REXO1_HUMAN
ID REXO1_HUMAN Reviewed; 1221 AA.
AC Q8N1G1; Q9ULT2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=RNA exonuclease 1 homolog;
DE EC=3.1.-.-;
DE AltName: Full=Elongin-A-binding protein 1;
DE Short=EloA-BP1;
DE AltName: Full=Transcription elongation factor B polypeptide 3-binding protein 1;
GN Name=REXO1; Synonyms=ELOABP1, KIAA1138, TCEB3BP1;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH ELOA AND TCEA2, AND VARIANT PRO-759.
RX PubMed=12943681; DOI=10.1016/s0006-291x(03)01556-0;
RA Tamura K., Miyata K., Sugahara K., Onishi S., Shuin T., Aso T.;
RT "Identification of EloA-BP1, a novel Elongin A binding protein with an
RT exonuclease homology domain.";
RL Biochem. Biophys. Res. Commun. 309:189-195(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-759.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-759 AND GLY-886.
RC TISSUE=Duodenum;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-499; SER-610 AND
RP SER-914, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-191, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Seems to have no detectable effect on transcription
CC elongation in vitro. {ECO:0000269|PubMed:12943681}.
CC -!- SUBUNIT: Interacts with TCEA2 and ELOA. {ECO:0000269|PubMed:12943681}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12943681}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12943681}.
CC -!- SIMILARITY: Belongs to the REXO1/REXO3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86452.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB032964; BAA86452.1; ALT_INIT; mRNA.
DR EMBL; AC012615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032244; AAH32244.1; -; mRNA.
DR CCDS; CCDS32866.1; -.
DR RefSeq; NP_065746.3; NM_020695.3.
DR AlphaFoldDB; Q8N1G1; -.
DR SMR; Q8N1G1; -.
DR BioGRID; 121526; 13.
DR IntAct; Q8N1G1; 5.
DR STRING; 9606.ENSP00000170168; -.
DR iPTMnet; Q8N1G1; -.
DR PhosphoSitePlus; Q8N1G1; -.
DR BioMuta; REXO1; -.
DR DMDM; 296452990; -.
DR EPD; Q8N1G1; -.
DR jPOST; Q8N1G1; -.
DR MassIVE; Q8N1G1; -.
DR MaxQB; Q8N1G1; -.
DR PaxDb; Q8N1G1; -.
DR PeptideAtlas; Q8N1G1; -.
DR PRIDE; Q8N1G1; -.
DR ProteomicsDB; 71599; -.
DR Antibodypedia; 22810; 183 antibodies from 27 providers.
DR DNASU; 57455; -.
DR Ensembl; ENST00000170168.9; ENSP00000170168.3; ENSG00000079313.15.
DR GeneID; 57455; -.
DR KEGG; hsa:57455; -.
DR MANE-Select; ENST00000170168.9; ENSP00000170168.3; NM_020695.4; NP_065746.3.
DR UCSC; uc002lua.5; human.
DR CTD; 57455; -.
DR DisGeNET; 57455; -.
DR GeneCards; REXO1; -.
DR HGNC; HGNC:24616; REXO1.
DR HPA; ENSG00000079313; Low tissue specificity.
DR MIM; 609614; gene.
DR neXtProt; NX_Q8N1G1; -.
DR OpenTargets; ENSG00000079313; -.
DR PharmGKB; PA142671077; -.
DR VEuPathDB; HostDB:ENSG00000079313; -.
DR eggNOG; KOG2248; Eukaryota.
DR GeneTree; ENSGT00940000158590; -.
DR HOGENOM; CLU_006810_2_1_1; -.
DR InParanoid; Q8N1G1; -.
DR OMA; YKRPTPQ; -.
DR OrthoDB; 227856at2759; -.
DR PhylomeDB; Q8N1G1; -.
DR TreeFam; TF350172; -.
DR PathwayCommons; Q8N1G1; -.
DR SignaLink; Q8N1G1; -.
DR BioGRID-ORCS; 57455; 54 hits in 1082 CRISPR screens.
DR ChiTaRS; REXO1; human.
DR GenomeRNAi; 57455; -.
DR Pharos; Q8N1G1; Tdark.
DR PRO; PR:Q8N1G1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N1G1; protein.
DR Bgee; ENSG00000079313; Expressed in right testis and 99 other tissues.
