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Q99383

- HRP1_YEAST

UniProt

Q99383 - HRP1_YEAST

Protein

Nuclear polyadenylated RNA-binding protein 4

Gene

HRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.4 Publications

    GO - Molecular functioni

    1. mRNA binding Source: SGD
    2. nucleotide binding Source: InterPro
    3. protein binding Source: IntAct
    4. RNA binding Source: SGD

    GO - Biological processi

    1. mRNA cleavage Source: SGD
    2. mRNA polyadenylation Source: SGD
    3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33519-MONOMER.
    ReactomeiREACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear polyadenylated RNA-binding protein 4
    Alternative name(s):
    Cleavage factor IB
    Short name:
    CFIB
    Gene namesi
    Name:HRP1
    Synonyms:NAB4, NAB5
    Ordered Locus Names:YOL123W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL123w.
    SGDiS000005483. HRP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. cytoplasmic stress granule Source: SGD
    3. mRNA cleavage factor complex Source: SGD
    4. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 534534Nuclear polyadenylated RNA-binding protein 4PRO_0000081658Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine3 Publications
    Modified residuei3 – 31Phosphoserine3 Publications
    Modified residuei206 – 2061Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphothreonine1 Publication
    Modified residuei462 – 4621Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99383.
    PaxDbiQ99383.
    PeptideAtlasiQ99383.

    Expressioni

    Gene expression databases

    GenevestigatoriQ99383.

    Interactioni

    Subunit structurei

    Interacts with NAM7.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NAB2P325053EBI-11783,EBI-11770

    Protein-protein interaction databases

    BioGridi34252. 61 interactions.
    DIPiDIP-1371N.
    IntActiQ99383. 33 interactions.
    MINTiMINT-395353.

    Structurei

    Secondary structure

    1
    534
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi157 – 1593
    Beta strandi160 – 1634
    Helixi172 – 1798
    Turni180 – 1823
    Beta strandi185 – 1895
    Turni194 – 1963
    Beta strandi203 – 2097
    Helixi211 – 2188
    Beta strandi223 – 2264
    Helixi236 – 2416
    Beta strandi243 – 2508
    Helixi256 – 2649
    Beta strandi265 – 2673
    Beta strandi270 – 2734
    Beta strandi277 – 2815
    Beta strandi284 – 29310
    Helixi294 – 3029
    Beta strandi304 – 3063
    Beta strandi308 – 3114
    Beta strandi313 – 3175

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CJKNMR-A156-322[»]
    2KM8NMR-C156-322[»]
    ProteinModelPortaliQ99383.
    SMRiQ99383. Positions 117-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99383.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini159 – 24183RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini243 – 32078RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    GeneTreeiENSGT00730000110184.
    HOGENOMiHOG000248803.
    KOiK14411.
    OMAiYQKMQEY.
    OrthoDBiEOG706125.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99383-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSDEEDFND IYGDDKPTTT EEVKKEEEQN KAGSGTSQLD QLAALQALSS    50
    SLNKLNNPNS NNSSSNNSNQ DTSSSKQDGT ANDKEGSNED TKNEKKQESA 100
    TSANANANAS SAGPSGLPWE QLQQTMSQFQ QPSSQSPPQQ QVTQTKEERS 150
    KADLSKESCK MFIGGLNWDT TEDNLREYFG KYGTVTDLKI MKDPATGRSR 200
    GFGFLSFEKP SSVDEVVKTQ HILDGKVIDP KRAIPRDEQD KTGKIFVGGI 250
    GPDVRPKEFE EFFSQWGTII DAQLMLDKDT GQSRGFGFVT YDSADAVDRV 300
    CQNKFIDFKD RKIEIKRAEP RHMQQKSSNN GGNNGGNNMN RRGGNFGNQG 350
    DFNQMYQNPM MGGYNPMMNP QAMTDYYQKM QEYYQQMQKQ TGMDYTQMYQ 400
    QQMQQMAMMM PGFAMPPNAM TLNQPQQDSN ATQGSPAPSD SDNNKSNDVQ 450
    TIGNTSNTDS GSPPLNLPNG PKGPSQYNDD HNSGYGYNRD RGDRDRNDRD 500
    RDYNHRSGGN HRRNGRGGRG GYNRRNNGYH PYNR 534
    Length:534
    Mass (Da):59,650
    Last modified:November 1, 1997 - v1
    Checksum:i1B231069437B093D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35737 Genomic DNA. Translation: AAA79097.1.
    U38535 Genomic DNA. Translation: AAB18142.1.
    X95258 Genomic DNA. Translation: CAA64546.1.
    Z74865 Genomic DNA. Translation: CAA99142.1.
    BK006948 Genomic DNA. Translation: DAA10661.1.
    PIRiS66820.
    RefSeqiNP_014518.1. NM_001183377.1.

    Genome annotation databases

    EnsemblFungiiYOL123W; YOL123W; YOL123W.
    GeneIDi853997.
    KEGGisce:YOL123W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35737 Genomic DNA. Translation: AAA79097.1 .
    U38535 Genomic DNA. Translation: AAB18142.1 .
    X95258 Genomic DNA. Translation: CAA64546.1 .
    Z74865 Genomic DNA. Translation: CAA99142.1 .
    BK006948 Genomic DNA. Translation: DAA10661.1 .
    PIRi S66820.
    RefSeqi NP_014518.1. NM_001183377.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CJK NMR - A 156-322 [» ]
    2KM8 NMR - C 156-322 [» ]
    ProteinModelPortali Q99383.
    SMRi Q99383. Positions 117-322.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34252. 61 interactions.
    DIPi DIP-1371N.
    IntActi Q99383. 33 interactions.
    MINTi MINT-395353.

    Proteomic databases

    MaxQBi Q99383.
    PaxDbi Q99383.
    PeptideAtlasi Q99383.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL123W ; YOL123W ; YOL123W .
    GeneIDi 853997.
    KEGGi sce:YOL123W.

    Organism-specific databases

    CYGDi YOL123w.
    SGDi S000005483. HRP1.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00730000110184.
    HOGENOMi HOG000248803.
    KOi K14411.
    OMAi YQKMQEY.
    OrthoDBi EOG706125.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33519-MONOMER.
    Reactomei REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei Q99383.
    NextBioi 975491.
    PROi Q99383.

    Gene expression databases

    Genevestigatori Q99383.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Oberdorf A.M., Anderson J.T., Devore D.R., Swanson M.S.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Potential RNA binding proteins in Saccharomyces cerevisiae identified as suppressors of temperature-sensitive mutations in NPL3."
      Henry M., Borland C.Z., Bossie M., Silver P.A.
      Genetics 142:103-115(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "DNA sequence analysis of a 10 624 bp fragment of the left arm of chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein, a mitochondrial protein, two ribosomal proteins and two new open reading frames."
      Lafuente M.J., Gamo F.-J., Gancedo C.
      Yeast 12:1041-1045(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3'-end formation in yeast."
      Kessler M.M., Henry M.F., Shen E., Zhao J., Gross S., Silver P.A., Moore C.L.
      Genes Dev. 11:2545-2556(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-189 AND 245-257, FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
    7. "Control of cleavage site selection during mRNA 3' end formation by a yeast hnRNP."
      Minvielle-Sebastia L., Beyer K., Krecic A.M., Hector R.E., Swanson M.S., Keller W.
      EMBO J. 17:7454-7468(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "A specific RNA-protein interaction at yeast polyadenylation efficiency elements."
      Chen S., Hyman L.E.
      Nucleic Acids Res. 26:4965-4974(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    9. "The yeast hnRNP-like protein Hrp1/Nab4 marks a transcript for nonsense-mediated mRNA decay."
      Gonzalez C.I., Ruiz-Echevarria M.J., Vasudevan S., Henry M.F., Peltz S.W.
      Mol. Cell 5:489-499(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NMD, INTERACTION WITH NAM7.
    10. "Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."
      Gross S., Moore C.
      Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA 3'-END FORMATION.
    11. Cited for: SUBCELLULAR LOCATION.
    12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-206; THR-458 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHRP1_YEAST
    AccessioniPrimary (citable) accession number: Q99383
    Secondary accession number(s): D6W1U5, Q02741
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3