MEX3B_HUMAN
ID MEX3B_HUMAN Reviewed; 569 AA.
AC Q6ZN04; Q4G0W1; Q8IVG2; Q9H0J0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=RNA-binding protein MEX3B;
DE AltName: Full=RING finger and KH domain-containing protein 3;
DE AltName: Full=RING finger protein 195;
GN Name=MEX3B; Synonyms=KIAA2009, RKHD3, RNF195;
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), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND MUTAGENESIS OF GLY-177.
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-569.
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 [6]
RP PHOSPHORYLATION AT SER-462, AND SUBCELLULAR LOCATION.
RX PubMed=18779327; DOI=10.1074/jbc.m802927200;
RA Courchet J., Buchet-Poyau K., Potemski A., Bres A., Jariel-Encontre I.,
RA Billaud M.;
RT "Interaction with 14-3-3 adaptors regulates the sorting of hMex-3B RNA-
RT binding protein to distinct classes of RNA granules.";
RL J. Biol. Chem. 283:32131-32142(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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).
CC -!- FUNCTION: RNA-binding protein. May be involved in post-transcriptional
CC regulatory mechanisms.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18779327}. Cytoplasm
CC {ECO:0000269|PubMed:18779327}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:18779327}. Cytoplasmic granule
CC {ECO:0000269|PubMed:18779327}. Note=Predominantly expressed in the
CC cytoplasm and shuttles between the cytoplasm and the nucleus through
CC the CRM1 export pathway. Localization to P-bodies is dependent on 14-3-
CC 3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN04-3; Sequence=VSP_041891, VSP_041892;
CC -!- TISSUE SPECIFICITY: Highest levels found in fetal brain and testis.
CC Detected in the adult intestinal epithelium, specifically in goblet
CC cell at protein level. {ECO:0000269|PubMed:17267406}.
CC -!- DOMAIN: Binds RNA through its KH domains.
CC -!- PTM: Phosphorylation at Ser-462 creates a docking site for 14-3-3,
CC which stabilizes the protein and modulates its ability to bind RNA.
CC {ECO:0000269|PubMed:17267406, ECO:0000269|PubMed:18779327}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC23105.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY950678; AAY34146.1; -; mRNA.
DR EMBL; AK131424; BAD18571.1; -; mRNA.
DR EMBL; AB095929; BAC23105.1; ALT_SEQ; mRNA.
DR EMBL; BC036211; AAH36211.1; -; mRNA.
DR EMBL; BC111545; AAI11546.1; -; mRNA.
DR EMBL; AL136778; CAB66712.2; -; mRNA.
DR CCDS; CCDS10319.1; -. [Q6ZN04-1]
DR RefSeq; NP_115622.2; NM_032246.4. [Q6ZN04-1]
DR AlphaFoldDB; Q6ZN04; -.
DR SMR; Q6ZN04; -.
DR BioGRID; 123945; 216.
DR IntAct; Q6ZN04; 9.
DR MINT; Q6ZN04; -.
DR STRING; 9606.ENSP00000329918; -.
DR iPTMnet; Q6ZN04; -.
DR PhosphoSitePlus; Q6ZN04; -.
DR BioMuta; MEX3B; -.
DR DMDM; 74762391; -.
DR EPD; Q6ZN04; -.
DR jPOST; Q6ZN04; -.
DR MassIVE; Q6ZN04; -.
DR MaxQB; Q6ZN04; -.
DR PaxDb; Q6ZN04; -.
DR PeptideAtlas; Q6ZN04; -.
DR PRIDE; Q6ZN04; -.
DR ProteomicsDB; 67950; -. [Q6ZN04-1]
DR ProteomicsDB; 67951; -. [Q6ZN04-3]
DR Antibodypedia; 28006; 109 antibodies from 25 providers.
DR DNASU; 84206; -.
DR Ensembl; ENST00000329713.5; ENSP00000329918.4; ENSG00000183496.6. [Q6ZN04-1]
DR Ensembl; ENST00000558133.1; ENSP00000456938.1; ENSG00000183496.6. [Q6ZN04-3]
DR GeneID; 84206; -.
DR KEGG; hsa:84206; -.
DR MANE-Select; ENST00000329713.5; ENSP00000329918.4; NM_032246.6; NP_115622.2.
DR UCSC; uc002bgq.3; human. [Q6ZN04-1]
DR CTD; 84206; -.
DR DisGeNET; 84206; -.
DR GeneCards; MEX3B; -.
DR HGNC; HGNC:25297; MEX3B.
DR HPA; ENSG00000183496; Group enriched (cervix, testis).
DR MIM; 611008; gene.
DR neXtProt; NX_Q6ZN04; -.
DR OpenTargets; ENSG00000183496; -.
DR PharmGKB; PA162395820; -.
DR VEuPathDB; HostDB:ENSG00000183496; -.
DR eggNOG; KOG2113; Eukaryota.
DR GeneTree; ENSGT00940000160013; -.
DR HOGENOM; CLU_025598_2_0_1; -.
DR InParanoid; Q6ZN04; -.
DR OMA; QFERGPA; -.
DR OrthoDB; 814376at2759; -.
DR PhylomeDB; Q6ZN04; -.
DR TreeFam; TF315107; -.
DR PathwayCommons; Q6ZN04; -.
DR SignaLink; Q6ZN04; -.
DR BioGRID-ORCS; 84206; 13 hits in 1083 CRISPR screens.
DR GeneWiki; MEX3B; -.
DR GenomeRNAi; 84206; -.
DR Pharos; Q6ZN04; Tbio.
DR PRO; PR:Q6ZN04; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6ZN04; protein.
DR Bgee; ENSG00000183496; Expressed in sperm and 101 other tissues.
DR Genevisible; Q6ZN04; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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 SMART; SM00184; RING; 1.
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 Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..569
FT /note="RNA-binding protein MEX3B"
FT /id="PRO_0000278784"
FT DOMAIN 66..127
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 160..221
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 518..558
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18779327"
FT VAR_SEQ 87..158
FT /note="CKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIR
FT ASRNKNTALNGAVPGPPNLP -> RSRRDGEVGGGGVGSQATASRGRRVQYRDPRRGVP
FT WGERKSRAMGRRPRQRKCRQAVSRSRAAALAGCTFFC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_041891"
FT VAR_SEQ 159..569
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_041892"
FT MUTAGEN 177
FT /note="G->D: Prevents RNA binding."
FT /evidence="ECO:0000269|PubMed:17267406"
FT CONFLICT 414
FT /note="G -> S (in Ref. 4; AAH36211)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="N -> S (in Ref. 4; AAH36211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 58832 MW; DA5D014C4D8E1BB8 CRC64;
MPSSLFADLE RNGSGGGGGG SSGGGETLDD QRALQLALDQ LSLLGLDSDE GASLYDSEPR
KKSVNMTECV PVPSSEHVAE IVGRQGCKIK ALRAKTNTYI KTPVRGEEPV FVVTGRKEDV
AMARREIISA AEHFSMIRAS RNKNTALNGA VPGPPNLPGQ TTIQVRVPYR VVGLVVGPKG
ATIKRIQQQT HTYIVTPSRD KEPVFEVTGM PENVDRAREE IEAHIALRTG GIIELTDEND
FHANGTDVGF DLHHGSGGSG PGSLWSKPTP SITPTPGRKP FSSYRNDSSS SLGSASTDSY
FGGGTSSSAA ATQRLADYSP PSPALSFAHN GNNNNNGNGY TYTAGGEASV PSPDGCPELQ
PTFDPAPAPP PGAPLIWAQF ERSPGGGPAA PVSSSCSSSA SSSASSSSVV FPGGGASAPS
NANLGLLVHR RLHPGTSCPR LSPPLHMAPG AGEHHLARRV RSDPGGGGLA YAAYANGLGA
QLPGLQPSDT SGSSSSSSSS SSSSSSSSGL RRKGSRDCSV CFESEVIAAL VPCGHNLFCM
ECANRICEKS EPECPVCHTA VTQAIRIFS
