Protein pelota homolog - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9BRX2 (PELO_HUMAN)

Last modified July 7, 2009. Version 62. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Protein pelota homolog
EC=3.1.-.-

Gene names

Name:	PELO
ORF Names:	CGI-17

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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.
Cofactor	Divalent metal cations Potential.
Subcellular location	Nucleus Potential. Cytoplasm By similarity.
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity Potential.
Sequence similarities	Belongs to the eukaryotic release factor 1 family. Pelota subfamily.

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Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ABCD3	P28288	1	EBI-1043580,EBI-80992
AIFM1	O95831	1	EBI-1043580,EBI-356440
MCM7	P33993	1	EBI-1043580,EBI-355924
MYO1D	O94832	1	EBI-1043580,EBI-355634
PTPLAD1	Q9P035	1	EBI-1043580,EBI-359013
QIL1	Q5XKP0	1	EBI-1043580,EBI-1053887
RUVBL1	Q9Y265	1	EBI-1043580,EBI-353675
SLC25A12	O75746	1	EBI-1043580,EBI-1047585
TIMM50	Q3ZCQ8	1	EBI-1043580,EBI-355175

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 385

385

Protein pelota homolog

PRO_0000143188

Amino acid modifications

Modified residue

374

Phosphoserine Ref.5 Ref.6 Ref.7

Modified residue

380

Phosphoserine Ref.5 Ref.6 Ref.7

Modified residue

381

Phosphoserine Ref.5 Ref.6 Ref.7

Modified residue

382

Phosphoserine Ref.5 Ref.6 Ref.7

Natural variations

Natural variant

221

M → L: dbSNP rs1499280.

VAR_019777

Experimental info

Sequence conflict

135

A → D in AAG22574. Ref.1

Sequence conflict

135

A → D in AAG22575. Ref.1

Sequence conflict

235

E → G in AAD27726. Ref.3

Sequence conflict

263 – 264

AS → LA in AAD27726. Ref.3

Sequence conflict

281

F → S in AAD27726. Ref.3

Sequence conflict

352

S → Y in AAG22574. Ref.1

Sequence conflict

352

S → Y in AAG22575. Ref.1

Secondary structure

385

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9BRX2-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9F18271347760578
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FASTA

385

43,377

        10         20         30         40         50         60 
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR 

        70         80         90        100        110        120 
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV 

       130        140        150        160        170        180 
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR 

       190        200        210        220        230        240 
ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY MFQQAVKTDN KLLLENRSKF 

       250        260        270        280        290        300 
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE 

       310        320        330        340        350        360 
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT 

       370        380 
GVAAILRFPV PELSDQEGDS SSEED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11060452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. 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].
[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: 10810093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Skin and Uterus.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND SER-382, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND SER-382, MASS SPECTROMETRY. Tissue: Platelet.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND SER-382, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"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.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF139828 mRNA. Translation: AAG22574.1.
AF143952 Genomic DNA. Translation: AAG22575.1.
AY117399 mRNA. Translation: AAM89414.1.
AF132951 mRNA. Translation: AAD27726.1.
BC005889 mRNA. Translation: AAH05889.1.
BC007249 mRNA. Translation: AAH07249.1.
BC007650 mRNA. Translation: AAH07650.1.
BC022789 mRNA. Translation: AAH22789.1.

IPI

IPI00106698.

RefSeq

NP_057030.3.

UniGene

Hs.644352
Hs.669791

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X52	NMR	-	A	261-371	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BRX2. 12 interactions.

PTM databases

PhosphoSite

Q9BRX2.

Proteomic databases

PRIDE

Q9BRX2.

Genome annotation databases

Ensembl

ENSG00000152684. Homo sapiens. [Contig view]

GeneID

53918.

KEGG

hsa:53918.

UCSC

uc003jos.1. human.

Organism-specific databases

GeneCards

GC05P052120.

HGNC

HGNC:8829. PELO.

MIM

605757. gene.

PharmGKB

PA33174.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9BRX2.

Gene expression databases

ArrayExpress

Q9BRX2.

Bgee

Q9BRX2.

CleanEx

HS_PELO.

GermOnline

ENSG00000152684. Homo sapiens.

Family and domain databases

InterPro

IPR005140. eRF1_1.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR004405. PelA.
[Graphical view]

PANTHER

PTHR10853. PelA. 1 hit.

Pfam

PF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00111. pelota. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

56232.

SOURCE

Search...

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Entry information

Entry name

PELO_HUMAN

Accession

Primary (citable) accession number: Q9BRX2
Secondary accession number(s): Q9GZS6, Q9Y306

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	June 1, 2001
Last modified:	July 7, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents