P61158 (ARP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-related protein 3

Alternative name(s):
Actin-like protein 3

Gene names

Name:	ACTR3
Synonyms:	ARP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	418 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	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.14
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. Ref.1 Ref.7 Ref.12
Subcellular location	Cytoplasm › cytoskeleton. Cell projection Ref.1 Ref.7.
Sequence similarities	Belongs to the actin family. ARP3 subfamily.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cell projection Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Arp2/3 complex-mediated actin nucleation Inferred from electronic annotation. Source: InterPro Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome asymmetric cell division Inferred from electronic annotation. Source: Compara cellular component movement Traceable author statement Ref.1. Source: UniProtKB cilium morphogenesis Inferred from mutant phenotype Ref.14. Source: UniProtKB cytokinesis after meiosis Inferred from electronic annotation. Source: Compara establishment or maintenance of cell polarity Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome meiotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of dendrite morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of filopodium assembly Inferred from electronic annotation. Source: Compara positive regulation of lamellipodium assembly Inferred from electronic annotation. Source: Compara positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara regulation of myosin II filament organization Inferred from electronic annotation. Source: Compara response to antibiotic Inferred from electronic annotation. Source: Compara response to carbohydrate stimulus Inferred from electronic annotation. Source: Compara spindle localization Inferred from electronic annotation. Source: Compara
Cellular_component	Arp2/3 protein complex Traceable author statement Ref.1. Source: UniProtKB Golgi membrane Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome excitatory synapse Inferred from electronic annotation. Source: Compara hemidesmosome Inferred from electronic annotation. Source: Compara lamellipodium Inferred from electronic annotation. Source: Compara podosome Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JUND	P17535	2	EBI-351428,EBI-2682803

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 418	417	Actin-related protein 3		PRO_0000089079
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	240	1	N6-acetyllysine Ref.13
	Modified residue	244	1	N6-acetyllysine Ref.13
	Modified residue	251	1	N6-acetyllysine Ref.13
	Modified residue	254	1	N6-acetyllysine Ref.13
	Modified residue	418	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61158 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 23E5564198B81C63	FASTA	418	47,371
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, 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]	"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, MASS SPECTROMETRY.
[14]	"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.
[15]	"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.
IPI	IPI00028091.
RefSeq	NP_005712.1. NM_005721.4.
UniGene	Hs.433512. Hs.595349.
3D structure databases
ProteinModelPortal	P61158.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33140N.
IntAct	P61158. 14 interactions.
MINT	MINT-3022340.
STRING	9606.ENSP00000263238.
PTM databases
PhosphoSite	P61158.
Polymorphism databases
DMDM	47117647.
2D gel databases
OGP	P32391.
Proteomic databases
PeptideAtlas	P61158.
PRIDE	P61158.
Protocols and materials databases
DNASU	10096.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263238; ENSP00000263238; ENSG00000115091.
GeneID	10096.
KEGG	hsa:10096.
UCSC	uc002tkx.1. human.
Organism-specific databases
CTD	10096.
GeneCards	GC02P114647.
HGNC	HGNC:170. ACTR3.
HPA	CAB005085.
MIM	604222. gene.
neXtProt	NX_P61158.
PharmGKB	PA24489.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000233339.
HOVERGEN	HBG003771.
InParanoid	P61158.
OMA	DNVIQNC.
OrthoDB	EOG4XKV6W.
PhylomeDB	P61158.
Enzyme and pathway databases
SignaLink	P61158.
Gene expression databases
ArrayExpress	P61158.
Bgee	P61158.
CleanEx	HS_ACTR3.
Genevestigator	P61158.
GermOnline	ENSG00000115091. Homo sapiens.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR020902. Actin/actin-like_CS. IPR015623. Arp3. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 1 hit. PTHR11937:SF31. PTHR11937:SF31. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACTR3. human.
GenomeRNAi	10096.
NextBio	38185.
PMAP-CutDB	P61158.
SOURCE	Search...

Entry information

Entry name

ARP3_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.