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Protein

ERI1 exoribonuclease 3

Gene

ERI3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Magnesium 1By similarity
Metal bindingi150 – 1501Magnesium 2By similarity
Active sitei152 – 1521Proton acceptorSequence Analysis
Metal bindingi152 – 1521Magnesium 1By similarity
Binding sitei152 – 1521AMPBy similarity
Metal bindingi249 – 2491Magnesium 2By similarity
Active sitei307 – 3071Proton acceptorSequence Analysis
Binding sitei307 – 3071AMPBy similarity
Metal bindingi312 – 3121Magnesium 1By similarity

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: GO_Central
  2. metal ion binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ERI1 exoribonuclease 3 (EC:3.1.-.-)
Alternative name(s):
Prion interactor 1
Prion protein-interacting protein
Gene namesi
Name:ERI3
Synonyms:PINT1, PRNPIP, PRNPIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:17276. ERI3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. nucleolus Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164719272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337ERI1 exoribonuclease 3PRO_0000317626Add
BLAST

Proteomic databases

MaxQBiO43414.
PaxDbiO43414.
PRIDEiO43414.

PTM databases

PhosphoSiteiO43414.

Expressioni

Gene expression databases

BgeeiO43414.
CleanExiHS_ERI3.
ExpressionAtlasiO43414. baseline and differential.
GenevestigatoriO43414.

Organism-specific databases

HPAiHPA027147.
HPA029895.

Interactioni

Subunit structurei

Interacts with PRNP.By similarity

Protein-protein interaction databases

BioGridi122498. 3 interactions.
IntActiO43414. 2 interactions.
STRINGi9606.ENSP00000361331.

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi144 – 1496Combined sources
Beta strandi165 – 17410Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 1878Combined sources
Beta strandi191 – 1933Combined sources
Helixi198 – 2047Combined sources
Helixi208 – 2114Combined sources
Helixi217 – 23014Combined sources
Turni231 – 2344Combined sources
Beta strandi240 – 2478Combined sources
Helixi248 – 2514Combined sources
Helixi253 – 2619Combined sources
Helixi267 – 2693Combined sources
Beta strandi272 – 2743Combined sources
Helixi275 – 2839Combined sources
Turni288 – 2903Combined sources
Helixi291 – 2977Combined sources
Helixi309 – 32517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRIX-ray2.15A137-337[»]
ProteinModelPortaliO43414.
SMRiO43414. Positions 136-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 320175ExonucleaseAdd
BLAST

Sequence similaritiesi

Contains 1 exonuclease domain.Curated

Phylogenomic databases

eggNOGiCOG5018.
GeneTreeiENSGT00530000063205.
HOVERGENiHBG108293.
InParanoidiO43414.
KOiK18418.
PhylomeDBiO43414.
TreeFamiTF313449.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43414-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATASPAADG GRGRPWEGGL VSWPPAPPLT LPWTWMGPSW GQHPGHWGFP
60 70 80 90 100
ALTEPSASPA AGLGIFEVRR VLDASGCSML APLQTGAARF SSYLLSRARK
110 120 130 140 150
VLGSHLFSPC GVPEFCSIST RKLAAHGFGA SMAAMVSFPP QRYHYFLVLD
160 170 180 190 200
FEATCDKPQI HPQEIIEFPI LKLNGRTMEI ESTFHMYVQP VVHPQLTPFC
210 220 230 240 250
TELTGIIQAM VDGQPSLQQV LERVDEWMAK EGLLDPNVKS IFVTCGDWDL
260 270 280 290 300
KVMLPGQCQY LGLPVADYFK QWINLKKAYS FAMGCWPKNG LLDMNKGLSL
310 320 330
QHIGRPHSGI DDCKNIANIM KTLAYRGFIF KQTSKPF
Length:337
Mass (Da):37,238
Last modified:March 18, 2008 - v2
Checksum:i28E8A691659B4D67
GO
Isoform 2 (identifier: O43414-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: MATASPAADG...TCDKPQIHPQ → MFVMLQVPWL...MEVLAGQYGM

Show »
Length:222
Mass (Da):25,009
Checksum:i5DF6E20F9B256DC4
GO
Isoform 3 (identifier: O43414-3) [UniParc]FASTAAdd to basket

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

Show »
Length:128
Mass (Da):14,542
Checksum:i3DB7393DB221D90F
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 209209Missing in isoform 3. 1 PublicationVSP_031104Add
BLAST
Alternative sequencei1 – 163163MATAS…QIHPQ → MFVMLQVPWLQSCANLVQIG APLPLLGCLGQYFEVLGSME VLAGQYGM in isoform 2. CuratedVSP_031103Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30696.1. [O43414-1]
RefSeqiNP_001288627.1. NM_001301698.1.
NP_001288628.1. NM_001301699.1.
NP_001288629.1. NM_001301700.1.
NP_001288630.1. NM_001301701.1.
NP_076971.1. NM_024066.2. [O43414-1]
UniGeneiHs.731413.

Genome annotation databases

EnsembliENST00000372257; ENSP00000361331; ENSG00000117419. [O43414-1]
ENST00000372259; ENSP00000361333; ENSG00000117419. [O43414-2]
GeneIDi79033.
KEGGihsa:79033.
UCSCiuc001clt.3. human. [O43414-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30696.1. [O43414-1]
RefSeqiNP_001288627.1. NM_001301698.1.
NP_001288628.1. NM_001301699.1.
NP_001288629.1. NM_001301700.1.
NP_001288630.1. NM_001301701.1.
NP_076971.1. NM_024066.2. [O43414-1]
UniGeneiHs.731413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRIX-ray2.15A137-337[»]
ProteinModelPortaliO43414.
SMRiO43414. Positions 136-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122498. 3 interactions.
IntActiO43414. 2 interactions.
STRINGi9606.ENSP00000361331.

PTM databases

PhosphoSiteiO43414.

Proteomic databases

MaxQBiO43414.
PaxDbiO43414.
PRIDEiO43414.

Protocols and materials databases

DNASUi79033.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372257; ENSP00000361331; ENSG00000117419. [O43414-1]
ENST00000372259; ENSP00000361333; ENSG00000117419. [O43414-2]
GeneIDi79033.
KEGGihsa:79033.
UCSCiuc001clt.3. human. [O43414-1]

Organism-specific databases

CTDi79033.
GeneCardsiGC01M044686.
HGNCiHGNC:17276. ERI3.
HPAiHPA027147.
HPA029895.
MIMi609917. gene.
neXtProtiNX_O43414.
PharmGKBiPA164719272.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5018.
GeneTreeiENSGT00530000063205.
HOVERGENiHBG108293.
InParanoidiO43414.
KOiK18418.
PhylomeDBiO43414.
TreeFamiTF313449.

Miscellaneous databases

ChiTaRSiERI3. human.
EvolutionaryTraceiO43414.
GenomeRNAii79033.
NextBioi67747.
PROiO43414.
SOURCEiSearch...

Gene expression databases

BgeeiO43414.
CleanExiHS_ERI3.
ExpressionAtlasiO43414. baseline and differential.
GenevestigatoriO43414.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERI3_HUMAN
AccessioniPrimary (citable) accession number: O43414
Secondary accession number(s): B1AK98
, Q5T2T7, Q5T2T9, Q5TG35, Q9BQA0, Q9UEB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: March 4, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.