Actin-related protein 2/3 complex subunit 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53731 (ARPC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin-related protein 2/3 complex subunit 2

Alternative name(s):
Arp2/3 complex 34 kDa subunit
Short name=p34-ARC

Gene names

Name:	ARC35
Ordered Locus Names:	YNR035C
ORF Names:	N3296

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament By similarity.
Subunit structure	Component of the Arp2/3 complex composed of ARP2, ARP3, ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and ARC16/p16-ARC. Ref.3
Subcellular location	Cytoplasm › cytoskeleton › actin patch.
Miscellaneous	Present with 13400 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ARPC2 family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from genetic interaction PubMed 14554195. Source: SGD microtubule cytoskeleton organization Inferred from physical interaction PubMed 14554195. Source: SGD mitochondrion inheritance Traceable author statement PubMed 11248049. Source: SGD receptor-mediated endocytosis Inferred from mutant phenotype PubMed 7929582. Source: SGD regulation of actin filament polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	Arp2/3 protein complex Inferred from direct assay PubMed 10377407 Ref.3. Source: SGD actin cortical patch Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from physical interaction PubMed 14554195. Source: SGD
Molecular_function	structural molecule activity Inferred from mutant phenotype PubMed 10377407. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ARC18	Q05933	5	EBI-2770,EBI-2764
ARC19	P33204	3	EBI-2770,EBI-2757
ARC40	P38328	7	EBI-2770,EBI-2777
ARP2	P32381	8	EBI-2770,EBI-2927

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 342

342

Actin-related protein 2/3 complex subunit 2

PRO_0000124041

Amino acid modifications

Modified residue

155

Phosphothreonine Ref.7

Modified residue

324

Phosphoserine Ref.6 Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P53731 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9AF71A93688729F6
Show »

FASTA

342

39,566

        10         20         30         40         50         60 
MLHLQPQNLL IQKTLNEAIE ALRKGSPLTM DRIVSDFDYT TYHISNTAED KSILLLSVKT 

        70         80         90        100        110        120 
KAWVSVSECQ LDGSLTLLKF LADHYSSLGG VTIPSEVEPG YDYTLQITLA ELVQESILQL 

       130        140        150        160        170        180 
SVLKTIILSF PFELAISKFI ELSQQQPAPV EAEITGGEVA ANGDNTLFTI KYRDEENIFI 

       190        200        210        220        230        240 
KPSNDRVTII FETIFQDETD KIFGKVFLQE FVDARKRNRQ IQSAPQVLYS HEPPLELKRL 

       250        260        270        280        290        300 
YQPPKVAEQS RRFITFVLFP RHFQTKELQF HSICQLTLFR NYFHYHIKCS KAYMHSRMRF 

       310        320        330        340 
RVDSFIKVLN RAKVDEDDEN DELSAEGRQQ ARRTFTGRKI VY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches." Winter D., Podtelejnikov A.V., Mann M., Li R. Curr. Biol. 7:519-529(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ARP2/3 COMPLEX.
[4]	Erratum Winter D., Podtelejnikov A.V., Mann M., Li R. Curr. Biol. 7:R593-R593(1997)
[5]	"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].
[6]	"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 SER-324, MASS SPECTROMETRY.
[7]	"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-155 AND SER-324, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71650 Genomic DNA. Translation: CAA96315.1. BK006947 Genomic DNA. Translation: DAA10577.1.
PIR	S63366.
RefSeq	NP_014433.1. NM_001183212.1.
3D structure databases
ProteinModelPortal	P53731.
SMR	P53731. Positions 1-315.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2304N.
IntAct	P53731. 17 interactions.
MINT	MINT-498308.
STRING	4932.YNR035C.
Proteomic databases
PaxDb	P53731.
PeptideAtlas	P53731.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNR035C; YNR035C; YNR035C.
GeneID	855771.
KEGG	sce:YNR035C.
Organism-specific databases
CYGD	YNR035c.
SGD	S000005318. ARC35.
Phylogenomic databases
eggNOG	NOG327379.
GeneTree	ENSGT00390000016794.
HOGENOM	HOG000212535.
KO	K05758.
OMA	NYFHYHI.
OrthoDB	EOG4CRQ7S.
Enzyme and pathway databases
BioCyc	YEAST:G3O-33345-MONOMER.
Gene expression databases
Genevestigator	P53731.
GermOnline	YNR035C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007188. P34-arc. [Graphical view]
PANTHER	PTHR12058. PTHR12058. 1 hit.
Pfam	PF04045. P34-Arc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980223.

Entry information

Entry name

ARPC2_YEAST

Accession

Primary (citable) accession number: P53731
Secondary accession number(s): D6W1L1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIV

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents