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)

Q02455

- MLP1_YEAST

UniProt

Q02455 - MLP1_YEAST

Protein

Protein MLP1

Gene

MLP1

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 133 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved together with the closely related MLP2 in the structural and functional organization of perinuclear chromatin. MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery. According to PubMed:11862215 some telomeres are tethered to the nuclear periphery through MLP1/MLP2, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing. According to PubMed:12490156 MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring. MLP1 also recognizes the 5'-splice site of pre-mRNAs and retains unspliced pre-mRNA in the nucleus without affecting splicing itself.6 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribonucleoprotein complex binding Source: SGD

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. negative regulation of protein import into nucleus during spindle assembly checkpoint Source: SGD
    3. nuclear retention of unspliced pre-mRNA at the site of transcription Source: SGD
    4. poly(A)+ mRNA export from nucleus Source: SGD
    5. protein import into nucleus Source: SGD
    6. protein localization to nuclear pore Source: SGD
    7. telomere tethering at nuclear periphery Source: SGD
    8. transcriptional activation by promoter-terminator looping Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair, mRNA transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32058-MONOMER.

    Protein family/group databases

    TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein MLP1
    Alternative name(s):
    Myosin-like protein 1
    Gene namesi
    Name:MLP1
    Ordered Locus Names:YKR095W
    ORF Names:YKR415
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKR095w.
    SGDiS000001803. MLP1.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Distributed fairly evenly along a C-shaped portion of the nuclear periphery, where the spindle pole body localizes in 90% of the cases.

    GO - Cellular componenti

    1. nuclear envelope Source: SGD
    2. nuclear pore nuclear basket Source: SGD
    3. nucleoplasm Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 18751874Protein MLP1PRO_0000096501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei337 – 3371Phosphothreonine3 Publications
    Modified residuei379 – 3791Phosphoserine2 Publications
    Modified residuei1670 – 16701Phosphoserine2 Publications
    Modified residuei1710 – 17101Phosphoserine3 Publications
    Modified residuei1733 – 17331Phosphoserine2 Publications
    Modified residuei1803 – 18031Phosphoserine2 Publications

    Post-translational modificationi

    May be phosphorylated by CDC28.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ02455.
    PaxDbiQ02455.
    PeptideAtlasiQ02455.
    PRIDEiQ02455.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02455.

    Interactioni

    Subunit structurei

    Interacts with NAB2, a hnRNP required for mRNA export. Also interacts with MLP2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLP2P404572EBI-11009,EBI-25261
    NAB2P325054EBI-11009,EBI-11770

    Protein-protein interaction databases

    BioGridi34226. 101 interactions.
    DIPiDIP-6675N.
    IntActiQ02455. 8 interactions.
    MINTiMINT-622372.
    STRINGi4932.YKR095W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02455.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili69 – 487419Sequence AnalysisAdd
    BLAST
    Coiled coili531 – 16781148Sequence AnalysisAdd
    BLAST
    Coiled coili1834 – 186633Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1496 – 156570Required for nuclear localizationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1804 – 186562Glu-richAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00730000111014.
    HOGENOMiHOG000113604.
    KOiK09291.
    OMAiTRESTEN.
    OrthoDBiEOG7BP89V.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR012929. TPR_MLP1_2.
    [Graphical view]
    PfamiPF07926. TPR_MLP1_2. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q02455-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDHDTPMES IQNGENSDER LNAIASFFGC SLEQVKSFDG DVVKHLNDKL     50
    LQFNELKSEN LKVTVSFDEL KASSLKKIDG LKTEMENVIR ENDKIRKERN 100
    DTFVKFESVE NEKMKLSSEL EFVKRKLDDL TEEKKETQSN QQRTLKILDE 150
    RLKEIELVRV ENNRSNSECK KLRSTIMDLE TKQQGYITND LNSRTELERK 200
    TQELTLLQSN NDWLEKELRS KNEQYLSYRQ KTDKVILDIR NELNRLRNDF 250
    QMERTNNDVL KQKNNELSKS LQEKLLEIKG LSDSLNSEKQ EFSAEMSLKQ 300
    RLVDLLESQL NAVKEELNSI RELNTAKVIA DDSKKQTPEN EDLLKELQLT 350
    KEKLAQCEKE CLRLSSITDE ADEDNENLSA KSSSDFIFLK KQLIKERRTK 400
    EHLQNQIETF IVELEHKVPI INSFKERTDM LENELNNAAL LLEHTSNEKN 450
    AKVKELNAKN QKLVECENDL QTLTKQRLDL CRQIQYLLIT NSVSNDSKGP 500
    LRKEEIQFIQ NIMQEDDSTI TESDSQKVVT ERLVEFKNII QLQEKNAELL 550
    KVVRNLADKL ESKEKKSKQS LQKIESETVN EAKEAIITLK SEKMDLESRI 600
    EELQKELEEL KTSVPNEDAS YSNVTIKQLT ETKRDLESQV QDLQTRISQI 650
    TRESTENMSL LNKEIQDLYD SKSDISIKLG KEKSSRILAE ERFKLLSNTL 700
    DLTKAENDQL RKRFDYLQNT ILKQDSKTHE TLNEYVSCKS KLSIVETELL 750
    NLKEEQKLRV HLEKNLKQEL NKLSPEKDSL RIMVTQLQTL QKEREDLLEE 800
    TRKSCQKKID ELEDALSELK KETSQKDHHI KQLEEDNNSN IEWYQNKIEA 850
    LKKDYESVIT SVDSKQTDIE KLQYKVKSLE KEIEEDKIRL HTYNVMDETI 900
    NDDSLRKELE KSKINLTDAY SQIKEYKDLY ETTSQSLQQT NSKLDESFKD 950
    FTNQIKNLTD EKTSLEDKIS LLKEQMFNLN NELDLQKKGM EKEKADFKKR 1000
    ISILQNNNKE VEAVKSEYES KLSKIQNDLD QQTIYANTAQ NNYEQELQKH 1050
    ADVSKTISEL REQLHTYKGQ VKTLNLSRDQ LENALKENEK SWSSQKESLL 1100
    EQLDLSNSRI EDLSSQNKLL YDQIQIYTAA DKEVNNSTNG PGLNNILITL 1150
    RRERDILDTK VTVAERDAKM LRQKISLMDV ELQDARTKLD NSRVEKENHS 1200
    SIIQQHDDIM EKLNQLNLLR ESNITLRNEL ENNNNKKKEL QSELDKLKQN 1250
    VAPIESELTA LKYSMQEKEQ ELKLAKEEVH RWKKRSQDIL EKHEQLSSSD 1300
    YEKLESEIEN LKEELENKER QGAEAEEKFN RLRRQAQERL KTSKLSQDSL 1350
    TEQVNSLRDA KNVLENSLSE ANARIEELQN AKVAQGNNQL EAIRKLQEDA 1400
    EKASRELQAK LEESTTSYES TINGLNEEIT TLKEEIEKQR QIQQQLQATS 1450
    ANEQNDLSNI VESMKKSFEE DKIKFIKEKT QEVNEKILEA QERLNQPSNI 1500
    NMEEIKKKWE SEHEQEVSQK IREAEEALKK RIRLPTEEKI NKIIERKKEE 1550
    LEKEFEEKVE ERIKSMEQSG EIDVVLRKQL EAKVQEKQKE LENEYNKKLQ 1600
    EELKDVPHSS HISDDERDKL RAEIESRLRE EFNNELQAIK KKSFDEGKQQ 1650
    AMMKTTLLER KLAKMESQLS ETKQSAESPP KSVNNVQNPL LGLPRKIEEN 1700
    SNSPFNPLLS GEKLLKLNSK SSSGGFNPFT SPSPNKHLQN DNDKRESLAN 1750
    KTDPPTHLEP SFNIPASRGL ISSSSTLSTD TNDEELTSNN PAQKDSSNRN 1800
    VQSEEDTEKK KEGEPVKRGE AIEEQTKSNK RPIDEVGELK NDEDDTTENI 1850
    NESKKIKTED EEEKETDKVN DENSI 1875
    Length:1,875
    Mass (Da):218,456
    Last modified:June 1, 1994 - v2
    Checksum:i683A0D34C9066867
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti301 – 3011R → A in AAA34783. (PubMed:8483450)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01992 Genomic DNA. Translation: AAA34783.1.
    X73541 Genomic DNA. Translation: CAA51948.1.
    Z28320 Genomic DNA. Translation: CAA82174.1.
    BK006944 Genomic DNA. Translation: DAA09245.1.
    PIRiS38173.
    RefSeqiNP_013021.1. NM_001179885.1.

