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P07866 (LTE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Guanine nucleotide exchange factor LTE1
Alternative name(s):
Low temperature essential protein 1
Gene names
Name:LTE1
Synonyms:EIS4, MSI2
Ordered Locus Names:YAL024C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1435 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KEL1P388534EBI-10243,EBI-9619
RAS2P011205EBI-10243,EBI-14838

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14351435Guanine nucleotide exchange factor LTE1
PRO_0000068884

Regions

Domain25 – 157133N-terminal Ras-GEF
Domain1194 – 1434241Ras-GEF

Amino acid modifications

Modified residue2711Phosphoserine Ref.24
Modified residue5591Phosphoserine Ref.25
Modified residue6891Phosphoserine Ref.25
Modified residue6911Phosphothreonine Ref.25
Modified residue8081Phosphoserine Ref.25
Modified residue8101Phosphoserine Ref.25
Modified residue10281Phosphoserine Ref.24 Ref.25
Modified residue11091Phosphoserine Ref.25

Experimental info

Sequence conflict998 – 100912TNSNI…SVLTM → LIVHIRKCIDN in BAA04820. Ref.4
Sequence conflict1161 – 11633AAQ → GE in AAA34746. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P07866 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: EED7E5150BECA3DE

FASTA1,435163,150
        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 

« Hide

References

« Hide '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 204508 / S288c.
[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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[24]"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-271 AND SER-1028, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559; SER-689; THR-691; SER-808; SER-810; SER-1028 AND SER-1109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRBVBYL1. S51997.
RefSeqNP_009378.1. NM_001178169.1.

3D structure databases

ProteinModelPortalP07866.
SMRP07866. Positions 14-139, 1195-1434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31742. 389 interactions.
DIPDIP-337N.
IntActP07866. 56 interactions.
MINTMINT-620988.
STRING4932.YAL024C.

Proteomic databases

PaxDbP07866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL024C; YAL024C; YAL024C.
GeneID851209.
KEGGsce:YAL024C.

Organism-specific databases

CYGDYAL024c.
SGDS000000022. LTE1.

Phylogenomic databases

eggNOGNOG330349.
HOGENOMHOG000066134.
KOK06681.
OMAFILMYDS.
OrthoDBEOG75QRC8.

Enzyme and pathway databases

BioCycYEAST:G3O-28835-MONOMER.

Gene expression databases

GenevestigatorP07866.

Family and domain databases

Gene3D1.10.840.10. 1 hit.
InterProIPR000651. 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]
PANTHERPTHR23113. PTHR23113. 1 hit.
PfamPF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
SMARTSM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 2 hits.
PROSITEPS00720. RASGEF. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968082.

Entry information

Entry nameLTE1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

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

Yeast

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

SIMILARITY comments

Index of protein domains and families