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P47170

- IML1_YEAST

UniProt

P47170 - IML1_YEAST

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Protein

Vacuolar membrane-associated protein IML1

Gene

IML1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.1 Publication

GO - Molecular functioni

  1. GTPase activator activity Source: SGD

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. positive regulation of GTPase activity Source: GOC
  3. protein transport Source: UniProtKB-KW
  4. regulation of autophagic vacuole assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31754-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar membrane-associated protein IML1
Alternative name(s):
Increased minichromosome loss protein 1
SEH-associated protein 1
Gene namesi
Name:IML1
Synonyms:SEA1
Ordered Locus Names:YJR138W
ORF Names:J2129
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR138w.
SGDiS000003899. IML1.

Subcellular locationi

Vacuole membrane 2 Publications; Peripheral membrane protein 2 Publications

GO - Cellular componenti

  1. extrinsic component of fungal-type vacuolar membrane Source: SGD
  2. Iml1 complex Source: SGD
  3. Seh1-associated complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15841584Vacuolar membrane-associated protein IML1PRO_0000203123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei680 – 6801Phosphoserine3 Publications
Modified residuei737 – 7371Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47170.
PaxDbiP47170.
PeptideAtlasiP47170.

Expressioni

Gene expression databases

GenevestigatoriP47170.

Interactioni

Subunit structurei

Component of the SEA complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VAC8P399681EBI-25710,EBI-20212

Protein-protein interaction databases

BioGridi33894. 34 interactions.
DIPiDIP-2589N.
IntActiP47170. 21 interactions.
MINTiMINT-423965.
STRINGi4932.YJR138W.

Structurei

3D structure databases

ProteinModelPortaliP47170.
SMRiP47170. Positions 1206-1271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1198 – 127376DEPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the IML1 family.Curated
Contains 1 DEP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG235380.
GeneTreeiENSGT00390000016559.
HOGENOMiHOG000093241.
InParanoidiP47170.
OMAiSMSNEIH.
OrthoDBiEOG7M3J7T.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR027244. IML1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13179. PTHR13179. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF12257. DUF3608. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 1 hit.
[Graphical view]
PROSITEiPS50186. DEP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47170-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFAKLHGKKQ RPISSINSQT PRTSNTTHAN SISLSSGNLI VGSNRNLRQK
60 70 80 90 100
KEQFGSQQRA SGRKLISNKE NDDNVNNGGD NNYDNGERVH RHHIPGLKIK
110 120 130 140 150
AYQAELGYHE SRFSENLVML NLVEFPDIKP GDLVELKTYH KNPSASNGDK
160 170 180 190 200
KIYFIAKDFD GETKRRAKTS NVSILSGQLQ TLLDLPSRSR IWIKLKPNKF
210 220 230 240 250
DLQADVVEFN IKDCLLNRGD MWVLSSKLVD TCVFMDQRLA FLDSIRGTIK
260 270 280 290 300
GIYRNGKKIV SGYIGEQTRI IFRSESARLI FLIQITDEMW NFEETGEQLF
310 320 330 340 350
QKMVNSFFPK IFKKWKDVDT HHTITIAFAI SMDLSDTSFK DLTPGESLKN
360 370 380 390 400
SQDYFRIVVD QVSIIHWVDI METLREEFME IRKDLLNKQT DKGYSVANGR
410 420 430 440 450
FSPVIKSNFL ELVNFATTIL TDPFKQLDLR HTTTHVMIIS PGSGLFDVDY
460 470 480 490 500
SLLRLTGKKL LSLEMTMDLI CLSKAPLHIV PLFRYRDFEN KLHHCVPLWL
510 520 530 540 550
SVFFWNDHDK KSNSEWTPRC KIYDLQMMGI TENELIREVD VEYLQLNKKV
560 570 580 590 600
KSLSEFMNDY DKNAFEVKIL CAGSNTKQSK KLNSKFDTVF ENDVVVKARK
610 620 630 640 650
IPATATTTHG NTKFIWRGPK VALPAIKDIQ KPNVIPDLSI KTIEASFYDD
660 670 680 690 700
CNTTNDKIST PTTSNNDNLE MNDSLVSVRS ADNQNTSLAL DSLKGLSKRN
710 720 730 740 750
SLKDFTQRVI TKFISNIDTS KNKKIKSTLL RDDVDNSPLG SNTPLPSSES
760 770 780 790 800
KISGLKLQQK GLADENVISK RGNLIIKKNL SIFGLPSNEI MSGSPSSYLG
810 820 830 840 850
SSHTRTSSKL SNMSDKAAFI TEGQKSKHDD SNTYSLTQQL KHRISETWVD
860 870 880 890 900
IKSPSIPVSS EFANELLPIR WKDVWPKYVA RKYSKWRSFT TPAELPITIS
910 920 930 940 950
DFPSKDDFDR NFIFRNHSVT LNTDQEQYNQ TYKDLLRDMI YMRLLTGFQI
960 970 980 990 1000
CVGRQVEKIE LSRESGESET VVNKYLDFNQ NDAFKLYLMI DSEIHRITCS
1010 1020 1030 1040 1050
SSGIIDVERY LRKDEANLFD QVPSYIPLVK TRYESSFRDA MIDPLHVKRE
1060 1070 1080 1090 1100
SLNWNQIDQV LAGYGDNLID RKWHGFRAKY VVLPTDIPPN TYSMVINGKS
1110 1120 1130 1140 1150
ETLNPEEIRV EGLRRLIGSI TRSRLRTEKE KKGRKTKREE IQPEVMFYTG
1160 1170 1180 1190 1200
PLYNFINEQQ TSLESSAINF KDSIFVNDNN LLNRNVELSK LAYQIQRGED
1210 1220 1230 1240 1250
RITLVNRKWH WKKHEKCFVG SEMVNWLIRN FSDIDTREDA IKYGQKVMKE
1260 1270 1280 1290 1300
GLFVHVLNKH NFLDGHYFYQ FSPEYVMDTN KLEKTNSHRS TLSDPKQMLR
1310 1320 1330 1340 1350
KASTGSSNDP SAMTPFSSVV PAISASNASV ADAKEPSRPI LMLSNSLVID
1360 1370 1380 1390 1400
VDPAGKSSKQ ESCTVHYDRV HNPDHCFHIR LEWLTTTPKL IDDLVGNWSR
1410 1420 1430 1440 1450
LCERYGLKMI EIPWEELCTI PSVNPFHSFV EIKLAINPWE DPEFKDRELF
1460 1470 1480 1490 1500
AKSKFYYHVY LLKASGFLLD NRASKFLQNQ DIEFDIMYSW GKPQFKYVQY
1510 1520 1530 1540 1550
IHHTGAYVAE LRENGCLFLA PNNIYISRVN PGNIIGKIHS ASSSSLDAQK
1560 1570 1580
VILNFKSTCL DYQKLRSIFL DAKEMWITGK IVED
Length:1,584
Mass (Da):181,949
Last modified:February 1, 1996 - v1
Checksum:iBB8E73FF5B70CCDF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49638 Genomic DNA. Translation: CAA89670.1.
BK006943 Genomic DNA. Translation: DAA08923.1.
PIRiS57161.
RefSeqiNP_012672.1. NM_001181796.2.

Genome annotation databases

EnsemblFungiiYJR138W; YJR138W; YJR138W.
GeneIDi853603.
KEGGisce:YJR138W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49638 Genomic DNA. Translation: CAA89670.1 .
BK006943 Genomic DNA. Translation: DAA08923.1 .
PIRi S57161.
RefSeqi NP_012672.1. NM_001181796.2.

3D structure databases

ProteinModelPortali P47170.
SMRi P47170. Positions 1206-1271.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33894. 34 interactions.
DIPi DIP-2589N.
IntActi P47170. 21 interactions.
MINTi MINT-423965.
STRINGi 4932.YJR138W.

Proteomic databases

MaxQBi P47170.
PaxDbi P47170.
PeptideAtlasi P47170.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR138W ; YJR138W ; YJR138W .
GeneIDi 853603.
KEGGi sce:YJR138W.

Organism-specific databases

CYGDi YJR138w.
SGDi S000003899. IML1.

Phylogenomic databases

eggNOGi NOG235380.
GeneTreei ENSGT00390000016559.
HOGENOMi HOG000093241.
InParanoidi P47170.
OMAi SMSNEIH.
OrthoDBi EOG7M3J7T.

Enzyme and pathway databases

BioCyci YEAST:G3O-31754-MONOMER.

Miscellaneous databases

NextBioi 974433.
PROi P47170.

Gene expression databases

Genevestigatori P47170.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR000591. DEP_dom.
IPR027244. IML1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR13179. PTHR13179. 1 hit.
Pfami PF00610. DEP. 1 hit.
PF12257. DUF3608. 1 hit.
[Graphical view ]
SMARTi SM00049. DEP. 1 hit.
[Graphical view ]
PROSITEi PS50186. DEP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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-680 AND SER-737, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically associates with the vacuole in Saccharomyces cerevisiae."
    Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P., Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C., Rout M.P., Dargemont C.
    Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, FUNCTION.

Entry informationi

Entry nameiIML1_YEAST
AccessioniPrimary (citable) accession number: P47170
Secondary accession number(s): D6VWV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 111 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 279 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3