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Protein

Protein pelota homolog

Gene

Pelo

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential).By similarityCurated

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein pelota homolog (EC:3.1.-.-)
Gene namesi
Name:Pelo
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1359591. Pelo.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Protein pelota homologPRO_0000232836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei374 – 3741PhosphoserineCombined sources
Modified residuei380 – 3801PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei382 – 3821PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5XIP1.
PRIDEiQ5XIP1.

PTM databases

PhosphoSiteiQ5XIP1.

Expressioni

Gene expression databases

GenevisibleiQ5XIP1. RN.

Interactioni

Protein-protein interaction databases

IntActiQ5XIP1. 1 interaction.
STRINGi10116.ENSRNOP00000038406.

Structurei

3D structure databases

ProteinModelPortaliQ5XIP1.
SMRiQ5XIP1. Positions 261-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity (Potential).Curated

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2869. Eukaryota.
COG1537. LUCA.
GeneTreeiENSGT00390000016326.
HOGENOMiHOG000184162.
HOVERGENiHBG053560.
InParanoidiQ5XIP1.
KOiK06965.
OMAiAFYGKKH.
OrthoDBiEOG76X60C.
PhylomeDBiQ5XIP1.
TreeFamiTF105733.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR029064. L30e-like.
IPR004405. Transl-rel_pelota.
[Graphical view]
PANTHERiPTHR10853. PTHR10853. 1 hit.
PfamiPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SMARTiSM01194. eRF1_1. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
TIGRFAMsiTIGR00111. pelota. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5XIP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVRKDIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE
60 70 80 90 100
SSTGSVGSNR VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH
110 120 130 140 150
TIELEPNRQF TLAKKQWDSV VLERIEQACD PAWSADVAAV VMQEGLAHVC
160 170 180 190 200
LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR ALERFYEQVV QAIQRHINFE
210 220 230 240 250
VVKCILVASP GFVREQFCDY MFQQAVKTDN KVLLENRSKF LQVHASSGHK
260 270 280 290 300
YSLKEVLCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
310 320 330 340 350
RANEALAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH
360 370 380
VSGEQLGQLT GVAAILRFPV PELSDQEDDS SSEED
Length:385
Mass (Da):43,407
Last modified:November 23, 2004 - v1
Checksum:i7C50D96BA28C48E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083637 mRNA. Translation: AAH83637.1.
RefSeqiNP_001007635.1. NM_001007634.1.
UniGeneiRn.3842.

Genome annotation databases

EnsembliENSRNOT00000091499; ENSRNOP00000075562; ENSRNOG00000061128.
GeneIDi294754.
KEGGirno:294754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083637 mRNA. Translation: AAH83637.1.
RefSeqiNP_001007635.1. NM_001007634.1.
UniGeneiRn.3842.

3D structure databases

ProteinModelPortaliQ5XIP1.
SMRiQ5XIP1. Positions 261-371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5XIP1. 1 interaction.
STRINGi10116.ENSRNOP00000038406.

PTM databases

PhosphoSiteiQ5XIP1.

Proteomic databases

PaxDbiQ5XIP1.
PRIDEiQ5XIP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091499; ENSRNOP00000075562; ENSRNOG00000061128.
GeneIDi294754.
KEGGirno:294754.

Organism-specific databases

CTDi53918.
RGDi1359591. Pelo.

Phylogenomic databases

eggNOGiKOG2869. Eukaryota.
COG1537. LUCA.
GeneTreeiENSGT00390000016326.
HOGENOMiHOG000184162.
HOVERGENiHBG053560.
InParanoidiQ5XIP1.
KOiK06965.
OMAiAFYGKKH.
OrthoDBiEOG76X60C.
PhylomeDBiQ5XIP1.
TreeFamiTF105733.

Miscellaneous databases

NextBioi638529.
PROiQ5XIP1.

Gene expression databases

GenevisibleiQ5XIP1. RN.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR029064. L30e-like.
IPR004405. Transl-rel_pelota.
[Graphical view]
PANTHERiPTHR10853. PTHR10853. 1 hit.
PfamiPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SMARTiSM01194. eRF1_1. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
TIGRFAMsiTIGR00111. pelota. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPELO_RAT
AccessioniPrimary (citable) accession number: Q5XIP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 23, 2004
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.