Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O00541 (PESC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pescadillo homolog
Gene names
Name:PES1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with IRS1 and UBTF. May interact with MAP1B By similarity. Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and WDR12. The PeBoW complex also associates with the 66S pre-ribosome. Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm. Chromosome. Note: Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli By similarity. Ref.6 Ref.8 Ref.10 Ref.12

Tissue specificity

Significant levels are detected in a variety of cancer cell lines, including glioblastoma, breast carcinoma, colon carcinoma and cervical carcinoma cells. Levels are abnormally elevated in malignant tumors of astrocytic origin.

Induction

By MYC. Ref.9

Post-translational modification

Sumoylated. HAMAP-Rule MF_03028

Sequence similarities

Belongs to the pescadillo family.

Contains 1 BRCT domain.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.10. Source: UniProtKB

maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.10Ref.11. Source: UniProtKB

nucleolus organization

Inferred from electronic annotation. Source: Ensembl

protein localization to organelle

Inferred from electronic annotation. Source: Ensembl

rRNA processing

Inferred from mutant phenotype Ref.10. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype Ref.10. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred by curator Ref.10Ref.11. Source: UniProtKB

   Cellular_componentPeBoW complex

Inferred from direct assay Ref.9Ref.10Ref.11. Source: UniProtKB

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay Ref.10. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

preribosome, large subunit precursor

Inferred from direct assay Ref.10Ref.11. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

ribonucleoprotein complex binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BOP1Q141373EBI-1053271,EBI-1050828

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00541-1)

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.
Isoform 2 (identifier: O00541-2)

The sequence of this isoform differs from the canonical sequence as follows:
     306-310: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Pescadillo homolog HAMAP-Rule MF_03028
PRO_0000186188

Regions

Domain322 – 41594BRCT
Region1 – 257257Sufficient for nucleolar localization HAMAP-Rule MF_03028
Region1 – 5454Required for 28S ribosomal RNA processing HAMAP-Rule MF_03028
Region306 – 415110Sufficient for interaction with MAP1B By similarity
Region539 – 58850Required for 28S ribosomal RNA processing HAMAP-Rule MF_03028
Compositional bias456 – 53176Glu-rich HAMAP-Rule MF_03028

Amino acid modifications

Modified residue981N6-acetyllysine Ref.14

Natural variations

Alternative sequence306 – 3105Missing in isoform 2.
VSP_013023
Natural variant2641T → S.
Corresponds to variant rs42942 [ dbSNP | Ensembl ].
VAR_034375
Natural variant3701D → H.
Corresponds to variant rs11541876 [ dbSNP | Ensembl ].
VAR_053570
Natural variant4111A → T.
Corresponds to variant rs34123894 [ dbSNP | Ensembl ].
VAR_053571

Experimental info

Mutagenesis3271F → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. Ref.12
Mutagenesis3471I → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. Ref.12
Mutagenesis3801R → W: Slightly impairs nucleolar localization. Ref.12
Mutagenesis3971W → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. Ref.12

Secondary structure

..................... 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: CB6201D6E34D82B1

FASTA58868,003
        10         20         30         40         50         60 
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA 

        70         80         90        100        110        120 
ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNTVERLKDN KPNYKLDHII 

       130        140        150        160        170        180 
KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFMH YIIAARALRK 

       190        200        210        220        230        240 
VFLSIKGIYY QAEVLGQPIV WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ 

       250        260        270        280        290        300 
LLNLHYPPKL EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF 

       310        320        330        340        350        360 
PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF GGEVSWDKSL 

       370        380        390        400        410        420 
CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD SVNARLLLPV AEYFSGVQLP 

       430        440        450        460        470        480 
PHLSPFVTEK EGDYVPPEKL KLLALQRGED PGNLNESEEE EEEDDNNEGD GDEEGENEEE 

       490        500        510        520        530        540 
EEDAEAGSEK EEEARLAALE EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM 

       550        560        570        580 
KKREKYLYQK IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE 

« Hide

Isoform 2 [UniParc].

