SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P40457

- MLP2_YEAST

UniProt

P40457 - MLP2_YEAST

(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)

Protein
Protein MLP2
Gene
MLP2, YIL149C
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 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 1 Publication 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 1 Publication 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.7 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. ribonucleoprotein complex binding Source: SGD
Complete GO annotation...

GO - Biological processi

  1. negative regulation of protein import into nucleus during spindle assembly checkpoint Source: SGD
  2. poly(A)+ mRNA export from nucleus Source: SGD
  3. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  4. protein import into nucleus Source: InterPro
  5. regulation of transcription, DNA-templated Source: SGD
  6. spindle pole body organization Source: SGD
  7. telomere tethering at nuclear periphery Source: SGD
  8. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-31398-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MLP2
Alternative name(s):
Myosin-like protein 2
Gene namesi
Name:MLP2
Ordered Locus Names:YIL149C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL149c.
SGDiS000001411. MLP2.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body
Note: Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear envelope Source: SGD
  3. nuclear pore nuclear basket Source: SGD
  4. nucleoplasm Source: SGD
  5. spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16791679Protein MLP2
PRO_0000096502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1512 – 15121Phosphoserine1 Publication
Modified residuei1670 – 16701Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40457.
PaxDbiP40457.
PRIDEiP40457.

Expressioni

Gene expression databases

GenevestigatoriP40457.

Interactioni

Subunit structurei

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 MLP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MLP1Q024552EBI-25261,EBI-11009
SPC110P323803EBI-25261,EBI-12369
SPC29P334192EBI-25261,EBI-12041
SPC42P360943EBI-25261,EBI-17777

Protein-protein interaction databases

BioGridi34843. 91 interactions.
DIPiDIP-2388N.
IntActiP40457. 13 interactions.
MINTiMINT-707166.
STRINGi4932.YIL149C.

Structurei

3D structure databases

ProteinModelPortaliP40457.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili32 – 176145 Reviewed prediction
Add
BLAST
Coiled coili233 – 466234 Reviewed prediction
Add
BLAST
Coiled coili516 – 1064549 Reviewed prediction
Add
BLAST
Coiled coili1099 – 1491393 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi417 – 43317Bipartite nuclear localization signal 1
Add
BLAST
Motifi639 – 65517Bipartite nuclear localization signal 2
Add
BLAST
Motifi1433 – 144917Bipartite nuclear localization signal 3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi467 – 4704Poly-Leu
Compositional biasi1393 – 1508116Glu-rich
Add
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000111014.
KOiK09291.
OMAiMETRINI.
OrthoDBiEOG7BP89V.

Family and domain databases

InterProiIPR012929. TPR_MLP1_2.
[Graphical view]
PfamiPF07926. TPR_MLP1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40457-1 [UniParc]FASTAAdd to Basket

« Hide

MEDKISEFLN VPFESLQGVT YPVLRKLYKK IAKFERSEEE VTKLNVLVDE     50
IKSQYYSRIS KLKQLLDESS EQKNTAKEEL NGLKDQLNEE RSRYRREIDA 100
LKKQLHVSHE AMREVNDEKR VKEEYDIWQS RDQGNDSLND DLNKENKLLR 150
RKLMEMENIL QRCKSNAISL QLKYDTSVQE KELMLQSKKL IEEKLSSFSK 200
KTLTEEVTKS SHVENLEEKL YQMQSNYESV FTYNKFLLNQ NKQLSQSVEE 250
KVLEMKNLKD TASVEKAEFS KEMTLQKNMN DLLRSQLTSL EKDCSLRAIE 300
KNDDNSCRNP EHTDVIDELI DTKLRLEKSK NECQRLQNIV MDCTKEEEAT 350
MTTSAVSPTV GKLFSDIKVL KRQLIKERNQ KFQLQNQLED FILELEHKTP 400
ELISFKERTK SLEHELKRST ELLETVSLTK RKQEREITSL RQKINGCEAN 450
IHSLVKQRLD LARQVKLLLL NTSAIQETAS PLSQDELISL RKILESSNIV 500
NENDSQAIIT ERLVEFSNVN ELQEKNVELL NCIRILADKL ENYEGKQDKT 550
LQKVENQTIK EAKDAIIELE NINAKMETRI NILLRERDSY KLLASTEENK 600
ANTNSVTSME AAREKKIREL EAELSSTKVE NSAIIQNLRK ELLIYKKSQC 650
KKKTTLEDFE NFKGLAKEKE RMLEEAIDHL KAELEKQKSW VPSYIHVEKE 700
RASTELSQSR IKIKSLEYEI SKLKKETASF IPTKESLTRD FEQCCKEKKE 750
LQMRLKESEI SHNENKMDFS SKEGQYKAKI KELENNLERL RSDLQSKIQE 800
IESIRSCKDS QLKWAQNTID DTEMKMKSLL TELSNKETTI EKLSSEIENL 850
DKELRKTKFQ YKFLDQNSDA STLEPTLRKE LEQIQVQLKD ANSQIQAYEE 900
IISSNENALI ELKNELAKTK ENYDAKIELE KKEKWAREED LSRLRGELGE 950
IRALQPKLKE GALHFVQQSE KLRNEVERIQ KMIEKIEKMS TIVQLCKKKE 1000
MSQYQSTMKE NKDLSELVIR LEKDAADCQA ELTKTKSSLY SAQDLLDKHE 1050
RKWMEEKADY ERELISNIEQ TESLRVENSV LIEKVDDTAA NNGDKDHLKL 1100
VSLFSNLRHE RNSLETKLTT CKRELAFVKQ KNDSLEKTIN DLQRTQTLSE 1150
KEYQCSAVII DEFKDITKEV TQVNILKENN AILQKSLKNV TEKNREIYKQ 1200
LNDRQEEISR LQRDLIQTKE QVSINSNKIL VYESEMEQCK QRYQDLSQQQ 1250
KDAQKKDIEK LTNEISDLKG KLSSAENANA DLENKFNRLK KQAHEKLDAS 1300
KKQQAALTNE LNELKAIKDK LEQDLHFENA KVIDLDTKLK AHELQSEDVS 1350
RDHEKDTYRT LMEEIESLKK ELQIFKTANS SSDAFEKLKV NMEKEKDRII 1400
DERTKEFEKK LQETLNKSTS SEAEYSKDIE TLKKEWLKEY EDETLRRIKE 1450
AEENLKKRIR LPSEERIQKI ISKRKEELEE EFRKKLKENA GSLTFLDNKG 1500
SGEDAEEELW NSPSKGNSER PSAVAGFINQ KNLKPQEQLK NVKNDVSFND 1550
SQSMVTNKEN NIVDSSAAGN KAIPTFSFGK PFFSSNTSSL QSFQNPFTAS 1600
QSNINTNAPL RTLNIQPEVA VKAAINFSNV TDLTNNSTDG AKITEIGSTS 1650
KRPIESGTSS DPDTKKVKES PANDQASNE 1679
Length:1,679
Mass (Da):195,141
Last modified:February 1, 1995 - v1
Checksum:i298950CC52202D8F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86129.1.
BK006942 Genomic DNA. Translation: DAA08404.1.
PIRiS48385.
RefSeqiNP_012117.3. NM_001179497.3.

Genome annotation databases

EnsemblFungiiYIL149C; YIL149C; YIL149C.
GeneIDi854657.
KEGGisce:YIL149C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86129.1 .
BK006942 Genomic DNA. Translation: DAA08404.1 .
PIRi S48385.
RefSeqi NP_012117.3. NM_001179497.3.

3D structure databases

ProteinModelPortali P40457.
ModBasei Search...

Protein-protein interaction databases

BioGridi 34843. 91 interactions.
DIPi DIP-2388N.
IntActi P40457. 13 interactions.
MINTi MINT-707166.
STRINGi 4932.YIL149C.

Proteomic databases

MaxQBi P40457.
PaxDbi P40457.
PRIDEi P40457.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL149C ; YIL149C ; YIL149C .
GeneIDi 854657.
KEGGi sce:YIL149C.

Organism-specific databases

CYGDi YIL149c.
SGDi S000001411. MLP2.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000111014.
KOi K09291.
OMAi METRINI.
OrthoDBi EOG7BP89V.

Enzyme and pathway databases

BioCyci YEAST:G3O-31398-MONOMER.

Miscellaneous databases

NextBioi 977220.
PROi P40457.

Gene expression databases

Genevestigatori P40457.

Family and domain databases

InterProi IPR012929. TPR_MLP1_2.
[Graphical view ]
Pfami PF07926. TPR_MLP1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. 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].

Entry informationi

Entry nameiMLP2_YEAST
AccessioniPrimary (citable) accession number: P40457
Secondary accession number(s): D6VVD8
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi