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Protein

Actin-related protein 2

Gene

ACTR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 1623ATPBy similarity
Nucleotide bindingi214 – 2185ATPBy similarity
Nucleotide bindingi305 – 3106ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP61160.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2
Alternative name(s):
Actin-like protein 2
Gene namesi
Name:ACTR2
Synonyms:ARP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:169. ACTR2.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Cell projection 1 Publication

GO - Cellular componenti

  • actin cap Source: Ensembl
  • actin cytoskeleton Source: UniProtKB
  • Arp2/3 protein complex Source: UniProtKB
  • cell projection Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24488.

Polymorphism and mutation databases

BioMutaiACTR2.
DMDMi47117648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Actin-related protein 2PRO_0000089067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-acetyllysine1 Publication
Modified residuei322 – 3221N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP61160.
PaxDbiP61160.
PRIDEiP61160.

2D gel databases

SWISS-2DPAGEP61160.

PTM databases

PhosphoSiteiP61160.

Expressioni

Gene expression databases

BgeeiP61160.
CleanExiHS_ACTR2.
ExpressionAtlasiP61160. baseline and differential.
GenevisibleiP61160. HS.

Organism-specific databases

HPAiCAB005083.
HPA015050.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi115404. 71 interactions.
DIPiDIP-33165N.
IntActiP61160. 8 interactions.
MINTiMINT-5000145.
STRINGi9606.ENSP00000367220.

Structurei

3D structure databases

ProteinModelPortaliP61160.
SMRiP61160. Positions 4-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP2 subfamily.Curated

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00760000119313.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP61160.
KOiK17260.
OMAiDYTFNEK.
OrthoDBiEOG78D7K6.
PhylomeDBiP61160.
TreeFamiTF300467.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR027306. Arp2.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF149. PTHR11937:SF149. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P61160-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI
60 70 80 90 100
EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI
110 120 130 140 150
DTRNCKILLT EPPMNPTKNR EKIVEVMFET YQFSGVYVAI QAVLTLYAQG
160 170 180 190 200
LLTGVVVDSG DGVTHICPVY EGFSLPHLTR RLDIAGRDIT RYLIKLLLLR
210 220 230 240 250
GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL VESYTLPDGR
260 270 280 290 300
IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH
310 320 330 340 350
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR
360 370 380 390
KHMVFLGGAV LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR
Length:394
Mass (Da):44,761
Last modified:May 10, 2004 - v1
Checksum:i1BFA6B442ED1A797
GO
Isoform 2 (identifier: P61160-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: K → KNNKKM

Note: No experimental confirmation available.
Show »
Length:399
Mass (Da):45,377
Checksum:iCF06512483DAD60A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671M → T in AAH14546 (PubMed:15489334).Curated
Sequence conflicti172 – 1721G → S in AAH14546 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 531K → KNNKKM in isoform 2. 1 PublicationVSP_046178

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1881.1. [P61160-1]
CCDS46307.1. [P61160-2]
RefSeqiNP_001005386.1. NM_001005386.2. [P61160-2]
NP_005713.1. NM_005722.3. [P61160-1]
UniGeneiHs.643727.
Hs.744913.

Genome annotation databases

EnsembliENST00000260641; ENSP00000260641; ENSG00000138071. [P61160-1]
ENST00000377982; ENSP00000367220; ENSG00000138071. [P61160-2]
GeneIDi10097.
KEGGihsa:10097.
UCSCiuc002sdq.3. human. [P61160-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1881.1. [P61160-1]
CCDS46307.1. [P61160-2]
RefSeqiNP_001005386.1. NM_001005386.2. [P61160-2]
NP_005713.1. NM_005722.3. [P61160-1]
UniGeneiHs.643727.
Hs.744913.

3D structure databases

ProteinModelPortaliP61160.
SMRiP61160. Positions 4-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115404. 71 interactions.
DIPiDIP-33165N.
IntActiP61160. 8 interactions.
MINTiMINT-5000145.
STRINGi9606.ENSP00000367220.

Chemistry

ChEMBLiCHEMBL6090.

PTM databases

PhosphoSiteiP61160.

Polymorphism and mutation databases

BioMutaiACTR2.
DMDMi47117648.

2D gel databases

SWISS-2DPAGEP61160.

Proteomic databases

MaxQBiP61160.
PaxDbiP61160.
PRIDEiP61160.

Protocols and materials databases

DNASUi10097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260641; ENSP00000260641; ENSG00000138071. [P61160-1]
ENST00000377982; ENSP00000367220; ENSG00000138071. [P61160-2]
GeneIDi10097.
KEGGihsa:10097.
UCSCiuc002sdq.3. human. [P61160-1]

Organism-specific databases

CTDi10097.
GeneCardsiGC02P065454.
HGNCiHGNC:169. ACTR2.
HPAiCAB005083.
HPA015050.
MIMi604221. gene.
neXtProtiNX_P61160.
PharmGKBiPA24488.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00760000119313.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP61160.
KOiK17260.
OMAiDYTFNEK.
OrthoDBiEOG78D7K6.
PhylomeDBiP61160.
TreeFamiTF300467.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP61160.

Miscellaneous databases

ChiTaRSiACTR2. human.
GeneWikiiACTR2.
GenomeRNAii10097.
NextBioi38189.
PROiP61160.
SOURCEiSearch...

Gene expression databases

BgeeiP61160.
CleanExiHS_ACTR2.
ExpressionAtlasiP61160. baseline and differential.
GenevisibleiP61160. HS.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR027306. Arp2.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF149. PTHR11937:SF149. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiARP2_HUMAN
AccessioniPrimary (citable) accession number: P61160
Secondary accession number(s): B2RCP5
, D6W5F4, E9PF41, O15142, Q96C82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: June 24, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.