CPEB2_HUMAN
ID CPEB2_HUMAN Reviewed; 589 AA.
AC Q7Z5Q1; E7EPM3; F5H160; Q3B8N6; Q3MI89; Q3MI90; Q3MI92; Q7Z5Q0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 2;
DE Short=CPE-BP2;
DE Short=CPE-binding protein 2;
DE Short=hCPEB-2;
GN Name=CPEB2;
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 [MRNA] (ISOFORMS 1 AND 4).
RA Huang C.Q., Wu S.L., Shan Y.X., Xiao P.J.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
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 [4]
RP FUNCTION.
RX PubMed=26398195; DOI=10.1371/journal.pone.0138794;
RA Giangarra V., Igea A., Castellazzi C.L., Bava F.A., Mendez R.;
RT "Global analysis of CPEBs reveals sequential and non-redundant functions in
RT mitotic cell cycle.";
RL PLoS ONE 10:E0138794-E0138794(2015).
CC -!- FUNCTION: May play a role in translational regulation of stored mRNAs
CC in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA
CC oligomers (By similarity). Required for cell cycle progression,
CC specifically for the transition from metaphase to anaphase
CC (PubMed:26398195). {ECO:0000250|UniProtKB:Q812E0,
CC ECO:0000269|PubMed:26398195}.
CC -!- SUBUNIT: Interacts with TENT2/GLD2. {ECO:0000250|UniProtKB:Q812E0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q812E0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q7Z5Q1-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5Q1-3; Sequence=VSP_022030, VSP_027372;
CC Name=3;
CC IsoId=Q7Z5Q1-4; Sequence=VSP_022032;
CC Name=4; Synonyms=CPEB2b;
CC IsoId=Q7Z5Q1-5; Sequence=VSP_022031;
CC Name=5;
CC IsoId=Q7Z5Q1-6; Sequence=VSP_022031, VSP_027372;
CC Name=6;
CC IsoId=Q7Z5Q1-7; Sequence=VSP_022030, VSP_022032, VSP_027372;
CC Name=7;
CC IsoId=Q7Z5Q1-8; Sequence=VSP_055670, VSP_022032, VSP_027372;
CC Name=8;
CC IsoId=Q7Z5Q1-9; Sequence=VSP_055670, VSP_027372;
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AY247744; AAP37585.1; -; mRNA.
DR EMBL; AY255519; AAP41553.1; -; mRNA.
DR EMBL; AC098829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103939; AAI03940.2; -; mRNA.
DR EMBL; BC103940; AAI03941.1; -; mRNA.
DR EMBL; BC103941; AAI03942.1; -; mRNA.
DR EMBL; BC103942; AAI03943.1; -; mRNA.
DR EMBL; BC105925; AAI05926.1; -; mRNA.
DR CCDS; CCDS56325.1; -. [Q7Z5Q1-9]
DR CCDS; CCDS56326.1; -. [Q7Z5Q1-8]
DR RefSeq; NP_001170852.1; NM_001177381.1. [Q7Z5Q1-8]
DR RefSeq; NP_001170853.1; NM_001177382.1. [Q7Z5Q1-9]
DR RefSeq; NP_001170854.1; NM_001177383.1.
DR RefSeq; NP_001170855.1; NM_001177384.1.
DR RefSeq; NP_872291.2; NM_182485.2.
DR RefSeq; NP_872587.2; NM_182646.2.
DR AlphaFoldDB; Q7Z5Q1; -.
DR SMR; Q7Z5Q1; -.
DR BioGRID; 126338; 42.
DR IntAct; Q7Z5Q1; 1.
DR STRING; 9606.ENSP00000443985; -.
DR iPTMnet; Q7Z5Q1; -.
DR PhosphoSitePlus; Q7Z5Q1; -.
DR BioMuta; CPEB2; -.
DR DMDM; 158937340; -.
DR EPD; Q7Z5Q1; -.
DR jPOST; Q7Z5Q1; -.
DR MassIVE; Q7Z5Q1; -.
DR MaxQB; Q7Z5Q1; -.
DR PaxDb; Q7Z5Q1; -.
DR PeptideAtlas; Q7Z5Q1; -.
DR PRIDE; Q7Z5Q1; -.
DR ProteomicsDB; 17391; -.
DR ProteomicsDB; 25551; -.
DR ProteomicsDB; 69342; -. [Q7Z5Q1-2]
DR ProteomicsDB; 69343; -. [Q7Z5Q1-3]
DR ProteomicsDB; 69344; -. [Q7Z5Q1-4]
DR ProteomicsDB; 69345; -. [Q7Z5Q1-5]
DR ProteomicsDB; 69346; -. [Q7Z5Q1-6]
DR ProteomicsDB; 69347; -. [Q7Z5Q1-7]
DR Antibodypedia; 22933; 119 antibodies from 18 providers.
DR DNASU; 132864; -.