    Genome annotation databases

    EnsemblFungiiYKR095W; YKR095W; YKR095W.
    GeneIDi853970.
    KEGGisce:YKR095W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01992 Genomic DNA. Translation: AAA34783.1 .
    X73541 Genomic DNA. Translation: CAA51948.1 .
    Z28320 Genomic DNA. Translation: CAA82174.1 .
    BK006944 Genomic DNA. Translation: DAA09245.1 .
    PIRi S38173.
    RefSeqi NP_013021.1. NM_001179885.1.

    3D structure databases

    ProteinModelPortali Q02455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34226. 101 interactions.
    DIPi DIP-6675N.
    IntActi Q02455. 8 interactions.
    MINTi MINT-622372.
    STRINGi 4932.YKR095W.

    Protein family/group databases

    TCDBi 1.I.1.1.1. the nuclear pore complex (npc) family.

    Proteomic databases

    MaxQBi Q02455.
    PaxDbi Q02455.
    PeptideAtlasi Q02455.
    PRIDEi Q02455.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKR095W ; YKR095W ; YKR095W .
    GeneIDi 853970.
    KEGGi sce:YKR095W.

    Organism-specific databases

    CYGDi YKR095w.
    SGDi S000001803. MLP1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00730000111014.
    HOGENOMi HOG000113604.
    KOi K09291.
    OMAi TRESTEN.
    OrthoDBi EOG7BP89V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32058-MONOMER.

    Miscellaneous databases

    NextBioi 975413.
    PROi Q02455.

    Gene expression databases

    Genevestigatori Q02455.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR012929. TPR_MLP1_2.
    [Graphical view ]
    Pfami PF07926. TPR_MLP1_2. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new yeast gene with a myosin-like heptad repeat structure."
      Koelling R., Nguyen T., Chen E.Y., Botstein D.
      Mol. Gen. Genet. 237:359-369(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "The complete sequence of a 15,820 bp segment of Saccharomyces cerevisiae chromosome XI contains the UBI2 and MPL1 genes and three new open reading frames."
      Bou G., Esteban P.F., Baladron V., Gonzalez G.A., Cantalejo J.G., Remacha M.A., Jimenez A., del Rey F., Ballesta J.P.G., Revuelta J.L.
      Yeast 9:1349-1354(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Proteins connecting the nuclear pore complex with the nuclear interior."
      Strambio-de-Castillia C., Blobel G., Rout M.P.
      J. Cell Biol. 144:839-855(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FORMATION OF CHROMATIN EXCLUDING FILAMENTOUS STRUCTURES WITH MLP2.
    6. "Nuclear pore complexes in the organization of silent telomeric chromatin."
      Galy V., Olivo-Marin J.-C., Scherthan H., Doye V., Rascalou N., Nehrbass U.
      Nature 403:108-112(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PERINUCLEAR TELOMERE CLUSTERING.
    7. "Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast."
      Feuerbach F., Galy V., Trelles-Sticken E., Fromont-Racine M., Jacquier A., Gilson E., Olivo-Marin J.-C., Scherthan H., Nehrbass U.
      Nat. Cell Biol. 4:214-221(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PERINUCLEAR-DEPENDENT SILENCING.
    8. "Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tel1 pathway of telomere length control."
      Hediger F., Dubrana K., Gasser S.M.
      J. Struct. Biol. 140:79-91(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TELOMERE LENGTH REGULATION.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export."
      Green D.M., Johnson C.P., Hagan H., Corbett A.H.
      Proc. Natl. Acad. Sci. U.S.A. 100:1010-1015(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NAB2.
    11. "Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1."
      Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., Nehrbass U.
      Cell 116:63-73(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR RETENTION OF UNSPLICED PRE-MRNA.
    12. Cited for: PHOSPHORYLATION BY CDC28.
    13. "The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly."
      Niepel M., Strambio-de-Castillia C., Fasolo J., Chait B.T., Rout M.P.
      J. Cell Biol. 170:225-235(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLP2, SUBCELLULAR LOCATION.
    14. "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-337; SER-379; SER-1670; SER-1710 AND SER-1803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 THR-337; SER-1710 AND SER-1733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMLP1_YEAST
    AccessioniPrimary (citable) accession number: Q02455
    Secondary accession number(s): D6VXF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2710 molecules/cell in log phase SD medium.1 Publication

    Caution

    PubMed:8154186 misquoted the gene name as 'MPL1'.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3