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P40457 (MLP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. 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 MLP2
Alternative name(s):
Myosin-like protein 2
Gene names
Name:MLP2
Ordered Locus Names:YIL149C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1679 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved together with the closely related MLP1 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.6 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.7 MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring. MLP2 plays a role in the incorporation of components into the spindle pole body. MLP2 is also involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Subunit structure

Component of the spindle pole body core in which it interacts directly with SPC110, SPC42 and SPC29. Interacts with NUP60 and NIC96, which tether it to the nuclear pore complex. Also interacts with YKU70 (HDF1) and MLP1. Ref.4 Ref.5 Ref.6 Ref.10

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body. Note: Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus. Ref.9 Ref.10

Miscellaneous

Present with 2770 molecules/cell in log phase SD medium.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of protein import into nucleus during spindle assembly checkpoint

Inferred from genetic interaction PubMed 23177738. Source: SGD

poly(A)+ mRNA export from nucleus

Inferred from mutant phenotype PubMed 21036941. Source: SGD

posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20932479. Source: SGD

protein import into nucleus

Inferred from electronic annotation. Source: InterPro

regulation of transcription, DNA-templated

Inferred from genetic interaction PubMed 15692572. Source: SGD

spindle pole body organization

Inferred from mutant phenotype Ref.10. Source: SGD

telomere tethering at nuclear periphery

Inferred from genetic interaction Ref.5. Source: SGD

transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 20932479. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from direct assay Ref.3. Source: SGD

nuclear pore nuclear basket

Inferred from direct assay PubMed 24152732. Source: SGD

nucleoplasm

Inferred from direct assay Ref.3. Source: SGD

spindle pole body

Inferred from physical interaction Ref.10. Source: SGD

   Molecular_functionprotein binding

Inferred from physical interaction Ref.10. Source: IntAct

ribonucleoprotein complex binding

Inferred from genetic interaction PubMed 15692572. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16791679Protein MLP2
PRO_0000096502

Regions

Coiled coil32 – 176145 Potential
Coiled coil233 – 466234 Potential
Coiled coil516 – 1064549 Potential
Coiled coil1099 – 1491393 Potential
Motif417 – 43317Bipartite nuclear localization signal 1
Motif639 – 65517Bipartite nuclear localization signal 2
Motif1433 – 144917Bipartite nuclear localization signal 3
Compositional bias467 – 4704Poly-Leu
Compositional bias1393 – 1508116Glu-rich

Amino acid modifications

Modified residue15121Phosphoserine Ref.11
Modified residue16701Phosphoserine Ref.12

Sequences

Sequence LengthMass (Da)Tools
P40457 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 298950CC52202D8F

FASTA1,679195,141
        10         20         30         40         50         60 
MEDKISEFLN VPFESLQGVT YPVLRKLYKK IAKFERSEEE VTKLNVLVDE IKSQYYSRIS 

        70         80         90        100        110        120 
KLKQLLDESS EQKNTAKEEL NGLKDQLNEE RSRYRREIDA LKKQLHVSHE AMREVNDEKR 

       130        140        150        160        170        180 
VKEEYDIWQS RDQGNDSLND DLNKENKLLR RKLMEMENIL QRCKSNAISL QLKYDTSVQE 

       190        200        210        220        230        240 
KELMLQSKKL IEEKLSSFSK KTLTEEVTKS SHVENLEEKL YQMQSNYESV FTYNKFLLNQ 

       250        260        270        280        290        300 
NKQLSQSVEE KVLEMKNLKD TASVEKAEFS KEMTLQKNMN DLLRSQLTSL EKDCSLRAIE 

       310        320        330        340        350        360 
KNDDNSCRNP EHTDVIDELI DTKLRLEKSK NECQRLQNIV MDCTKEEEAT MTTSAVSPTV 

       370        380        390        400        410        420 
GKLFSDIKVL KRQLIKERNQ KFQLQNQLED FILELEHKTP ELISFKERTK SLEHELKRST 

       430        440        450        460        470        480 
ELLETVSLTK RKQEREITSL RQKINGCEAN IHSLVKQRLD LARQVKLLLL NTSAIQETAS 

       490        500        510        520        530        540 
PLSQDELISL RKILESSNIV NENDSQAIIT ERLVEFSNVN ELQEKNVELL NCIRILADKL 

       550        560        570        580        590        600 
ENYEGKQDKT LQKVENQTIK EAKDAIIELE NINAKMETRI NILLRERDSY KLLASTEENK 

       610        620        630        640        650        660 
ANTNSVTSME AAREKKIREL EAELSSTKVE NSAIIQNLRK ELLIYKKSQC KKKTTLEDFE 

       670        680        690        700        710        720 
NFKGLAKEKE RMLEEAIDHL KAELEKQKSW VPSYIHVEKE RASTELSQSR IKIKSLEYEI 

