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P39960

- BEM2_YEAST

UniProt

P39960 - BEM2_YEAST

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Protein
GTPase-activating protein BEM2/IPL2
Gene
BEM2, IPL2, SUP9, YER155C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21672167GTPase-activating protein BEM2/IPL2
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini592 – 859268Ras-GEF
Add
BLAST
Domaini1846 – 1948103PH
Add
BLAST
Domaini1967 – 2165199Rho-GAP
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 Ras-GEF domain.
Contains 1 Rho-GAP domain.

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 136 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.

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

Similar proteinsi