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P15891 (ABP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. 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:
Actin-binding protein
Gene names
Name:ABP1
Ordered Locus Names:YCR088W
ORF Names:YCR88W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. recruits components of the endocytotic machinery to cortical actin patches, known sites of endocytosis. Ref.7

Subunit structure

Binds F-actin, but not G-actin. Interacts with the ARP2/3 complex. Interacts with APP1, ARK1, PRK1, SCP1, SRV2 and YIR003W via its SH3 domain. Interacts with the SH3 domain of RVS167 and with SLA1. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.18

Subcellular location

Cytoplasmcytoskeletonactin patch. Note: Cortical actin patches. Ref.8 Ref.9 Ref.19

Post-translational modification

The actin depolymerizing factor homology (ADF) domain mediates actin filament binding.

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ABP1 family.

Contains 1 ADF-H domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 592591Actin-binding protein
PRO_0000064429

Regions

Domain7 – 136130ADF-H
Repeat200 – 209101
Repeat436 – 445102
Domain532 – 59261SH3
Repeat566 – 575103
Region200 – 5753763 X 10 AA approximate repeats (acidic)
Compositional bias518 – 5225Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.16
Modified residue1651Phosphothreonine Ref.15
Modified residue1671Phosphoserine Ref.15
Modified residue1691Phosphoserine Ref.13 Ref.14 Ref.15
Modified residue1811Phosphothreonine Ref.12 Ref.13 Ref.14 Ref.15
Modified residue1831Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue3131Phosphoserine Ref.14 Ref.15
Modified residue3651Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue3891Phosphoserine Ref.13 Ref.14
Modified residue4581Phosphoserine Ref.14
Modified residue4811Phosphoserine Ref.12 Ref.14

Experimental info

Mutagenesis211K → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-24. Ref.19
Mutagenesis241R → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-21. Ref.19
Mutagenesis801K → A in ABP1-2; strongly reduces actin binding and abolishes ARP2/3 complex activation. Ref.19
Mutagenesis941K → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-96. Ref.19
Mutagenesis961R → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-94. Ref.19
Mutagenesis1221D → A in ABP1-4; no effect; when associated with A-125. Ref.19
Mutagenesis1251D → A in ABP1-4; no effect; when associated with A-122. Ref.19
Mutagenesis1341K → A in ABP1-5; moderately reduces actin binding and abolishes ARP2/3 complex activation. Ref.19
Mutagenesis201 – 2033DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. Ref.7
Mutagenesis437 – 4393DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. Ref.7
Mutagenesis5691W → A: Abolishes protein binding. Ref.18
Sequence conflict581L → S in CAA36075. Ref.1
Sequence conflict3121K → I in CAA36075. Ref.1

Secondary structure

................................. 592
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15891 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 39523510704D94AA

FASTA59265,576
        10         20         30         40         50         60 
MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS SFHDFLQLFD 

        70         80         90        100        110        120 
ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA ANFAAVANNL FKGYHVQVTA 

       130        140        150        160        170        180 
RDEDDLDENE LLMKISNAAG ARYSIQTSSK QQGKASTPPV KKSFTPSKSP APVSKKEPVK 

       190        200        210        220        230        240 
TPSPAPAAKI SSRVNDNNDD DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE 

       250        260        270        280        290        300 
KAKEDPRLVQ KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND 

       310        320        330        340        350        360 
DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP DVKDLKSKFE 

       370        380        390        400        410        420 
GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV KAEEAEQPKT DYKKIGNPLP 

       430        440        450        460        470        480 
GMHIEADNEE EPEENDDDWD DDEDEAAQPP LPSRNVASGA PVQKEEPEQE EIAPSLPSRN 

       490        500        510        520        530        540 
SIPAPKQEEA PEQAPEEEIE EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE 

       550        560        570        580        590 
YDYDAAEDNE LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN 

« Hide

References

« Hide 'large scale' references
[1]"Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I."
Drubin D.G., Mulholland J., Zhu Z., Botstein D.
Nature 343:288-290(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [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]Bienvenut W.V., Peters C.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13 AND 97-112, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization."
Freeman N.L., Lila T., Mintzer K.A., Chen Z., Pahk A.J., Ren R., Drubin D.G., Field J.
Mol. Cell. Biol. 16:548-556(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRV2.
[6]"In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions."
Colwill K., Field D., Moore L., Friesen J., Andrews B.
Genetics 152:881-893(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RVS167.
[7]"Activation of the Arp2/3 complex by the actin filament binding protein Abp1p."
Goode B.L., Rodal A.A., Barnes G., Drubin D.G.
J. Cell Biol. 153:627-634(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACTIN AND ARP2/3 COMPLEX, MUTAGENESIS OF 201-ASP--TRP-203 AND 437-ASP--TRP-439.
[8]"Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics."
Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.
J. Cell Sci. 115:1703-1715(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLA1, SUBCELLULAR LOCATION.
[9]"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].
[10]"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].
[11]"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 APP1; PRK1; SCP1 AND YIR003W.
[12]"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-181; SER-183; SER-365 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[13]"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-169; THR-181; SER-183 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-169; THR-181; SER-183; SER-313; SER-365; SER-389; SER-458 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-165; SER-167; SER-169; THR-181; SER-313 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF SH3 DOMAIN, MUTAGENESIS OF TRP-569, INTERACTION WITH ARK1 AND PRK1.
[19]"Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions."
Quintero-Monzon O., Rodal A.A., Strokopytov B., Almo S.C., Goode B.L.
Mol. Biol. Cell 16:3128-3139(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF ADF DOMAIN, MUTAGENESIS OF LYS-21; ARG-24; LYS-80; LYS-94; ARG-96; ASP-122; ASP-125 AND LYS-134, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51780 Genomic DNA. Translation: CAA36075.1.
X59720 Genomic DNA. Translation: CAA42253.1.
BK006937 Genomic DNA. Translation: DAA07557.1.
PIRLLBY. S19503.
RefSeqNP_010012.1. NM_001178794.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQZX-ray2.101/2/3/4/5/6/7/8/91-141[»]
1JO8X-ray1.30A535-592[»]
2K3BNMR-A535-592[»]
2RPNNMR-A535-592[»]
DisProtDP00634.
ProteinModelPortalP15891.
SMRP15891. Positions 3-141, 535-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31060. 87 interactions.
DIPDIP-534N.
IntActP15891. 35 interactions.
MINTMINT-370108.
STRING4932.YCR088W.

Proteomic databases

PaxDbP15891.
PeptideAtlasP15891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR088W; YCR088W; YCR088W.
GeneID850450.
KEGGsce:YCR088W.

Organism-specific databases

SGDS000000684. ABP1.

Phylogenomic databases

eggNOGNOG265859.
HOGENOMHOG000246671.
OMAIINIEFV.
OrthoDBEOG7B05P0.

Enzyme and pathway databases

BioCycYEAST:G3O-29382-MONOMER.

Gene expression databases

GenevestigatorP15891.

Family and domain databases

InterProIPR002108. ADF-H.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15891.
NextBio966066.
PROP15891.

Entry information

Entry nameABP1_YEAST
AccessionPrimary (citable) accession number: P15891
Secondary accession number(s): D6VR88
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: 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