Full text data of ERI3
ERI3
(PINT1, PRNPIP, PRNPIP1)
[Confidence: low (only semi-automatic identification from reviews)]
ERI1 exoribonuclease 3; 3.1.-.- (Prion interactor 1; Prion protein-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ERI1 exoribonuclease 3; 3.1.-.- (Prion interactor 1; Prion protein-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43414
ID ERI3_HUMAN Reviewed; 337 AA.
AC O43414; B1AK98; Q5T2T7; Q5T2T9; Q5TG35; Q9BQA0; Q9UEB4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 90.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP SPLICING (ISOFORM 2).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
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 [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC -!- SUBUNIT: Interacts with PRNP (By similarity).
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 -!- SIMILARITY: Contains 1 exonuclease domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19158.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF007157; AAC19158.1; ALT_INIT; mRNA.
DR EMBL; AK290567; BAF83256.1; -; mRNA.
DR EMBL; AL390776; CAI12491.1; -; Genomic_DNA.
DR EMBL; AL035417; CAI12491.1; JOINED; Genomic_DNA.
DR EMBL; AL390776; CAI12494.1; -; Genomic_DNA.
DR EMBL; AL035417; CAI12494.1; JOINED; Genomic_DNA.
DR EMBL; AL035417; CAI23194.1; -; Genomic_DNA.
DR EMBL; AL390776; CAI23194.1; JOINED; Genomic_DNA.
DR EMBL; AL035417; CAI23196.1; -; Genomic_DNA.
DR EMBL; AL390776; CAI23196.1; JOINED; Genomic_DNA.
DR EMBL; AC004254; AAC04618.1; -; Genomic_DNA.
DR EMBL; BC001072; AAH01072.1; -; mRNA.
DR EMBL; BC004456; AAH04456.1; -; mRNA.
DR RefSeq; NP_076971.1; NM_024066.1.
DR UniGene; Hs.731413; -.
DR PDB; 2XRI; X-ray; 2.15 A; A=137-337.
DR PDBsum; 2XRI; -.
DR ProteinModelPortal; O43414; -.
DR SMR; O43414; 136-336.
DR STRING; 9606.ENSP00000361331; -.
DR PhosphoSite; O43414; -.
DR PaxDb; O43414; -.
DR PRIDE; O43414; -.
DR DNASU; 79033; -.
DR Ensembl; ENST00000372257; ENSP00000361331; ENSG00000117419.
DR Ensembl; ENST00000372259; ENSP00000361333; ENSG00000117419.
DR GeneID; 79033; -.
DR KEGG; hsa:79033; -.
DR UCSC; uc001clt.3; human.
DR CTD; 79033; -.
DR GeneCards; GC01M044686; -.
DR HGNC; HGNC:17276; ERI3.
DR HPA; HPA027147; -.
DR MIM; 609917; gene.
DR neXtProt; NX_O43414; -.
DR PharmGKB; PA164719272; -.
DR eggNOG; COG5018; -.
DR HOVERGEN; HBG108293; -.
DR EvolutionaryTrace; O43414; -.
DR GenomeRNAi; 79033; -.
DR NextBio; 67747; -.
DR PRO; PR:O43414; -.
DR ArrayExpress; O43414; -.
DR Bgee; O43414; -.
DR CleanEx; HS_ERI3; -.
DR Genevestigator; O43414; -.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_dom.
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; Complete proteome; Exonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1 337 ERI1 exoribonuclease 3.
FT /FTId=PRO_0000317626.
FT DOMAIN 146 320 Exonuclease.
FT ACT_SITE 152 152 Proton acceptor (Potential).
FT ACT_SITE 307 307 Proton acceptor (Potential).
FT METAL 150 150 Magnesium 1 (By similarity).
FT METAL 150 150 Magnesium 2 (By similarity).
FT METAL 152 152 Magnesium 1 (By similarity).
FT METAL 249 249 Magnesium 2 (By similarity).
FT METAL 312 312 Magnesium 1 (By similarity).
FT BINDING 152 152 AMP (By similarity).
FT BINDING 307 307 AMP (By similarity).
FT VAR_SEQ 1 209 Missing (in isoform 3).
FT /FTId=VSP_031104.
FT VAR_SEQ 1 163 MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWG
FT QHPGHWGFPALTEPSASPAAGLGIFEVRRVLDASGCSMLAP
FT LQTGAARFSSYLLSRARKVLGSHLFSPCGVPEFCSISTRKL
FT AAHGFGASMAAMVSFPPQRYHYFLVLDFEATCDKPQIHPQ
FT -> MFVMLQVPWLQSCANLVQIGAPLPLLGCLGQYFEVLGS
FT MEVLAGQYGM (in isoform 2).
