient 3'-end
CC processing by stabilizing the complex between histone pre-mRNA and U7
CC small nuclear ribonucleoprotein (snRNP), via the histone downstream
CC element (HDE) (PubMed:8957003, PubMed:9049306, PubMed:12588979,
CC PubMed:19155325). Plays an important role in targeting mature histone
CC mRNA from the nucleus to the cytoplasm and to the translation machinery
CC (PubMed:8957003, PubMed:9049306, PubMed:12588979, PubMed:19155325).
CC Stabilizes mature histone mRNA and could be involved in cell-cycle
CC regulation of histone gene expression (PubMed:8957003, PubMed:9049306,
CC PubMed:12588979, PubMed:19155325). Involved in the mechanism by which
CC growing oocytes accumulate histone proteins that support early
CC embryogenesis (By similarity). Binds to the 5' side of the stem-loop
CC structure of histone pre-mRNAs (By similarity).
CC {ECO:0000250|UniProtKB:P97440, ECO:0000269|PubMed:12588979,
CC ECO:0000269|PubMed:19155325, ECO:0000269|PubMed:8957003,
CC ECO:0000269|PubMed:9049306}.
CC -!- SUBUNIT: Monomer (PubMed:22439849). SLBP/pre-mRNA complex interacts
CC with ZNF473 (PubMed:11782445). Interacts with the Importin
CC alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1
CC (PubMed:15829567, PubMed:16086026, PubMed:18025107). Interaction with
CC LSM1 occurs when histone mRNA is being rapidly degraded during the S
CC phase (PubMed:18172165). Found in a ternary complex with ERI1 and the
CC stem-loop structure of the 3' end of histone mRNA (PubMed:16912046).
CC Associates with polyribosomes (PubMed:12588979). Identified in a
CC histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC SNRPB, SYNCRIP and YBX1 (By similarity). Binds in a cooperative manner
CC with ERI1 to the mature 3'-end of histone mRNAs (By similarity).
CC {ECO:0000250|UniProtKB:P97440, ECO:0000269|PubMed:11782445,
CC ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567,
CC ECO:0000269|PubMed:16086026, ECO:0000269|PubMed:16912046,
CC ECO:0000269|PubMed:18025107, ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:22439849}.
CC -!- INTERACTION:
CC Q14493; Q8IV48: ERI1; NbExp=2; IntAct=EBI-2696402, EBI-5459222;
CC Q14493; A9UHW6: MIF4GD; NbExp=10; IntAct=EBI-2696402, EBI-373498;
CC Q14493; Q14493: SLBP; NbExp=8; IntAct=EBI-2696402, EBI-2696402;
CC Q14493; Q92900: UPF1; NbExp=3; IntAct=EBI-2696402, EBI-373471;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12588979,
CC ECO:0000269|PubMed:15829567}. Nucleus {ECO:0000269|PubMed:12588979,
CC ECO:0000269|PubMed:15829567}. Note=Polyribosome-associated
CC (PubMed:12588979). Localizes predominantly in the nucleus at the G1/G2
CC phases and the beginning of S phase (PubMed:12588979). Through the S
CC phase, partially redistributes to the cytoplasm (PubMed:12588979).
CC Binding to histone mRNA is necessary for cytoplasmic localization
CC (PubMed:12588979). Shuttles between the nucleus and the cytoplasm
CC (PubMed:15829567). Imported in the nucleus by the Importin
CC alpha/Importin beta receptor (PubMed:15829567).
CC {ECO:0000269|PubMed:12588979, ECO:0000269|PubMed:15829567}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14493-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14493-2; Sequence=VSP_042164;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9049306}.
CC -!- DEVELOPMENTAL STAGE: Regulated during the cell cycle: protein levels
CC increase 10 to 20 fold in the late G1 and decrease at the S/G2 border.
CC -!- DOMAIN: Amino acids 31-34, 96-99 and 241-244 are necessary for
CC interaction with the Importin alpha/Importin beta receptor. The first
CC 18 amino acids, amino acids 69-76 and 179-182 are necessary for
CC interaction with TNPO3. Amino acids 31-34, 96-99 and 241-244 are
CC necessary for nuclear localization. {ECO:0000269|PubMed:15829567}.
CC -!- PTM: Phosphorylated on Thr-61 and Thr-62 in the S-phase.
CC Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by
CC CK2. Phosphorylation of Thr-62 is required for its degradation by the
CC proteasome at the end of the S phase. Its degradation is not required
CC for histone mRNA degradation at the end of the S phase. All the
CC phosphorylated forms detected are present in the cytoplasm. Both
CC unphosphorylated and phosphorylated forms bind the stem-loop structure
CC of histone mRNAs. Phosphorylation at Thr-171 increases affinity for
CC histone mRNAs. {ECO:0000269|PubMed:12588979,
CC ECO:0000269|PubMed:18490441, ECO:0000269|PubMed:22439849}.
CC -!- PTM: Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C)
CC complexes, leading to its degradation. {ECO:0000269|PubMed:28118078}.
CC -!- SIMILARITY: Belongs to the SLBP family. {ECO:0000305}.
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DR EMBL; M63544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U75679; AAB97091.1; -; mRNA.
DR EMBL; Z71188; CAA94918.1; -; mRNA.
DR EMBL; AK091735; BAG52407.1; -; mRNA.
DR EMBL; AC016773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82579.1; -; Genomic_DNA.
DR EMBL; BC014908; AAH14908.1; -; mRNA.
DR EMBL; BC015703; AAH15703.1; -; mRNA.
DR CCDS; CCDS3350.1; -. [Q14493-1]
DR CCDS; CCDS82903.1; -. [Q14493-2]
DR RefSeq; NP_001293003.1; NM_001306074.1.
DR RefSeq; NP_001293004.1; NM_001306075.1. [Q14493-2]
DR RefSeq; NP_006518.1; NM_006527.3. [Q14493-1]
DR PDB; 2KJM; NMR; -; A=129-158.
DR PDB; 4L8R; X-ray; 2.60 A; C=125-223.
DR PDB; 4QOZ; X-ray; 2.30 A; C=125-223.
DR PDBsum; 2KJM; -.
DR PDBsum; 4L8R; -.
DR PDBsum; 4QOZ; -.
DR AlphaFoldDB; Q14493; -.
DR BMRB; Q14493; -.
DR SMR; Q14493; -.
DR BioGRID; 113627; 67.
DR ComplexPortal; CPX-1313; SLBP-SLIP1 complex.
DR DIP; DIP-57045N; -.
DR IntAct; Q14493; 17.
DR MINT; Q14493; -.
DR STRING; 9606.ENSP00000417686; -.
DR GlyGen; Q14493; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14493; -.
DR PhosphoSitePlus; Q14493; -.
DR BioMuta; SLBP; -.
DR DMDM; 9789785; -.
DR EPD; Q14493; -.
DR jPOST; Q14493; -.
DR MassIVE; Q14493; -.
DR MaxQB; Q14493; -.
DR PaxDb; Q14493; -.
DR PeptideAtlas; Q14493; -.
DR PRIDE; Q14493; -.
DR ProteomicsDB; 60001; -. [Q14493-1]
DR ProteomicsDB; 60002; -. [Q14493-2]
DR Antibodypedia; 8450; 84 antibodies from 23 providers.
DR DNASU; 7884; -.
DR Ensembl; ENST00000429429.6; ENSP00000406322.2; ENSG00000163950.13. [Q14493-2]
DR Ensembl; ENST00000489418.6; ENSP00000417686.1; ENSG00000163950.13. [Q14493-1]
DR GeneID; 7884; -.
DR KEGG; hsa:7884; -.
DR MANE-Select; ENST00000489418.6; ENSP00000417686.1; NM_006527.4; NP_006518.1.
DR UCSC; uc003gdk.2; human. [Q14493-1]
DR CTD; 7884; -.
DR DisGeNET; 7884; -.
DR GeneCards; SLBP; -.
DR HGNC; HGNC:10904; SLBP.
DR HPA; ENSG00000163950; Low tissue specificity.
DR MIM; 602422; gene.
DR neXtProt; NX_Q14493; -.
DR OpenTargets; ENSG00000163950; -.
DR PharmGKB; PA35804; -.
DR VEuPathDB; HostDB:ENSG00000163950; -.
DR eggNOG; KOG3934; Eukaryota.
DR GeneTree; ENSGT00390000008738; -.
DR HOGENOM; CLU_093199_1_0_1; -.
DR InParanoid; Q14493; -.
DR PhylomeDB; Q14493; -.
DR TreeFam; TF316521; -.
DR PathwayCommons; Q14493; -.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR SignaLink; Q14493; -.
DR SIGNOR; Q14493; -.
DR BioGRID-ORCS; 7884; 369 hits in 1083 CRISPR screens.
DR ChiTaRS; SLBP; human.
DR EvolutionaryTrace; Q14493; -.
DR GeneWiki; SLBP; -.
DR GenomeRNAi; 7884; -.
DR Pharos; Q14493; Tbio.
DR PRO; PR:Q14493; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14493; protein.
