Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39960

- BEM2_YEAST

UniProt

P39960 - BEM2_YEAST

Protein

GTPase-activating protein BEM2/IPL2

Gene

BEM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GTPase-activating protein (GAP) for RHO1 and RHO2. Involved in the control of cellular morphogenesis. Required for proper bud site selection and bud emergence.

    GO - Molecular functioni

    1. guanyl-nucleotide exchange factor activity Source: InterPro
    2. protein binding Source: IntAct
    3. Rho GTPase activator activity Source: SGD

    GO - Biological processi

    1. actin cytoskeleton organization Source: SGD
    2. establishment of cell polarity Source: SGD
    3. negative regulation of Rho protein signal transduction Source: SGD
    4. positive regulation of Rho GTPase activity Source: GOC
    5. small GTPase mediated signal transduction Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30316-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTPase-activating protein BEM2/IPL2
    Alternative name(s):
    Bud emergence protein 2
    Gene namesi
    Name:BEM2
    Synonyms:IPL2, SUP9
    Ordered Locus Names:YER155C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER155c.
    SGDiS000000957. BEM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: SGD
    2. cellular bud tip Source: SGD
    3. cytoplasm Source: SGD
    4. incipient cellular bud site Source: SGD
    5. mating projection tip Source: SGD
    6. plasma membrane Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21672167GTPase-activating protein BEM2/IPL2PRO_0000068858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei129 – 1291Phosphoserine2 Publications
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei1012 – 10121Phosphoserine2 Publications
    Modified residuei1016 – 10161Phosphoserine1 Publication
    Modified residuei1038 – 10381Phosphothreonine1 Publication
    Modified residuei1046 – 10461Phosphoserine2 Publications
    Modified residuei1054 – 10541Phosphoserine1 Publication
    Modified residuei1128 – 11281Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39960.
    PaxDbiP39960.
    PeptideAtlasiP39960.

    Expressioni

    Gene expression databases

    GenevestigatoriP39960.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BUD14P276373EBI-3517,EBI-20747

    Protein-protein interaction databases

    BioGridi36905. 294 interactions.
    DIPiDIP-6580N.
    IntActiP39960. 45 interactions.
    MINTiMINT-651655.
    STRINGi4932.YER155C.

    Structurei

    3D structure databases

    ProteinModelPortaliP39960.
    SMRiP39960. Positions 1948-2144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini592 – 859268Ras-GEFPROSITE-ProRule annotationAdd
    BLAST
    Domaini1846 – 1948103PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini1967 – 2165199Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi16 – 2510Poly-Ser
    Compositional biasi35 – 439Poly-Ser
    Compositional biasi58 – 636Poly-His
    Compositional biasi198 – 20811Poly-AsnAdd
    BLAST
    Compositional biasi253 – 2608Poly-Ser
    Compositional biasi1161 – 11655Poly-Thr

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-GEF domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG279563.
    GeneTreeiENSGT00730000110473.
    HOGENOMiHOG000095195.
    OMAiFGWIIEN.
    OrthoDBiEOG769ZST.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR000651. Ras-like_Gua-exchang_fac_N.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF00617. RasGEF. 1 hit.
    PF00618. RasGEF_N. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF48366. SSF48366. 5 hits.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39960-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLLWSKNR KSSTASASSS STSTSHKTTT ASTASSSSPS SSSQTIRNST     50
    SGASPYMHSH HHHGQGHSHH RGEDNNRDKR KSSVFPPSKQ YTSTSSSQVN 100
    LGMYHSDTNT RSSRSIASTL KDDSPSVCSE DEISNSSSQK SNAQDETPIA 150
    YKKSAHSKDS LLPSRSSSLS PPQSRCSTGT TLEKSLNTSG ISNSSGTNNN 200
    NSNNNNDNEQ KQRNVIHLNS ENYDTTVFKT GWVNKSHGQT VATNYNSSMT 250
    APSSSSSSSS QNLRNDAYSR NRESRFYGND GSSLKNDDSS STTATNSGND 300
    VASARSSMAI DPQMLVPDYR LYRAQLKGCV LNLYKSGLNS NIKFFDPTLP 350
    ASNSSIANEN HQQKKQQTNN QAQAEALHQK QSFGQMGEPI TLDLKYLSEV 400
    YPHPDLRQDS DGKIISGTIE SLCHTVLFYP GPKQSDVPNE KSLSKTHRAV 450
    INLLLMFPLL DHFIKFLKVF NQFGLSFTKN KSRLTNNSTQ FYNISPAVDD 500
    SMTQRLALTA KTILDVFPGF LLDEPMLKTI ISLLDTISLH NDEISNNLKI 550
    KIANKHNELM KLTAFTRSLP MATSSTHELE IILDPSHFLS LDITTLADEV 600
    HHINLKFDKV WAPKFDYSLL YDSKFINRRI VSLNPLVFNN DQNIHFLGRL 650
    LISHLFPTNP EFSKKVTPKV RAELLDKWVQ IGCRFEHLGD MVSWLAVATI 700
    ICSIPVLRSS SWKYVPDQSL KTIFKDWVPT IIQLERRQRT SKSTSSVFIL 750
    APPNLDDDFT RANVISYFGD LLIHADDLPS DTKFKYLEKK INRTKNAFHK 800
    WQQRLQAIDS TRHKTNSTEN VRDNDSPNNV VYQLWKFHLS QPPLNIEGIM 850
    KLSVQHEPPI IDQKAYSTIG SQRSALVTGS YLPILFNELF PNYSLFPKNT 900
    LVGAASDAKL PPPRSSARLS KSLSISEPIP IASNSHTMGS LTDDAMSSKN 950
    DNNKVTGVGK IDGPVIKEMS SKQSNKQRLL KSVRDVFNID MDVFHISDEL 1000
    VFKSVYDNDG KSRPASMVIE TPKRFSQHSS MLINNPATPN QKMRDSLDTT 1050
    GRLSKTLENM DFFNNIGQVS DSLKESIIRV VLKSSSLEKI FDLLVLTSNI 1100
    FSKLVDTKDL ENYYYHQRQR GHSTRGLSDD NIGLLDYAFV KLTMDNDIFT 1150
    ETFFNTYKSF TTTTTVLENM AKRYVGAKSC SVSISKILDR SDDSKMKINE 1200
    DTNLVSSSLY DQNFPVWDMK VTDDENINLI YMAKIQIGAA EAILHLVKNH 1250
    YSDFTDDLCN NSTLLDIIKI MEQEVSTEWP TRIANSKLQK SLPENFVIET 1300
    ENLLTTLTDL FHGIKSAYQK QLYRPIGVNR TQKRITDILN SFNTFSFTDL 1350
    NNIIDDPSFS DDMIRSFQKL HSTNYEDILE WIYQLDNFIS KKFNLVSKKD 1400
    WIVLFQELEL LSKESLVSFF NYPLHFKSSK LINPGYLQLH EFEISNLFTW 1450
    ISTLILKDDN GTESLFFEKL PQSIKLLIKL HTSLTTFFVM EISNVNKSSS 1500
    ERLTTCKVIL QILNYIRWKN GSLDLFDSEE DESPHAICPH IPAFIETAIA 1550
    HAIISPESRN YELSWIKASE KLSDPTKGTQ NLRSISNVLE KIDDIHIKRF 1600
    IEIDDVFSKN CKNLCPCPGW FISRLLEISQ FVPNMSITNS KLINFDKRRF 1650
    VNNIISNVLD LIPNEREFPL DIEMSDENPS KRTTFGRILF NNFEDVNKVY 1700
    RKKTKKVSES EAISERFQEQ GVFNEILVNE IEKIKREARK LEVLLDQEKI 1750
    LKNSAALHQA VPKKNRKSVI ISGTHSDNDH SYNINKNTGQ TPSLGSVMES 1800
    NNSARNRRDS RASFSTNRSS VVSNSSHNGV SKKIGGFFRR PFSIGGFNTS 1850
    SSNYSLNSIL SQEVSSNKSI LPSILPEVDS MQLHDLKPSY SLKTFEIKSI 1900
    MEIINHRNIP AYYYAFKIVM QNGHEYLIQT ASSSDLTEWI KMIKASKRFS 1950
    FHSKKYKGKT HNKIFGVPLE DVCERENTLI PTIVVKLLEE IELRGLDEVG 2000
    LYRIPGSIGS INALKNAFDE EGATDNSFTL EDDRWFEVNA IAGCFKMYLR 2050
    ELPDSLFSHA MVNDFTDLAI KYKAHAMVNE EYKRMMNELL QKLPTCYYQT 2100
    LKRIVFHLNK VHQHVVNNKM DASNLAIVFS MSFINQEDLA NSMGSRLGAV 2150
    QTILQDFIKN PNDYFKQ 2167
    Length:2,167
    Mass (Da):245,430
    Last modified:February 1, 1995 - v1
    Checksum:iDB7F4CD417E898F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35159 Genomic DNA. Translation: CAA84524.1.
    L33832 Genomic DNA. Translation: AAA57132.1.
    U18917 Genomic DNA. Translation: AAB64682.1.
    BK006939 Genomic DNA. Translation: DAA07816.1.
    PIRiS50658.
    RefSeqiNP_011082.3. NM_001179045.3.

    Genome annotation databases

    EnsemblFungiiYER155C; YER155C; YER155C.
    GeneIDi856899.
    KEGGisce:YER155C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35159 Genomic DNA. Translation: CAA84524.1 .
    L33832 Genomic DNA. Translation: AAA57132.1 .
    U18917 Genomic DNA. Translation: AAB64682.1 .
    BK006939 Genomic DNA. Translation: DAA07816.1 .
    PIRi S50658.
    RefSeqi NP_011082.3. NM_001179045.3.

    3D structure databases

    ProteinModelPortali P39960.
    SMRi P39960. Positions 1948-2144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36905. 294 interactions.
    DIPi DIP-6580N.
    IntActi P39960. 45 interactions.
    MINTi MINT-651655.
    STRINGi 4932.YER155C.

    Proteomic databases

    MaxQBi P39960.
    PaxDbi P39960.
    PeptideAtlasi P39960.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER155C ; YER155C ; YER155C .
    GeneIDi 856899.
    KEGGi sce:YER155C.

    Organism-specific databases

    CYGDi YER155c.
    SGDi S000000957. BEM2.

    Phylogenomic databases

    eggNOGi NOG279563.
    GeneTreei ENSGT00730000110473.
    HOGENOMi HOG000095195.
    OMAi FGWIIEN.
    OrthoDBi EOG769ZST.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30316-MONOMER.

    Miscellaneous databases

    NextBioi 983319.

    Gene expression databases

    Genevestigatori P39960.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR000651. Ras-like_Gua-exchang_fac_N.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF00617. RasGEF. 1 hit.
    PF00618. RasGEF_N. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF48366. SSF48366. 5 hits.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Control of cellular morphogenesis by the Ip12/Bem2 GTPase-activating protein: possible role of protein phosphorylation."
      Kim Y., Francisco L., Chen G., Marcotte E., Chan C.S.
      J. Cell Biol. 127:1381-1394(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast."
      Peterson J., Zheng Y., Bender L., Myers A., Cerione R., Bender A.
      J. Cell Biol. 127:1395-1406(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast."
      Chan C.S., Botstein D.
      Genetics 135:677-691(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "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-1012; SER-1016 AND SER-1046, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012; SER-1046 AND SER-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-129 AND SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-129; SER-283; THR-1038 AND SER-1128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBEM2_YEAST
    AccessioniPrimary (citable) accession number: P39960
    Secondary accession number(s): D3DM62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 137 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 1230 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3