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Protein

Bud emergence protein 1

Gene

BEM1

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

Functioni

Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.1 Publication

GO - Molecular functioni

  • phosphatidylinositol-3-phosphate binding Source: SGD
  • protein complex scaffold Source: SGD

GO - Biological processi

  • cell morphogenesis involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29141-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bud emergence protein 1
Alternative name(s):
Suppressor of RHO3 protein 1
Gene namesi
Name:BEM1
Synonyms:SRO1
Ordered Locus Names:YBR200W
ORF Names:YBR1412
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR200W.
SGDiS000000404. BEM1.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • cellular bud tip Source: SGD
  • cytoplasm Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • incipient cellular bud site Source: SGD
  • site of polarized growth Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000649081 – 551Bud emergence protein 1Add BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei47PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei258PhosphoserineCombined sources1
Modified residuei458PhosphoserineCombined sources1
Modified residuei461PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP29366.
PRIDEiP29366.

PTM databases

iPTMnetiP29366.

Interactioni

Subunit structurei

Interacts with AXL2 and BUD5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BOI1P380415EBI-3508,EBI-3719
BOI2P399696EBI-3508,EBI-3727
CAF130P532803EBI-3508,EBI-23322
CDC24P1143313EBI-3508,EBI-4220
CLA4P485623EBI-3508,EBI-4750
MPS1P541993EBI-3508,EBI-11224
NBA1Q082296EBI-3508,EBI-36841
STE20Q0349711EBI-3508,EBI-18285

GO - Molecular functioni

  • protein complex scaffold Source: SGD

Protein-protein interaction databases

BioGridi32897. 478 interactors.
DIPiDIP-688N.
IntActiP29366. 52 interactors.
MINTiMINT-581819.

Structurei

Secondary structure

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi160 – 164Combined sources5
Beta strandi170 – 173Combined sources4
Beta strandi178 – 182Combined sources5
Turni189 – 191Combined sources3
Beta strandi192 – 195Combined sources4
Beta strandi198 – 201Combined sources4
Beta strandi205 – 209Combined sources5
Beta strandi217 – 220Combined sources4
Helixi222 – 224Combined sources3
Helixi227 – 231Combined sources5
Turni232 – 235Combined sources4
Helixi239 – 245Combined sources7
Turni246 – 248Combined sources3
Beta strandi283 – 294Combined sources12
Beta strandi297 – 306Combined sources10
Beta strandi311 – 316Combined sources6
Helixi318 – 331Combined sources14
Turni333 – 337Combined sources5
Helixi363 – 381Combined sources19
Helixi385 – 388Combined sources4
Helixi391 – 395Combined sources5
Beta strandi401 – 404Combined sources4
Beta strandi406 – 408Combined sources3
Beta strandi479 – 483Combined sources5
Beta strandi490 – 494Combined sources5
Helixi500 – 511Combined sources12
Beta strandi516 – 520Combined sources5
Beta strandi523 – 525Combined sources3
Helixi533 – 541Combined sources9
Beta strandi546 – 550Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IP9NMR-A472-551[»]
1IPGNMR-A472-551[»]
2CZONMR-A269-418[»]
2KFKNMR-A477-551[»]
2RQVNMR-A156-260[»]
2RQWNMR-A156-260[»]
2V6VX-ray1.50A/B266-413[»]
ProteinModelPortaliP29366.
SMRiP29366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29366.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 132SH3 1PROSITE-ProRule annotationAdd BLAST61
Domaini155 – 217SH3 2PROSITE-ProRule annotationAdd BLAST63
Domaini278 – 404PXPROSITE-ProRule annotationAdd BLAST127
Domaini478 – 551PB1PROSITE-ProRule annotationAdd BLAST74

Sequence similaritiesi

Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

HOGENOMiHOG000246638.
InParanoidiP29366.
KOiK11237.
OMAiKRIMPYI.
OrthoDBiEOG092C1KS9.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR030507. Bem1/Scd2.
IPR000270. PB1_dom.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF182. PTHR10663:SF182. 1 hit.
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKNFKLSKR DSNGSKGRIT SADISTPSHD NGSVIKHIKT VPVRYLSSSS
60 70 80 90 100
TPVKSQRDSS PKNRHNSKDI TSPEKVIKAK YSYQAQTSKE LSFMEGEFFY
110 120 130 140 150
VSGDEKDWYK ASNPSTGKEG VVPKTYFEVF DRTKPSSVNG SNSSSRKVTN
160 170 180 190 200
DSLNMGSLYA IVLYDFKAEK ADELTTYVGE NLFICAHHNC EWFIAKPIGR
210 220 230 240 250
LGGPGLVPVG FVSIIDIATG YATGNDVIED IKSVNLPTVQ EWKSNIARYK
260 270 280 290 300
ASNISLGSVE QQQQQSITKP QNKSAKLVDG ELLVKASVES FGLEDEKYWF
310 320 330 340 350
LVCCELSNGK TRQLKRYYQD FYDLQVQLLD AFPAEAGKLR DAGGQWSKRI
360 370 380 390 400
MPYIPGPVPY VTNSITKKRK EDLNIYVADL VNLPDYISRS EMVHSLFVVL
410 420 430 440 450
NNGFDREFER DENQNNIKTL QENDTATFAT ASQTSNFAST NQDNTLTGED
460 470 480 490 500
LKLNKKLSDL SLSGSKQAPA QSTSGLKTTK IKFYYKDDIF ALMLKGDTTY
510 520 530 540 550
KELRSKIAPR IDTDNFKLQT KLFDGSGEEI KTDSQVSNII QAKLKISVHD

I
Length:551
Mass (Da):61,605
Last modified:December 1, 1992 - v1
Checksum:iFB6C525AE9A19181
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63826 Genomic DNA. Translation: CAA45320.1.
Z21487 Genomic DNA. Translation: CAA79687.1.
Z36069 Genomic DNA. Translation: CAA85162.1.
BK006936 Genomic DNA. Translation: DAA07316.1.
PIRiS23400.
RefSeqiNP_009759.3. NM_001178548.3.

Genome annotation databases

EnsemblFungiiYBR200W; YBR200W; YBR200W.
GeneIDi852499.
KEGGisce:YBR200W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63826 Genomic DNA. Translation: CAA45320.1.
Z21487 Genomic DNA. Translation: CAA79687.1.
Z36069 Genomic DNA. Translation: CAA85162.1.
BK006936 Genomic DNA. Translation: DAA07316.1.
PIRiS23400.
RefSeqiNP_009759.3. NM_001178548.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IP9NMR-A472-551[»]
1IPGNMR-A472-551[»]
2CZONMR-A269-418[»]
2KFKNMR-A477-551[»]
2RQVNMR-A156-260[»]
2RQWNMR-A156-260[»]
2V6VX-ray1.50A/B266-413[»]
ProteinModelPortaliP29366.
SMRiP29366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32897. 478 interactors.
DIPiDIP-688N.
IntActiP29366. 52 interactors.
MINTiMINT-581819.

PTM databases

iPTMnetiP29366.

Proteomic databases

MaxQBiP29366.
PRIDEiP29366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR200W; YBR200W; YBR200W.
GeneIDi852499.
KEGGisce:YBR200W.

Organism-specific databases

EuPathDBiFungiDB:YBR200W.
SGDiS000000404. BEM1.

Phylogenomic databases

HOGENOMiHOG000246638.
InParanoidiP29366.
KOiK11237.
OMAiKRIMPYI.
OrthoDBiEOG092C1KS9.

Enzyme and pathway databases

BioCyciYEAST:G3O-29141-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP29366.
PROiP29366.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR030507. Bem1/Scd2.
IPR000270. PB1_dom.
IPR001683. Phox.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF182. PTHR10663:SF182. 1 hit.
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00312. PX. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS51745. PB1. 1 hit.
PS50195. PX. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBEM1_YEAST
AccessioniPrimary (citable) accession number: P29366
Secondary accession number(s): D6VQJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 172 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 6490 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.