ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P46680

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AIP1_YEAST
Primary accession number P46680
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 79)
Name and origin of the protein
Protein name Actin-interacting protein 1
Synonyms None
Gene name
Name: AIP1
OrderedLocusNames: YMR092C
ORFNames: YM9582.17C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Amberg D.C., Botstein D.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan]
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
Nature 387:90-93(1997).
[3]
 INTERACTION WITH COFILIN, AND FUNCTION.
DOI=10.1083/jcb.145.6.1251; PubMed=10366597 [NCBI, ExPASy, EBI, Israel, Japan]
Rodal A.A., Tetreault J.W., Lappalainen P., Drubin D.G., Amberg D.C.;
"Aip1p interacts with cofilin to disassemble actin filaments.";
J. Cell Biol. 145:1251-1264(1999).
[4]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND TYR-355, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U35666; AAA79141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49259; CAA89239.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S54468; S54468.
RefSeq NP_013810.1; -.
3D structure databases
PDB
1PGU; X-ray; 2.30 A; A/B=1-615.[ExPASy / RCSB / EBI]
1PI6; X-ray; 2.50 A; A=1-615.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PGU; -.
1PI6; -.
ModBase P46680.
Protein-protein interaction databases
DIP DIP:890N; -.
IntAct P46680; -.
Organism-specific databases
CYGD YMR092c; -.
SGD S000004698; AIP1.
Yeast-GFP YMR092C.
Gene expression databases
ArrayExpress P46680; -.
GermOnline YMR092C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030479; Cellular component: actin cortical patch (traceable author statement from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0003779; Molecular function: actin binding (inferred from physical interaction from UniProtKB).
GO:0030042; Biological process: actin filament depolymerization (inferred from genetic interaction from SGD).
GO:0006970; Biological process: response to osmotic stress (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR015943; WD40/YVTN_repeat-like.
IPR001680; WD40_repeat.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
Pfam PF00400; WD40; 5.
Pfam graphical view of domain structure.
PRINTS PR00320; GPROTEINBRPT.
SMART SM00320; WD40; 10.
SMART graphical view of domain structure.
PROSITE PS00678; WD_REPEATS_1; FALSE_NEG.
PS50082; WD_REPEATS_2; 2.
PS50294; WD_REPEATS_REGION; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P46680.
Proteomic databases
PeptideAtlas P46680; -.
Genome annotation databases
Ensembl YMR092C; Saccharomyces cerevisiae. [Contig view]
GeneID 855117; -.
GenomeReviews Z71257_GR; YMR092C.
KEGG sce:YMR092C; -.
NMPDR fig|4932.3.peg.4857; -.
Phylogenomic databases
HOGENOM P46680; -.
Other
LinkHub P46680; -.
ProtoNet P46680.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat; WD repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   615  615     Actin-interacting protein 1. PRO_0000050841
REPEAT   62   109  48     WD 1. 
REPEAT   114   157  44     WD 2. 
REPEAT   158   201  44     WD 3. 
REPEAT   204   244  41     WD 4. 
REPEAT   251   289  39     WD 5. 
REPEAT   337   367  31     WD 6. 
REPEAT   370   406  37     WD 7. 
REPEAT   442   481  40     WD 8. 
REPEAT   486   525  40     WD 9. 
REPEAT   529   578  50     WD 10. 
REPEAT   583   613  31     WD 11. 
COMPBIAS   363   366  4     Poly-Ser. 
MOD_RES   354   354        Phosphoserine. 
MOD_RES   355   355        Phosphotyrosine. 
STRAND   4    10  7      
STRAND   25    27  3      
TURN   28    31  4      
STRAND   32    37  6      
STRAND   40    45  6      
STRAND   55    59  5      
TURN   61    64  4      
STRAND   67    72  6      
STRAND   80    85  6      
STRAND   88    98  11      
TURN   99   102  4      
STRAND   103   113  11      
STRAND   119   124  6      
STRAND   128   135  8      
STRAND   141   146  6      
TURN   147   149  3      
STRAND   152   155  4      
STRAND   163   168  6      
STRAND   170   173  4      
STRAND   175   180  6      
TURN   181   183  3      
STRAND   184   189  6      
TURN   190   192  3      
STRAND   193   199  7      
STRAND   201   203  3      
STRAND   209   214  6      
STRAND   221   226  6      
STRAND   231   235  5      
TURN   236   238  3      
STRAND   241   244  4      
STRAND   256   271  16      
STRAND   274   280  7      
TURN   281   284  4      
STRAND   285   291  7      
HELIX   297   299  3      
STRAND   301   308  8      
STRAND   311   316  6      
STRAND   321   325  5      
STRAND   328   335  8      
STRAND   342   346  5      
TURN   347   350  4      
STRAND   351   354  4      
STRAND   359   361  3      
TURN   362   365  4      
STRAND   366   368  3      
STRAND   375   379  5      
STRAND   387   390  4      
TURN   391   393  3      
STRAND   394   397  4      
STRAND   400   404  5      
STRAND   409   414  6      
STRAND   416   424  9      
STRAND   427   433  7      
TURN   434   436  3      
STRAND   439   444  6      
STRAND   449   454  6      
STRAND   456   463  8      
TURN   464   466  3      
STRAND   469   473  5      
STRAND   476   482  7      
STRAND   491   496  6      
STRAND   500   507  8      
STRAND   512   516  5      
TURN   517   520  4      
STRAND   521   524  4      
STRAND   534   539  6      
STRAND   555   560  6      
STRAND   565   571  7      
STRAND   577   579  3      
STRAND   587   594  8      
STRAND   597   602  6      
STRAND   607   612  6      
Sequence information
Length: 615 AA [This is the length of the unprocessed precursor] Molecular weight: 67326 Da [This is the MW of the unprocessed precursor] CRC64: B8340BF68DD08257 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSSISLKEII PPQPSTQRNF TTHLSYDPTT NAIAYPCGKS AFVRCLDDGD SKVPPVVQFT 

        70         80         90        100        110        120 
GHGSSVVTTV KFSPIKGSQY LCSGDESGKV IVWGWTFDKE SNSVEVNVKS EFQVLAGPIS 

       130        140        150        160        170        180 
DISWDFEGRR LCVVGEGRDN FGVFISWDSG NSLGEVSGHS QRINACHLKQ SRPMRSMTVG 

       190        200        210        220        230        240 
DDGSVVFYQG PPFKFSASDR THHKQGSFVR DVEFSPDSGE FVITVGSDRK ISCFDGKSGE 

       250        260        270        280        290        300 
FLKYIEDDQE PVQGGIFALS WLDSQKFATV GADATIRVWD VTTSKCVQKW TLDKQQLGNQ 

       310        320        330        340        350        360 
QVGVVATGNG RIISLSLDGT LNFYELGHDE VLKTISGHNK GITALTVNPL ISGSYDGRIM 

       370        380        390        400        410        420 
EWSSSSMHQD HSNLIVSLDN SKAQEYSSIS WDDTLKVNGI TKHEFGSQPK VASANNDGFT 

       430        440        450        460        470        480 
AVLTNDDDLL ILQSFTGDII KSVRLNSPGS AVSLSQNYVA VGLEEGNTIQ VFKLSDLEVS 

       490        500        510        520        530        540 
FDLKTPLRAK PSYISISPSE TYIAAGDVMG KILLYDLQSR EVKTSRWAFH TSKINAISWK 

       550        560        570        580        590        600 
PAEKGANEEE IEEDLVATGS LDTNIFIYSV KRPMKIIKAL NAHKDGVNNL LWETPSTLVS 

       610 
SGADACIKRW NVVLE
P46680 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!