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O00541

- PESC_HUMAN

UniProt

O00541 - PESC_HUMAN

Protein

Pescadillo homolog

Gene

PES1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.3 PublicationsUniRule annotation

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. ribonucleoprotein complex binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
    3. maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
    4. nucleolus organization Source: Ensembl
    5. protein localization to organelle Source: Ensembl
    6. regulation of cell cycle Source: UniProtKB
    7. ribosomal large subunit biogenesis Source: UniProtKB
    8. rRNA processing Source: MGI

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Enzyme and pathway databases

    SignaLinkiO00541.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pescadillo homologUniRule annotation
    Gene namesi
    Name:PES1UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:8848. PES1.

    Subcellular locationi

    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.UniRule annotation

    GO - Cellular componenti

    1. condensed chromosome Source: Ensembl
    2. cytoplasm Source: HPA
    3. membrane Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleoplasm Source: UniProtKB
    6. PeBoW complex Source: UniProtKB
    7. preribosome, large subunit precursor Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi327 – 3271F → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication
    Mutagenesisi347 – 3471I → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication
    Mutagenesisi380 – 3801R → W: Slightly impairs nucleolar localization. 1 Publication
    Mutagenesisi397 – 3971W → R: Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA. 1 Publication

    Organism-specific databases

    PharmGKBiPA33190.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 588588Pescadillo homologPRO_0000186188Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981N6-acetyllysine1 Publication

    Post-translational modificationi

    Sumoylated.

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiO00541.
    PaxDbiO00541.
    PRIDEiO00541.

    2D gel databases

    SWISS-2DPAGEO00541.

    PTM databases

    PhosphoSiteiO00541.

    Expressioni

    Tissue specificityi

    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.

    Inductioni

    By MYC.1 Publication

    Gene expression databases

    ArrayExpressiO00541.
    BgeeiO00541.
    CleanExiHS_PES1.
    GenevestigatoriO00541.

    Organism-specific databases

    HPAiHPA040210.
    HPA062439.

    Interactioni

    Subunit structurei

    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.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BOP1Q141373EBI-1053271,EBI-1050828

    Protein-protein interaction databases

    BioGridi117040. 23 interactions.
    IntActiO00541. 5 interactions.
    MINTiMINT-2997852.
    STRINGi9606.ENSP00000346725.

    Structurei

    Secondary structure

    1
    588
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi331 – 3333
    Beta strandi336 – 3383
    Helixi340 – 34910
    Beta strandi353 – 3553
    Turni358 – 3603
    Beta strandi375 – 3773
    Turni381 – 3833
    Beta strandi390 – 3934
    Helixi396 – 4049
    Turni410 – 4123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EP8NMR-A322-414[»]
    ProteinModelPortaliO00541.
    SMRiO00541. Positions 322-414.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00541.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini322 – 41594BRCTUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 257257Sufficient for nucleolar localizationAdd
    BLAST
    Regioni1 – 5454Required for 28S ribosomal RNA processingAdd
    BLAST
    Regioni306 – 415110Sufficient for interaction with MAP1BBy similarityAdd
    BLAST
    Regioni539 – 58850Required for 28S ribosomal RNA processingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi456 – 53176Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the pescadillo family.UniRule annotation
    Contains 1 BRCT domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG5163.
    HOGENOMiHOG000006022.
    HOVERGENiHBG023409.
    InParanoidiO00541.
    KOiK14843.
    OMAiFKGLKFF.
    OrthoDBiEOG7X9G6N.
    PhylomeDBiO00541.
    TreeFamiTF300671.

    Family and domain databases

    Gene3Di3.40.50.10190. 1 hit.
    HAMAPiMF_03028. Pescadillo.
    InterProiIPR001357. BRCT_dom.
    IPR010613. PES.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF06732. Pescadillo_N. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00541-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH    50
    KKKVNKGSTA ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE 100
    WNTVERLKDN KPNYKLDHII KERYPTFIDA LRDLDDALSM CFLFSTFPRT 150
    GKCHVQTIQL CRRLTVEFMH YIIAARALRK VFLSIKGIYY QAEVLGQPIV 200
    WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ LLNLHYPPKL 250
    EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF 300
    PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF 350
    GGEVSWDKSL CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD 400
    SVNARLLLPV AEYFSGVQLP PHLSPFVTEK EGDYVPPEKL KLLALQRGED 450
    PGNLNESEEE EEEDDNNEGD GDEEGENEEE EEDAEAGSEK EEEARLAALE 500
    EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM KKREKYLYQK 550
    IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE 588
    Length:588
    Mass (Da):68,003
    Last modified:July 1, 1997 - v1
    Checksum:iCB6201D6E34D82B1
    GO
    Isoform 2 (identifier: O00541-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:583
    Mass (Da):67,456
    Checksum:i89BEC8BB4328F707
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti264 – 2641T → S.
    Corresponds to variant rs42942 [ dbSNP | Ensembl ].
    VAR_034375
    Natural varianti370 – 3701D → H.
    Corresponds to variant rs11541876 [ dbSNP | Ensembl ].
    VAR_053570
    Natural varianti411 – 4111A → T.
    Corresponds to variant rs34123894 [ dbSNP | Ensembl ].
    VAR_053571

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei306 – 3105Missing in isoform 2. 1 PublicationVSP_013023

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78310 mRNA. Translation: AAB61140.1.
    CR456539 mRNA. Translation: CAG30425.1.
    AC005006 Genomic DNA. No translation available.
    BC032489 mRNA. Translation: AAH32489.1.
    CCDSiCCDS13880.1. [O00541-1]
    CCDS58802.1. [O00541-2]
    RefSeqiNP_001230154.1. NM_001243225.1. [O00541-2]
    NP_055118.1. NM_014303.3. [O00541-1]
    UniGeneiHs.517543.

    Genome annotation databases

    EnsembliENST00000335214; ENSP00000334612; ENSG00000100029. [O00541-2]
    ENST00000354694; ENSP00000346725; ENSG00000100029. [O00541-1]
    GeneIDi23481.
    KEGGihsa:23481.
    UCSCiuc003aij.2. human. [O00541-1]
    uc003aik.2. human. [O00541-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78310 mRNA. Translation: AAB61140.1 .
    CR456539 mRNA. Translation: CAG30425.1 .
    AC005006 Genomic DNA. No translation available.
    BC032489 mRNA. Translation: AAH32489.1 .
    CCDSi CCDS13880.1. [O00541-1 ]
    CCDS58802.1. [O00541-2 ]
    RefSeqi NP_001230154.1. NM_001243225.1. [O00541-2 ]
    NP_055118.1. NM_014303.3. [O00541-1 ]
    UniGenei Hs.517543.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EP8 NMR - A 322-414 [» ]
    ProteinModelPortali O00541.
    SMRi O00541. Positions 322-414.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117040. 23 interactions.
    IntActi O00541. 5 interactions.
    MINTi MINT-2997852.
    STRINGi 9606.ENSP00000346725.

    PTM databases

    PhosphoSitei O00541.

    2D gel databases

    SWISS-2DPAGE O00541.

    Proteomic databases

    MaxQBi O00541.
    PaxDbi O00541.
    PRIDEi O00541.

    Protocols and materials databases

    DNASUi 23481.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335214 ; ENSP00000334612 ; ENSG00000100029 . [O00541-2 ]
    ENST00000354694 ; ENSP00000346725 ; ENSG00000100029 . [O00541-1 ]
    GeneIDi 23481.
    KEGGi hsa:23481.
    UCSCi uc003aij.2. human. [O00541-1 ]
    uc003aik.2. human. [O00541-2 ]

    Organism-specific databases

    CTDi 23481.
    GeneCardsi GC22M030972.
    HGNCi HGNC:8848. PES1.
    HPAi HPA040210.
    HPA062439.
    MIMi 605819. gene.
    neXtProti NX_O00541.
    PharmGKBi PA33190.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5163.
    HOGENOMi HOG000006022.
    HOVERGENi HBG023409.
    InParanoidi O00541.
    KOi K14843.
    OMAi FKGLKFF.
    OrthoDBi EOG7X9G6N.
    PhylomeDBi O00541.
    TreeFami TF300671.

    Enzyme and pathway databases

    SignaLinki O00541.

    Miscellaneous databases

    ChiTaRSi PES1. human.
    EvolutionaryTracei O00541.
    GeneWikii PES1.
    GenomeRNAii 23481.
    NextBioi 45839.
    PROi O00541.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00541.
    Bgeei O00541.
    CleanExi HS_PES1.
    Genevestigatori O00541.

    Family and domain databases

    Gene3Di 3.40.50.10190. 1 hit.
    HAMAPi MF_03028. Pescadillo.
    InterProi IPR001357. BRCT_dom.
    IPR010613. PES.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF06732. Pescadillo_N. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. 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.

    Entry informationi

    Entry nameiPESC_HUMAN
    AccessioniPrimary (citable) accession number: O00541
    Secondary accession number(s): Q6IC29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 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 22
      Human chromosome 22: 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

    External Data

    Dasty 3