位置:首页 > 蛋白库 > ERI3_HUMAN
ERI3_HUMAN
ID   ERI3_HUMAN              Reviewed;         337 AA.
AC   O43414; B1AK98; Q5T2T7; Q5T2T9; Q5TG35; Q9BQA0; Q9UEB4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=ERI1 exoribonuclease 3;
DE            EC=3.1.-.-;
DE   AltName: Full=Prion interactor 1;
DE   AltName: Full=Prion protein-interacting protein;
GN   Name=ERI3; Synonyms=PINT1, PRNPIP, PRNPIP1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Yu W., Sarginson J., Gibbs R.A.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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 GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORM 2).
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Lung;
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   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., Buerckstuemmer T.,
RA   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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with PRNP. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O43414-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43414-2; Sequence=VSP_031103;
CC       Name=3;
CC         IsoId=O43414-3; Sequence=VSP_031104;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC19158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF007157; AAC19158.1; ALT_INIT; mRNA.
DR   EMBL; AK290567; BAF83256.1; -; mRNA.
DR   EMBL; AL035417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL390776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004254; AAC04618.1; -; Genomic_DNA.
DR   EMBL; BC001072; AAH01072.1; -; mRNA.
DR   EMBL; BC004456; AAH04456.1; -; mRNA.
DR   CCDS; CCDS30696.1; -. [O43414-1]
DR   RefSeq; NP_001288627.1; NM_001301698.1.
DR   RefSeq; NP_001288628.1; NM_001301699.1.
DR   RefSeq; NP_001288629.1; NM_001301700.1.
DR   RefSeq; NP_001288630.1; NM_001301701.1.
DR   RefSeq; NP_076971.1; NM_024066.2. [O43414-1]
DR   PDB; 2XRI; X-ray; 2.15 A; A=137-337.
DR   PDB; 7K05; X-ray; 1.85 A; A/B=137-337.
DR   PDB; 7K06; X-ray; 1.95 A; A/B=137-337.
DR   PDB; 7K07; X-ray; 2.15 A; A/B=137-337.
DR   PDB; 7LPY; X-ray; 1.85 A; A/B=137-337.
DR   PDB; 7LPZ; X-ray; 1.55 A; A/B=137-337.
DR   PDB; 7LQ0; X-ray; 1.60 A; A/B=137-337.
DR   PDBsum; 2XRI; -.
DR   PDBsum; 7K05; -.
DR   PDBsum; 7K06; -.
DR   PDBsum; 7K07; -.
DR   PDBsum; 7LPY; -.
DR   PDBsum; 7LPZ; -.
DR   PDBsum; 7LQ0; -.
DR   AlphaFoldDB; O43414; -.
DR   SMR; O43414; -.
DR   BioGRID; 122498; 24.
DR   IntAct; O43414; 17.
DR   MINT; O43414; -.
DR   STRING; 9606.ENSP00000361331; -.
DR   iPTMnet; O43414; -.
DR   PhosphoSitePlus; O43414; -.
DR   SwissPalm; O43414; -.
DR   BioMuta; ERI3; -.
DR   EPD; O43414; -.
DR   jPOST; O43414; -.
DR   MassIVE; O43414; -.
DR   MaxQB; O43414; -.
DR   PaxDb; O43414; -.
DR   PeptideAtlas; O43414; -.
DR   PRIDE; O43414; -.
DR   ProteomicsDB; 48930; -. [O43414-1]
DR   ProteomicsDB; 48931; -. [O43414-2]
DR   ProteomicsDB; 48932; -. [O43414-3]
DR   Antibodypedia; 18452; 81 antibodies from 18 providers.
DR   DNASU; 79033; -.
DR   Ensembl; ENST00000372257.7; ENSP00000361331.2; ENSG00000117419.16. [O43414-1]
DR   Ensembl; ENST00000372259.9; ENSP00000361333.5; ENSG00000117419.16. [O43414-2]
DR   GeneID; 79033; -.
DR   KEGG; hsa:79033; -.
DR   MANE-Select; ENST00000372257.7; ENSP00000361331.2; NM_024066.3; NP_076971.1.
DR   UCSC; uc001clt.4; human. [O43414-1]
DR   CTD; 79033; -.
DR   GeneCards; ERI3; -.
DR   HGNC; HGNC:17276; ERI3.
DR   HPA; ENSG00000117419; Low tissue specificity.
DR   MIM; 609917; gene.
DR   neXtProt; NX_O43414; -.
DR   OpenTargets; ENSG00000117419; -.
DR   PharmGKB; PA164719272; -.
DR   VEuPathDB; HostDB:ENSG00000117419; -.
DR   eggNOG; KOG0542; Eukaryota.
DR   GeneTree; ENSGT00530000063205; -.
DR   HOGENOM; CLU_037266_0_0_1; -.
DR   InParanoid; O43414; -.
DR   OMA; YTWASYG; -.
DR   PhylomeDB; O43414; -.
DR   TreeFam; TF313449; -.
DR   PathwayCommons; O43414; -.
DR   SignaLink; O43414; -.
DR   BioGRID-ORCS; 79033; 8 hits in 1075 CRISPR screens.
DR   ChiTaRS; ERI3; human.
DR   EvolutionaryTrace; O43414; -.
DR   GenomeRNAi; 79033; -.
DR   Pharos; O43414; Tbio.
DR   PRO; PR:O43414; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O43414; protein.
DR   Bgee; ENSG00000117419; Expressed in left testis and 147 other tissues.
DR   ExpressionAtlas; O43414; baseline and differential.
DR   Genevisible; O43414; HS.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Exonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..337
FT                   /note="ERI1 exoribonuclease 3"
FT                   /id="PRO_0000317626"
FT   DOMAIN          146..320
FT                   /note="Exonuclease"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..209
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031104"
FT   VAR_SEQ         1..163
FT                   /note="MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWGQHPGHWGFPAL
FT                   TEPSASPAAGLGIFEVRRVLDASGCSMLAPLQTGAARFSSYLLSRARKVLGSHLFSPCG
FT                   VPEFCSISTRKLAAHGFGASMAAMVSFPPQRYHYFLVLDFEATCDKPQIHPQ -> MFV
FT                   MLQVPWLQSCANLVQIGAPLPLLGCLGQYFEVLGSMEVLAGQYGM (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031103"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   STRAND          180..187
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           198..204
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           217..231
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   TURN            232..234
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   STRAND          240..247
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           253..261
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           267..270
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           275..283
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           290..297
FT                   /evidence="ECO:0007829|PDB:7K05"
FT   HELIX           309..325
FT                   /evidence="ECO:0007829|PDB:7K05"
SQ   SEQUENCE   337 AA;  37238 MW;  28E8A691659B4D67 CRC64;
     MATASPAADG GRGRPWEGGL VSWPPAPPLT LPWTWMGPSW GQHPGHWGFP ALTEPSASPA
     AGLGIFEVRR VLDASGCSML APLQTGAARF SSYLLSRARK VLGSHLFSPC GVPEFCSIST
     RKLAAHGFGA SMAAMVSFPP QRYHYFLVLD FEATCDKPQI HPQEIIEFPI LKLNGRTMEI
     ESTFHMYVQP VVHPQLTPFC TELTGIIQAM VDGQPSLQQV LERVDEWMAK EGLLDPNVKS
     IFVTCGDWDL KVMLPGQCQY LGLPVADYFK QWINLKKAYS FAMGCWPKNG LLDMNKGLSL
     QHIGRPHSGI DDCKNIANIM KTLAYRGFIF KQTSKPF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024