EPAB2_HUMAN
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 03-AUG-2022, entry version 114.
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. [A6NDY0-1]
DR AlphaFoldDB; A6NDY0; -.
DR SMR; A6NDY0; -.
DR BioGRID; 133674; 29.
DR STRING; 9606.ENSP00000408598; -.
DR iPTMnet; A6NDY0; -.
DR PhosphoSitePlus; A6NDY0; -.
DR BioMuta; PABPN1L; -.
DR jPOST; A6NDY0; -.
DR MassIVE; A6NDY0; -.
DR MaxQB; A6NDY0; -.
DR PaxDb; A6NDY0; -.
DR PRIDE; A6NDY0; -.
DR TopDownProteomics; A6NDY0-3; -. [A6NDY0-3]
DR Antibodypedia; 50156; 61 antibodies from 12 providers.
DR DNASU; 390748; -.
DR Ensembl; ENST00000411789.6; ENSP00000405259.2; ENSG00000205022.9. [A6NDY0-2]
DR Ensembl; ENST00000419291.6; 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 CTD; 390748; -.
DR DisGeNET; 390748; -.
DR GeneCards; PABPN1L; -.
DR HGNC; HGNC:37237; PABPN1L.
DR HPA; ENSG00000205022; Tissue enhanced (adrenal).
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; MWPFLSH; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; A6NDY0; -.
DR TreeFam; TF105907; -.
DR PathwayCommons; A6NDY0; -.
DR BioGRID-ORCS; 390748; 75 hits in 1060 CRISPR screens.
DR GenomeRNAi; 390748; -.
DR Pharos; A6NDY0; Tdark.
DR PRO; PR:A6NDY0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; A6NDY0; protein.
DR Bgee; ENSG00000205022; Expressed in right hemisphere of cerebellum and 71 other tissues.
DR ExpressionAtlas; A6NDY0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 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
