P07866 (LTE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide exchange factor LTE1

Alternative name(s):
Low temperature essential protein 1

Gene names

Name:	LTE1
Synonyms:	EIS4, MSI2
Ordered Locus Names:	YAL024C

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	1435 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GDP-GTP exchange factor for TEM1, a Ras-like protein, component of the mitotic exit network (MEN). Activation of TEM1 by LTE1 in the bud ultimately leads to activation of CDC15 followed by the release of CDC14 from the nucleolus, which then inactivates cyclin-dependent kinases (CDKs) activity by several mechanism. Required for TEM1 localization to the bud cortex during mitotic exit. Fine-tunes the timing of the mitotic exit and couples this event with cytokinesis. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Involved in proprotein-processing like proalpha factor-processing in the secretory pathway. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22
Subunit structure	Interacts with CDC24, CDC42, KEL1, KEL2, RAS2 and TEM1. Ref.13 Ref.14 Ref.17
Subcellular location	Cytoplasm. Bud. Note: The localization to the bud requires interaction with KEL1, as well as the presence of septins, CDC42, CLA4 and RAS2. Ref.9 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21
Post-translational modification	Phosphorylated by CDC28 in a cell cycle-dependent manner and in response to nocodazole. Dephosphorylion by CDC14 triggers LTE1 release from bud cortex during the exit of mitosis. Ref.12 Ref.13 Ref.14 Ref.15
Miscellaneous	Present with 304 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the LTE1 family. Contains 1 N-terminal Ras-GEF domain. Contains 1 Ras-GEF domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic spindle orientation checkpoint Traceable author statement PubMed 16039591. Source: SGD regulation of exit from mitosis Traceable author statement Ref.8PubMed 16039591. Source: SGD regulation of small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Inferred from genetic interaction Ref.22. Source: SGD
Cellular_component	cellular bud Inferred from direct assay Ref.17. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	guanyl-nucleotide exchange factor activity Inferred from sequence or structural similarity Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KEL1	P38853	4	EBI-10243,EBI-9619
RAS2	P01120	5	EBI-10243,EBI-14838

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1435	1435	Guanine nucleotide exchange factor LTE1		PRO_0000068884
Regions
	Domain	25 – 157	133	N-terminal Ras-GEF
	Domain	1194 – 1434	241	Ras-GEF
Amino acid modifications
	Modified residue	219	1	Phosphoserine Ref.23
	Modified residue	222	1	Phosphoserine Ref.23
	Modified residue	247	1	Phosphoserine Ref.23
	Modified residue	249	1	Phosphoserine Ref.23
	Modified residue	271	1	Phosphoserine Ref.23
	Modified residue	306	1	Phosphoserine Ref.23
	Modified residue	527	1	Phosphoserine Ref.23
	Modified residue	689	1	Phosphoserine Ref.23
	Modified residue	793	1	Phosphothreonine Ref.23
	Modified residue	948	1	Phosphoserine Ref.23
	Modified residue	956	1	Phosphoserine Ref.23
	Modified residue	1028	1	Phosphoserine Ref.23
Experimental info
	Sequence conflict	998 – 1009	12	TNSNI…SVLTM → LIVHIRKCIDN in BAA04820. Ref.4
	Sequence conflict	1161 – 1163	3	AAQ → GE in AAA34746. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P07866 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: EED7E5150BECA3DE	FASTA	1,435	163,150
	10 20 30 40 50 60 MEIFSQKDYY PTPSSNVISY ESDCVSKPVN SADLPALIVH LSSPLEGVDY NASADFFLIY 70 80 90 100 110 120 RNFITPQDLH DLLIYRFRWC IREITTNAAK AKRRRIGEVA LVRTFVLLRH SILNYFVQDF 130 140 150 160 170 180 LPNITLRLRL IEFLNDKHIE QYPKIISSCI INLKKNWVHC SKLVWENIEL NEPDKLDFDA 190 200 210 220 230 240 WLHYSLKDFT QLESLHKRGS RLSIYARQSF ASPDFRNQSV LSLYKTSDVF RLPEKLQSSN 250 260 270 280 290 300 SSKNQRSPSM LLFPDNTSNV YSKHRIAKEP SVDNESEDMS DSKQKISHLS KVTLVSTLMK 310 320 330 340 350 360 GVDYPSSYAV DKIMPPTPAK KVEFILNSLY IPEDLNEQSG TLQGTSTTSS LDNNSNSNSR 370 380 390 400 410 420 SNTSSMSVLH RSAIGLLAKW MKNHNRHDSS NDKKFMSAIK PANQKPEMDA FVKYVVSISS 430 440 450 460 470 480 LNRKSSKEEE EEFLNSDSSK FDILSARTID EVESLLHLQN QLIEKVQTHS NNNRGPTVNV 490 500 510 520 530 540 DCERREHIHD IKILQQNSFK PSNDNFSAMD NLDLYQTVSS IAQSVISLTN TLNKQLQNNE 550 560 570 580 590 600 SNMQPSPSYD ALQRRKVKSL TTAYYNKMHG SYSAESMRLF DKDNSSSRTD ENGPQRLLFH 610 620 630 640 650 660 ETDKTNSEAI TNMTPRRKNH SQSQKSMTSS PLKNVLPDLK ESSPLNDSRE DTESITYSYD 670 680 690 700 710 720 SELSSSSPPR DTVTKKSRKV RNIVNNTDSP TLKTKTGFLN LREFTFEDTK SLDEKKSTID 730 740 750 760 770 780 GLEKNYDNKE NQESEYESTK KLDNSLDASS EANNYDITTR KKHSSCNHKI KQAVVRPASG 790 800 810 820 830 840 RISISRVQSI AITPTKELSI VDPEQNKSNS VIEEISEIEP LNLEYNKKSA LYSDTSSTVI 850 860 870 880 890 900 SISTSKLFES AQNSPLKQTQ NPQREFPNGT SVSETNRIRL SIAPTIESVV SDLNSITTGS 910 920 930 940 950 960 TVETFETSRD LPVPHQRIIN LREEYQRGNQ DIISNTSSLH ELKTIDLSDS NNDLESPSTH 970 980 990 1000 1010 1020 AKNNKYFFSP DDGSIDVASP MKNVEELKSK FLKNESETNS NISGSVLTMD DIDINDTSSA 1030 1040 1050 1060 1070 1080 RNTRRANSES AFTGSLNKKN LNEIANMLDD SINDDPITVA LMKLEGTYEK IPEKPENTKS 1090 1100 1110 1120 1130 1140 SDAIGIKTSK LADEVEMLNL NNLPSFQNSP AEKRKSLLIE RRRQTIMNIP FTPDQSEKEG 1150 1160 1170 1180 1190 1200 FTSSSPEKID VSANVDVAVQ AAQIQELIGQ YRIHDSRLMI SNNESHVPFI LMYDSLSVAQ 1210 1220 1230 1240 1250 1260 QMTLIEKEIL GEIDWKDLLD LKMKHEGPQV ISWLQLLVRN ETLSGIDLAI SRFNLTVDWI 1270 1280 1290 1300 1310 1320 ISEILLTKSS KMKRNVIQRF IHVADHCRTF QNFNTLMEII LALSSSVVQK FTDAWRLIEP 1330 1340 1350 1360 1370 1380 GDLLTWEELK KIPSLDRNYS TIRNLLNSVN PLVGCVPFIV VYLSDLSANA EKKDWILEDK 1390 1400 1410 1420 1430 VVNYNKFDTN VQIVKNFIQR VQWSKFYTFK VNHELLSKCV YISTLTQEEI NELST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LTE1 of Saccharomyces cerevisiae is a 1435 codon open reading frame that has sequence similarities to guanine nucleotide releasing factors." Keng T., Clark M.W., Storms R.K., Fortin N., Zhong W., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H. Yeast 10:953-958(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Isolation of a CDC25 family gene, MSI2/LTE1, as a multicopy suppressor of ira1." Shirayama M., Matsui Y., Tanaka K., Toh-e A. Yeast 10:451-461(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[5]	"Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: isolation of the MAK16 gene and analysis of an adjacent gene essential for growth at low temperatures." Wickner R.B., Koh T.J., Crowley J.C., O'Neil J., Kaback D.B. Yeast 3:51-57(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1127-1435, FUNCTION.
[6]	"Host function of MAK16: G1 arrest by a mak16 mutant of Saccharomyces cerevisiae." Wickner R.B. Proc. Natl. Acad. Sci. U.S.A. 85:6007-6011(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1404-1435.
[7]	"The yeast TEM1 gene, which encodes a GTP-binding protein, is involved in termination of M phase." Shirayama M., Matsui Y., Toh-e A. Mol. Cell. Biol. 14:7476-7482(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from nucleolar RENT complex." Shou W., Seol J.H., Shevchenko A., Baskerville C., Moazed D., Chen Z.W.S., Jang J., Shevchenko A., Charbonneau H., Deshaies R.J. Cell 97:233-244(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"A mechanism for coupling exit from mitosis to partitioning of the nucleus." Bardin A.J., Visintin R., Amon A. Cell 102:21-31(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Nud1p links astral microtubule organization and the control of exit from mitosis." Gruneberg U., Campbell K., Simpson C., Grindlay J., Schiebel E. EMBO J. 19:6475-6488(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"The surveillance mechanism of the spindle position checkpoint in yeast." Adames N.R., Oberle J.R., Cooper J.A. J. Cell Biol. 153:159-168(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"The Bub2-dependent mitotic pathway in yeast acts every cell cycle and regulates cytokinesis." Lee S.E., Jensen S., Frenz L.M., Johnson A.L., Fesquet D., Johnston L.H. J. Cell Sci. 114:2345-2354(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[13]	"Control of Lte1 localization by cell polarity determinants and Cdc14." Seshan A., Bardin A.J., Amon A. Curr. Biol. 12:2098-2110(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH KEL1.
[14]	"A role for cell polarity proteins in mitotic exit." Hoefken T., Schiebel E. EMBO J. 21:4851-4862(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH CDC24; CDC42; KEL1; KEL2 AND TEM1.
[15]	"Spatial regulation of the guanine nucleotide exchange factor Lte1 in Saccharomyces cerevisiae." Jensen S., Geymonat M., Johnson A.L., Segal M., Johnston L.H. J. Cell Sci. 115:4977-4991(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDC28, DEPHOSPHORYLATION BY CDC14.
[16]	"Septins have a dual role in controlling mitotic exit in budding yeast." Castillon G.A., Adames N.R., Rosello C.H., Seidel H.S., Longtine M.S., Cooper J.A., Heil-Chapdelaine R.A. Curr. Biol. 13:654-658(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]	"Ras recruits mitotic exit regulator Lte1 to the bud cortex in budding yeast." Yoshida S., Ichihashi R., Toh-e A. J. Cell Biol. 161:889-897(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAS2.
[18]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[19]	"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].
[20]	"Temporal coupling of spindle disassembly and cytokinesis is disrupted by deletion of LTE1 in budding yeast." Jensen S., Johnson A.L., Johnston L.H., Segal M. Cell Cycle 3:817-822(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"The differential roles of budding yeast Tem1p, Cdc15p, and Bub2p protein dynamics in mitotic exit." Molk J.N., Schuyler S.C., Liu J.Y., Evans J.G., Salmon E.D., Pellman D., Bloom K. Mol. Biol. Cell 15:1519-1532(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[22]	"A role for Lte1p (a low temperature essential protein involved in mitosis) in proprotein processing in the yeast secretory pathway." Zhao X., Chang A.Y., Toh-e A., Arvan P. J. Biol. Chem. 282:1670-1678(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"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-219; SER-222; SER-247; SER-249; SER-271; SER-306; SER-527; SER-689; THR-793; SER-948; SER-956 AND SER-1028, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L20125 Genomic DNA. Translation: AAA50468.1. U12980 Genomic DNA. Translation: AAC05008.1. D21354 Genomic DNA. Translation: BAA04820.1. M16076 Genomic DNA. Translation: AAA34746.1. J03852 Genomic DNA. Translation: AAA34751.1. BK006935 Genomic DNA. Translation: DAA06964.1.
PIR	BVBYL1. S51997.
RefSeq	NP_009378.1. NM_001178169.1.
3D structure databases
ProteinModelPortal	P07866.
SMR	P07866. Positions 1195-1412.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-337N.
IntAct	P07866. 54 interactions.
MINT	MINT-620988.
STRING	4932.YAL024C.
Proteomic databases
PaxDb	P07866.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL024C; YAL024C; YAL024C.
GeneID	851209.
KEGG	sce:YAL024C.
Organism-specific databases
CYGD	YAL024c.
SGD	S000000022. LTE1.
Phylogenomic databases
eggNOG	NOG330349.
HOGENOM	HOG000066134.
KO	K06681.
OMA	FILMYDS.
OrthoDB	EOG4643NH.
Gene expression databases
Genevestigator	P07866.
GermOnline	YAL024C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.840.10. 1 hit.
InterPro	IPR000651. Ras-like_Gua-exchang_fac_N. IPR019804. Ras_G-nucl-exch_fac_CS. IPR008937. Ras_GEF. IPR023578. Ras_GEF_dom. IPR001895. RasGRF_CDC25. [Graphical view]
PANTHER	PTHR23113. PTHR23113. 1 hit.
Pfam	PF00617. RasGEF. 1 hit. PF00618. RasGEF_N. 1 hit. [Graphical view]
SMART	SM00147. RasGEF. 1 hit. SM00229. RasGEFN. 1 hit. [Graphical view]
SUPFAM	SSF48366. Ras_GEF. 1 hit.
PROSITE	PS00720. RASGEF. 1 hit. PS50009. RASGEF_CAT. 1 hit. PS50212. RASGEF_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968082.

Entry information

Entry name

LTE1_YEAST

Accession

Primary (citable) accession number: P07866
Secondary accession number(s): D6VPJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program