PABP3_HUMAN
ID PABP3_HUMAN Reviewed; 631 AA.
AC Q9H361; Q8NHV0; Q9H086;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Polyadenylate-binding protein 3;
DE Short=PABP-3;
DE Short=Poly(A)-binding protein 3;
DE AltName: Full=Testis-specific poly(A)-binding protein;
GN Name=PABPC3; Synonyms=PABP3, PABPL3;
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], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11328870; DOI=10.1093/nar/29.9.1872;
RA Feral C., Guellaen G., Pawlak A.;
RT "Human testis expresses a specific poly(A)-binding protein.";
RL Nucleic Acids Res. 29:1872-1883(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 STRUCTURE BY NMR OF 286-376.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain 4 in polyadenylation binding
RT protein 3.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. May be involved in
CC cytoplasmic regulatory processes of mRNA metabolism. Binds poly(A) with
CC a slightly lower affinity as compared to PABPC1.
CC -!- INTERACTION:
CC Q9H361; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1055272, EBI-1055254;
CC Q9H361; Q8NEK8: TENT5D; NbExp=3; IntAct=EBI-1055272, EBI-744726;
CC Q9H361; O76024: WFS1; NbExp=3; IntAct=EBI-1055272, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11328870}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; AF132026; AAG38953.1; -; mRNA.
DR EMBL; AL136900; CAB66834.2; -; mRNA.
DR EMBL; BC027617; AAH27617.1; -; mRNA.
DR CCDS; CCDS9311.1; -.
DR RefSeq; NP_112241.2; NM_030979.2.
DR PDB; 2D9P; NMR; -; A=286-375.
DR PDB; 4IVE; X-ray; 2.30 A; A/B/C/D=535-631.
DR PDBsum; 2D9P; -.
DR PDBsum; 4IVE; -.
DR AlphaFoldDB; Q9H361; -.
DR SMR; Q9H361; -.
DR BioGRID; 111079; 64.
DR IntAct; Q9H361; 25.
DR MINT; Q9H361; -.
DR STRING; 9606.ENSP00000281589; -.
DR iPTMnet; Q9H361; -.
DR MetOSite; Q9H361; -.
DR PhosphoSitePlus; Q9H361; -.
DR SwissPalm; Q9H361; -.
DR BioMuta; PABPC3; -.
DR DMDM; 28201852; -.
DR EPD; Q9H361; -.
DR jPOST; Q9H361; -.
DR MassIVE; Q9H361; -.
DR MaxQB; Q9H361; -.
DR PaxDb; Q9H361; -.
DR PeptideAtlas; Q9H361; -.
DR PRIDE; Q9H361; -.
DR ProteomicsDB; 80679; -.
DR Antibodypedia; 22538; 106 antibodies from 26 providers.
DR DNASU; 5042; -.
DR Ensembl; ENST00000281589.5; ENSP00000281589.3; ENSG00000151846.9.
DR GeneID; 5042; -.
DR KEGG; hsa:5042; -.
DR MANE-Select; ENST00000281589.5; ENSP00000281589.3; NM_030979.3; NP_112241.2.
DR UCSC; uc001upy.4; human.
DR CTD; 5042; -.
DR DisGeNET; 5042; -.
DR GeneCards; PABPC3; -.
DR HGNC; HGNC:8556; PABPC3.
DR HPA; ENSG00000151846; Tissue enriched (testis).
DR MIM; 604680; gene.
DR neXtProt; NX_Q9H361; -.
DR OpenTargets; ENSG00000151846; -.
DR PharmGKB; PA32882; -.
DR VEuPathDB; HostDB:ENSG00000151846; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000153773; -.
DR HOGENOM; CLU_012062_22_2_1; -.
DR InParanoid; Q9H361; -.
DR OMA; SCNVVCD; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; Q9H361; -.
DR TreeFam; TF300458; -.
DR PathwayCommons; Q9H361; -.
DR SignaLink; Q9H361; -.
DR SIGNOR; Q9H361; -.
DR BioGRID-ORCS; 5042; 7 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; Q9H361; -.
DR GeneWiki; PABPC3; -.
DR GenomeRNAi; 5042; -.
DR Pharos; Q9H361; Tbio.
DR PRO; PR:Q9H361; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9H361; protein.
DR Bgee; ENSG00000151846; Expressed in parotid gland and 165 other tissues.
DR ExpressionAtlas; Q9H361; baseline and differential.
DR Genevisible; Q9H361; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0016071; P:mRNA metabolic process; NAS:UniProtKB.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..631
FT /note="Polyadenylate-binding protein 3"
FT /id="PRO_0000081702"
FT DOMAIN 11..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 99..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 191..268
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..370
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 537..614
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 361
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 364
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 426
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 430
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 449
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 501
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT MOD_RES 513
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13310"
FT CONFLICT 221..222
FT /note="KV -> EL (in Ref. 2; CAB66834)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> R (in Ref. 1; AAG38953)"
FT /evidence="ECO:0000305"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:4IVE"
FT HELIX 550..568
FT /evidence="ECO:0007829|PDB:4IVE"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:4IVE"
FT HELIX 573..580
FT /evidence="ECO:0007829|PDB:4IVE"
FT HELIX 585..592
FT /evidence="ECO:0007829|PDB:4IVE"
FT HELIX 595..609
FT /evidence="ECO:0007829|PDB:4IVE"
SQ SEQUENCE 631 AA; 70031 MW; 2F8C5BF6F508AAEF CRC64;
MNPSTPSYPT ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RICRDLITSG SSNYAYVNFQ
HTKDAEHALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFVKNLDKSI NNKALYDTVS
AFGNILSCNV VCDENGSKGY GFVHFETHEA AERAIKKMNG MLLNGRKVFV GQFKSRKERE
AELGARAKEF PNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRTF EQMKQDRITR YQVVNLYVKN
LDDGIDDERL RKAFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAYLTN EYMQRMASVR AVPNQRAPPS GYFMTAVPQT QNHAAYYPPS
QIARLRPSPR WTAQGARPHP FQNKPSAIRP GAPRVPFSTM RPASSQVPRV MSTQRVANTS
TQTVGPRPAA AAAAAATPAV RTVPRYKYAA GVRNPQQHRN AQPQVTMQQL AVHVQGQETL
TASRLASAPP QKQKQMLGER LFPLIQAMHP TLAGKITGML LEIDNSELLY MLESPESLRS
KVDEAVAVLQ AHQAKEATQK AVNSATGVPT V
