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P40563 (AIM21_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Altered inheritance of mitochondria protein 21
Gene names
Name:AIM21
Ordered Locus Names:YIR003W
ORF Names:YIB3W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in mitochondrial migration along actin filaments. Ref.14

Subunit structure

Interacts with ribosomes. Interacts with ABP1. Ref.4 Ref.7

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: Cortical actin patches. Localizes at the shmoo tip. Ref.5 Ref.13

Disruption phenotype

Increases the sensitivity to farnesol. Ref.9

Miscellaneous

Present with 450 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the AIM21 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrion migration along actin filament

Inferred from mutant phenotype Ref.14. Source: SGD

   Cellular_componentactin cortical patch

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 679679Altered inheritance of mitochondria protein 21
PRO_0000203003

Regions

Region383 – 39614Interaction with SH3 domain of ABP1

Amino acid modifications

Modified residue181Phosphothreonine Ref.10 Ref.15
Modified residue361Phosphoserine Ref.10 Ref.12 Ref.15
Modified residue581Phosphothreonine Ref.10 Ref.15
Modified residue701Phosphoserine Ref.15
Modified residue851Phosphothreonine Ref.10 Ref.15
Modified residue1041Phosphoserine Ref.15
Modified residue1831Phosphoserine Ref.10 Ref.15
Modified residue2061Phosphoserine Ref.15
Modified residue2311Phosphoserine Ref.12
Modified residue2771Phosphothreonine Ref.10 Ref.12 Ref.15
Modified residue2841Phosphoserine Ref.15
Modified residue3241Phosphoserine Ref.12
Modified residue5521Phosphothreonine Ref.15
Modified residue5761Phosphoserine Ref.12 Ref.15
Modified residue6201Phosphoserine Ref.12 Ref.15
Modified residue6231Phosphoserine Ref.15
Modified residue6251Phosphoserine Ref.10
Modified residue6271Phosphoserine Ref.15
Modified residue6671Phosphoserine Ref.15
Modified residue6711Phosphoserine Ref.12 Ref.15
Modified residue6751Phosphoserine Ref.15
Modified residue6781Phosphoserine Ref.10 Ref.15

Sequences

Sequence LengthMass (Da)Tools
P40563 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 9DF79500375339E7

FASTA67974,763
        10         20         30         40         50         60 
MPSEVTPKVP ERPSRRKTSE LFPLSGSESG DIKANSEPPT PAGTPNVPTR RPILKAKTMT 

        70         80         90        100        110        120 
SFESGMDQES LPKVPLQRPV RRSTTEELNN VMNNTSKELE EIESLISKHN IHNVSRKKSP 

       130        140        150        160        170        180 
TSVEEGKVAA IHQNGQRSAS DNKTSTNPSP LEKNEHEGAE GNESAISPSN LVNKSNNEVT 

       190        200        210        220        230        240 
EHSDSEDLTE KQKVHAALDN EAGDRSHFEE KLIPGDMKVQ VDVSKDVEEG SLNALPPSGI 

       250        260        270        280        290        300 
TESDDKAEKF TKHPESSLEE LQKHQEQQEE KIFQNPTDEE STTSLNEKQE GKDNMEVNSQ 

       310        320        330        340        350        360 
PQGPSDTETV IAATSSNVPS QIASEEENDV PVIPRSRPKK DFEAHVQKEE LPNTQEKRVS 

       370        380        390        400        410        420 
EECDSTLIST EEESKIPKIP SERPKRRAPP PVPKKPSSRI AAFQEMLQKQ QQQDLHNNGN 

       430        440        450        460        470        480 
SSATTASADI AKKHTDSSIT SDTTKADFTS KLNGLFALPG MVNPGQLPPS LEKKLSSPDT 

       490        500        510        520        530        540 
ESKLGPQDQS QAKTGPLGGT RRGRGPRGRK LPSKVASVEK IEEDDNTNKI EIFNNWNVSS 

       550        560        570        580        590        600 
SFSKEKVLID TTPGEQAERA LDEKSKSIPE EQREQSPNKM EAALCPFELD EKEKLPANAE 

       610        620        630        640        650        660 
SDPLSQLPQT NAVGNRKAIS EESLSPSEAI ANRDQNDTTE IQEQQMEDQM EVDMERELSG 

       670 
GYEDVDSALH SEEASFHSL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX."
Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W.
Yeast 11:61-78(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis."
Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K., Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.
J. Biol. Chem. 277:5290-5298(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABP1.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"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].
[7]"Protein interaction networks by proteome peptide scanning."
Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L., Schneider-Mergener J., Volkmer-Engert R., Cesareni G.
PLoS Biol. 2:94-103(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABP1.
[8]"Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: COPURIFICATION WITH RIBOSOMAL COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"A chemogenomic screen in Saccharomyces cerevisiae uncovers a primary role for the mitochondria in farnesol toxicity and its regulation by the Pkc1 pathway."
Fairn G.D., Macdonald K., McMaster C.R.
J. Biol. Chem. 282:4868-4874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[10]"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 THR-18; SER-36; THR-58; THR-85; SER-183; THR-277; SER-625 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-36; SER-231; THR-277; SER-324; SER-576; SER-620 AND SER-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Systematic definition of protein constituents along the major polarization axis reveals an adaptive reuse of the polarization machinery in pheromone-treated budding yeast."
Narayanaswamy R., Moradi E.K., Niu W., Hart G.T., Davis M., McGary K.L., Ellington A.D., Marcotte E.M.
J. Proteome Res. 8:6-19(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis."
Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J., Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M., Troyanskaya O.G., Caudy A.A.
PLoS Genet. 5:E1000407-E1000407(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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 THR-18; SER-36; THR-58; SER-70; THR-85; SER-104; SER-183; SER-206; THR-277; SER-284; THR-552; SER-576; SER-620; SER-623; SER-627; SER-667; SER-671; SER-675 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79743 Genomic DNA. No translation available.
Z38062 Genomic DNA. Translation: CAA86205.1.
BK006942 Genomic DNA. Translation: DAA08549.1.
PIRS48437.
RefSeqNP_012268.3. NM_001179525.3.

3D structure databases

ProteinModelPortalP40563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34994. 34 interactions.
DIPDIP-5096N.
IntActP40563. 19 interactions.
MINTMINT-554749.
STRING4932.YIR003W.

Proteomic databases

PaxDbP40563.
PeptideAtlasP40563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIR003W; YIR003W; YIR003W.
GeneID854819.
KEGGsce:YIR003W.

Organism-specific databases

CYGDYIR003w.
SGDS000001442. AIM21.

Phylogenomic databases

eggNOGNOG12793.
OMAINADSAN.
OrthoDBEOG79GTG2.

Enzyme and pathway databases

BioCycYEAST:G3O-31424-MONOMER.

Gene expression databases

GenevestigatorP40563.

Family and domain databases

InterProIPR021582. DUF3210.
[Graphical view]
PfamPF11489. DUF3210. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977663.

Entry information

Entry nameAIM21_YEAST
AccessionPrimary (citable) accession number: P40563
Secondary accession number(s): D6VVT3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 105 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 IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families