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Protein

Protein pelota homolog

Gene

PELO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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
ORF Names:CGI-17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:8829. PELO.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33174.

Polymorphism and mutation databases

BioMutaiPELO.
DMDMi322510057.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Protein pelota homologPRO_0000143188Add
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

EPDiQ9BRX2.
MaxQBiQ9BRX2.
PaxDbiQ9BRX2.
PeptideAtlasiQ9BRX2.
PRIDEiQ9BRX2.

PTM databases

iPTMnetiQ9BRX2.
PhosphoSiteiQ9BRX2.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9BRX2.
CleanExiHS_PELO.
GenevisibleiQ9BRX2. HS.

Organism-specific databases

HPAiHPA031458.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HBS1LD9YZV03EBI-1043580,EBI-10297269

Protein-protein interaction databases

BioGridi119818. 32 interactions.
IntActiQ9BRX2. 14 interactions.
MINTiMINT-3372932.
STRINGi9606.ENSP00000274311.

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi269 – 28618Combined sources
Helixi289 – 2913Combined sources
Beta strandi292 – 2954Combined sources
Helixi296 – 3049Combined sources
Beta strandi308 – 3147Combined sources
Helixi315 – 3184Combined sources
Helixi323 – 33816Combined sources
Beta strandi342 – 3465Combined sources
Beta strandi348 – 3503Combined sources
Helixi351 – 3577Combined sources
Turni358 – 3614Combined sources
Beta strandi362 – 3687Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X52NMR-A261-371[»]
ProteinModelPortaliQ9BRX2.
SMRiQ9BRX2. Positions 8-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BRX2.

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.
InParanoidiQ9BRX2.
KOiK06965.
OMAiAFYGKKH.
OrthoDBiEOG76X60C.
PhylomeDBiQ9BRX2.
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.

Q9BRX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE
60 70 80 90 100
SSTGSVGSNR VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH
110 120 130 140 150
TIELEPNRQF TLAKKQWDSV VLERIEQACD PAWSADVAAV VMQEGLAHIC
160 170 180 190 200
LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR ALERFYEQVV QAIQRHIHFD
210 220 230 240 250
VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF LQVHASSGHK
260 270 280 290 300
YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
310 320 330 340 350
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH
360 370 380
VSGEQLSQLT GVAAILRFPV PELSDQEGDS SSEED
Length:385
Mass (Da):43,359
Last modified:February 8, 2011 - v2
Checksum:i8A0D264202995B76
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351A → D in AAG22574 (PubMed:11060452).Curated
Sequence conflicti135 – 1351A → D in AAG22575 (PubMed:11060452).Curated
Sequence conflicti235 – 2351E → G in AAD27726 (PubMed:10810093).Curated
Sequence conflicti263 – 2642AS → LA in AAD27726 (PubMed:10810093).Curated
Sequence conflicti281 – 2811F → S in AAD27726 (PubMed:10810093).Curated
Sequence conflicti352 – 3521S → Y in AAG22574 (PubMed:11060452).Curated
Sequence conflicti352 – 3521S → Y in AAG22575 (PubMed:11060452).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211L → M.4 Publications
Corresponds to variant rs1499280 [ dbSNP | Ensembl ].
VAR_019777

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139828 mRNA. Translation: AAG22574.1.
AF143952 Genomic DNA. Translation: AAG22575.1.
AY117399 mRNA. Translation: AAM89414.1.
AF132951 mRNA. Translation: AAD27726.1.
AC026230 Genomic DNA. No translation available.
BC005889 mRNA. Translation: AAH05889.1.
BC007249 mRNA. Translation: AAH07249.1.
BC007650 mRNA. Translation: AAH07650.1.
BC022789 mRNA. Translation: AAH22789.1.
CCDSiCCDS3956.1.
RefSeqiNP_057030.3. NM_015946.4.
UniGeneiHs.644352.

Genome annotation databases

EnsembliENST00000274311; ENSP00000274311; ENSG00000152684.
GeneIDi53918.
KEGGihsa:53918.
UCSCiuc003jos.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139828 mRNA. Translation: AAG22574.1.
AF143952 Genomic DNA. Translation: AAG22575.1.
AY117399 mRNA. Translation: AAM89414.1.
AF132951 mRNA. Translation: AAD27726.1.
AC026230 Genomic DNA. No translation available.
BC005889 mRNA. Translation: AAH05889.1.
BC007249 mRNA. Translation: AAH07249.1.
BC007650 mRNA. Translation: AAH07650.1.
BC022789 mRNA. Translation: AAH22789.1.
CCDSiCCDS3956.1.
RefSeqiNP_057030.3. NM_015946.4.
UniGeneiHs.644352.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X52NMR-A261-371[»]
ProteinModelPortaliQ9BRX2.
SMRiQ9BRX2. Positions 8-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119818. 32 interactions.
IntActiQ9BRX2. 14 interactions.
MINTiMINT-3372932.
STRINGi9606.ENSP00000274311.

PTM databases

iPTMnetiQ9BRX2.
PhosphoSiteiQ9BRX2.

Polymorphism and mutation databases

BioMutaiPELO.
DMDMi322510057.

Proteomic databases

EPDiQ9BRX2.
MaxQBiQ9BRX2.
PaxDbiQ9BRX2.
PeptideAtlasiQ9BRX2.
PRIDEiQ9BRX2.

Protocols and materials databases

DNASUi53918.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274311; ENSP00000274311; ENSG00000152684.
GeneIDi53918.
KEGGihsa:53918.
UCSCiuc003jos.5. human.

Organism-specific databases

CTDi53918.
GeneCardsiPELO.
H-InvDBHIX0004852.
HGNCiHGNC:8829. PELO.
HPAiHPA031458.
MIMi605757. gene.
neXtProtiNX_Q9BRX2.
PharmGKBiPA33174.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2869. Eukaryota.
COG1537. LUCA.
GeneTreeiENSGT00390000016326.
HOGENOMiHOG000184162.
HOVERGENiHBG053560.
InParanoidiQ9BRX2.
KOiK06965.
OMAiAFYGKKH.
OrthoDBiEOG76X60C.
PhylomeDBiQ9BRX2.
TreeFamiTF105733.

Miscellaneous databases

EvolutionaryTraceiQ9BRX2.
GeneWikiiPELO.
GenomeRNAii53918.
PROiQ9BRX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BRX2.
CleanExiHS_PELO.
GenevisibleiQ9BRX2. HS.

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

« Hide 'large scale' publications
  1. "Molecular cloning, expression and chromosome location of the human pelota gene PELO."
    Shamsadin R., Adham I.M., von Beust G., Engel W.
    Cytogenet. Cell Genet. 90:75-78(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT MET-221.
    Tissue: Testis.
  2. "Gene structure prediction and evidence of alternative splicing in the human pelota gene."
    Shamsadin R.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-221.
  3. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-221.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT MET-221.
    Tissue: Brain, Skin and Uterus.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [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].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Solution structure of the C-terminal domain of the human pelota homolog (CGI-17)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 261-371.

Entry informationi

Entry nameiPELO_HUMAN
AccessioniPrimary (citable) accession number: Q9BRX2
Secondary accession number(s): Q9GZS6, Q9Y306
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: February 8, 2011
Last modified: July 6, 2016
This is version 129 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.