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P61160 (ARP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 2
Alternative name(s):
Actin-like protein 2
Gene names
Name:ACTR2
Synonyms:ARP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
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. Ref.7

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. Ref.7

Subcellular location

Cytoplasmcytoskeleton. Cell projection Ref.7.

Sequence similarities

Belongs to the actin family. ARP2 subfamily.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
ATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processArp2/3 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: Ensembl

cellular component movement

Traceable author statement Ref.1. Source: UniProtKB

cytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

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

spindle localization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentArp2/3 protein complex

Traceable author statement Ref.1. Source: UniProtKB

actin cap

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Traceable author statement Ref.1. Source: UniProtKB

cell projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61160-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P61160-2)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: K → KNNKKM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Actin-related protein 2
PRO_0000089067

Regions

Nucleotide binding160 – 1623ATP By similarity
Nucleotide binding214 – 2185ATP By similarity
Nucleotide binding305 – 3106ATP By similarity

Amino acid modifications

Modified residue2991N6-acetyllysine Ref.9
Modified residue3221N6-acetyllysine Ref.9

Natural variations

Alternative sequence531K → KNNKKM in isoform 2.
VSP_046178

Experimental info

Sequence conflict671M → T in AAH14546. Ref.6
Sequence conflict1721G → S in AAH14546. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: 1BFA6B442ED1A797

FASTA39444,761
        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 

« Hide

Isoform 2 [UniParc].

Checksum: CF06512483DAD60A
Show »

FASTA39945,377

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] (ISOFORM 1).
[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. 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] (ISOFORM 1).
Tissue: Tongue.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[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.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 (SEP-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] (ISOFORM 1).
Tissue: Skeletal muscle.
[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: PARTIAL PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
[8]"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.
[9]"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-299 AND LYS-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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
AF006082 mRNA. Translation: AAB64187.1.
AK315205 mRNA. Translation: BAG37642.1.
BX649080 mRNA. No translation available.
AC007318 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99908.1.
CH471053 Genomic DNA. Translation: EAW99910.1.
CH471053 Genomic DNA. Translation: EAW99912.1.
CH471053 Genomic DNA. Translation: EAW99913.1.
BC014546 mRNA. Translation: AAH14546.1.
RefSeqNP_001005386.1. NM_001005386.2.
NP_005713.1. NM_005722.3.
UniGeneHs.643727.
Hs.744913.

3D structure databases

ProteinModelPortalP61160.
SMRP61160. Positions 4-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115404. 66 interactions.
DIPDIP-33165N.
IntActP61160. 8 interactions.
MINTMINT-5000145.
STRING9606.ENSP00000367220.

Chemistry

ChEMBLCHEMBL6090.

PTM databases

PhosphoSiteP61160.

Polymorphism databases

DMDM47117648.

2D gel databases

SWISS-2DPAGEP61160.

Proteomic databases

PaxDbP61160.
PRIDEP61160.

Protocols and materials databases

DNASU10097.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260641; ENSP00000260641; ENSG00000138071. [P61160-1]
ENST00000377982; ENSP00000367220; ENSG00000138071. [P61160-2]
GeneID10097.
KEGGhsa:10097.
UCSCuc002sdq.3. human. [P61160-1]

Organism-specific databases

CTD10097.
GeneCardsGC02P065454.
HGNCHGNC:169. ACTR2.
HPACAB005083.
HPA015050.
MIM604221. gene.
neXtProtNX_P61160.
PharmGKBPA24488.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5277.
HOGENOMHOG000233340.
HOVERGENHBG003771.
KOK17260.
OMAETMFEKY.
OrthoDBEOG78D7K6.
PhylomeDBP61160.
TreeFamTF300467.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP61160.

Gene expression databases

ArrayExpressP61160.
BgeeP61160.
CleanExHS_ACTR2.
GenevestigatorP61160.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR027306. Arp2.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF37. PTHR11937:SF37. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTR2. human.
GeneWikiACTR2.
GenomeRNAi10097.
NextBio38189.
PROP61160.
SOURCESearch...

Entry information

Entry nameARP2_HUMAN
AccessionPrimary (citable) accession number: P61160
Secondary accession number(s): B2RCP5 expand/collapse secondary AC list , D6W5F4, E9PF41, O15142, Q96C82
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 103 of the entry and version 1 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