DR Bgee; ENSG00000163950; Expressed in oocyte and 207 other tissues.
DR ExpressionAtlas; Q14493; baseline and differential.
DR Genevisible; Q14493; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0062073; C:histone mRNA stem-loop binding complex; IPI:ComplexPortal.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0071208; F:histone pre-mRNA DCP binding; ISS:UniProtKB.
DR GO; GO:0071207; F:histone pre-mRNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0002191; P:cap-dependent translational initiation; IDA:ComplexPortal.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR DisProt; DP01987; -.
DR Gene3D; 1.10.8.1120; -; 1.
DR InterPro; IPR026502; SLBP1/SLBP2.
DR InterPro; IPR029344; SLBP_RNA_bind.
DR InterPro; IPR038294; SLBP_RNA_bind_sf.
DR PANTHER; PTHR17408; PTHR17408; 1.
DR Pfam; PF15247; SLBP_RNA_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Isopeptide bond;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..270
FT /note="Histone RNA hairpin-binding protein"
FT /id="PRO_0000100356"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..198
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:8957003"
FT REGION 215..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..34
FT /note="Nuclear localization signal NLS1"
FT /evidence="ECO:0000269|PubMed:15829567"
FT MOTIF 96..99
FT /note="Nuclear localization signal NLS2"
FT /evidence="ECO:0000269|PubMed:15829567"
FT COMPBIAS 36..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 61
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:12588979,
FT ECO:0000269|PubMed:18490441"
FT MOD_RES 62
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:12588979,
FT ECO:0000269|PubMed:18490441, ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22439849,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 20..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042164"
FT MUTAGEN 31..34
FT /note="RKRR->AAAA: Reduces interaction with the importin
FT alpha/importin beta receptor. Abolishes interaction with
FT the importin alpha/importin beta receptor; when associated
FT with A-96; A-97; A-98 and A-99 or with A-241; A-242; A-243
FT and A-244."
FT /evidence="ECO:0000269|PubMed:15829567"
FT MUTAGEN 59..63
FT /note="SFTTP->AAAA: Does not increase its stability at the
FT end of the S phase and through G2 and mitosis."
FT /evidence="ECO:0000269|PubMed:18490441"
FT MUTAGEN 59
FT /note="S->A: Does not increase its stability at the end of
FT the S phase and through G2 and mitosis."
FT /evidence="ECO:0000269|PubMed:12588979"
FT MUTAGEN 61
FT /note="T->A: Increases its stability at the end of the S
FT phase and through G2 and mitosis. Active in histone pre-
FT mRNA processing during the G2 phase."
FT /evidence="ECO:0000269|PubMed:12588979,
FT ECO:0000269|PubMed:18490441"
FT MUTAGEN 62
FT /note="T->A: Increases its stability at the end of the S
FT phase and through G2 and mitosis."
FT /evidence="ECO:0000269|PubMed:12588979,
FT ECO:0000269|PubMed:18490441"
FT MUTAGEN 63
FT /note="P->A: Increases its stability at the end of the S
FT phase and through G2 and mitosis."
FT /evidence="ECO:0000269|PubMed:12588979"
FT MUTAGEN 96..99
FT /note="KRKL->AAAA: Increases its stability at the end of
FT the S phase and through G2 and mitosis. Inhibits
FT phosphorylation of T-62. Localizes in the nucleus. Reduces
FT interaction with the importin alpha/importin beta receptor.
FT Abolishes interaction with the importin alpha/importin beta
FT receptor; when associated with A-31; A-32; A-33 and A-34 or
FT with A-241; A-242; A-243 and A-244."
FT /evidence="ECO:0000269|PubMed:12588979,
FT ECO:0000269|PubMed:15829567, ECO:0000269|PubMed:18490441"
FT MUTAGEN 137
FT /note="R->A: Inhibits histone RNA-binding and localization
FT to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:15829567"
FT MUTAGEN 138
FT /note="R->A: Inhibits histone RNA-binding and localization
FT to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:15829567"
FT MUTAGEN 230..270
FT /note="Missing: Decrease in 3'-end processing efficiency."
FT /evidence="ECO:0000269|PubMed:11782445"
FT MUTAGEN 241..244
FT /note="KVRH->AAAA: Reduces interaction with the importin
FT alpha/importin beta receptor. Abolishes interaction with
FT the importin alpha/importin beta receptor; when associated
FT with A-31; A-32; A-33 and A-34 or with A-96; A-97; A-98 and
FT A-99."
FT /evidence="ECO:0000269|PubMed:15829567"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:4QOZ"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:4QOZ"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4QOZ"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:4QOZ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4QOZ"
SQ 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
