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Protein

Actin-related protein 3

Gene

ACTR3

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. Plays a role in ciliogenesis.2 Publications

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

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.
SignaLinkiP61158.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 3
Alternative name(s):
Actin-like protein 3
Gene namesi
Name:ACTR3
Synonyms:ARP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:170. ACTR3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • Arp2/3 protein complex Source: UniProtKB
  • brush border Source: Ensembl
  • cell-cell junction Source: Ensembl
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: Ensembl
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24489.

Polymorphism and mutation databases

DMDMi47117647.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 418417Actin-related protein 3PRO_0000089079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei240 – 2401N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysine1 Publication
Modified residuei251 – 2511N6-acetyllysine1 Publication
Modified residuei254 – 2541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PeptideAtlasiP61158.
PRIDEiP61158.

2D gel databases

OGPiP32391.

PTM databases

PhosphoSiteiP61158.

Miscellaneous databases

PMAP-CutDBP61158.

Expressioni

Gene expression databases

BgeeiP61158.
CleanExiHS_ACTR3.
ExpressionAtlasiP61158. baseline and differential.
GenevisibleiP61158. HS.

Organism-specific databases

HPAiCAB005085.
HPA047016.
HPA051683.

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. Interacts with WHDC1. Interacts weakly with MEFV.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
JUNDP175352EBI-351428,EBI-2682803

Protein-protein interaction databases

BioGridi115403. 58 interactions.
DIPiDIP-33140N.
IntActiP61158. 15 interactions.
MINTiMINT-3022340.
STRINGi9606.ENSP00000263238.

Structurei

3D structure databases

ProteinModelPortaliP61158.
SMRiP61158. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP3 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074695.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiP61158.
OMAiKMQRYAV.
OrthoDBiEOG7TMZRM.
PhylomeDBiP61158.
TreeFamiTF300644.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF175. PTHR11937:SF175. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61158-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR
60 70 80 90 100
VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY
110 120 130 140 150
LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FESFNVPGLY IAVQAVLALA
160 170 180 190 200
ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI
210 220 230 240 250
TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK EFNKYDTDGS
260 270 280 290 300
KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
310 320 330 340 350
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS
360 370 380 390 400
EELSGGRLKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY
410
EEIGPSICRH NPVFGVMS
Length:418
Mass (Da):47,371
Last modified:January 23, 2007 - v3
Checksum:i23E5564198B81C63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33277.1.
RefSeqiNP_005712.1. NM_005721.4.
UniGeneiHs.433512.
Hs.595349.

Genome annotation databases

EnsembliENST00000263238; ENSP00000263238; ENSG00000115091.
GeneIDi10096.
UCSCiuc002tkx.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33277.1.
RefSeqiNP_005712.1. NM_005721.4.
UniGeneiHs.433512.
Hs.595349.

3D structure databases

ProteinModelPortaliP61158.
SMRiP61158. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115403. 58 interactions.
DIPiDIP-33140N.
IntActiP61158. 15 interactions.
MINTiMINT-3022340.
STRINGi9606.ENSP00000263238.

PTM databases

PhosphoSiteiP61158.

Polymorphism and mutation databases

DMDMi47117647.

2D gel databases

OGPiP32391.

Proteomic databases

PeptideAtlasiP61158.
PRIDEiP61158.

Protocols and materials databases

DNASUi10096.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263238; ENSP00000263238; ENSG00000115091.
GeneIDi10096.
UCSCiuc002tkx.2. human.

Organism-specific databases

CTDi10096.
GeneCardsiGC02P114647.
HGNCiHGNC:170. ACTR3.
HPAiCAB005085.
HPA047016.
HPA051683.
MIMi604222. gene.
neXtProtiNX_P61158.
PharmGKBiPA24489.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00550000074695.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiP61158.
OMAiKMQRYAV.
OrthoDBiEOG7TMZRM.
PhylomeDBiP61158.
TreeFamiTF300644.

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.
SignaLinkiP61158.

Miscellaneous databases

ChiTaRSiACTR3. human.
GeneWikiiACTR3.
GenomeRNAii10096.
NextBioi38185.
PMAP-CutDBP61158.
PROiP61158.
SOURCEiSearch...

Gene expression databases

BgeeiP61158.
CleanExiHS_ACTR3.
ExpressionAtlasiP61158. baseline and differential.
GenevisibleiP61158. HS.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF175. PTHR11937:SF175. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
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], 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. 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], CLEAVAGE OF INITIATOR METHIONINE [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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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 nameiARP3_HUMAN
AccessioniPrimary (citable) accession number: P61158
Secondary accession number(s): P32391, Q53QM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 123 of the entry and version 3 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.