FT /FTId=VSP_031103.
FT STRAND 144 149
FT STRAND 165 174
FT TURN 175 177
FT STRAND 180 187
FT STRAND 191 193
FT HELIX 198 204
FT HELIX 208 211
FT HELIX 217 230
FT TURN 231 234
FT STRAND 240 247
FT HELIX 248 251
FT HELIX 253 261
FT HELIX 267 269
FT STRAND 272 274
FT HELIX 275 283
FT TURN 288 290
FT HELIX 291 297
FT HELIX 309 325
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
//
ID ERI3_HUMAN Reviewed; 337 AA.
AC O43414; B1AK98; Q5T2T7; Q5T2T9; Q5TG35; Q9BQA0; Q9UEB4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 90.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP SPLICING (ISOFORM 2).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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.,
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 [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC -!- SUBUNIT: Interacts with PRNP (By similarity).
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 -!- SIMILARITY: Contains 1 exonuclease domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19158.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF007157; AAC19158.1; ALT_INIT; mRNA.
DR EMBL; AK290567; BAF83256.1; -; mRNA.
DR EMBL; AL390776; CAI12491.1; -; Genomic_DNA.
DR EMBL; AL035417; CAI12491.1; JOINED; Genomic_DNA.
DR EMBL; AL390776; CAI12494.1; -; Genomic_DNA.
DR EMBL; AL035417; CAI12494.1; JOINED; Genomic_DNA.
DR EMBL; AL035417; CAI23194.1; -; Genomic_DNA.
DR EMBL; AL390776; CAI23194.1; JOINED; Genomic_DNA.
DR EMBL; AL035417; CAI23196.1; -; Genomic_DNA.
DR EMBL; AL390776; CAI23196.1; JOINED; Genomic_DNA.
DR EMBL; AC004254; AAC04618.1; -; Genomic_DNA.
DR EMBL; BC001072; AAH01072.1; -; mRNA.
DR EMBL; BC004456; AAH04456.1; -; mRNA.
DR RefSeq; NP_076971.1; NM_024066.1.
DR UniGene; Hs.731413; -.
DR PDB; 2XRI; X-ray; 2.15 A; A=137-337.
DR PDBsum; 2XRI; -.
DR ProteinModelPortal; O43414; -.
DR SMR; O43414; 136-336.
DR STRING; 9606.ENSP00000361331; -.
DR PhosphoSite; O43414; -.
DR PaxDb; O43414; -.
DR PRIDE; O43414; -.
DR DNASU; 79033; -.
DR Ensembl; ENST00000372257; ENSP00000361331; ENSG00000117419.
DR Ensembl; ENST00000372259; ENSP00000361333; ENSG00000117419.
DR GeneID; 79033; -.
DR KEGG; hsa:79033; -.
DR UCSC; uc001clt.3; human.
DR CTD; 79033; -.
DR GeneCards; GC01M044686; -.
DR HGNC; HGNC:17276; ERI3.
DR HPA; HPA027147; -.
DR MIM; 609917; gene.
DR neXtProt; NX_O43414; -.
DR PharmGKB; PA164719272; -.
DR eggNOG; COG5018; -.
DR HOVERGEN; HBG108293; -.
DR EvolutionaryTrace; O43414; -.
DR GenomeRNAi; 79033; -.
DR NextBio; 67747; -.
DR PRO; PR:O43414; -.
DR ArrayExpress; O43414; -.
DR Bgee; O43414; -.
DR CleanEx; HS_ERI3; -.
DR Genevestigator; O43414; -.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR006055; Exonuclease.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_dom.
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; Complete proteome; Exonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1 337 ERI1 exoribonuclease 3.
FT /FTId=PRO_0000317626.
FT DOMAIN 146 320 Exonuclease.
FT ACT_SITE 152 152 Proton acceptor (Potential).
FT ACT_SITE 307 307 Proton acceptor (Potential).
FT METAL 150 150 Magnesium 1 (By similarity).
FT METAL 150 150 Magnesium 2 (By similarity).
FT METAL 152 152 Magnesium 1 (By similarity).
FT METAL 249 249 Magnesium 2 (By similarity).
FT METAL 312 312 Magnesium 1 (By similarity).
FT BINDING 152 152 AMP (By similarity).
FT BINDING 307 307 AMP (By similarity).
FT VAR_SEQ 1 209 Missing (in isoform 3).
FT /FTId=VSP_031104.
FT VAR_SEQ 1 163 MATASPAADGGRGRPWEGGLVSWPPAPPLTLPWTWMGPSWG
FT QHPGHWGFPALTEPSASPAAGLGIFEVRRVLDASGCSMLAP
FT LQTGAARFSSYLLSRARKVLGSHLFSPCGVPEFCSISTRKL
FT AAHGFGASMAAMVSFPPQRYHYFLVLDFEATCDKPQIHPQ
FT -> MFVMLQVPWLQSCANLVQIGAPLPLLGCLGQYFEVLGS
FT MEVLAGQYGM (in isoform 2).
FT /FTId=VSP_031103.
FT STRAND 144 149
FT STRAND 165 174
FT TURN 175 177
FT STRAND 180 187
FT STRAND 191 193
FT HELIX 198 204
FT HELIX 208 211
FT HELIX 217 230
FT TURN 231 234
FT STRAND 240 247
FT HELIX 248 251
FT HELIX 253 261
FT HELIX 267 269
FT STRAND 272 274
FT HELIX 275 283
FT TURN 288 290
FT HELIX 291 297
FT HELIX 309 325
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
//
MIM
609917
*RECORD*
*FIELD* NO
609917
*FIELD* TI
*609917 PRION PROTEIN-INTERACTING PROTEIN; PRNPIP
;;PRION INTERACTOR 1; PINT1
*FIELD* TX
read more
CLONING
Using mouse prion protein (PRNP; 176640) as bait in a yeast 2-hybrid
screen of a mouse brain cDNA library, Spielhaupter and Schatzl (2001)
cloned Prnpip, which they called Pint1. The deduced protein contains 162
amino acids. Northern blot analysis detected a 3.8-kb Pint1 transcript
in all mouse tissues examined. RNA dot blot analysis of mouse tissues
revealed strong Pint1 expression in brain, heart, thyroid, and testis.
Weak expression was detected in muscle cells, liver, pancreas, and
kidney, and no expression was detected in mouse embryos or other tissues
examined. By database analysis, Spielhaupter and Schatzl (2001)
identified human PRNPIP.
GENE FUNCTION
By immunoprecipitation of transfected baby hamster kidney cells,
Spielhaupter and Schatzl (2001) identified mouse Pint1 in a complex with
Prnp, synapsin Ib (SYN1; 313440), and the adaptor protein Grb2 (108355).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PRNPIP
gene to chromosome 1 (TMAP RH93060).
*FIELD* RF
1. Spielhaupter, C.; Schatzl, H. M.: PrP(C) directly interacts with
proteins involved in signaling pathways. J. Biol. Chem. 276: 44604-44612,
2001.
*FIELD* CD
Patricia A. Hartz: 2/23/2006
*FIELD* ED
mgross: 02/23/2006
*RECORD*
*FIELD* NO
609917
*FIELD* TI
*609917 PRION PROTEIN-INTERACTING PROTEIN; PRNPIP
;;PRION INTERACTOR 1; PINT1
*FIELD* TX
read more
CLONING
Using mouse prion protein (PRNP; 176640) as bait in a yeast 2-hybrid
screen of a mouse brain cDNA library, Spielhaupter and Schatzl (2001)
cloned Prnpip, which they called Pint1. The deduced protein contains 162
amino acids. Northern blot analysis detected a 3.8-kb Pint1 transcript
in all mouse tissues examined. RNA dot blot analysis of mouse tissues
revealed strong Pint1 expression in brain, heart, thyroid, and testis.
Weak expression was detected in muscle cells, liver, pancreas, and
kidney, and no expression was detected in mouse embryos or other tissues
examined. By database analysis, Spielhaupter and Schatzl (2001)
identified human PRNPIP.
GENE FUNCTION
By immunoprecipitation of transfected baby hamster kidney cells,
Spielhaupter and Schatzl (2001) identified mouse Pint1 in a complex with
Prnp, synapsin Ib (SYN1; 313440), and the adaptor protein Grb2 (108355).
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PRNPIP
gene to chromosome 1 (TMAP RH93060).
*FIELD* RF
1. Spielhaupter, C.; Schatzl, H. M.: PrP(C) directly interacts with
proteins involved in signaling pathways. J. Biol. Chem. 276: 44604-44612,
2001.
*FIELD* CD
Patricia A. Hartz: 2/23/2006
*FIELD* ED
mgross: 02/23/2006