DR Ensembl; ENST00000442003.6; ENSP00000414270.2; ENSG00000137449.17. [Q7Z5Q1-8]
DR Ensembl; ENST00000538197.7; ENSP00000443985.1; ENSG00000137449.17. [Q7Z5Q1-9]
DR GeneID; 132864; -.
DR KEGG; hsa:132864; -.
DR MANE-Select; ENST00000538197.7; ENSP00000443985.1; NM_001177382.2; NP_001170853.1. [Q7Z5Q1-9]
DR UCSC; uc003gnk.2; human. [Q7Z5Q1-2]
DR CTD; 132864; -.
DR DisGeNET; 132864; -.
DR GeneCards; CPEB2; -.
DR HGNC; HGNC:21745; CPEB2.
DR HPA; ENSG00000137449; Tissue enhanced (brain).
DR MIM; 610605; gene.
DR neXtProt; NX_Q7Z5Q1; -.
DR OpenTargets; ENSG00000137449; -.
DR PharmGKB; PA134864048; -.
DR VEuPathDB; HostDB:ENSG00000137449; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000160357; -.
DR HOGENOM; CLU_014948_2_0_1; -.
DR InParanoid; Q7Z5Q1; -.
DR OMA; NNCERSP; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q7Z5Q1; -.
DR TreeFam; TF317658; -.
DR PathwayCommons; Q7Z5Q1; -.
DR BioGRID-ORCS; 132864; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; CPEB2; human.
DR GenomeRNAi; 132864; -.
DR Pharos; Q7Z5Q1; Tbio.
DR PRO; PR:Q7Z5Q1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q7Z5Q1; protein.
DR Bgee; ENSG00000137449; Expressed in sperm and 186 other tissues.
DR ExpressionAtlas; Q7Z5Q1; baseline and differential.
DR Genevisible; Q7Z5Q1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:UniProtKB.
DR GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
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; 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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..589
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 2"
FT /id="PRO_0000269259"
FT DOMAIN 332..423
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 440..522
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812E0"
FT VAR_SEQ 1
FT /note="M -> MRDFGFGVLQTAPLRSSSPGPLFCGEAYGPYAVGSVNPLPSATPFGP
FT LSPPPLPVTGFLEAASPFSVPLGGGAGSPAAAASSSSPFLAHQQTMQDELLLGLTQQPA
FT RPLSGAAATEKLPDHHPGGGTIAGVTHLLPSQDFKPSLHHPSSSSASSCCCCRTSSPQD
FT FSKRQQQQLSSQKRKEFSPPHLPHPPDSKPPPPPPPLHCPGRFSPPPPPAGPLLQPAQL
FT AQRQQQQPPQQFSLLHQQHLSPQDFAPRQRPADLPPLPQLPPSPPAAPRRRHGGAGSPR
FT KTPAAGEGSAAESPNAGLASSTPVNPAPGSMESPNHPLLNSPSNLLPGGALGAGAFSSL
FT QSPDLPHPGGGGGGGGGGPPGGGGGGGSASPPPLPGFGTPWSVQTASPPPQPQQPPPTQ
FT PQQQPPPPQQPPQPQPQPPGSSATTPGGGSGGSLSAM (in isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_055670"
FT VAR_SEQ 43..64
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022030"
FT VAR_SEQ 212..241
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_022031"
FT VAR_SEQ 214..241
FT /note="SSLQLPAWGSDSLQDSWCTAAGTSRIDQ -> M (in isoform 3,
FT isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022032"
FT VAR_SEQ 288
FT /note="N -> NARSYGRRR (in isoform 2, isoform 5, isoform 6,
FT isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027372"
FT CONFLICT 50
FT /note="G -> GG (in Ref. 2; AAI03942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 64944 MW; E0A16772D2E3091A CRC64;
MPPPSPDSEN GFYPGLPSSM NPAFFPSFSP VSPHGCTGLS VPTSGGGGGG FGGPFSATAV
PPPPPPAMNI PQQQPPPPAA PQQPQSRRSP VSPQLQQQHQ AAAAAFLQQR NSYNHHQPLL
KQSPWSNHQS SGWGTGSMSW GAMHGRDHRR TGNMGIPGTM NQISPLKKPF SGNVIAPPKF
TRSTPSLTPK SWIEDNVFRT DNNSNTLLPL QVRSSLQLPA WGSDSLQDSW CTAAGTSRID
QDRSRMYDSL NMHSLENSLI DIMRAEHDPL KGRLSYPHPG TDNLLMLNGR SSLFPIDDGL
LDDGHSDQVG VLNSPTCYSA HQNGERIERF SRKVFVGGLP PDIDEDEITA SFRRFGPLVV
DWPHKAESKS YFPPKGYAFL LFQEESSVQA LIDACIEEDG KLYLCVSSPT IKDKPVQIRP
WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM DRLYGGVCYA GIDTDPELKY
PKGAGRVAFS NQQSYIAAIS ARFVQLQHGD IDKRVEVKPY VLDDQMCDEC QGARCGGKFA
PFFCANVTCL QYYCEFCWAN IHSRAGREFH KPLVKEGADR PRQIHFRWN
