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Protein

Actin-binding protein

Gene

ABP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • actin filament binding Source: SGD

GO - Biological processi

  • actin cortical patch assembly Source: SGD
  • barbed-end actin filament capping Source: SGD
  • protein localization Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29382-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-binding protein
Gene namesi
Name:ABP1
Ordered Locus Names:YCR088W
ORF Names:YCR88W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR088W.
SGDiS000000684. ABP1.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • cell cortex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21K → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-24. 1 Publication1
Mutagenesisi24R → A in ABP1-1; moderately reduces actin binding and partially reduces ARP2/3 complex activation; when associated with A-21. 1 Publication1
Mutagenesisi80K → A in ABP1-2; strongly reduces actin binding and abolishes ARP2/3 complex activation. 1 Publication1
Mutagenesisi94K → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-96. 1 Publication1
Mutagenesisi96R → A in ABP1-3; reduces actin binding and abolishes ARP2/3 complex activation; when associated with A-94. 1 Publication1
Mutagenesisi122D → A in ABP1-4; no effect; when associated with A-125. 1 Publication1
Mutagenesisi125D → A in ABP1-4; no effect; when associated with A-122. 1 Publication1
Mutagenesisi134K → A in ABP1-5; moderately reduces actin binding and abolishes ARP2/3 complex activation. 1 Publication1
Mutagenesisi201 – 203DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication3
Mutagenesisi437 – 439DDW → AAA: Abolishes ARP2/3 complex activation, but not actin binding. 1 Publication3
Mutagenesisi569W → A: Abolishes protein binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000644292 – 592Actin-binding proteinAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei165PhosphothreonineCombined sources1
Modified residuei167PhosphoserineCombined sources1
Modified residuei169PhosphoserineCombined sources1
Modified residuei181PhosphothreonineCombined sources1
Modified residuei183PhosphoserineCombined sources1
Modified residuei313PhosphoserineCombined sources1
Modified residuei365PhosphoserineCombined sources1
Modified residuei389PhosphoserineCombined sources1
Modified residuei458PhosphoserineCombined sources1
Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei481PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP15891.
PRIDEiP15891.

PTM databases

iPTMnetiP15891.

Interactioni

Subunit structurei

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 SLA1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIM21P4056310EBI-2036,EBI-25376
APP1P539339EBI-2036,EBI-28798
ARK1P5397411EBI-2036,EBI-9817
BSP1Q066042EBI-2036,EBI-37047
HUA2Q121343EBI-2036,EBI-37262
INP52P509422EBI-2036,EBI-28834
LSB3P436036EBI-2036,EBI-22980
PRK1P4049410EBI-2036,EBI-9703
RVS167P397436EBI-2036,EBI-14500
SCP1Q088736EBI-2036,EBI-33137
SLA1P327904EBI-2036,EBI-17313
SRV2P175559EBI-2036,EBI-4024
YSC84P327933EBI-2036,EBI-24460

GO - Molecular functioni

  • actin filament binding Source: SGD

Protein-protein interaction databases

BioGridi31060. 85 interactors.
DIPiDIP-534N.
IntActiP15891. 35 interactors.
MINTiMINT-370108.

Structurei

Secondary structure

1592
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 24Combined sources13
Beta strandi32 – 37Combined sources6
Beta strandi43 – 50Combined sources8
Helixi52 – 56Combined sources5
Beta strandi65 – 71Combined sources7
Beta strandi80 – 86Combined sources7
Helixi93 – 109Combined sources17
Beta strandi115 – 122Combined sources8
Helixi123 – 126Combined sources4
Helixi128 – 136Combined sources9
Beta strandi537 – 541Combined sources5
Beta strandi546 – 550Combined sources5
Beta strandi558 – 563Combined sources6
Beta strandi566 – 574Combined sources9
Turni575 – 577Combined sources3
Beta strandi580 – 584Combined sources5
Helixi585 – 587Combined sources3
Beta strandi588 – 590Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
DisProtiDP00634.
ProteinModelPortaliP15891.
SMRiP15891.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15891.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 136ADF-HPROSITE-ProRule annotationAdd BLAST130
Repeati200 – 209110
Repeati436 – 445210
Domaini532 – 592SH3PROSITE-ProRule annotationAdd BLAST61
Repeati566 – 575310

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 5753 X 10 AA approximate repeats (acidic)Add BLAST376

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi518 – 522Poly-Pro5

Sequence similaritiesi

Belongs to the ABP1 family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

HOGENOMiHOG000246671.
InParanoidiP15891.
KOiK20520.
OMAiYFTSHLA.
OrthoDBiEOG092C1L4H.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15891-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS
60 70 80 90 100
SFHDFLQLFD ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA
110 120 130 140 150
ANFAAVANNL FKGYHVQVTA RDEDDLDENE LLMKISNAAG ARYSIQTSSK
160 170 180 190 200
QQGKASTPPV KKSFTPSKSP APVSKKEPVK TPSPAPAAKI SSRVNDNNDD
210 220 230 240 250
DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE KAKEDPRLVQ
260 270 280 290 300
KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND
310 320 330 340 350
DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP
360 370 380 390 400
DVKDLKSKFE GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV
410 420 430 440 450
KAEEAEQPKT DYKKIGNPLP GMHIEADNEE EPEENDDDWD DDEDEAAQPP
460 470 480 490 500
LPSRNVASGA PVQKEEPEQE EIAPSLPSRN SIPAPKQEEA PEQAPEEEIE
510 520 530 540 550
EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE YDYDAAEDNE
560 570 580 590
LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN
Length:592
Mass (Da):65,576
Last modified:January 23, 2007 - v4
Checksum:i39523510704D94AA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58L → S in CAA36075 (PubMed:2405279).Curated1
Sequence conflicti312K → I in CAA36075 (PubMed:2405279).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51780 Genomic DNA. Translation: CAA36075.1.
X59720 Genomic DNA. Translation: CAA42253.1.
BK006937 Genomic DNA. Translation: DAA07557.1.
PIRiS19503. LLBY.
RefSeqiNP_010012.1. NM_001178794.1.

Genome annotation databases

EnsemblFungiiCAA42253; CAA42253; CAA42253.
YCR088W; YCR088W; YCR088W.
GeneIDi850450.
KEGGisce:YCR088W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51780 Genomic DNA. Translation: CAA36075.1.
X59720 Genomic DNA. Translation: CAA42253.1.
BK006937 Genomic DNA. Translation: DAA07557.1.
PIRiS19503. LLBY.
RefSeqiNP_010012.1. NM_001178794.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
DisProtiDP00634.
ProteinModelPortaliP15891.
SMRiP15891.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31060. 85 interactors.
DIPiDIP-534N.
IntActiP15891. 35 interactors.
MINTiMINT-370108.

PTM databases

iPTMnetiP15891.

Proteomic databases

MaxQBiP15891.
PRIDEiP15891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42253; CAA42253; CAA42253.
YCR088W; YCR088W; YCR088W.
GeneIDi850450.
KEGGisce:YCR088W.

Organism-specific databases

EuPathDBiFungiDB:YCR088W.
SGDiS000000684. ABP1.

Phylogenomic databases

HOGENOMiHOG000246671.
InParanoidiP15891.
KOiK20520.
OMAiYFTSHLA.
OrthoDBiEOG092C1L4H.

Enzyme and pathway databases

BioCyciYEAST:G3O-29382-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP15891.
PROiP15891.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiABP1_YEAST
AccessioniPrimary (citable) accession number: P15891
Secondary accession number(s): D6VR88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.