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P38822 (BZZ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein BZZ1
Alternative name(s):
LAS17-binding protein 7
Gene names
Name:BZZ1
Synonyms:LSB7
Ordered Locus Names:YHR114W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. Ref.4 Ref.6

Subunit structure

Interacts with LAS17 and MYO5. Ref.4

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: localizes in cortical actin patches in a LAS17-dependent manner. Ref.4

Miscellaneous

Present with 5440 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the BZZ1 family.

Contains 1 FCH domain.

Contains 2 SH3 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Protein BZZ1
PRO_0000065033

Regions

Domain5 – 6864FCH
Domain493 – 55563SH3 1
Domain577 – 63357SH3 2
Coiled coil138 – 21073 Potential

Amino acid modifications

Modified residue3271Phosphoserine Ref.7
Modified residue4631Phosphoserine Ref.7 Ref.8
Modified residue4721Phosphoserine Ref.7 Ref.8
Modified residue4761Phosphoserine Ref.7 Ref.8

Experimental info

Sequence conflict1961E → G in AAS56434. Ref.3

Secondary structure

................. 633
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38822 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 5C73DACC69611B41

FASTA63371,171
        10         20         30         40         50         60 
MSADLSIGNE IKDSFKETHK WVQNNLKWLK DIEQFYRERA KLEKDYSERL SRLSAEYFNK 

        70         80         90        100        110        120 
KSSTSVPISV GDTPTTTPGS IEAAGVVAWN EILSQTDMIS KDHDQLSTDF ENHVANQLSG 

       130        140        150        160        170        180 
LFTKLDMTLS KINGFNNDMV NKKDNIYHEL EKAKKDYDEA CSTMEMARNR YTKASNDRNK 

       190        200        210        220        230        240 
KKLDEKEMEM NKCKNEYLIK INQANRTKDK YYFQDVPEVL DLLQDVNEAK TLFLNDLWLK 

       250        260        270        280        290        300 
AASVENDLGA NVSKRLQAAN SVVKQNKPSL NTAIFIKHNL KNWKEPQDFV YKPSPVWHDD 

       310        320        330        340        350        360 
EKFAVPSSLE VEDLRIKLAK AENDYNSLQD KTQNELSKLS TLNKIKHEMK TNEDNINATK 

       370        380        390        400        410        420 
FYDTLKEYLN VVSPFTSHET LKLQAEVQIE SIQNNVPEEY DLSTDNIDLS KTKKKSGIFS 

       430        440        450        460        470        480 
KFKHNILNVD SKPSSGGSTG NGNGGPLHIT SLFNTSRRTR LGSAPNNAGE DSDNNSIRTT 

       490        500        510        520        530        540 
STNNTKKTTQ NSSDDGKNKV LYAYVQKDDD EITITPGDKI SLVARDTGSG WTKINNDTTG 

       550        560        570        580        590        600 
ETGLVPTTYI RISSAATVKA NDRGPAPEVP PPRRSTLPVR TMEAIYAYEA QGDDEISIDP 

       610        620        630 
GDIITVIRGD DGSGWTYGEC DGLKGLFPTS YCK 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [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]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro."
Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R., Winsor B.
Mol. Cell. Biol. 22:7889-7906(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LAS17 AND MYO5.
[5]"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].
[6]"The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis."
Soulard A., Friant S., Fitterer C., Orange C., Kaneva G., Mirey G., Winsor B.
Protoplasma 226:89-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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-327; SER-463; SER-472 AND SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-463; SER-472 AND SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Structural genomics of yeast SH3 domains."
Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M.
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 498-633.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00059 Genomic DNA. Translation: AAB68850.1.
AY558108 Genomic DNA. Translation: AAS56434.1.
BK006934 Genomic DNA. Translation: DAA06808.1.
PIRS48956.
RefSeqNP_011982.1. NM_001179244.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZUUX-ray0.97A498-552[»]
2A28X-ray1.07A/B/C/D582-633[»]
ProteinModelPortalP38822.
SMRP38822. Positions 14-243, 497-552, 582-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36547. 124 interactions.
DIPDIP-2143N.
IntActP38822. 101 interactions.
MINTMINT-474480.
STRING4932.YHR114W.

Proteomic databases

MaxQBP38822.
PaxDbP38822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR114W; YHR114W; YHR114W.
GeneID856514.
KEGGsce:YHR114W.

Organism-specific databases

CYGDYHR114w.
SGDS000001156. BZZ1.

Phylogenomic databases

eggNOGNOG323796.
HOGENOMHOG000185865.
OMANIYHELE.
OrthoDBEOG78SQSK.

Enzyme and pathway databases

BioCycYEAST:G3O-31156-MONOMER.

Gene expression databases

GenevestigatorP38822.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38822.
NextBio982260.
PROP38822.

Entry information

Entry nameBZZ1_YEAST
AccessionPrimary (citable) accession number: P38822
Secondary accession number(s): D3DL64, E9P8V2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references