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O43414 (ERI3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ERI1 exoribonuclease 3

EC=3.1.-.-
Alternative name(s):
Prion interactor 1
Prion protein-interacting protein
Gene names
Name:ERI3
Synonyms:PINT1, PRNPIP, PRNPIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Subunit structure

Interacts with PRNP By similarity.

Sequence similarities

Contains 1 exonuclease domain.

Sequence caution

The sequence AAC19158.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43414-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43414-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: MATASPAADG...TCDKPQIHPQ → MFVMLQVPWL...MEVLAGQYGM
Isoform 3 (identifier: O43414-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-209: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337ERI1 exoribonuclease 3
PRO_0000317626

Regions

Domain146 – 320175Exonuclease

Sites

Active site1521Proton acceptor Potential
Active site3071Proton acceptor Potential
Metal binding1501Magnesium 1 By similarity
Metal binding1501Magnesium 2 By similarity
Metal binding1521Magnesium 1 By similarity
Metal binding2491Magnesium 2 By similarity
Metal binding3121Magnesium 1 By similarity
Binding site1521AMP By similarity
Binding site3071AMP By similarity

Natural variations

Alternative sequence1 – 209209Missing in isoform 3.
VSP_031104
Alternative sequence1 – 163163MATAS…QIHPQ → MFVMLQVPWLQSCANLVQIG APLPLLGCLGQYFEVLGSME VLAGQYGM in isoform 2.
VSP_031103

Secondary structure

................................ 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 28E8A691659B4D67

FASTA33737,238
        10         20         30         40         50         60 
MATASPAADG GRGRPWEGGL VSWPPAPPLT LPWTWMGPSW GQHPGHWGFP ALTEPSASPA 

        70         80         90        100        110        120 
AGLGIFEVRR VLDASGCSML APLQTGAARF SSYLLSRARK VLGSHLFSPC GVPEFCSIST 

       130        140        150        160        170        180 
RKLAAHGFGA SMAAMVSFPP QRYHYFLVLD FEATCDKPQI HPQEIIEFPI LKLNGRTMEI 

       190        200        210        220        230        240 
ESTFHMYVQP VVHPQLTPFC TELTGIIQAM VDGQPSLQQV LERVDEWMAK EGLLDPNVKS 

       250        260        270        280        290        300 
IFVTCGDWDL KVMLPGQCQY LGLPVADYFK QWINLKKAYS FAMGCWPKNG LLDMNKGLSL 

       310        320        330 
QHIGRPHSGI DDCKNIANIM KTLAYRGFIF KQTSKPF 

« Hide

Isoform 2 [UniParc].

Checksum: 5DF6E20F9B256DC4
Show »

FASTA22225,009
Isoform 3 [UniParc].

Checksum: 3DB7393DB221D90F
Show »

FASTA12814,542

References

[1]Yu W., Sarginson J., Gibbs R.A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Lung.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007157 mRNA. Translation: AAC19158.1. Different initiation.
AK290567 mRNA. Translation: BAF83256.1.
AL390776, AL035417 Genomic DNA. Translation: CAI12491.1.
AL390776, AL035417 Genomic DNA. Translation: CAI12494.1.
AL035417, AL390776 Genomic DNA. Translation: CAI23194.1.
AL035417, AL390776 Genomic DNA. Translation: CAI23196.1.
AC004254 Genomic DNA. Translation: AAC04618.1.
BC001072 mRNA. Translation: AAH01072.1.
BC004456 mRNA. Translation: AAH04456.1.
CCDSCCDS30696.1. [O43414-1]
RefSeqNP_076971.1. NM_024066.1. [O43414-1]
UniGeneHs.731413.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRIX-ray2.15A137-337[»]
ProteinModelPortalO43414.
SMRO43414. Positions 136-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122498. 4 interactions.
STRING9606.ENSP00000361331.

PTM databases

PhosphoSiteO43414.

Proteomic databases

MaxQBO43414.
PaxDbO43414.
PRIDEO43414.

Protocols and materials databases

DNASU79033.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372257; ENSP00000361331; ENSG00000117419. [O43414-1]
ENST00000372259; ENSP00000361333; ENSG00000117419. [O43414-2]
GeneID79033.
KEGGhsa:79033.
UCSCuc001clt.3. human. [O43414-1]

Organism-specific databases

CTD79033.
GeneCardsGC01M044686.
HGNCHGNC:17276. ERI3.
HPAHPA027147.
HPA029895.
HPA056253.
HPA058538.
MIM609917. gene.
neXtProtNX_O43414.
PharmGKBPA164719272.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5018.
HOVERGENHBG108293.
PhylomeDBO43414.
TreeFamTF313449.

Gene expression databases

ArrayExpressO43414.
BgeeO43414.
CleanExHS_ERI3.
GenevestigatorO43414.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO43414.
GenomeRNAi79033.
NextBio67747.
PROO43414.
SOURCESearch...

Entry information

Entry nameERI3_HUMAN
AccessionPrimary (citable) accession number: O43414
Secondary accession number(s): B1AK98 expand/collapse secondary AC list , Q5T2T7, Q5T2T9, Q5TG35, Q9BQA0, Q9UEB4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM