Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P36102

- PAN3_YEAST

UniProt

P36102 - PAN3_YEAST

Protein

PAB-dependent poly(A)-specific ribonuclease subunit PAN3

Gene

PAN3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA when the poly(A) stretch is bound by poly(A)-binding protein PAB1, which is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs.. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei325 – 3251ATPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri8 – 3730C3H1-typeUniRule annotationAdd
    BLAST
    Nucleotide bindingi305 – 3139ATPUniRule annotation
    Nucleotide bindingi376 – 3816ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein kinase activity Source: InterPro

    GO - Biological processi

    1. DNA repair Source: SGD
    2. mRNA 3'-end processing Source: SGD
    3. postreplication repair Source: SGD
    4. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31832-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PAB-dependent poly(A)-specific ribonuclease subunit PAN3UniRule annotation
    Alternative name(s):
    PAB1P-dependent poly(A)-nucleaseUniRule annotation
    PAN deadenylation complex subunit 3UniRule annotation
    Gene namesi
    Name:PAN3UniRule annotation
    Synonyms:ECM35
    Ordered Locus Names:YKL025C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKL025c.
    SGDiS000001508. PAN3.

    Subcellular locationi

    Cytoplasm 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. PAN complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi156 – 1561F → A: Significantly decreases interaction with PAN1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 679679PAB-dependent poly(A)-specific ribonuclease subunit PAN3PRO_0000058223Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphothreonine2 Publications
    Modified residuei252 – 2521Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by the cyclin-CDK complex PCL1-PHO85.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP36102.
    PaxDbiP36102.
    PeptideAtlasiP36102.

    Expressioni

    Gene expression databases

    GenevestigatoriP36102.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate-specificity of the enzyme complex.4 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAB1P041475EBI-12895,EBI-12823
    PAN2P530103EBI-12895,EBI-12887

    Protein-protein interaction databases

    BioGridi34106. 52 interactions.
    DIPiDIP-3987N.
    IntActiP36102. 8 interactions.
    MINTiMINT-480456.
    STRINGi4932.YKL025C.

    Structurei

    Secondary structure

    1
    679
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi15 – 195
    Helixi24 – 274

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CYKNMR-A1-41[»]
    4Q8JX-ray3.80B/C/E/F/H/I/K/L226-679[»]
    ProteinModelPortaliP36102.
    SMRiP36102. Positions 259-674.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini299 – 549251Protein kinaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni560 – 679120Interaction with PAN2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi143 – 16321PABPC1-interacting motif-2 (PAM-2)Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi114 – 20188Asn-richAdd
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive. However it still binds ATP and ATP-binding is required for mRNA degradation.UniRule annotation

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. PAN3 family.UniRule annotation
    Contains 1 C3H1-type zinc finger.UniRule annotation
    Contains 1 protein kinase domain.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri8 – 3730C3H1-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG260889.
    GeneTreeiENSGT00390000001504.
    HOGENOMiHOG000007619.
    KOiK12572.
    OMAiGPHSQNT.
    OrthoDBiEOG7XM36Z.

    Family and domain databases

    HAMAPiMF_03181. PAN3.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR000571. Znf_CCCH.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P36102-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI    50
    DVGEATTPTM TSVPKFNAKV SASFTPMTVG SDSLTTVTNT TSAATNATGN 100
    IAMAATSATA STVNPMINPI VNSSLVNNNN NNSNISISIP TTASSSNYDP 150
    FNAPIFTPSS TSSIHTNANA HSFPFPSIAN SGGININATD DNSNNMSMAN 200
    NVPPPMQPPP IESSNLKYPR IYPPPHSLLQ YHLYAPEQPS SLKSLLKPNE 250
    RSADQLFIPN NIREDLTKKN LSILQVFPSS GKVIPSIVQD YFNLVPLNFN 300
    NNDFLNKTTL FKVFSNYDGK AYVLKRLPNI DKSMNPNKIS KIYQIWSKIN 350
    CTNLIKFRDI FQTTKFGDLS ICLVFDYYPN SLSLYDYHFV NFPKFPITNN 400
    YLWIYLVQLT NVINSIHSQN LSIGNTLNWR KVLITGDPGR IKLSHCNFMD 450
    LLFNDDTDTV VSSGGSTIEG QQQLDYKYLG ELLFNLSINI ENSNNNTAPK 500
    EYRLEEITPQ SIDDMRQIDD KFKDVLKYLI SDNGDSKKSI HDLTSHFYDK 550
    MFMVLESSQT YTEYMESVLS RELENGRLFR LVNKLNCIFG RIESRIDINW 600
    SESGTKFPII LFYDYVFHQV DSNGKPIMDL THVLRCLNKL DAGIQEKLML 650
    VTPDELNCII ISYKELKDLI ESTFRSITQ 679
    Length:679
    Mass (Da):76,455
    Last modified:June 1, 1994 - v1
    Checksum:iDE03E15BF4A5DA7C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z28025 Genomic DNA. Translation: CAA81860.1.
    BK006944 Genomic DNA. Translation: DAA09129.1.
    PIRiS37842.
    RefSeqiNP_012900.1. NM_001179591.1.

    Genome annotation databases

    EnsemblFungiiYKL025C; YKL025C; YKL025C.
    GeneIDi853843.
    KEGGisce:YKL025C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z28025 Genomic DNA. Translation: CAA81860.1 .
    BK006944 Genomic DNA. Translation: DAA09129.1 .
    PIRi S37842.
    RefSeqi NP_012900.1. NM_001179591.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CYK NMR - A 1-41 [» ]
    4Q8J X-ray 3.80 B/C/E/F/H/I/K/L 226-679 [» ]
    ProteinModelPortali P36102.
    SMRi P36102. Positions 259-674.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34106. 52 interactions.
    DIPi DIP-3987N.
    IntActi P36102. 8 interactions.
    MINTi MINT-480456.
    STRINGi 4932.YKL025C.

    Proteomic databases

    MaxQBi P36102.
    PaxDbi P36102.
    PeptideAtlasi P36102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL025C ; YKL025C ; YKL025C .
    GeneIDi 853843.
    KEGGi sce:YKL025C.

    Organism-specific databases

    CYGDi YKL025c.
    SGDi S000001508. PAN3.

    Phylogenomic databases

    eggNOGi NOG260889.
    GeneTreei ENSGT00390000001504.
    HOGENOMi HOG000007619.
    KOi K12572.
    OMAi GPHSQNT.
    OrthoDBi EOG7XM36Z.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31832-MONOMER.

    Miscellaneous databases

    NextBioi 975058.

    Gene expression databases

    Genevestigatori P36102.

    Family and domain databases

    HAMAPi MF_03181. PAN3.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR000571. Znf_CCCH.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50103. ZF_C3H1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae."
      Brown C.E., Tarun S.Z. Jr., Boeck R., Sachs A.B.
      Mol. Cell. Biol. 16:5744-5753(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 443-453 AND 517-524, FUNCTION, INTERACTION WITH PAN2.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "3'-UTR-dependent deadenylation by the yeast poly(A) nuclease."
      Lowell J.E., Rudner D.Z., Sachs A.B.
      Genes Dev. 6:2088-2099(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation."
      Brown C.E., Sachs A.B.
      Mol. Cell. Biol. 18:6548-6559(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Posttranscriptional regulation of the RAD5 DNA repair gene by the Dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks."
      Hammet A., Pike B.L., Heierhorst J.
      J. Biol. Chem. 277:22469-22474(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DUN1.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. Cited for: INTERACTION WITH PAN2 AND PAB1.
    10. "Yeast mRNA poly(A) tail length control can be reconstituted in vitro in the absence of Pab1p-dependent poly(A) nuclease activity."
      Dheur S., Nykamp K.R., Viphakone N., Swanson M.S., Minvielle-Sebastia L.
      J. Biol. Chem. 280:24532-24538(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Combining chemical genetics and proteomics to identify protein kinase substrates."
      Dephoure N., Howson R.W., Blethrow J.D., Shokat K.M., O'Shea E.K.
      Proc. Natl. Acad. Sci. U.S.A. 102:17940-17945(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PCL1-PHO85.
    12. "Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein."
      Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K.
      J. Biol. Chem. 282:25067-25075(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1, MUTAGENESIS OF PHE-156.
    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 THR-57 AND SER-252, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPAN3_YEAST
    AccessioniPrimary (citable) accession number: P36102
    Secondary accession number(s): D6VXQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1600 molecules/cell in log phase SD medium.1 Publication

    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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3