CPEB1_MOUSE
ID CPEB1_MOUSE Reviewed; 561 AA.
AC P70166; Q8C5P9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=mCPEB;
DE Short=mCPEB-1;
GN Name=Cpeb1; Synonyms=Cpeb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=8962099; DOI=10.1073/pnas.93.25.14602;
RA Gebauer F., Richter J.D.;
RT "Mouse cytoplasmic polyadenylation element binding protein: an
RT evolutionarily conserved protein that interacts with the cytoplasmic
RT polyadenylation elements of c-mos mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14602-14607(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-561.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9856468; DOI=10.1016/s0896-6273(00)80630-3;
RA Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A., Quinlan E.,
RA Heynen A., Fallon J.R., Richter J.D.;
RT "CPEB-mediated cytoplasmic polyadenylation and the regulation of
RT experience-dependent translation of alpha-CaMKII mRNA at synapses.";
RL Neuron 21:1129-1139(1998).
RN [4]
RP FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=11526086; DOI=10.1242/dev.128.14.2815;
RA Hodgman R., Tay J., Mendez R., Richter J.D.;
RT "CPEB phosphorylation and cytoplasmic polyadenylation are catalyzed by the
RT kinase IAK1/Eg2 in maturing mouse oocytes.";
RL Development 128:2815-2822(2001).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT THR-171 BY AURKA MUTAGENESIS OF THR-171,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11980711; DOI=10.1093/emboj/21.9.2139;
RA Huang Y.-S., Jung M.-Y., Sarkissian M., Richter J.D.;
RT "N-methyl-D-aspartate receptor signaling results in Aurora kinase-catalyzed
RT CPEB phosphorylation and alpha CaMKII mRNA polyadenylation at synapses.";
RL EMBO J. 21:2139-2148(2002).
RN [6]
RP FUNCTION, INTERACTION WITH DYNEIN AND KINESIN, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12629046; DOI=10.1101/gad.1053003;
RA Huang Y.-S., Carson J.H., Barbarese E., Richter J.D.;
RT "Facilitation of dendritic mRNA transport by CPEB.";
RL Genes Dev. 17:638-653(2003).
RN [7]
RP PHOSPHORYLATION AT THR-171 BY AURKA, DEPHOSPHORYLATION AT THR-171 BY PP1,
RP MUTAGENESIS OF THR-171, AND DEVELOPMENTAL STAGE.
RX PubMed=12815066; DOI=10.1101/gad.1071403;
RA Tay J., Hodgman R., Sarkissian M., Richter J.D.;
RT "Regulated CPEB phosphorylation during meiotic progression suggests a
RT mechanism for temporal control of maternal mRNA translation.";
RL Genes Dev. 17:1457-1462(2003).
RN [8]
RP TISSUE SPECIFICITY, AND ABSENCE OF KAINATE INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA Theis M., Si K., Kandel E.R.;
RT "Two previously undescribed members of the mouse CPEB family of genes and
RT their inducible expression in the principal cell layers of the
RT hippocampus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN [9]
RP PHOSPHORYLATION AT THR-171 BY CAMK2A, MUTAGENESIS OF THR-171, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15175389; DOI=10.1523/jneurosci.0854-04.2004;
RA Atkins C.M., Nozaki N., Shigeri Y., Soderling T.R.;
RT "Cytoplasmic polyadenylation element binding protein-dependent protein
RT synthesis is regulated by calcium/calmodulin-dependent protein kinase II.";
RL J. Neurosci. 24:5193-5201(2004).
RN [10]
RP PHOSPHORYLATION AT THR-171 BY CAMK2A, AND DEPHOSPHORYLATION AT THR-171.
RX PubMed=15944388; DOI=10.1523/jneurosci.5051-04.2005;
RA Atkins C.M., Davare M.A., Oh M.C., Derkach V., Soderling T.R.;
RT "Bidirectional regulation of cytoplasmic polyadenylation element-binding
RT protein phosphorylation by Ca2+/calmodulin-dependent protein kinase II and
RT protein phosphatase 1 during hippocampal long-term potentiation.";
RL J. Neurosci. 25:5604-5610(2005).
RN [11]
RP INTERACTION WITH APLP1; APLP2 AND APP, PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16314516; DOI=10.1128/mcb.25.24.10930-10939.2005;
RA Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
RT "Amyloid precursor proteins anchor CPEB to membranes and promote
RT polyadenylation-induced translation.";
RL Mol. Cell. Biol. 25:10930-10939(2005).
RN [12]
RP INTERACTION WITH NGDN.
RX PubMed=16705177; DOI=10.1128/mcb.02470-05;
RA Jung M.-Y., Lorenz L., Richter J.D.;
RT "Translational control by neuroguidin, a eukaryotic initiation factor 4E
RT and CPEB binding protein.";
RL Mol. Cell. Biol. 26:4277-4287(2006).
RN [13]
RP INTERACTION WITH TENT2.
RX PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M.,
RA Kashiwabara S., Baba T.;
RT "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT polyadenylation status in oocytes and somatic cells.";
RL Biochem. Biophys. Res. Commun. 364:14-19(2007).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA
CC cytoplasmic polyadenylation and translation initiation during oocyte
CC maturation, early development and at postsynapse sites of neurons.
CC Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich
CC sequence element (consensus sequence 5'-UUUUUAU-3') within the 3'-UTR
CC of mRNAs. In absence of phosphorylation and in association with TACC3
CC is also involved as a repressor of translation of CPE-containing mRNA;
CC a repression that is relieved by phosphorylation or degradation (By
CC similarity). Involved in the transport of CPE-containing mRNA to
CC dendrites; those mRNAs may be transported to dendrites in a
CC translationally dormant form and translationally activated at synapses.
CC Its interaction with APLP1 promotes local CPE-containing mRNA
CC polyadenylation and translation activation. Induces the assembly of
CC stress granules in the absence of stress (By similarity). Required for
CC cell cycle progression, specifically for prophase entry (By
CC similarity). {ECO:0000250|UniProtKB:Q9BZB8,
CC ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711,
CC ECO:0000269|PubMed:12629046}.
CC -!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, TENT2/GLD2 and
CC APP. Both phosphorylated and non phosphorylated forms interact with
CC APLP1 (PubMed:12629046, PubMed:16314516, PubMed:16705177,
CC PubMed:17927953). Interacts with TENT4B; the interaction is required
CC for TENT4B-mediated translational control (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZB8, ECO:0000269|PubMed:12629046,
CC ECO:0000269|PubMed:16314516, ECO:0000269|PubMed:16705177,
CC ECO:0000269|PubMed:17927953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
CC Membrane {ECO:0000250}. Postsynaptic density {ECO:0000250}.
CC Note=Localizes in synaptosomes at dendritic synapses of neurons.
CC Strongly enriched in postsynaptic density (PSD) fractions. Transported
CC into dendrites in a microtubule-dependent fashion and colocalizes in
CC mRNA-containing particles with TACC3, dynein and kinesin. Membrane-
CC associated. Colocalizes at excitatory synapses with members of the
CC polyadenylation and translation complex factors (CPSF, APLP1, TACC3,
CC AURKA, SYP, etc.) including CPE-containing RNAs. In P-bodies and stress
CC granules (By similarity). Recruited to stress granules (SGs) upon
CC arsenite treatment (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus, cerebral cortex and
CC oocytes (at protein level). Expressed in brain, heart, kidney, lung and
CC ovary and testis. Weakly expressed in granular cells of dentate gyrus
CC and the pyramidal cells of CA3 and CA1 of the hippocampus.
CC {ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711,
CC ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:8962099,
CC ECO:0000269|PubMed:9856468}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic ovaries at 14.5, 16.5 and
CC 18.5 dpc (at protein level). {ECO:0000269|PubMed:12815066}.
CC -!- INDUCTION: Not induced by kainate.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA. The interdomain linker (411-429) acts as a
CC hinge to fix the relative orientation of the 2 RRMs. The ZZ domain
CC (509-566) coordinates 2 Zn ions and is probably implicated in mediating
CC interactions with other proteins in addition to increasing the affinity
CC of the RRMs for the CPEs. A continuous hydrophobic interface is formed
CC between the 2 RRM. {ECO:0000250|UniProtKB:Q9BZB8}.
CC -!- PTM: Phosphorylated on serine/threonine residues by AURKA within
CC positions 165 and 196 (By similarity). Phosphorylation and
CC dephosphorylation on Thr-171 regulates cytoplasmic polyadenylation and
CC translation of CPE-containing mRNAs. Phosphorylation on Thr-171 by
CC AURKA in embryonic ovaries at 16.5 dpc (mostly pachytene oocytes)
CC activates CPEB1. Not phosphorylated on Thr-171 in embryonic ovaries
CC between 18.5 dpc (diplotene oocytes) and metaphase I. Dephosphorylation
CC on Thr-171 by PP1 in embryonic ovaries at 18.5 dpc (mostly diplotene
CC oocytes) inactivates CPEB1. In maturing oocytes, re-phosphorylation on
CC Thr-171 by AURKA reactivates CPEB1. Phosphorylation on Thr-171 by
CC CAMK2A in depolarized hippocampal neurons activates CPEB1.
CC Dephosphorylation on Thr-171 (indirectly by PP1) in hippocampal neurons
CC inactivates CPEB1. Phosphorylation on Thr-171 may be promoted by APLP1.
CC Phosphorylation increases binding to RNA. {ECO:0000250,
CC ECO:0000269|PubMed:11526086, ECO:0000269|PubMed:11980711,
CC ECO:0000269|PubMed:12815066, ECO:0000269|PubMed:15175389,
CC ECO:0000269|PubMed:15944388, ECO:0000269|PubMed:16314516}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y08260; CAA69588.1; -; mRNA.
DR EMBL; AK077799; BAC37017.1; -; mRNA.
DR CCDS; CCDS40007.1; -.
DR RefSeq; NP_001239454.1; NM_001252525.1.
DR RefSeq; NP_001239455.1; NM_001252526.1.
DR RefSeq; NP_031781.1; NM_007755.5.
DR AlphaFoldDB; P70166; -.
DR BMRB; P70166; -.
DR SMR; P70166; -.
DR BioGRID; 198856; 7.
DR DIP; DIP-41380N; -.
DR IntAct; P70166; 1.
DR MINT; P70166; -.
DR STRING; 10090.ENSMUSP00000095936; -.
DR iPTMnet; P70166; -.
DR PhosphoSitePlus; P70166; -.
DR MaxQB; P70166; -.
DR PaxDb; P70166; -.
DR PRIDE; P70166; -.
DR ProteomicsDB; 283814; -.
DR Ensembl; ENSMUST00000098331; ENSMUSP00000095936; ENSMUSG00000025586.
DR GeneID; 12877; -.
DR KEGG; mmu:12877; -.
DR UCSC; uc009ibw.2; mouse.
DR CTD; 64506; -.
DR MGI; MGI:108442; Cpeb1.
DR VEuPathDB; HostDB:ENSMUSG00000025586; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000155524; -.
DR InParanoid; P70166; -.
DR OMA; NCYGPLS; -.
DR OrthoDB; 1075356at2759; -.
DR TreeFam; TF317658; -.
DR BioGRID-ORCS; 12877; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cpeb1; mouse.
DR PRO; PR:P70166; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70166; protein.
DR Bgee; ENSMUSG00000025586; Expressed in primary oocyte and 167 other tissues.
DR ExpressionAtlas; P70166; baseline and differential.
DR Genevisible; P70166; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0006417; P:regulation of translation; IDA:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
DR CDD; cd12723; RRM1_CPEB1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032292; CEBP1_N.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR034977; CPEB1_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR12566; PTHR12566; 1.
DR Pfam; PF16368; CEBP1_N; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Membrane; Metal-binding; mRNA processing;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; Synapse; Translation regulation; Zinc.
FT CHAIN 1..561
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000269252"
FT DOMAIN 310..407
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 429..510
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 159..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..561
FT /note="Necessary for stress granule assembly and correct
FT localization in dcp1 bodies"
FT /evidence="ECO:0000250"
FT COMPBIAS 173..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT SITE 410
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT MOD_RES 171
FT /note="Phosphothreonine; by AURKA and CAMK2A"
FT /evidence="ECO:0000269|PubMed:11980711,
FT ECO:0000269|PubMed:12815066, ECO:0000269|PubMed:15175389,
FT ECO:0000269|PubMed:15944388"
FT MUTAGEN 171
FT /note="T->A: Inhibits CPE-containing cytoplasmic
FT polyadenylation and translation activation."
FT /evidence="ECO:0000269|PubMed:12815066,
FT ECO:0000269|PubMed:15175389"
SQ SEQUENCE 561 AA; 61917 MW; CB7958885AB13FF6 CRC64;
MAFSLEEAAG RIKDCWDNQE VPALSTCSNA NIFRRINAIL DDSLDFSKVC TTPINRGIHD
QLPDFQDSEE TVTSRMLFPT SAQESPRGLP DANGLCLGLQ SLSLTGWDRP WSTQDSDSSA
QSSTQSVLSM LQNPLGNVLG KAPLSFLSLD PLGSDLDKFP APSVRGSRLD TRPILDSRSS
SPSDSDTSGF SSGSDHLSDL ISSLRISPPL PFLSMTGNGP RDPLKMGVGS RMDQEQAALA
AVAPSPTSAP KRWPGASVWP SWDLLGAPKD PFSIEREARL HRQAAAVNEA TCTWSGQLPP
RNYKNPIYSC KVFLGGVPWD ITEAGLVNTF RVFGSLSVEW PGKDGKHPRC PPKGNMPKGY
VYLVFELEKS VRALLQACSH DPLSPDGLSE YYFKMSSRRM RCKEVQVIPW VLADSNFVWS
PSQRLDPSRT VFVGALHGML NAEALAAILN DLFGGVVYAG IDTDKHKYPI GSGRVTFNNQ
RSYLKAVTAA FVEIKTTKFT KKVQIDPYLE DSLCLICSSQ PGPFFCRDQV CFKYFCRSCW
HWRHSMEGLR HHSPLMRNQK N