DR ExpressionAtlas; Q8N1G1; baseline and differential.
DR Genevisible; Q8N1G1; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd06145; REX1_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR031736; EloA-BP1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034922; REX1-like_exo.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF15870; EloA-BP1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Exonuclease; Hydrolase; Methylation; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1221
FT /note="RNA exonuclease 1 homolog"
FT /id="PRO_0000239232"
FT DOMAIN 1060..1209
FT /note="Exonuclease"
FT REGION 37..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..577
FT /note="Interaction with ELOA"
FT /evidence="ECO:0000269|PubMed:12943681"
FT REGION 619..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..115
FT /evidence="ECO:0000255"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 191
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT28"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT28"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT28"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 408
FT /note="V -> A (in dbSNP:rs10415018)"
FT /id="VAR_057148"
FT VARIANT 759
FT /note="S -> P (in dbSNP:rs4807145)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:12943681, ECO:0000269|PubMed:15489334"
FT /id="VAR_060444"
FT VARIANT 804
FT /note="I -> V (in dbSNP:rs34831403)"
FT /id="VAR_057149"
FT VARIANT 886
FT /note="S -> G (in dbSNP:rs2396359)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026587"
FT CONFLICT 39
FT /note="S -> P (in Ref. 2; BAA86452 and 4; AAH32244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1221 AA; 131510 MW; 4165C5394664B021 CRC64;
MLRSTGFFRA IDCPYWSGAP GGPCRRPYCH FRHRGARGSG APGDGGEAPP AAGLGYDPYN
PELPKPPAQR ENGTLGLGEE PRPDVLELEL VNQAIEAVRS EVELEQRRYR ELLETTREHR
SAEAPALAPR GPNASPTVGP DEDAFPLAFD YSPGSHGLLS PDAGYQPTPL AAPAEPGSKY
SLASLDRGQG RGGGGGGALE YVPKAVSQPR RHSRPVPSGK YVVDNSRPPT DLEYDPLSNY
SARHLSRASS RDERAAKRPR GSRGSEPYTP APKKLCDPFG SCDARFSDSE DEAATVPGNE
PTTASTPKAR ADPEIKATGQ PPSKEGLEAE GGGLRETKET AVQCDVGDLQ PPPAKPASPA
QVQSSQDGGC PKEGKPKKKK TGAPPAPSCK DGAQGKDKTK DKGRGRPVEK PRADKKGPQA
SSPRRKAERP EGTKKKPSSA TPVATSGKGR PDRPARRPSP TSGDSRPAAG RGPPRPLQLP
DRKSTKAPSG KLVERKARSL DEGASQDAPK LKKRALSHAD LFGDESEDEA AGPGVPSVWP
SALPSLSSDS DSDSDSSLGF PEAQGPPKRL KASPPPSPAP SSSSSSSSST SSAGADVDYS
ALEKEVDFDS DPMEECLRIF NESTSVKTED RGRLARQPPK EEKSEEKGLS GLTTLFPGQK
RRISHLSKQG QEVEPPRRGP AVPPARPPTA QEVCYLRAQQ AQRASASLLQ APARLAEKSP
SVHISAPGEK RRIAHIPNPR LAAAPTGAKR TLAASGSQSS NGPEPGGQQL KTRTLSGMAS
KTTTTIIPKR IAHSPSLQSL KKPIIPKEFG GKVPTVIRQR YLNLFIEECL KFCTSNQEAI
EKALNEEKVA YDRSPSKNIY LNVAVNTLKK LRGLAPSAVP GLSKTSGRRV VSHEVVLGGR
LAAKTSFSLS RPSSPRVEDL KGAALYSRLR EYLLTQDQLK ENGYPFPHPE RPGGAIIFTA
EEKRPKDSSC RTCCRCGTEY LVSSSGRCIR DEECYYHWGR LRRNRVAGGW ETQYMCCSAA
AGSVGCQVAK QHVQDGRKER LEGFVKTFEK ELSGDTHPGI YALDCEMSYT TYGLELTRVT
VVDTDVHVVY DTFVKPDNEI VDYNTRFSGV TEADLADTSV TLRDVQAVLL SMFSADTILI
GHSLESDLLA LKVIHSTVVD TSVLFPHRLG LPYKRSLRNL MADYLRQIIQ DNVDGHSSSE
DAGACMHLVI WKVREDAKTK R
