Reviewed, UniProtKB/Swiss-Prot P61160 (ARP2_HUMAN)

Names and origin

Protein names

Recommended name:
    Actin-related protein 2
Alternative name(s):
    Actin-like protein 2

Gene names

Name:	ACTR2
Synonyms:	ARP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.5
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.
Subcellular location	Cytoplasm › cytoskeleton. Cell projection. Ref.5
Sequence similarities	Belongs to the actin family. ARP2 subfamily.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell motion Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	Arp2/3 protein complex Ref.1 Traceable author statement. Source: UniProtKB cell projection Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR3B	Q9P1U1	1	EBI-353580,EBI-1047175
BAK1	Q16611	1	EBI-353580,EBI-519866

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	Actin-related protein 2		PRO_0000089067
Regions
	Nucleotide binding	160 – 162	3	ATP By similarity
	Nucleotide binding	214 – 218	5	ATP By similarity
	Nucleotide binding	305 – 310	6	ATP By similarity
Amino acid modifications
	Modified residue	299	1	N6-acetyllysine Ref.8
	Modified residue	322	1	N6-acetyllysine Ref.8
Experimental info
	Sequence conflict	67	1	M → T in AAH14546. Ref.4
	Sequence conflict	172	1	G → S in AAH14546. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P61160-1 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: 1BFA6B442ED1A797	FASTA	394	44,761
	10 20 30 40 50 60 MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE 70 80 90 100 110 120 ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR 130 140 150 160 170 180 EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR 190 200 210 220 230 240 RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL 250 260 270 280 290 300 VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH 310 320 330 340 350 360 IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV 370 380 390 LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR

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: 9230079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[3]	Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[5]	"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: 9000076] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
[6]	"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: 11741539] [Abstract] Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299 AND LYS-322, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF006082 mRNA. Translation: AAB64187.1. AK315205 mRNA. Translation: BAG37642.1. CH471053 Genomic DNA. Translation: EAW99908.1. BC014546 mRNA. Translation: AAH14546.1.
IPI	IPI00005159.
RefSeq	NP_001005386.1. NP_005713.1.
UniGene	Hs.643727
3D structure databases
HSSP	HSSP built from PDB template 1K8K based on UniProtKB P32391.
SMR	P61160. Positions 143-350.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61160. 10 interactions.
STRING	P61160.
PTM databases
PhosphoSite	P61160.
2-D gel databases
SWISS-2DPAGE	P61160.
Proteomic databases
PRIDE	P61160.
Genome annotation databases
Ensembl	ENST00000260641; ENSP00000260641; ENSG00000138071; Homo sapiens. [Genome view] ENST00000377982; ENSP00000367220; ENSG00000138071; Homo sapiens. [Genome view]
GeneID	10097.
UCSC	uc002sdq.1. human.
Organism-specific databases
CTD	10097.
GeneCards	GC02P065366.
HGNC	HGNC:169. ACTR2.
HPA	CAB005083. HPA015050.
MIM	604221. gene.
PharmGKB	PA24488.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P61160.
Gene expression databases
ArrayExpress	P61160.
Bgee	P61160.
CleanEx	HS_ACTR2.
Genevestigator	P61160.
GermOnline	ENSG00000138071. Homo sapiens.
Family and domain databases
InterPro	IPR004000. Actin-like. [Graphical view]
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	38189.
SOURCE	Search...

Entry information

Entry name

ARP2_HUMAN

Accession

Primary (citable) accession number: P61160
Secondary accession number(s): B2RCP5, O15142, Q96C82

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.