Protein BIM1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40013 (BIM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein BIM1

Gene names

Name:	BIM1
Ordered Locus Names:	YER016W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds microtubules.
Subcellular location	Cytoplasm › cytoskeleton.
Miscellaneous	Present with 3630 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the MAPRE family. Contains 1 CH (calponin-homology) domain. Contains 1 EB1 C-terminal domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule depolymerization Inferred from mutant phenotype PubMed 10352017. Source: SGD microtubule nucleation Inferred from physical interaction PubMed 9153752. Source: SGD mitotic sister chromatid cohesion Inferred from mutant phenotype PubMed 14742714. Source: SGD mitotic spindle assembly checkpoint Traceable author statement PubMed 10935617. Source: SGD negative regulation of microtubule depolymerization Inferred from mutant phenotype PubMed 10352017. Source: SGD nuclear migration along microtubule Inferred from mutant phenotype PubMed 10352017. Source: SGD positive regulation of microtubule polymerization Inferred from direct assay PubMed 20392838. Source: SGD
Cellular_component	cytoplasmic microtubule Inferred from direct assay PubMed 10352017. Source: SGD microtubule plus end Inferred from direct assay PubMed 20392838. Source: SGD spindle midzone Inferred from direct assay PubMed 10352017. Source: SGD spindle pole body Inferred from direct assay PubMed 9585415. Source: SGD
Molecular_function	microtubule plus-end binding Inferred from direct assay PubMed 20392838. Source: SGD protein homodimerization activity Inferred from direct assay PubMed 20392838. Source: SGD structural constituent of cytoskeleton Inferred from physical interaction PubMed 9585415. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAM1	P53267	2	EBI-3614,EBI-23268

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 344

344

Protein BIM1

PRO_0000213432

Regions

Domain

8 – 107

100

Domain

188 – 281

EB1 C-terminal

Amino acid modifications

Modified residue

147

Phosphoserine Ref.6 Ref.7

Modified residue

148

Phosphoserine Ref.6 Ref.7

Modified residue

149

Phosphoserine Ref.7

Modified residue

150

Phosphothreonine Ref.6 Ref.7

Modified residue

165

Phosphoserine Ref.5

Modified residue

166

Phosphoserine Ref.6 Ref.7

Modified residue

175

Phosphothreonine Ref.7

Modified residue

176

Phosphoserine Ref.7

Secondary structure

344

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40013 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C9087CB46A32BD74
Show »

FASTA

344

38,362

        10         20         30         40         50         60 
MSAGIGESRT ELLTWLNGLL NLNYKKIEEC GTGAAYCQIM DSIYGDLPMN RVKFNATAEY 

        70         80         90        100        110        120 
EFQTNYKILQ SCFSRHGIEK TVYVDKLIRC KFQDNLEFLQ WLKKHWIRHK DESVYDPDAR 

       130        140        150        160        170        180 
RKYRPIITNN SATKPRTVSN PTTAKRSSST GTGSAMSGGL ATRHSSLGIN GSRKTSVTQG 

       190        200        210        220        230        240 
QLVAIQAELT KSQETIGSLN EEIEQYKGTV STLEIEREFY FNKLRDIEIL VHTTQDLINE 

       250        260        270        280        290        300 
GVYKFNDETI TGHGNGNGGA LLRFVKKVES ILYATAEGFE MNDGEDELND KNLGEHGTVP 

       310        320        330        340 
NQGGYANSNG EVNGNEGSNH DVIMQNDEGE VGVSNNLIID EETF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"BIM1 encodes a microtubule-binding protein in yeast." Schwartz K., Richards K., Botstein D. Mol. Biol. Cell 8:2677-2691(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[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]	"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-165, MASS SPECTROMETRY.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-148; THR-150 AND SER-166, MASS SPECTROMETRY.
[7]	"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-147; SER-148; SER-149; THR-150; SER-166; THR-175 AND SER-176, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18778 Genomic DNA. Translation: AAB64549.1.
BK006939 Genomic DNA. Translation: DAA07668.1.

PIR

S50474.

RefSeq

NP_010932.1. NM_001178907.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QJX	X-ray	1.90	A	1-124	[»]
4E61	X-ray	2.45	A/B	182-282	[»]

ProteinModelPortal

P40013.

SMR

P40013. Positions 8-124, 180-281.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1295N.

IntAct

P40013. 15 interactions.

MINT

MINT-410426.

STRING

4932.YER016W.

Proteomic databases

PaxDb

P40013.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YER016W; YER016W; YER016W.

GeneID

856736.

KEGG

sce:YER016W.

Organism-specific databases

CYGD

YER016w.

SGD

S000000818. BIM1.

Phylogenomic databases

eggNOG

COG5217.

GeneTree

ENSGT00490000043329.

HOGENOM

HOG000198048.

K10436.

OMA

IEECGTG.

OrthoDB

EOG4T7CCR.

Gene expression databases

Genevestigator

P40013.

GermOnline

YER016W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.

InterPro

IPR001715. CH-domain.
IPR004953. EB1_C.
IPR027328. MAPRE.
[Graphical view]

PANTHER

PTHR10623. PTHR10623. 1 hit.

Pfam

PF00307. CH. 1 hit.
PF03271. EB1. 1 hit.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.
SSF140612. SSF140612. 1 hit.

PROSITE

PS50021. CH. False negative.
PS51230. EB1_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40013.

NextBio

982858.

Entry information

Entry name

BIM1_YEAST

Accession

Primary (citable) accession number: P40013
Secondary accession number(s): D3DLR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents