ID   EPAB2_HUMAN             Reviewed;         278 AA.
AC   A6NDY0; A1L3B3; A2VDI2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 121.
DE   RecName: Full=Embryonic polyadenylate-binding protein 2;
DE            Short=Embryonic poly(A)-binding protein 2;
DE            Short=ePABP-2;
DE            Short=ePABP2;
DE   AltName: Full=Embryonic poly(A)-binding protein type II;
DE   AltName: Full=Poly(A)-binding protein nuclear-like 1;
GN   Name=PABPN1L; Synonyms=EPABP2, PABPNL1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary;
RX   PubMed=18483763; DOI=10.1007/s10815-008-9220-7;
RA   Sakugawa N., Miyamoto T., Sato H., Ishikawa M., Horikawa M., Hayashi H.,
RA   Ishikawa M., Sengoku K.;
RT   "Isolation of the human ePAB and ePABP2 cDNAs and analysis of the
RT   expression patterns.";
RL   J. Assist. Reprod. Genet. 25:215-221(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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).
CC   -!- FUNCTION: Binds the poly(A) tail of mRNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A6NDY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6NDY0-2; Sequence=VSP_035213, VSP_035214;
CC       Name=4;
CC         IsoId=A6NDY0-4; Sequence=VSP_040501;
CC       Name=3;
CC         IsoId=A6NDY0-3; Sequence=VSP_035211, VSP_035212;
CC   -!- TISSUE SPECIFICITY: Expressed in various adult tissues.
CC       {ECO:0000269|PubMed:18483763}.
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DR   EMBL; AC092384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC130001; AAI30002.1; -; mRNA.
DR   EMBL; BC130002; AAI30003.1; -; mRNA.
DR   CCDS; CCDS45547.2; -. [A6NDY0-1]
DR   CCDS; CCDS73925.1; -. [A6NDY0-2]
DR   RefSeq; NP_001073956.2; NM_001080487.2. [A6NDY0-1]
DR   RefSeq; NP_001281257.1; NM_001294328.1. [A6NDY0-2]
DR   RefSeq; XP_016878719.1; XM_017023230.1.
DR   AlphaFoldDB; A6NDY0; -.
DR   SMR; A6NDY0; -.
DR   BioGRID; 133674; 30.
DR   STRING; 9606.ENSP00000408598; -.
DR   iPTMnet; A6NDY0; -.
DR   PhosphoSitePlus; A6NDY0; -.
DR   BioMuta; PABPN1L; -.
DR   jPOST; A6NDY0; -.
DR   MassIVE; A6NDY0; -.
DR   MaxQB; A6NDY0; -.
DR   PaxDb; 9606-ENSP00000408598; -.
DR   PeptideAtlas; A6NDY0; -.
DR   TopDownProteomics; A6NDY0-3; -. [A6NDY0-3]
DR   Antibodypedia; 50156; 64 antibodies from 13 providers.
DR   DNASU; 390748; -.
DR   Ensembl; ENST00000411789.6; ENSP00000405259.2; ENSG00000205022.9. [A6NDY0-2]
DR   Ensembl; ENST00000419291.7; ENSP00000408598.2; ENSG00000205022.9. [A6NDY0-1]
DR   GeneID; 390748; -.
DR   KEGG; hsa:390748; -.
DR   MANE-Select; ENST00000419291.7; ENSP00000408598.2; NM_001080487.4; NP_001073956.2.
DR   UCSC; uc002fmi.4; human. [A6NDY0-1]
DR   AGR; HGNC:37237; -.
DR   CTD; 390748; -.
DR   DisGeNET; 390748; -.
DR   GeneCards; PABPN1L; -.
DR   HGNC; HGNC:37237; PABPN1L.
DR   HPA; ENSG00000205022; Tissue enhanced (adrenal gland, brain).
DR   neXtProt; NX_A6NDY0; -.
DR   OpenTargets; ENSG00000205022; -.
DR   VEuPathDB; HostDB:ENSG00000205022; -.
DR   eggNOG; KOG4209; Eukaryota.
DR   GeneTree; ENSGT00940000161325; -.
DR   HOGENOM; CLU_012062_23_2_1; -.
DR   InParanoid; A6NDY0; -.
DR   OMA; QAEGPPW; -.
DR   OrthoDB; 155884at2759; -.
DR   PhylomeDB; A6NDY0; -.
DR   TreeFam; TF105907; -.
DR   PathwayCommons; A6NDY0; -.
DR   Reactome; R-HSA-9820841; M-decay: degradation of maternal mRNAs by maternally stored factors.
DR   BioGRID-ORCS; 390748; 76 hits in 1134 CRISPR screens.
DR   GenomeRNAi; 390748; -.
DR   Pharos; A6NDY0; Tbio.
DR   PRO; PR:A6NDY0; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; A6NDY0; Protein.
DR   Bgee; ENSG00000205022; Expressed in right hemisphere of cerebellum and 72 other cell types or tissues.
DR   ExpressionAtlas; A6NDY0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR   GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IBA:GO_Central.
DR   CDD; cd12551; RRM_II_PABPN1L; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR23236:SF27; EMBRYONIC POLYADENYLATE-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR23236; EUKARYOTIC TRANSLATION INITIATION FACTOR 4B/4H; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Reference proteome; RNA-binding.
FT   CHAIN           1..278
FT                   /note="Embryonic polyadenylate-binding protein 2"
FT                   /id="PRO_0000349172"
FT   DOMAIN          147..224
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          21..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..63
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         154
FT                   /note="V -> LCLHRVCHQGLRAGRRGAGPEPLPGPGHQGAAEKNQLPWDQLHRPRG
FT                   PSRTPRLQGGTLPPQRPPGQAPAQTTRAEPGPWKILTMVFTVLKGRPDFERGAGAWIRS
FT                   KPLVLHPG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035211"
FT   VAR_SEQ         155..278
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035212"
FT   VAR_SEQ         190
FT                   /note="Y -> CCRKEPTSLGSAPQTAGAFEDTQAPGGHPSPTAASRAGPGSDHKGRT
FT                   GPVENSHHGFHRIKGKTRF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035213"
FT   VAR_SEQ         191..278
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035214"
FT   VAR_SEQ         267..278
FT                   /note="ARGKFSPWFSPY -> TPAALTPLWARPLPWVVVSHVIK (in isoform
FT                   4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040501"
SQ   SEQUENCE   278 AA;  30386 MW;  4662DAB7022CACD5 CRC64;
     MWPFPSRSLF PPPTQAWLQT VSSDPEAQGW GAWNETKEIL GPEGGEGKEE KEEEEDAEED
     QDGDAGFLLS LLEQENLAEC PLPDQELEAI KMKVCAMEQA EGTPRPPGVQ QQAEEEEGTA
     AGQLLSPETV GCPLSGTPEE KVEADHRSVY VGNVDYGGSA EELEAHFSRC GEVHRVTILC
     DKFSGHPKGY AYIEFATKGS VQAAVELDQS LFRGRVIKVL PKRTNFPGIS STDRGGLRGH
     PGSRGAPFPH SGLQGRPRLR PQGQNRARGK FSPWFSPY
//