MEX3D_HUMAN
ID MEX3D_HUMAN Reviewed; 651 AA.
AC Q86XN8; A0PJL8; A1L023; E9PAL6; Q71M49;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=RNA-binding protein MEX3D;
DE AltName: Full=RING finger and KH domain-containing protein 1;
DE AltName: Full=RING finger protein 193;
DE AltName: Full=TINO;
GN Name=MEX3D; Synonyms=KIAA2031, RKHD1, RNF193;
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.
RX PubMed=17267406; DOI=10.1093/nar/gkm016;
RA Buchet-Poyau K., Courchet J., Le Hir H., Seraphin B., Scoazec J.-Y.,
RA Duret L., Domon-Dell C., Freund J.-N., Billaud M.;
RT "Identification and characterization of human Mex-3 proteins, a novel
RT family of evolutionarily conserved RNA-binding proteins differentially
RT localized to processing bodies.";
RL Nucleic Acids Res. 35:1289-1300(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-651 (ISOFORM 1).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-651 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14769789; DOI=10.1074/jbc.m314071200;
RA Donnini M., Lapucci A., Papucci L., Witort E., Jacquier A., Brewer G.,
RA Nicolin A., Capaccioli S., Schiavone N.;
RT "Identification of TINO: a new evolutionarily conserved BCL-2 AU-rich
RT element RNA-binding protein.";
RL J. Biol. Chem. 279:20154-20166(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-651 (ISOFORM 2).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-510 AND SER-514, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP STRUCTURE BY NMR OF 272-343.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second KH domain in RING finger and KH domain-
RT containing protein 1.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: RNA binding protein, may be involved in post-transcriptional
CC regulatory mechanisms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly expressed in the cytoplasm and shuttles between the
CC cytoplasm and the nucleus through the CRM1 export pathway.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86XN8-1; Sequence=Displayed;
CC Name=2; Synonyms=TINO;
CC IsoId=Q86XN8-2; Sequence=VSP_024019;
CC Name=3;
CC IsoId=Q86XN8-3; Sequence=VSP_047662;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all the cell lines and
CC tissues tested. {ECO:0000269|PubMed:17267406}.
CC -!- DOMAIN: Binds RNA through its KH domains. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ04763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY950680; AAY34148.1; -; mRNA.
DR EMBL; AC005943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB107353; BAC67658.1; -; mRNA.
DR EMBL; AF458084; AAQ04763.1; ALT_INIT; mRNA.
DR EMBL; BC113384; AAI13385.1; -; mRNA.
DR EMBL; BC113741; AAI13742.2; -; mRNA.
DR CCDS; CCDS32865.2; -. [Q86XN8-1]
DR RefSeq; NP_001167589.1; NM_001174118.1. [Q86XN8-3]
DR RefSeq; NP_976049.3; NM_203304.3. [Q86XN8-1]
DR PDB; 2DGR; NMR; -; A=272-341.
DR PDBsum; 2DGR; -.
DR AlphaFoldDB; Q86XN8; -.
DR SMR; Q86XN8; -.
DR BioGRID; 134376; 41.
DR IntAct; Q86XN8; 11.
DR STRING; 9606.ENSP00000384398; -.
DR iPTMnet; Q86XN8; -.
DR PhosphoSitePlus; Q86XN8; -.
DR BioMuta; MEX3D; -.
DR DMDM; 134047829; -.
DR EPD; Q86XN8; -.
DR jPOST; Q86XN8; -.
DR MassIVE; Q86XN8; -.
DR MaxQB; Q86XN8; -.
DR PaxDb; Q86XN8; -.
DR PeptideAtlas; Q86XN8; -.
DR PRIDE; Q86XN8; -.
DR ProteomicsDB; 19040; -.
DR ProteomicsDB; 70305; -. [Q86XN8-1]
DR ProteomicsDB; 70306; -. [Q86XN8-2]
DR Antibodypedia; 22752; 42 antibodies from 20 providers.
DR DNASU; 399664; -.
DR Ensembl; ENST00000402693.5; ENSP00000384398.3; ENSG00000181588.17. [Q86XN8-1]
DR GeneID; 399664; -.
DR KEGG; hsa:399664; -.
DR MANE-Select; ENST00000402693.5; ENSP00000384398.3; NM_203304.4; NP_976049.3.
DR UCSC; uc060rdi.1; human. [Q86XN8-1]
DR CTD; 399664; -.
DR DisGeNET; 399664; -.
DR GeneCards; MEX3D; -.
DR HGNC; HGNC:16734; MEX3D.
DR HPA; ENSG00000181588; Tissue enriched (testis).
DR MIM; 611009; gene.
DR neXtProt; NX_Q86XN8; -.
DR OpenTargets; ENSG00000181588; -.
DR PharmGKB; PA162395829; -.
DR VEuPathDB; HostDB:ENSG00000181588; -.
DR eggNOG; KOG2113; Eukaryota.
DR GeneTree; ENSGT00940000162613; -.
DR HOGENOM; CLU_025598_2_1_1; -.
DR InParanoid; Q86XN8; -.
DR OMA; TTIWSPF; -.
DR OrthoDB; 814376at2759; -.
DR PhylomeDB; Q86XN8; -.
DR TreeFam; TF315107; -.
DR PathwayCommons; Q86XN8; -.
DR SignaLink; Q86XN8; -.
DR BioGRID-ORCS; 399664; 9 hits in 1113 CRISPR screens.
DR EvolutionaryTrace; Q86XN8; -.
DR GeneWiki; MEX3D; -.
DR GenomeRNAi; 399664; -.
DR Pharos; Q86XN8; Tdark.
DR PRO; PR:Q86XN8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86XN8; protein.
DR Bgee; ENSG00000181588; Expressed in right testis and 119 other tissues.
DR ExpressionAtlas; Q86XN8; baseline and differential.
DR Genevisible; Q86XN8; HS.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; NAS:BHF-UCL.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; NAS:BHF-UCL.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00013; KH_1; 2.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..651
FT /note="RNA-binding protein MEX3D"
FT /id="PRO_0000050123"
FT DOMAIN 179..240
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 273..334
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 600..640
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 648..651
FT /note="HIFS -> RVETPQPGGASALQRQY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14769789,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024019"
FT VAR_SEQ 648..651
FT /note="HIFS -> RVETETPQPGGASALQRQY (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047662"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:2DGR"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:2DGR"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:2DGR"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:2DGR"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2DGR"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2DGR"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:2DGR"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2DGR"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:2DGR"
SQ SEQUENCE 651 AA; 64883 MW; 5E056EE2D08BC4CD CRC64;
MPSSLGQPDG GGGGGGGGGG VGAAGEDPGP GPAPPPEGAQ EAAPAPRPPP EPDDAAAALR
LALDQLSALG LGGAGDTDEE GAAGDGAAAA GGADGGAAPE PVPPDGPEAG APPTLAPAVA
PGSLPLLDPN ASPPPPPPPR PSPPDVFAGF APHPAALGPP TLLADQMSVI GSRKKSVNMT
ECVPVPSSEH VAEIVGRQGC KIKALRAKTN TYIKTPVRGE EPVFIVTGRK EDVEMAKREI
LSAAEHFSII RATRSKAGGL PGAAQGPPNL PGQTTIQVRV PYRVVGLVVG PKGATIKRIQ
QRTHTYIVTP GRDKEPVFAV TGMPENVDRA REEIEAHITL RTGAFTDAGP DSDFHANGTD
VCLDLLGAAA SLWAKTPNQG RRPPTATAGL RGDTALGAPS APEAFYAGSR GGPSVPDPGP
ASPYSGSGNG GFAFGAEGPG APVGTAAPDD CDFGFDFDFL ALDLTVPAAA TIWAPFERAA
PLPAFSGCST VNGAPGPPAA GARRSSGAGT PRHSPTLPEP GGLRLELPLS RRGAPDPVGA
LSWRPPQGPV SFPGGAAFST ATSLPSSPAA AACAPLDSGA SENSRKPPSA SSAPALAREC
VVCAEGEVMA ALVPCGHNLF CMDCAVRICG KSEPECPACR TPATQAIHIF S
