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Database: UniProt
Entry: P61221
LinkDB: P61221
Original site: P61221 
ID   ABCE1_HUMAN             Reviewed;         599 AA.
AC   P61221; O88793; Q13181; Q13864; Q6NR76; Q96AL0; Q96B10; Q99K66;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   13-FEB-2019, entry version 159.
DE   RecName: Full=ATP-binding cassette sub-family E member 1;
DE   AltName: Full=2'-5'-oligoadenylate-binding protein;
DE   AltName: Full=HuHP68;
DE   AltName: Full=RNase L inhibitor;
DE   AltName: Full=Ribonuclease 4 inhibitor;
DE            Short=RNS4I;
GN   Name=ABCE1; Synonyms=RLI, RNASEL1, RNASELI, RNS4I;
GN   ORFNames=OK/SW-cl.40;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH
RP   RNASEL.
RX   PubMed=7539425; DOI=10.1074/jbc.270.22.13308;
RA   Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.;
RT   "Cloning and characterization of a RNase L inhibitor. A new component
RT   of the interferon-regulated 2-5A pathway.";
RL   J. Biol. Chem. 270:13308-13317(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8641422; DOI=10.1016/0014-5793(96)00099-3;
RA   Aubry F., Mattei M.-G., Barque J.-P., Galibert F.;
RT   "Chromosomal localization and expression pattern of the RNase L
RT   inhibitor gene.";
RL   FEBS Lett. 381:135-139(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-
RT   reactive CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Duodenum, and Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INDUCTION BY EMCV, AND FUNCTION.
RX   PubMed=9660177; DOI=10.1046/j.1432-1327.1998.2540248.x;
RA   Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C.;
RT   "RNase L inhibitor (RLI) antisense constructions block partially the
RT   down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-
RT   virus-(EMCV)-infected cells.";
RL   Eur. J. Biochem. 254:248-255(1998).
RN   [8]
RP   INDUCTION BY HIV-1, AND FUNCTION.
RX   PubMed=9847332;
RA   Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B.,
RA   Bisbal C.;
RT   "RNase L inhibitor is induced during human immunodeficiency virus type
RT   1 infection and down regulates the 2-5A/RNase L pathway in human T
RT   cells.";
RL   J. Virol. 73:290-296(1999).
RN   [9]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=11585831; DOI=10.1074/jbc.M107482200;
RA   Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B.,
RA   Salehzada T.;
RT   "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates
RT   mitochondrial mRNAs stability in interferon alpha-treated H9 cells.";
RL   J. Biol. Chem. 276:48473-48482(2001).
RN   [10]
RP   INTERACTION WITH HIV-1 VIF AND GAG PROTEINS (MICROBIAL INFECTION).
RX   PubMed=11780123; DOI=10.1038/415088a;
RA   Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L.,
RA   Riba S.C., Lingappa J.R.;
RT   "Identification of a host protein essential for assembly of immature
RT   HIV-1 capsids.";
RL   Nature 415:88-92(2002).
RN   [11]
RP   INTERACTION WITH HIV-2 PROTEIN GAG (MICROBIAL INFECTION).
RX   PubMed=14747530; DOI=10.1128/JVI.78.4.1645-1656.2004;
RA   Dooher J.E., Lingappa J.R.;
RT   "Conservation of a stepwise, energy-sensitive pathway involving HP68
RT   for assembly of primate lentivirus capsids in cells.";
RL   J. Virol. 78:1645-1656(2004).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND THR-550, AND
RP   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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   VARIANT CYS-489, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17488105; DOI=10.1021/pr0700908;
RA   Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA   Hendrickson R.C., Stephenson J.L. Jr.;
RT   "Detection and validation of non-synonymous coding SNPs from
RT   orthogonal analysis of shotgun proteomics data.";
RL   J. Proteome Res. 6:2331-2340(2007).
CC   -!- FUNCTION: Antagonizes the binding of 2-5A (5'-phosphorylated
CC       2',5'-linked oligoadenylates) by RNase L through direct
CC       interaction with RNase L and therefore inhibits its
CC       endoribonuclease activity. May play a central role in the
CC       regulation of mRNA turnover. Antagonizes the anti-viral effect of
CC       the interferon-regulated 2-5A/RNase L pathway. May act as a
CC       chaperone for post-translational events during HIV-1 capsid
CC       assembly. {ECO:0000269|PubMed:11585831,
CC       ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.
CC   -!- SUBUNIT: Probably heterodimerizes with RNASEL; this interaction
CC       inhibits the RNASEL.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 proteins Vif
CC       and Gag. {ECO:0000269|PubMed:11780123}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 protein Gag.
CC       {ECO:0000269|PubMed:14747530}.
CC   -!- INTERACTION:
CC       P03347-1:gag (xeno); NbExp=3; IntAct=EBI-2510446, EBI-10687478;
CC       Q9WH76:M (xeno); NbExp=3; IntAct=EBI-2510446, EBI-10823897;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}.
CC       Mitochondrion {ECO:0000269|PubMed:11585831}. Note=Localized to
CC       clusters of virus formation at the plasma membrane.
CC   -!- INDUCTION: Activated by encephalomyocarditis virus (EMCV) and HIV-
CC       1. {ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}.
CC   -!- MISCELLANEOUS: The ABC transporter domains seem not to be
CC       functional.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/abce1/";
CC   -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
CC       proteins;
CC       URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P61221";
DR   EMBL; X76388; CAA53972.1; -; mRNA.
DR   EMBL; X74987; CAA52920.1; -; mRNA.
DR   EMBL; AB062293; BAB93476.1; -; mRNA.
DR   EMBL; BT009779; AAP88781.1; -; mRNA.
DR   EMBL; DQ148409; AAZ38723.1; -; Genomic_DNA.
DR   EMBL; BC016283; AAH16283.1; -; mRNA.
DR   EMBL; BC016988; AAH16988.1; -; mRNA.
DR   CCDS; CCDS34071.1; -.
DR   PIR; A57017; A57017.
DR   PIR; S63672; S63672.
DR   RefSeq; NP_001035809.1; NM_001040876.1.
DR   RefSeq; NP_002931.2; NM_002940.2.
DR   UniGene; Hs.12013; -.
DR   ProteinModelPortal; P61221; -.
DR   SMR; P61221; -.
DR   BioGrid; 111986; 246.
DR   IntAct; P61221; 25.
DR   MINT; P61221; -.
DR   STRING; 9606.ENSP00000296577; -.
DR   CarbonylDB; P61221; -.
DR   iPTMnet; P61221; -.
DR   PhosphoSitePlus; P61221; -.
DR   SwissPalm; P61221; -.
DR   BioMuta; ABCE1; -.
DR   DMDM; 47117664; -.
DR   EPD; P61221; -.
DR   jPOST; P61221; -.
DR   MaxQB; P61221; -.
DR   PaxDb; P61221; -.
DR   PeptideAtlas; P61221; -.
DR   PRIDE; P61221; -.
DR   ProteomicsDB; 57276; -.
DR   DNASU; 6059; -.
DR   Ensembl; ENST00000296577; ENSP00000296577; ENSG00000164163.
DR   GeneID; 6059; -.
DR   KEGG; hsa:6059; -.
DR   UCSC; uc003ijy.4; human.
DR   CTD; 6059; -.
DR   DisGeNET; 6059; -.
DR   EuPathDB; HostDB:ENSG00000164163.10; -.
DR   GeneCards; ABCE1; -.
DR   HGNC; HGNC:69; ABCE1.
DR   HPA; CAB012476; -.
DR   HPA; HPA036846; -.
DR   MIM; 601213; gene.
DR   neXtProt; NX_P61221; -.
DR   OpenTargets; ENSG00000164163; -.
DR   PharmGKB; PA24404; -.
DR   eggNOG; KOG0063; Eukaryota.
DR   eggNOG; COG1245; LUCA.
DR   GeneTree; ENSGT00390000015089; -.
DR   HOVERGEN; HBG050439; -.
DR   InParanoid; P61221; -.
DR   KO; K06174; -.
DR   OMA; GQYFFLE; -.
DR   OrthoDB; 359213at2759; -.
DR   PhylomeDB; P61221; -.
DR   TreeFam; TF105206; -.
DR   Reactome; R-HSA-8983711; OAS antiviral response.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   ChiTaRS; ABCE1; human.
DR   GenomeRNAi; 6059; -.
DR   PRO; PR:P61221; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000164163; Expressed in 226 organ(s), highest expression level in female gonad.
DR   ExpressionAtlas; P61221; baseline and differential.
DR   Genevisible; P61221; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; TAS:Reactome.
DR   GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:GO_Central.
DR   GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013283; RLI1.
DR   InterPro; IPR034348; RLI_dom_1.
DR   InterPro; IPR007209; RNaseL-inhib_metal-bd_dom.
DR   PANTHER; PTHR19248; PTHR19248; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Host-virus interaction; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT   CHAIN         1    599       ATP-binding cassette sub-family E member
FT                                1.
FT                                /FTId=PRO_0000093316.
FT   DOMAIN        7     37       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       46     75       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       79    315       ABC transporter 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   DOMAIN      342    562       ABC transporter 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     110    117       ATP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     379    386       ATP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   MOD_RES     417    417       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     550    550       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VARIANT     489    489       S -> C (polymorphism; confirmed at
FT                                protein level; dbSNP:rs3816497).
FT                                {ECO:0000269|PubMed:17488105}.
FT                                /FTId=VAR_068914.
FT   CONFLICT    118    118       T -> A (in Ref. 1; CAA53972).
FT                                {ECO:0000305}.
FT   CONFLICT    174    179       DQIPKA -> ARFLRL (in Ref. 1; CAA53972).
FT                                {ECO:0000305}.
FT   CONFLICT    471    473       ALA -> RLR (in Ref. 1; CAA53972/
FT                                CAA52920). {ECO:0000305}.
SQ   SEQUENCE   599 AA;  67314 MW;  5D582B62E95BC7A6 CRC64;
     MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI
     CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL
     KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA
     KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF
     DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT
     MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF
     ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS
     TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA
     DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS
     KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD
//
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