P40457 (MLP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein MLP2

Alternative name(s):
Myosin-like protein 2

Gene names

Name:	MLP2
Ordered Locus Names:	YIL149C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1679 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle 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 component	Cytoplasm Cytoskeleton Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative 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-dependent 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
Cellular_component	integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nuclear envelope Inferred from direct assay Ref.3. Source: SGD nuclear pore Inferred from electronic annotation. Source: InterPro nucleoplasm Inferred from direct assay Ref.3. Source: SGD spindle pole body Inferred from physical interaction Ref.10. Source: SGD
Molecular_function	ribonucleoprotein complex binding Inferred from genetic interaction PubMed 15692572. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLP1	Q02455	2	EBI-25261,EBI-11009
SPC110	P32380	3	EBI-25261,EBI-12369
SPC29	P33419	2	EBI-25261,EBI-12041
SPC42	P36094	3	EBI-25261,EBI-17777

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1679	1679	Protein MLP2		PRO_0000096502
Regions
	Coiled coil	32 – 176	145	Potential
	Coiled coil	233 – 466	234	Potential
	Coiled coil	516 – 1064	549	Potential
	Coiled coil	1099 – 1491	393	Potential
	Motif	417 – 433	17	Bipartite nuclear localization signal 1
	Motif	639 – 655	17	Bipartite nuclear localization signal 2
	Motif	1433 – 1449	17	Bipartite nuclear localization signal 3
	Compositional bias	467 – 470	4	Poly-Leu
	Compositional bias	1393 – 1508	116	Glu-rich
Amino acid modifications
	Modified residue	1512	1	Phosphoserine Ref.11
	Modified residue	1659	1	Phosphoserine Ref.13
	Modified residue	1660	1	Phosphoserine Ref.12
	Modified residue	1670	1	Phosphoserine Ref.13

Sequences

	Sequence		Length	Mass (Da)
	P40457 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 298950CC52202D8F	FASTA	1,679	195,141
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1660, MASS SPECTROMETRY.
[13]	"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-1659 AND SER-1670, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38059 Genomic DNA. Translation: CAA86129.1. BK006942 Genomic DNA. Translation: DAA08404.1.
PIR	S48385.
RefSeq	NP_012117.3. NM_001179497.3.
3D structure databases
ProteinModelPortal	P40457.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2388N.
IntAct	P40457. 15 interactions.
MINT	MINT-707166.
STRING	4932.YIL149C.
Protein family/group databases
TCDB	9.A.14.1.1. nuclear pore complex (NPC) family.
Proteomic databases
PaxDb	P40457.
PRIDE	P40457.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL149C; YIL149C; YIL149C.
GeneID	854657.
KEGG	sce:YIL144W. sce:YIL149C.
Organism-specific databases
CYGD	YIL149c.
SGD	S000001411. MLP2.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00690000101702.
KO	K09291. K11547.
OMA	METRINI.
OrthoDB	EOG4QRMC3.
Gene expression databases
Genevestigator	P40457.
GermOnline	YIL149C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012929. TPR_MLP1_2. [Graphical view]
Pfam	PF07926. TPR_MLP1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977220.

Entry information

Entry name

MLP2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program