P15891 (ABP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-binding protein

Gene names

Name:	ABP1
Ordered Locus Names:	YCR088W
ORF Names:	YCR88W

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.12 Ref.18
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Note: Cortical actin patches. Ref.8 Ref.10 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch assembly Inferred from mutant phenotype PubMed 18177206Ref.1. Source: SGD protein localization Inferred from mutant phenotype Ref.18PubMed 15798181. Source: SGD
Cellular_component	actin cortical patch Inferred from direct assay PubMed 3060468PubMed 8163554. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD
Molecular_function	actin filament binding Inferred from direct assay PubMed 3060468. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AIM21	P40563	4	EBI-2036,EBI-25376
APP1	P53933	8	EBI-2036,EBI-28798
ARK1	P53974	4	EBI-2036,EBI-9817
HUA2	Q12134	3	EBI-2036,EBI-37262
PRK1	P40494	6	EBI-2036,EBI-9703
RVS167	P39743	3	EBI-2036,EBI-14500
SCP1	Q08873	5	EBI-2036,EBI-33137
SLA1	P32790	4	EBI-2036,EBI-17313
SRV2	P17555	5	EBI-2036,EBI-4024
YSC84	P32793	2	EBI-2036,EBI-24460

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 592

591

Actin-binding protein

PRO_0000064429

Regions

Domain

7 – 136

130

ADF-H

Repeat

200 – 209

10

1

Repeat

436 – 445

10

2

Domain

532 – 592

61

SH3

Repeat

566 – 575

10

3

Region

200 – 575

376

3 X 10 AA approximate repeats (acidic)

Compositional bias

518 – 522

5

Poly-Pro

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Modified residue

157

1

Phosphothreonine Ref.16 Ref.17

Modified residue

165

1

Phosphothreonine Ref.9 Ref.13 Ref.15 Ref.16 Ref.17

Modified residue

167

1

Phosphoserine Ref.16

Modified residue

169

1

Phosphoserine Ref.9 Ref.13 Ref.15 Ref.16 Ref.17

Modified residue

181

1

Phosphothreonine Ref.9 Ref.14 Ref.15 Ref.16 Ref.17

Modified residue

183

1

Phosphoserine Ref.9 Ref.14 Ref.15 Ref.16 Ref.17

Modified residue

223

1

Phosphoserine Ref.17

Modified residue

225

1

Phosphotyrosine Ref.17

Modified residue

282

1

Phosphoserine Ref.17

Modified residue

291

1

Phosphoserine Ref.17

Modified residue

293

1

Phosphothreonine Ref.17

Modified residue

313

1

Phosphoserine Ref.17

Modified residue

365

1

Phosphoserine Ref.14 Ref.16 Ref.17

Modified residue

389

1

Phosphoserine Ref.15 Ref.17

Modified residue

458

1

Phosphoserine Ref.16 Ref.17

Modified residue

475

1

Phosphoserine Ref.17

Modified residue

478

1

Phosphoserine Ref.16 Ref.17

Modified residue

481

1

Phosphoserine Ref.14 Ref.16 Ref.17

Modified residue

515

1

Phosphoserine Ref.17

Experimental info

Mutagenesis

21

1

K → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-24. Ref.19

Mutagenesis

24

1

R → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-21. Ref.19

Mutagenesis

80

1

K → A in ABP1-2; strongly reduces actin binding and abolishes ARP2/3 complex activation. Ref.19

Mutagenesis

94

1

K → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-96. Ref.19

Mutagenesis

96

1

R → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-94. Ref.19

Mutagenesis

122

1

D → A in ABP1-4; no effect; when associated with A-125. Ref.19

Mutagenesis

125

1

D → A in ABP1-4; no effect; when associated with A-122. Ref.19

Mutagenesis

134

1

K → A in ABP1-5; moderately reduces actin binding and abolishes ARP2/3 complex activation. Ref.19

Mutagenesis

201 – 203

3

DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. Ref.7

Mutagenesis

437 – 439

3

DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. Ref.7

Mutagenesis

569

1

W → A: Abolishes protein binding. Ref.18

Sequence conflict

58

1

L → S in CAA36075. Ref.1

Sequence conflict

312

1

K → I in CAA36075. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

.

.

592

Helix Strand Turn

Details...

Helix

12 – 24

13

Beta strand

32 – 37

6

Beta strand

43 – 50

8

Helix

52 – 56

5

Beta strand

65 – 71

7

Beta strand

80 – 86

7

Helix

93 – 109

17

Beta strand

115 – 122

8

Helix

123 – 126

4

Helix

128 – 136

9

Beta strand

537 – 541

5

Beta strand

546 – 550

5

Beta strand

558 – 563

6

Beta strand

566 – 574

9

Turn

575 – 577

3

Beta strand

580 – 584

5

Helix

585 – 587

3

Beta strand

588 – 590

3

Sequences

	Sequence		Length	Mass (Da)
	P15891 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 39523510704D94AA	FASTA	592	65,576
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-169; THR-181 AND SER-183, MASS SPECTROMETRY. Strain: 2124.
[10]	"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].
[11]	"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].
[12]	"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.
[13]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165 AND SER-169, MASS SPECTROMETRY. Strain: YAL6B.
[14]	"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, MASS SPECTROMETRY. Strain: ADR376.
[15]	"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 THR-165; SER-169; THR-181; SER-183 AND SER-389, MASS SPECTROMETRY.
[16]	"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 THR-157; THR-165; SER-167; SER-169; THR-181; SER-183; SER-365; SER-458; SER-478 AND SER-481, MASS SPECTROMETRY.
[17]	"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 THR-157; THR-165; SER-169; THR-181; SER-183; SER-223; TYR-225; SER-282; SER-291; THR-293; SER-313; SER-365; SER-389; SER-458; SER-475; SER-478; SER-481 AND SER-515, MASS SPECTROMETRY.
[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.

PIR

LLBY. S19503.

RefSeq

NP_010012.1. NM_001178794.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HQZ	X-ray	2.10	1/2/3/4/5/6/7/8/9	1-141	[»]
1JO8	X-ray	1.30	A	535-592	[»]
2K3B	NMR	-	A	535-592	[»]
2RPN	NMR	-	A	535-592	[»]

ProteinModelPortal

P15891.

SMR

P15891. Positions 3-141, 535-592.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-534N.

IntAct

P15891. 25 interactions.

MINT

MINT-370108.

STRING

4932.YCR088W.

Proteomic databases

PaxDb

P15891.

PeptideAtlas

P15891.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YCR088W; YCR088W; YCR088W.

GeneID

850450.

KEGG

sce:YCR088W.

Organism-specific databases

SGD

S000000684. ABP1.

Phylogenomic databases

eggNOG

NOG265859.

GeneTree

ENSGT00530000062953.

HOGENOM

HOG000246671.

OMA

FTGTKAP.

OrthoDB

EOG44BFBT.

Gene expression databases

Genevestigator

P15891.

GermOnline

YCR088W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002108. Actin-bd_cofilin/tropomyosin.
IPR000108. p67phox.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P15891.

NextBio

966066.

Entry information

Entry name

ABP1_YEAST

Accession

Primary (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 3, 2013
This is version 138 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program