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P61158 (ARP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-related protein 3
Alternative name(s):
Actin-like protein 3
Gene names
Name:ACTR3
Synonyms:ARP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as ATP-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 pointed end of the daughter actin filament. Plays a role in ciliogenesis. Ref.7 Ref.16

Subunit structure

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. Interacts with WHDC1. Interacts weakly with MEFV. Ref.1 Ref.7 Ref.12 Ref.14

Subcellular location

Cytoplasmcytoskeleton. Cell projection. Note: In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). Ref.1 Ref.7 Ref.14

Sequence similarities

Belongs to the actin family. ARP3 subfamily.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   LigandActin-binding
ATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

asymmetric cell division

Inferred from electronic annotation. Source: Ensembl

cellular component movement

Traceable author statement Ref.1. Source: UniProtKB

cilium morphogenesis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

meiotic cytokinesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of filopodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of myosin II filament organization

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

spindle localization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentArp2/3 protein complex

Traceable author statement Ref.1. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Traceable author statement Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

excitatory synapse

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

hemidesmosome

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

podosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20195357. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

JUNDP175352EBI-351428,EBI-2682803

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 418417Actin-related protein 3
PRO_0000089079

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.13
Modified residue2401N6-acetyllysine Ref.15
Modified residue2441N6-acetyllysine Ref.15
Modified residue2511N6-acetyllysine Ref.15
Modified residue2541N6-acetyllysine Ref.15

Sequences

Sequence LengthMass (Da)Tools
P61158 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 23E5564198B81C63

FASTA41847,371
        10         20         30         40         50         60 
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF 

        70         80         90        100        110        120 
FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP 

       130        140        150        160        170        180 
ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV 

       190        200        210        220        230        240 
AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK 

       250        260        270        280        290        300 
EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV 

       310        320        330        340        350        360 
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP 

       370        380        390        400        410 
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS 

« Hide

References

« Hide 'large scale' references
[1]"The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly."
Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.
J. Cell Biol. 138:375-384(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, SUBCELLULAR LOCATION.
[2]"Identification of human estrogen-inducible transcripts from a serum resistant variant of breast cancer MCF7 cells."
Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B., Sonnenschein C.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes."
Welch M.D., Iwamatsu A., Mitchison T.J.
Nature 385:265-269(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
[8]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[9]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 103-123 AND 199-209, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity."
Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.
Mol. Cell 8:1041-1052(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport."
Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.
Cell 134:148-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WHDC1.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin."
Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., Hong A., Fox M., Gumucio D.L.
Exp. Biol. Med. (Maywood) 234:40-52(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEFV.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-244; LYS-251 AND LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Functional genomic screen for modulators of ciliogenesis and cilium length."
Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006083 mRNA. Translation: AAB64188.1.
AF127773 mRNA. Translation: AAD51904.1.
AK312659 mRNA. Translation: BAG35542.1.
AC110769 Genomic DNA. Translation: AAX93226.1.
CH471103 Genomic DNA. Translation: EAW95179.1.
BC044590 mRNA. Translation: AAH44590.1.
CCDSCCDS33277.1.
RefSeqNP_005712.1. NM_005721.4.
UniGeneHs.433512.
Hs.595349.

3D structure databases

ProteinModelPortalP61158.
SMRP61158. Positions 3-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115403. 51 interactions.
DIPDIP-33140N.
IntActP61158. 14 interactions.
MINTMINT-3022340.
STRING9606.ENSP00000263238.

PTM databases

PhosphoSiteP61158.

Polymorphism databases

DMDM47117647.

2D gel databases

OGPP32391.

Proteomic databases

MaxQBP61158.
PeptideAtlasP61158.
PRIDEP61158.

Protocols and materials databases

DNASU10096.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263238; ENSP00000263238; ENSG00000115091.
GeneID10096.
KEGGhsa:10096.
UCSCuc002tkx.2. human.

Organism-specific databases

CTD10096.
GeneCardsGC02P114647.
HGNCHGNC:170. ACTR3.
HPACAB005085.
HPA047016.
HPA051683.
MIM604222. gene.
neXtProtNX_P61158.
PharmGKBPA24489.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000233339.
HOVERGENHBG003771.
InParanoidP61158.
OMAASWSSNR.
OrthoDBEOG7TMZRM.
PhylomeDBP61158.
TreeFamTF300644.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP61158.

Gene expression databases

ArrayExpressP61158.
BgeeP61158.
CleanExHS_ACTR3.
GenevestigatorP61158.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTR3. human.
GeneWikiACTR3.
GenomeRNAi10096.
NextBio38185.
PMAP-CutDBP61158.
PROP61158.
SOURCESearch...

Entry information

Entry nameARP3_HUMAN
AccessionPrimary (citable) accession number: P61158
Secondary accession number(s): P32391, Q53QM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM