Full text data of PELO
PELO
[Confidence: low (only semi-automatic identification from reviews)]
Protein pelota homolog; 3.1.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein pelota homolog; 3.1.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRX2
ID PELO_HUMAN Reviewed; 385 AA.
AC Q9BRX2; Q9GZS6; Q9Y306;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 08-FEB-2011, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.-;
GN Name=PELO; ORFNames=CGI-17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT MET-221.
RC TISSUE=Testis;
RX PubMed=11060452;
RA Shamsadin R., Adham I.M., von Beust G., Engel W.;
RT "Molecular cloning, expression and chromosome location of the human
RT pelota gene PELO.";
RL Cytogenet. Cell Genet. 90:75-78(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-221.
RA Shamsadin R.;
RT "Gene structure prediction and evidence of alternative splicing in the
RT human pelota gene.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221.
RC TISSUE=Brain, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381
RP AND SER-382, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-381, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381
RP AND SER-382, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP STRUCTURE BY NMR OF 261-371.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal domain of the human pelota
RT homolog (CGI-17).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Required for normal chromosome segregation during cell
CC division and genomic stability (By similarity). May function in
CC recognizing stalled ribosomes and triggering endonucleolytic
CC cleavage of the mRNA, a mechanism to release non-functional
CC ribosomes and degrade damaged mRNAs. May have ribonuclease
CC activity (Potential).
CC -!- COFACTOR: Divalent metal cations (Potential).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). Cytoplasm (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It may
CC harbor the endoribonuclease activity (Potential).
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC Pelota subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF139828; AAG22574.1; -; mRNA.
DR EMBL; AF143952; AAG22575.1; -; Genomic_DNA.
DR EMBL; AY117399; AAM89414.1; -; mRNA.
DR EMBL; AF132951; AAD27726.1; -; mRNA.
DR EMBL; AC026230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005889; AAH05889.1; -; mRNA.
DR EMBL; BC007249; AAH07249.1; -; mRNA.
DR EMBL; BC007650; AAH07650.1; -; mRNA.
DR EMBL; BC022789; AAH22789.1; -; mRNA.
DR RefSeq; NP_057030.3; NM_015946.4.
DR UniGene; Hs.644352; -.
DR PDB; 1X52; NMR; -; A=261-371.
DR PDBsum; 1X52; -.
DR ProteinModelPortal; Q9BRX2; -.
DR SMR; Q9BRX2; 8-372.
DR IntAct; Q9BRX2; 6.
DR MINT; MINT-3372932; -.
DR STRING; 9606.ENSP00000274311; -.
DR PhosphoSite; Q9BRX2; -.
DR DMDM; 54036246; -.
DR PaxDb; Q9BRX2; -.
DR PRIDE; Q9BRX2; -.
DR DNASU; 53918; -.
DR Ensembl; ENST00000274311; ENSP00000274311; ENSG00000152684.
DR GeneID; 53918; -.
DR KEGG; hsa:53918; -.
DR UCSC; uc003jos.3; human.
DR CTD; 53918; -.
DR GeneCards; GC05P052084; -.
DR H-InvDB; HIX0004852; -.
DR HGNC; HGNC:8829; PELO.
DR HPA; HPA031458; -.
DR MIM; 605757; gene.
DR neXtProt; NX_Q9BRX2; -.
DR PharmGKB; PA33174; -.
DR eggNOG; COG1537; -.
DR HOGENOM; HOG000184162; -.
DR HOVERGEN; HBG053560; -.
DR InParanoid; Q9BRX2; -.
DR KO; K06965; -.
DR OMA; KETKFAR; -.
DR OrthoDB; EOG76X60C; -.
DR EvolutionaryTrace; Q9BRX2; -.
DR GeneWiki; PELO; -.
DR GenomeRNAi; 53918; -.
DR NextBio; 56232; -.
DR PRO; PR:Q9BRX2; -.
DR Bgee; Q9BRX2; -.
DR CleanEx; HS_PELO; -.
DR Genevestigator; Q9BRX2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR004405; Transl_rel_pelota-like.
DR PANTHER; PTHR10853; PTHR10853; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 385 Protein pelota homolog.
FT /FTId=PRO_0000143188.
FT MOD_RES 374 374 Phosphoserine.
FT MOD_RES 380 380 Phosphoserine.
FT MOD_RES 381 381 Phosphoserine.
FT MOD_RES 382 382 Phosphoserine.
FT VARIANT 221 221 L -> M (in dbSNP:rs1499280).
FT /FTId=VAR_019777.
FT CONFLICT 135 135 A -> D (in Ref. 1; AAG22574/AAG22575).
FT CONFLICT 235 235 E -> G (in Ref. 3; AAD27726).
FT CONFLICT 263 264 AS -> LA (in Ref. 3; AAD27726).
FT CONFLICT 281 281 F -> S (in Ref. 3; AAD27726).
FT CONFLICT 352 352 S -> Y (in Ref. 1; AAG22574/AAG22575).
FT HELIX 269 286
FT HELIX 289 291
FT STRAND 292 295
FT HELIX 296 304
FT STRAND 308 314
FT HELIX 315 318
FT HELIX 323 338
FT STRAND 342 346
FT STRAND 348 350
FT HELIX 351 357
FT TURN 358 361
FT STRAND 362 368
SQ SEQUENCE 385 AA; 43359 MW; 8A0D264202995B76 CRC64;
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT
GVAAILRFPV PELSDQEGDS SSEED
//
ID PELO_HUMAN Reviewed; 385 AA.
AC Q9BRX2; Q9GZS6; Q9Y306;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 08-FEB-2011, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.-;
GN Name=PELO; ORFNames=CGI-17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT MET-221.
RC TISSUE=Testis;
RX PubMed=11060452;
RA Shamsadin R., Adham I.M., von Beust G., Engel W.;
RT "Molecular cloning, expression and chromosome location of the human
RT pelota gene PELO.";
RL Cytogenet. Cell Genet. 90:75-78(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-221.
RA Shamsadin R.;
RT "Gene structure prediction and evidence of alternative splicing in the
RT human pelota gene.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221.
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-221.
RC TISSUE=Brain, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381
RP AND SER-382, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND SER-381, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381
RP AND SER-382, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP STRUCTURE BY NMR OF 261-371.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal domain of the human pelota
RT homolog (CGI-17).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Required for normal chromosome segregation during cell
CC division and genomic stability (By similarity). May function in
CC recognizing stalled ribosomes and triggering endonucleolytic
CC cleavage of the mRNA, a mechanism to release non-functional
CC ribosomes and degrade damaged mRNAs. May have ribonuclease
CC activity (Potential).
CC -!- COFACTOR: Divalent metal cations (Potential).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). Cytoplasm (By
CC similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It may
CC harbor the endoribonuclease activity (Potential).
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC Pelota subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF139828; AAG22574.1; -; mRNA.
DR EMBL; AF143952; AAG22575.1; -; Genomic_DNA.
DR EMBL; AY117399; AAM89414.1; -; mRNA.
DR EMBL; AF132951; AAD27726.1; -; mRNA.
DR EMBL; AC026230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005889; AAH05889.1; -; mRNA.
DR EMBL; BC007249; AAH07249.1; -; mRNA.
DR EMBL; BC007650; AAH07650.1; -; mRNA.
DR EMBL; BC022789; AAH22789.1; -; mRNA.
DR RefSeq; NP_057030.3; NM_015946.4.
DR UniGene; Hs.644352; -.
DR PDB; 1X52; NMR; -; A=261-371.
DR PDBsum; 1X52; -.
DR ProteinModelPortal; Q9BRX2; -.
DR SMR; Q9BRX2; 8-372.
DR IntAct; Q9BRX2; 6.
DR MINT; MINT-3372932; -.
DR STRING; 9606.ENSP00000274311; -.
DR PhosphoSite; Q9BRX2; -.
DR DMDM; 54036246; -.
DR PaxDb; Q9BRX2; -.
DR PRIDE; Q9BRX2; -.
DR DNASU; 53918; -.
DR Ensembl; ENST00000274311; ENSP00000274311; ENSG00000152684.
DR GeneID; 53918; -.
DR KEGG; hsa:53918; -.
DR UCSC; uc003jos.3; human.
DR CTD; 53918; -.
DR GeneCards; GC05P052084; -.
DR H-InvDB; HIX0004852; -.
DR HGNC; HGNC:8829; PELO.
DR HPA; HPA031458; -.
DR MIM; 605757; gene.
DR neXtProt; NX_Q9BRX2; -.
DR PharmGKB; PA33174; -.
DR eggNOG; COG1537; -.
DR HOGENOM; HOG000184162; -.
DR HOVERGEN; HBG053560; -.
DR InParanoid; Q9BRX2; -.
DR KO; K06965; -.
DR OMA; KETKFAR; -.
DR OrthoDB; EOG76X60C; -.
DR EvolutionaryTrace; Q9BRX2; -.
DR GeneWiki; PELO; -.
DR GenomeRNAi; 53918; -.
DR NextBio; 56232; -.
DR PRO; PR:Q9BRX2; -.
DR Bgee; Q9BRX2; -.
DR CleanEx; HS_PELO; -.
DR Genevestigator; Q9BRX2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR004405; Transl_rel_pelota-like.
DR PANTHER; PTHR10853; PTHR10853; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 385 Protein pelota homolog.
FT /FTId=PRO_0000143188.
FT MOD_RES 374 374 Phosphoserine.
FT MOD_RES 380 380 Phosphoserine.
FT MOD_RES 381 381 Phosphoserine.
FT MOD_RES 382 382 Phosphoserine.
FT VARIANT 221 221 L -> M (in dbSNP:rs1499280).
FT /FTId=VAR_019777.
FT CONFLICT 135 135 A -> D (in Ref. 1; AAG22574/AAG22575).
FT CONFLICT 235 235 E -> G (in Ref. 3; AAD27726).
FT CONFLICT 263 264 AS -> LA (in Ref. 3; AAD27726).
FT CONFLICT 281 281 F -> S (in Ref. 3; AAD27726).
FT CONFLICT 352 352 S -> Y (in Ref. 1; AAG22574/AAG22575).
FT HELIX 269 286
FT HELIX 289 291
FT STRAND 292 295
FT HELIX 296 304
FT STRAND 308 314
FT HELIX 315 318
FT HELIX 323 338
FT STRAND 342 346
FT STRAND 348 350
FT HELIX 351 357
FT TURN 358 361
FT STRAND 362 368
SQ SEQUENCE 385 AA; 43359 MW; 8A0D264202995B76 CRC64;
MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY LFQQAVKTDN KLLLENRSKF
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT
GVAAILRFPV PELSDQEGDS SSEED
//
MIM
605757
*RECORD*
*FIELD* NO
605757
*FIELD* TI
*605757 PELOTA, DROSOPHILA, HOMOLOG OF; PELO
*FIELD* TX
CLONING
Using degenerate primers designed to the Drosophila pelota gene
read moresequence, Shamsadin et al. (2000) cloned a human PELO cDNA from a testis
cDNA library. Lai et al. (2000) also identified human PELO, which they
called CGI-17, by EST database searching against the C. elegans proteome
sequence. The PELO cDNA encodes a 385-amino acid protein with a
conserved nuclear localization signal. It shares 70%, 57%, and 36%
sequence identity with Drosophila pelota protein, C. elegans R74.6, and
yeast DOM34, respectively. By Northern blot analysis, Shamsadin et al.
(2000) detected a 1.6-kb PELO transcript in all tissues tested as well
as a 2.0-kb testis-specific transcript. By dot blot analysis, Lai et al.
(2000) detected PELO expression most abundantly in fetal kidney, spleen,
and lung, and in placenta, lung, spleen, kidney, and adrenal gland.
GENE FUNCTION
Shamsadin et al. (2000) noted that studies of the Drosophila pelota gene
indicate a role in spermatogenesis, mitotic division, and patterning,
and that mutations in the related yeast DOM34 gene result in
disturbances in the cell cycle and in meiotic cell division.
MAPPING
Shamsadin et al. (2000) mapped the PELO gene to 5q11.2 by fluorescence
in situ hybridization.
ANIMAL MODEL
Adham et al. (2003) developed mice deficient in Pelo and found that
homozygous deletion was embryonic lethal. Homozygous Pelo null embryos
failed to develop past embryonic day 7.5 (E7.5). In culture, mitotic
inactive trophoplasts survived, while mitotic active inner cell mass of
null blastocysts failed to expand in growth, indicating that the
lethality of Pelo null embryos was due to a defect in cell
proliferation. Analysis of the cellular DNA content revealed a
significant increase of aneuploid cells in Pelo null embryos at E7.5.
Adham et al. (2003) hypothesized that an increase in aneuploid cells at
E7.5 caused arrested development, suggesting that Pelo is required to
maintain genomic stability.
*FIELD* RF
1. Adham, I. M.; Sallam, M. A.; Steding, G.; Korabiowska, M.; Brinck,
U.; Hoyer-Fender, S.; Oh, C.; Engel, W.: Disruption of the pelota
gene causes early embryonic lethality and defects in cell cycle progression. Molec.
Cell. Biol. 23: 1470-1476, 2003.
2. Lai, C.-H.; Chou, C.-Y.; Ch'ang, L.-Y.; Liu, C.-S.; Lin, W.: Identification
of novel human genes evolutionarily conserved in Caenorhabditis elegans
by comparative proteomics. Genome Res. 10: 703-713, 2000.
3. Shamsadin, R.; Adham, I. M.; von Beust, G.; Engel, W.: Molecular
cloning, expression and chromosome location of the human pelota gene
PELO. Cytogenet. Cell Genet. 90: 75-78, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 03/27/2003
*FIELD* CD
Dawn Watkins-Chow: 3/22/2001
*FIELD* ED
mgross: 03/27/2003
carol: 3/22/2001
*RECORD*
*FIELD* NO
605757
*FIELD* TI
*605757 PELOTA, DROSOPHILA, HOMOLOG OF; PELO
*FIELD* TX
CLONING
Using degenerate primers designed to the Drosophila pelota gene
read moresequence, Shamsadin et al. (2000) cloned a human PELO cDNA from a testis
cDNA library. Lai et al. (2000) also identified human PELO, which they
called CGI-17, by EST database searching against the C. elegans proteome
sequence. The PELO cDNA encodes a 385-amino acid protein with a
conserved nuclear localization signal. It shares 70%, 57%, and 36%
sequence identity with Drosophila pelota protein, C. elegans R74.6, and
yeast DOM34, respectively. By Northern blot analysis, Shamsadin et al.
(2000) detected a 1.6-kb PELO transcript in all tissues tested as well
as a 2.0-kb testis-specific transcript. By dot blot analysis, Lai et al.
(2000) detected PELO expression most abundantly in fetal kidney, spleen,
and lung, and in placenta, lung, spleen, kidney, and adrenal gland.
GENE FUNCTION
Shamsadin et al. (2000) noted that studies of the Drosophila pelota gene
indicate a role in spermatogenesis, mitotic division, and patterning,
and that mutations in the related yeast DOM34 gene result in
disturbances in the cell cycle and in meiotic cell division.
MAPPING
Shamsadin et al. (2000) mapped the PELO gene to 5q11.2 by fluorescence
in situ hybridization.
ANIMAL MODEL
Adham et al. (2003) developed mice deficient in Pelo and found that
homozygous deletion was embryonic lethal. Homozygous Pelo null embryos
failed to develop past embryonic day 7.5 (E7.5). In culture, mitotic
inactive trophoplasts survived, while mitotic active inner cell mass of
null blastocysts failed to expand in growth, indicating that the
lethality of Pelo null embryos was due to a defect in cell
proliferation. Analysis of the cellular DNA content revealed a
significant increase of aneuploid cells in Pelo null embryos at E7.5.
Adham et al. (2003) hypothesized that an increase in aneuploid cells at
E7.5 caused arrested development, suggesting that Pelo is required to
maintain genomic stability.
*FIELD* RF
1. Adham, I. M.; Sallam, M. A.; Steding, G.; Korabiowska, M.; Brinck,
U.; Hoyer-Fender, S.; Oh, C.; Engel, W.: Disruption of the pelota
gene causes early embryonic lethality and defects in cell cycle progression. Molec.
Cell. Biol. 23: 1470-1476, 2003.
2. Lai, C.-H.; Chou, C.-Y.; Ch'ang, L.-Y.; Liu, C.-S.; Lin, W.: Identification
of novel human genes evolutionarily conserved in Caenorhabditis elegans
by comparative proteomics. Genome Res. 10: 703-713, 2000.
3. Shamsadin, R.; Adham, I. M.; von Beust, G.; Engel, W.: Molecular
cloning, expression and chromosome location of the human pelota gene
PELO. Cytogenet. Cell Genet. 90: 75-78, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 03/27/2003
*FIELD* CD
Dawn Watkins-Chow: 3/22/2001
*FIELD* ED
mgross: 03/27/2003
carol: 3/22/2001