<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. GTPase activator activity Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 23716719

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. intracellular signal transduction Source: InterPro
2. positive regulation of GTPase activity Source: GOC

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 23716719

3. protein transport Source: UniProtKB-KW
4. regulation of autophagic vacuole assembly Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 21900499

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Biological processⁱ

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. extrinsic component of fungal-type vacuolar membrane Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 21454883

2. Iml1 complex Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 21900499

3. Seh1-associated complex Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 21454883

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 1584	1584	Vacuolar membrane-associated protein IML1		PRO_0000203123	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	680 – 680	1	Phosphoserine3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.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]. Ref.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]. Ref.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].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	737 – 737	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.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].

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	1198 – 1273	76	DEPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00066			Add BLAST

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        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            

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

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. "The reference genome sequence of Saccharomyces cerevisiae: Then and now."
   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
   G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
   Cited for: GENOME REANNOTATION.
   Strain: ATCC 204508 / S288c.
   
3. "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].
4. "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].
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.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Miscellaneous

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

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

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