       730        740        750        760        770        780 
SKLKKETASF IPTKESLTRD FEQCCKEKKE LQMRLKESEI SHNENKMDFS SKEGQYKAKI 

       790        800        810        820        830        840 
KELENNLERL RSDLQSKIQE IESIRSCKDS QLKWAQNTID DTEMKMKSLL TELSNKETTI 

       850        860        870        880        890        900 
EKLSSEIENL DKELRKTKFQ YKFLDQNSDA STLEPTLRKE LEQIQVQLKD ANSQIQAYEE 

       910        920        930        940        950        960 
IISSNENALI ELKNELAKTK ENYDAKIELE KKEKWAREED LSRLRGELGE IRALQPKLKE 

       970        980        990       1000       1010       1020 
GALHFVQQSE KLRNEVERIQ KMIEKIEKMS TIVQLCKKKE MSQYQSTMKE NKDLSELVIR 

      1030       1040       1050       1060       1070       1080 
LEKDAADCQA ELTKTKSSLY SAQDLLDKHE RKWMEEKADY ERELISNIEQ TESLRVENSV 

      1090       1100       1110       1120       1130       1140 
LIEKVDDTAA NNGDKDHLKL VSLFSNLRHE RNSLETKLTT CKRELAFVKQ KNDSLEKTIN 

      1150       1160       1170       1180       1190       1200 
DLQRTQTLSE KEYQCSAVII DEFKDITKEV TQVNILKENN AILQKSLKNV TEKNREIYKQ 

      1210       1220       1230       1240       1250       1260 
LNDRQEEISR LQRDLIQTKE QVSINSNKIL VYESEMEQCK QRYQDLSQQQ KDAQKKDIEK 

      1270       1280       1290       1300       1310       1320 
LTNEISDLKG KLSSAENANA DLENKFNRLK KQAHEKLDAS KKQQAALTNE LNELKAIKDK 

      1330       1340       1350       1360       1370       1380 
LEQDLHFENA KVIDLDTKLK AHELQSEDVS RDHEKDTYRT LMEEIESLKK ELQIFKTANS 

      1390       1400       1410       1420       1430       1440 
SSDAFEKLKV NMEKEKDRII DERTKEFEKK LQETLNKSTS SEAEYSKDIE TLKKEWLKEY 

      1450       1460       1470       1480       1490       1500 
EDETLRRIKE AEENLKKRIR LPSEERIQKI ISKRKEELEE EFRKKLKENA GSLTFLDNKG 

      1510       1520       1530       1540       1550       1560 
SGEDAEEELW NSPSKGNSER PSAVAGFINQ KNLKPQEQLK NVKNDVSFND SQSMVTNKEN 

      1570       1580       1590       1600       1610       1620 
NIVDSSAAGN KAIPTFSFGK PFFSSNTSSL QSFQNPFTAS QSNINTNAPL RTLNIQPEVA 

      1630       1640       1650       1660       1670 
VKAAINFSNV TDLTNNSTDG AKITEIGSTS KRPIESGTSS DPDTKKVKES PANDQASNE 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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 MLP1.
[4]"Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p."
Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M., Aebi U., Hurt E.C.
J. Biol. Chem. 275:343-350(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NIC96.
[5]"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, DOUBLE-STRAND BREAK REPAIR, INTERACTION WITH YKU70 (HDF1).
[6]"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, INTERACTION WITH NUP60.
[7]"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.
[8]"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].
[9]"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.
[10]"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: IDENTIFICATION IN THE SPINDLE POLE BODY CORE COMPLEX, INTERACTION WITH MLP1; SPC110; SPC42 AND SPC29, SUBCELLULAR LOCATION, FUNCTION.
[11]"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-1512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[12]"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-1670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38059 Genomic DNA. Translation: CAA86129.1.
BK006942 Genomic DNA. Translation: DAA08404.1.
PIRS48385.
RefSeqNP_012117.3. NM_001179497.3.

3D structure databases

ProteinModelPortalP40457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34843. 91 interactions.
DIPDIP-2388N.
IntActP40457. 13 interactions.
MINTMINT-707166.
STRING4932.YIL149C.

Proteomic databases

MaxQBP40457.
PaxDbP40457.
PRIDEP40457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL149C; YIL149C; YIL149C.
GeneID854657.
KEGGsce:YIL149C.

Organism-specific databases

CYGDYIL149c.
SGDS000001411. MLP2.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00730000111014.
KOK09291.
OMAMETRINI.
OrthoDBEOG7BP89V.

Enzyme and pathway databases

BioCycYEAST:G3O-31398-MONOMER.

Gene expression databases

GenevestigatorP40457.

Family and domain databases

InterProIPR012929. TPR_MLP1_2.
[Graphical view]
PfamPF07926. TPR_MLP1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977220.
PROP40457.

Entry information

Entry nameMLP2_YEAST
AccessionPrimary (citable) accession number: P40457
Secondary accession number(s): D6VVD8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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