Q02455 (MLP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein MLP1

Alternative name(s):
Myosin-like protein 1

Gene names

Name:	MLP1
Ordered Locus Names:	YKR095W
ORF Names:	YKR415

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	1875 AA.
Sequence status	Complete.
Protein existence	Evidence 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'.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transport mRNA transport
Cellular component	Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of protein import into nucleus during spindle assembly checkpoint Inferred from genetic interaction PubMed 23177738. Source: SGD nuclear retention of unspliced pre-mRNA at the site of transcription Inferred from mutant phenotype Ref.11. Source: SGD poly(A)+ mRNA export from nucleus Inferred from mutant phenotype PubMed 21036941. Source: SGD protein import into nucleus Inferred from genetic interaction Ref.5. Source: SGD protein localization to nuclear pore Inferred from mutant phenotype PubMed 19933151. Source: SGD telomere tethering at nuclear periphery Inferred from genetic interaction Ref.6. Source: SGD transcriptional activation by promoter-terminator looping Inferred from mutant phenotype PubMed 19933151. Source: SGD
Cellular_component	integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD nuclear envelope Inferred from direct assay Ref.5. Source: SGD nuclear pore Inferred from electronic annotation. Source: InterPro nucleoplasm Inferred from direct assay Ref.5. 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
MLP2	P40457	2	EBI-11009,EBI-25261
NAB2	P32505	4	EBI-11009,EBI-11770

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1875	1875	Protein MLP1		PRO_0000096501
Regions
	Coiled coil	69 – 487	419	Potential
	Coiled coil	531 – 1678	1148	Potential
	Coiled coil	1834 – 1866	33	Potential
	Motif	1496 – 1565	70	Required for nuclear localization
	Compositional bias	1804 – 1865	62	Glu-rich
Amino acid modifications
	Modified residue	337	1	Phosphothreonine Ref.14 Ref.15
	Modified residue	368	1	Phosphothreonine Ref.15
	Modified residue	379	1	Phosphoserine Ref.15
	Modified residue	621	1	Phosphotyrosine Ref.15
	Modified residue	716	1	Phosphotyrosine Ref.15
	Modified residue	1467	1	Phosphoserine Ref.15
	Modified residue	1670	1	Phosphoserine Ref.15
	Modified residue	1678	1	Phosphoserine Ref.14 Ref.15
	Modified residue	1710	1	Phosphoserine Ref.14 Ref.15
	Modified residue	1723	1	Phosphoserine Ref.15
	Modified residue	1731	1	Phosphoserine Ref.15
	Modified residue	1733	1	Phosphoserine Ref.15
	Modified residue	1779	1	Phosphothreonine Ref.15
	Modified residue	1803	1	Phosphoserine Ref.15
Experimental info
	Sequence conflict	301	1	R → A in AAA34783. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02455 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 683A0D34C9066867	FASTA	1,875	218,456
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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]	"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 THR-337; SER-1678 AND SER-1710, MASS SPECTROMETRY.
[15]	"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; THR-368; SER-379; TYR-621; TYR-716; SER-1467; SER-1670; SER-1678; SER-1710; SER-1723; SER-1731; SER-1733; THR-1779 AND SER-1803, MASS SPECTROMETRY.
+	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.
PIR	S38173.
RefSeq	NP_013021.1. NM_001179885.1.
3D structure databases
ProteinModelPortal	Q02455.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6675N.
IntAct	Q02455. 7 interactions.
MINT	MINT-622372.
STRING	4932.YKR095W.
Protein family/group databases
TCDB	9.A.14.1.1. nuclear pore complex (NPC) family.
Proteomic databases
PaxDb	Q02455.
PeptideAtlas	Q02455.
PRIDE	Q02455.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKR095W; YKR095W; YKR095W.
GeneID	853970.
KEGG	sce:YKR095W.
Organism-specific databases
CYGD	YKR095w.
SGD	S000001803. MLP1.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00700000104019.
HOGENOM	HOG000113604.
KO	K09291.
OMA	TRESTEN.
OrthoDB	EOG4QRMC3.
Gene expression databases
Genevestigator	Q02455.
GermOnline	YKR095W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR012929. TPR_MLP1_2. [Graphical view]
Pfam	PF07926. TPR_MLP1_2. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975413.

Entry information

Entry name

MLP1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program