Checksum: 89BEC8BB4328F707
Show »

FASTA58367,456

References

« Hide 'large scale' references
[1]"Insertional mutagenesis in zebrafish identifies two novel genes, pescadillo and dead eye, essential for embryonic development."
Allende M.L., Amsterdam A., Becker T., Kawakami K., Gaiano N., Hopkins N.
Genes Dev. 10:3141-3155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 1).
Tissue: Mammary gland.
[5]"Pescadillo, a novel cell cycle regulatory protein abnormally expressed in malignant cells."
Kinoshita Y., Jarell A.D., Flaman J.-M., Foltz G., Schuster J., Sopher B.L., Irvin D.K., Kanning K., Kornblum H.I., Nelson P.S., Hieter P., Morrison R.S.
J. Biol. Chem. 276:6656-6665(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Yeast Pescadillo is required for multiple activities during 60S ribosomal subunit synthesis."
Oeffinger M., Leung A., Lamond A., Tollervey D.
RNA 8:626-636(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]Erratum
Oeffinger M., Leung A., Lamond A., Tollervey D.
RNA 8:851-851(2002)
[8]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation."
Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.
J. Cell Biol. 170:367-378(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BOP1 AND WDR12, INDUCTION.
[10]"Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex."
Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 34:3030-3043(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12, SUBCELLULAR LOCATION.
[11]"Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit."
Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.
Mol. Cell. Biol. 27:3682-3694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12.
[12]"The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing."
Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 35:789-800(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOP1 AND WDR12, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-327; ILE-347; ARG-380 AND TRP-397.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Solution structure of the BRCT domain from human pescadillo homolog 1."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 322-414.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U78310 mRNA. Translation: AAB61140.1.
CR456539 mRNA. Translation: CAG30425.1.
AC005006 Genomic DNA. No translation available.
BC032489 mRNA. Translation: AAH32489.1.
RefSeqNP_001230154.1. NM_001243225.1.
NP_055118.1. NM_014303.3.
UniGeneHs.517543.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EP8NMR-A322-414[»]
ProteinModelPortalO00541.
SMRO00541. Positions 322-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117040. 22 interactions.
IntActO00541. 5 interactions.
MINTMINT-2997852.
STRING9606.ENSP00000346725.

PTM databases

PhosphoSiteO00541.

2D gel databases

SWISS-2DPAGEO00541.

Proteomic databases

PaxDbO00541.
PRIDEO00541.

Protocols and materials databases

DNASU23481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335214; ENSP00000334612; ENSG00000100029. [O00541-2]
ENST00000354694; ENSP00000346725; ENSG00000100029. [O00541-1]
GeneID23481.
KEGGhsa:23481.
UCSCuc003aij.2. human. [O00541-1]
uc003aik.2. human. [O00541-2]

Organism-specific databases

CTD23481.
GeneCardsGC22M030972.
HGNCHGNC:8848. PES1.
HPAHPA040210.
HPA062439.
MIM605819. gene.
neXtProtNX_O00541.
PharmGKBPA33190.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5163.
HOGENOMHOG000006022.
HOVERGENHBG023409.
InParanoidO00541.
KOK14843.
OMAEEQRMEG.
OrthoDBEOG7X9G6N.
PhylomeDBO00541.
TreeFamTF300671.

Enzyme and pathway databases

SignaLinkO00541.

Gene expression databases

ArrayExpressO00541.
BgeeO00541.
CleanExHS_PES1.
GenevestigatorO00541.

Family and domain databases

Gene3D3.40.50.10190. 1 hit.
HAMAPMF_03028. Pescadillo.
InterProIPR001357. BRCT_dom.
IPR010613. PES.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF06732. Pescadillo_N. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPES1. human.
EvolutionaryTraceO00541.
GeneWikiPES1.
GenomeRNAi23481.
NextBio45839.
PROO00541.
SOURCESearch...

Entry information

Entry namePESC_HUMAN
AccessionPrimary (citable) accession number: O00541
Secondary accession number(s): Q6IC29
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM