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Q02455

- MLP1_YEAST

UniProt

Q02455 - MLP1_YEAST

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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 – 3371Phosphothreonine2 Publications
Modified residuei379 – 3791Phosphoserine1 Publication
Modified residuei1670 – 16701Phosphoserine1 Publication
Modified residuei1710 – 17101Phosphoserine2 Publications
Modified residuei1733 – 17331Phosphoserine1 Publication
Modified residuei1803 – 18031Phosphoserine1 Publication

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.
InParanoidiQ02455.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDHDTPMES IQNGENSDER LNAIASFFGC SLEQVKSFDG DVVKHLNDKL
60 70 80 90 100
LQFNELKSEN LKVTVSFDEL KASSLKKIDG LKTEMENVIR ENDKIRKERN
110 120 130 140 150
DTFVKFESVE NEKMKLSSEL EFVKRKLDDL TEEKKETQSN QQRTLKILDE
160 170 180 190 200
RLKEIELVRV ENNRSNSECK KLRSTIMDLE TKQQGYITND LNSRTELERK
210 220 230 240 250
TQELTLLQSN NDWLEKELRS KNEQYLSYRQ KTDKVILDIR NELNRLRNDF
260 270 280 290 300
QMERTNNDVL KQKNNELSKS LQEKLLEIKG LSDSLNSEKQ EFSAEMSLKQ
310 320 330 340 350
RLVDLLESQL NAVKEELNSI RELNTAKVIA DDSKKQTPEN EDLLKELQLT
360 370 380 390 400
KEKLAQCEKE CLRLSSITDE ADEDNENLSA KSSSDFIFLK KQLIKERRTK
410 420 430 440 450
EHLQNQIETF IVELEHKVPI INSFKERTDM LENELNNAAL LLEHTSNEKN
460 470 480 490 500
AKVKELNAKN QKLVECENDL QTLTKQRLDL CRQIQYLLIT NSVSNDSKGP
510 520 530 540 550
LRKEEIQFIQ NIMQEDDSTI TESDSQKVVT ERLVEFKNII QLQEKNAELL
560 570 580 590 600
KVVRNLADKL ESKEKKSKQS LQKIESETVN EAKEAIITLK SEKMDLESRI
610 620 630 640 650
EELQKELEEL KTSVPNEDAS YSNVTIKQLT ETKRDLESQV QDLQTRISQI
660 670 680 690 700
TRESTENMSL LNKEIQDLYD SKSDISIKLG KEKSSRILAE ERFKLLSNTL
710 720 730 740 750
DLTKAENDQL RKRFDYLQNT ILKQDSKTHE TLNEYVSCKS KLSIVETELL
760 770 780 790 800
NLKEEQKLRV HLEKNLKQEL NKLSPEKDSL RIMVTQLQTL QKEREDLLEE
810 820 830 840 850
TRKSCQKKID ELEDALSELK KETSQKDHHI KQLEEDNNSN IEWYQNKIEA
860 870 880 890 900
LKKDYESVIT SVDSKQTDIE KLQYKVKSLE KEIEEDKIRL HTYNVMDETI
910 920 930 940 950
NDDSLRKELE KSKINLTDAY SQIKEYKDLY ETTSQSLQQT NSKLDESFKD
960 970 980 990 1000
FTNQIKNLTD EKTSLEDKIS LLKEQMFNLN NELDLQKKGM EKEKADFKKR
1010 1020 1030 1040 1050
ISILQNNNKE VEAVKSEYES KLSKIQNDLD QQTIYANTAQ NNYEQELQKH
1060 1070 1080 1090 1100
ADVSKTISEL REQLHTYKGQ VKTLNLSRDQ LENALKENEK SWSSQKESLL
1110 1120 1130 1140 1150
EQLDLSNSRI EDLSSQNKLL YDQIQIYTAA DKEVNNSTNG PGLNNILITL
1160 1170 1180 1190 1200
RRERDILDTK VTVAERDAKM LRQKISLMDV ELQDARTKLD NSRVEKENHS
1210 1220 1230 1240 1250
SIIQQHDDIM EKLNQLNLLR ESNITLRNEL ENNNNKKKEL QSELDKLKQN
1260 1270 1280 1290 1300
VAPIESELTA LKYSMQEKEQ ELKLAKEEVH RWKKRSQDIL EKHEQLSSSD
1310 1320 1330 1340 1350
YEKLESEIEN LKEELENKER QGAEAEEKFN RLRRQAQERL KTSKLSQDSL
1360 1370 1380 1390 1400
TEQVNSLRDA KNVLENSLSE ANARIEELQN AKVAQGNNQL EAIRKLQEDA
1410 1420 1430 1440 1450
EKASRELQAK LEESTTSYES TINGLNEEIT TLKEEIEKQR QIQQQLQATS
1460 1470 1480 1490 1500
ANEQNDLSNI VESMKKSFEE DKIKFIKEKT QEVNEKILEA QERLNQPSNI
1510 1520 1530 1540 1550
NMEEIKKKWE SEHEQEVSQK IREAEEALKK RIRLPTEEKI NKIIERKKEE
1560 1570 1580 1590 1600
LEKEFEEKVE ERIKSMEQSG EIDVVLRKQL EAKVQEKQKE LENEYNKKLQ
1610 1620 1630 1640 1650
EELKDVPHSS HISDDERDKL RAEIESRLRE EFNNELQAIK KKSFDEGKQQ
1660 1670 1680 1690 1700
AMMKTTLLER KLAKMESQLS ETKQSAESPP KSVNNVQNPL LGLPRKIEEN
1710 1720 1730 1740 1750
SNSPFNPLLS GEKLLKLNSK SSSGGFNPFT SPSPNKHLQN DNDKRESLAN
1760 1770 1780 1790 1800
KTDPPTHLEP SFNIPASRGL ISSSSTLSTD TNDEELTSNN PAQKDSSNRN
1810 1820 1830 1840 1850
VQSEEDTEKK KEGEPVKRGE AIEEQTKSNK RPIDEVGELK NDEDDTTENI
1860 1870
NESKKIKTED EEEKETDKVN DENSI
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.
InParanoidi Q02455.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 134 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