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Q02455 (MLP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein MLP1
Alternative name(s):
Myosin-like protein 1
Gene names
Name:MLP1
Ordered Locus Names:YKR095W
ORF Names:YKR415
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1875 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 Ref.7 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 Ref.8 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with NAB2, a hnRNP required for mRNA export. Also interacts with MLP2. Ref.10 Ref.13

Subcellular location

Nucleus. Note: Distributed fairly evenly along a C-shaped portion of the nuclear periphery, where the spindle pole body localizes in 90% of the cases. Ref.11 Ref.13

Post-translational modification

May be phosphorylated by CDC28. Ref.12

Miscellaneous

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

Caution

Ref.2 misquoted the gene name as 'MPL1'.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLP2P404572EBI-11009,EBI-25261
NAB2P325054EBI-11009,EBI-11770

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 18751874Protein MLP1
PRO_0000096501

Regions

Coiled coil69 – 487419 Potential
Coiled coil531 – 16781148 Potential
Coiled coil1834 – 186633 Potential
Motif1496 – 156570Required for nuclear localization
Compositional bias1804 – 186562Glu-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.16
Modified residue3371Phosphothreonine Ref.14 Ref.15
Modified residue3791Phosphoserine Ref.14
Modified residue16701Phosphoserine Ref.14
Modified residue17101Phosphoserine Ref.14 Ref.15
Modified residue17331Phosphoserine Ref.15
Modified residue18031Phosphoserine Ref.14

Experimental info

Sequence conflict3011R → A in AAA34783. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q02455 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 683A0D34C9066867

FASTA1,875218,456
        10         20         30         40         50         60 
MSDHDTPMES IQNGENSDER LNAIASFFGC SLEQVKSFDG DVVKHLNDKL LQFNELKSEN 

        70         80         90        100        110        120 
LKVTVSFDEL KASSLKKIDG LKTEMENVIR ENDKIRKERN DTFVKFESVE NEKMKLSSEL 

       130        140        150        160        170        180 
EFVKRKLDDL TEEKKETQSN QQRTLKILDE RLKEIELVRV ENNRSNSECK KLRSTIMDLE 

       190        200        210        220        230        240 
TKQQGYITND LNSRTELERK TQELTLLQSN NDWLEKELRS KNEQYLSYRQ KTDKVILDIR 

       250        260        270        280        290        300 
NELNRLRNDF QMERTNNDVL KQKNNELSKS LQEKLLEIKG LSDSLNSEKQ EFSAEMSLKQ 

       310        320        330        340        350        360 
RLVDLLESQL NAVKEELNSI RELNTAKVIA DDSKKQTPEN EDLLKELQLT KEKLAQCEKE 

       370        380        390        400        410        420 
CLRLSSITDE ADEDNENLSA KSSSDFIFLK KQLIKERRTK EHLQNQIETF IVELEHKVPI 

       430        440        450        460        470        480 
INSFKERTDM LENELNNAAL LLEHTSNEKN AKVKELNAKN QKLVECENDL QTLTKQRLDL 

       490        500        510        520        530        540 
CRQIQYLLIT NSVSNDSKGP LRKEEIQFIQ NIMQEDDSTI TESDSQKVVT ERLVEFKNII 

       550        560        570        580        590        600 
QLQEKNAELL KVVRNLADKL ESKEKKSKQS LQKIESETVN EAKEAIITLK SEKMDLESRI 

       610        620        630        640        650        660 
EELQKELEEL KTSVPNEDAS YSNVTIKQLT ETKRDLESQV QDLQTRISQI TRESTENMSL 

       670        680        690        700        710        720 
LNKEIQDLYD SKSDISIKLG KEKSSRILAE ERFKLLSNTL DLTKAENDQL RKRFDYLQNT 

       730        740        750        760        770        780 
ILKQDSKTHE TLNEYVSCKS KLSIVETELL NLKEEQKLRV HLEKNLKQEL NKLSPEKDSL 

       790        800        810        820        830        840 
RIMVTQLQTL QKEREDLLEE TRKSCQKKID ELEDALSELK KETSQKDHHI KQLEEDNNSN 

       850        860        870        880        890        900 
IEWYQNKIEA LKKDYESVIT SVDSKQTDIE KLQYKVKSLE KEIEEDKIRL HTYNVMDETI 

       910        920        930        940        950        960 
NDDSLRKELE KSKINLTDAY SQIKEYKDLY ETTSQSLQQT NSKLDESFKD FTNQIKNLTD 

       970        980        990       1000       1010       1020 
EKTSLEDKIS LLKEQMFNLN NELDLQKKGM EKEKADFKKR ISILQNNNKE VEAVKSEYES 

      1030       1040       1050       1060       1070       1080 
KLSKIQNDLD QQTIYANTAQ NNYEQELQKH ADVSKTISEL REQLHTYKGQ VKTLNLSRDQ 

      1090       1100       1110       1120       1130       1140 
LENALKENEK SWSSQKESLL EQLDLSNSRI EDLSSQNKLL YDQIQIYTAA DKEVNNSTNG 

      1150       1160       1170       1180       1190       1200 
PGLNNILITL RRERDILDTK VTVAERDAKM LRQKISLMDV ELQDARTKLD NSRVEKENHS 

      1210       1220       1230       1240       1250       1260 
SIIQQHDDIM EKLNQLNLLR ESNITLRNEL ENNNNKKKEL QSELDKLKQN VAPIESELTA 

      1270       1280       1290       1300       1310       1320 
LKYSMQEKEQ ELKLAKEEVH RWKKRSQDIL EKHEQLSSSD YEKLESEIEN LKEELENKER 

      1330       1340       1350       1360       1370       1380 
QGAEAEEKFN RLRRQAQERL KTSKLSQDSL TEQVNSLRDA KNVLENSLSE ANARIEELQN 

      1390       1400       1410       1420       1430       1440 
AKVAQGNNQL EAIRKLQEDA EKASRELQAK LEESTTSYES TINGLNEEIT TLKEEIEKQR 

      1450       1460       1470       1480       1490       1500 
QIQQQLQATS ANEQNDLSNI VESMKKSFEE DKIKFIKEKT QEVNEKILEA QERLNQPSNI 

      1510       1520       1530       1540       1550       1560 
NMEEIKKKWE SEHEQEVSQK IREAEEALKK RIRLPTEEKI NKIIERKKEE LEKEFEEKVE 

      1570       1580       1590       1600       1610       1620 
ERIKSMEQSG EIDVVLRKQL EAKVQEKQKE LENEYNKKLQ EELKDVPHSS HISDDERDKL 

      1630       1640       1650       1660       1670       1680 
RAEIESRLRE EFNNELQAIK KKSFDEGKQQ AMMKTTLLER KLAKMESQLS ETKQSAESPP 

      1690       1700       1710       1720       1730       1740 
KSVNNVQNPL LGLPRKIEEN SNSPFNPLLS GEKLLKLNSK SSSGGFNPFT SPSPNKHLQN 

      1750       1760       1770       1780       1790       1800 
DNDKRESLAN KTDPPTHLEP SFNIPASRGL ISSSSTLSTD TNDEELTSNN PAQKDSSNRN 

      1810       1820       1830       1840       1850       1860 
VQSEEDTEKK KEGEPVKRGE AIEEQTKSNK RPIDEVGELK NDEDDTTENI NESKKIKTED 

      1870 
EEEKETDKVN DENSI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"Targets of the cyclin-dependent kinase Cdk1."
Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O.
Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01992 Genomic DNA. Translation: AAA34783.1.
X73541 Genomic DNA. Translation: CAA51948.1.
Z28320 Genomic DNA. Translation: CAA82174.1.
BK006944 Genomic DNA. Translation: DAA09245.1.
PIRS38173.
RefSeqNP_013021.1. NM_001179885.1.

3D structure databases

ProteinModelPortalQ02455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34226. 101 interactions.
DIPDIP-6675N.
IntActQ02455. 8 interactions.
MINTMINT-622372.
STRING4932.YKR095W.

Protein family/group databases

TCDB1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

PaxDbQ02455.
PeptideAtlasQ02455.
PRIDEQ02455.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR095W; YKR095W; YKR095W.
GeneID853970.
KEGGsce:YKR095W.

Organism-specific databases

CYGDYKR095w.
SGDS000001803. MLP1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00730000111014.
HOGENOMHOG000113604.
KOK09291.
OMATRESTEN.
OrthoDBEOG7BP89V.

Enzyme and pathway databases

BioCycYEAST:G3O-32058-MONOMER.

Gene expression databases

GenevestigatorQ02455.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR012929. TPR_MLP1_2.
[Graphical view]
PfamPF07926. TPR_MLP1_2. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975413.
PROQ02455.

Entry information

Entry nameMLP1_YEAST
AccessionPrimary (citable) accession number: Q02455
Secondary accession number(s): D6VXF5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD