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UniProtKB - P15891 (ABP1_YEAST)

Entry version 198 (26 Feb 2020)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-29382-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-6798695 Neutrophil degranulation
R-SCE-8856828 Clathrin-mediated endocytosis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Actin-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ABP1
Ordered Locus Names:YCR088W
ORF Names:YCR88W
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome III

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YCR088W

Saccharomyces Genome Database

More...SGDi		S000000684 ABP1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000644292 – 592Actin-binding proteinAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki464Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei481PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15891

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P15891

PRoteomics IDEntifications database

More...PRIDEi		P15891

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15891

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		31060, 165 interactors

Database of interacting proteins

More...DIPi		DIP-534N

Protein interaction database and analysis system

More...IntActi		P15891, 50 interactors

Molecular INTeraction database

More...MINTi		P15891

STRING: functional protein association networks

More...STRINGi		4932.YCR088W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P15891 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1592
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P15891

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15891

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 136ADF-HPROSITE-ProRule annotationAdd BLAST130
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati200 – 209110
Repeati436 – 445210
Domaini532 – 592SH3PROSITE-ProRule annotationAdd BLAST61
Repeati566 – 575310

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni200 – 5753 X 10 AA approximate repeats (acidic)Add BLAST376

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi518 – 522Poly-Pro5

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ABP1 family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_459326_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15891

KEGG Orthology (KO)

More...KOi		K20520

Identification of Orthologs from Complete Genome Data

More...OMAi		YKPTKPH

Family and domain databases

Conserved Domains Database

More...CDDi		cd11961 SH3_Abp1_fungi_C2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035718 Abp1_fungi_SH3_C2
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00241 Cofilin_ADF, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00452 SH3DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00102 ADF, 1 hit
SM00326 SH3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50044 SSF50044, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51263 ADF_H, 1 hit
PS50002 SH3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i39523510704D94AA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti58L → S in CAA36075 (PubMed:2405279).Curated1
Sequence conflicti312K → I in CAA36075 (PubMed:2405279).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X51780 Genomic DNA Translation: CAA36075.1
X59720 Genomic DNA Translation: CAA42253.1
BK006937 Genomic DNA Translation: DAA07557.1

Protein sequence database of the Protein Information Resource

More...PIRi		S19503 LLBY

NCBI Reference Sequences

More...RefSeqi		NP_010012.1, NM_001178794.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YCR088W_mRNA; YCR088W; YCR088W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		850450

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YCR088W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
SMRiP15891
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31060, 165 interactors
DIPiDIP-534N
IntActiP15891, 50 interactors
MINTiP15891
STRINGi4932.YCR088W

PTM databases

iPTMnetiP15891

Proteomic databases

MaxQBiP15891
PaxDbiP15891
PRIDEiP15891

Genome annotation databases

EnsemblFungiiYCR088W_mRNA; YCR088W; YCR088W
GeneIDi850450
KEGGisce:YCR088W

Organism-specific databases

EuPathDBiFungiDB:YCR088W
SGDiS000000684 ABP1

Phylogenomic databases

HOGENOMiCLU_459326_0_0_1
InParanoidiP15891
KOiK20520
OMAiYKPTKPH

Enzyme and pathway databases

BioCyciYEAST:G3O-29382-MONOMER
ReactomeiR-SCE-6798695 Neutrophil degranulation
R-SCE-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

EvolutionaryTraceiP15891

Protein Ontology

More...PROi		PR:P15891
RNActiP15891 protein

Family and domain databases

CDDicd11961 SH3_Abp1_fungi_C2, 1 hit
Gene3Di3.40.20.10, 1 hit
InterProiView protein in InterPro
IPR035718 Abp1_fungi_SH3_C2
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PfamiView protein in Pfam
PF00241 Cofilin_ADF, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00102 ADF, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS51263 ADF_H, 1 hit
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiABP1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15891
Secondary accession number(s): D6VR88
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: February 26, 2020
This is version 198 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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