P61158 (ARP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Actin-related protein 3 Alternative name(s): Actin-like protein 3 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.4 Ref.13 |
| 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.10 |
| Subcellular location | |
| 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 | cellular component movement Traceable author statement Ref.1. Source: UniProtKB cilium morphogenesisInferred from mutant phenotype Ref.13. Source: UniProtKB |
| Cellular component | Arp2/3 protein complex Traceable author statement Ref.1. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin bindingInferred 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.5 | ||||||
| Chain | 2 – 418 | 417 | Actin-related protein 3 | PRO_0000089079 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.5 Ref.11 | ||||||
| Modified residue | 16 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 202 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 231 | 1 | Phosphotyrosine Ref.8 Ref.9 | ||||||
| Modified residue | 240 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 244 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 251 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 254 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 418 | 1 | Phosphoserine By similarity | ||||||
Sequences
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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: 9230079] [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] | "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: Brain. |
| [4] | "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: PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION. |
| [5] | 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. |
| [6] | 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. |
| [7] | "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. |
| [8] | "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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, MASS SPECTROMETRY. |
| [9] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-16; TYR-202 AND TYR-231, MASS SPECTROMETRY. Tissue: Lung carcinoma. |
| [10] | "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: 18614018] [Abstract] Cited for: INTERACTION WITH WHDC1. |
| [11] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [12] | "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-240; LYS-244; LYS-251 AND LYS-254, MASS SPECTROMETRY. |
| [13] | "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: 20393563] [Abstract] Cited for: FUNCTION. |
| [14] | "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: 21269460] [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. BC044590 mRNA. Translation: AAH44590.1. |
| IPI | IPI00028091. |
| RefSeq | NP_005712.1. NM_005721.3. |
| UniGene | Hs.433512. |
3D structure databases | |
| ProteinModelPortal | P61158. |
| SMR | P61158. Positions 3-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-33140N. |
| IntAct | P61158. 10 interactions. |
| STRING | P61158. |
PTM databases | |
| PhosphoSite | P61158. |
Polymorphism databases | |
| DMDM | 47117647. |
2D gel databases | |
| OGP | P32391. |
Proteomic databases | |
| PeptideAtlas | P61158. |
| PRIDE | P61158. |
Protocols and materials databases | |
| 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. |
| H-InvDB | HIX0017317. |
| HGNC | HGNC:170. ACTR3. |
| HPA | CAB005085. |
| MIM | 604222. gene. |
| neXtProt | NX_P61158. |
| PharmGKB | PA24489. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG12759. |
| HOGENOM | HBG559892. |
| HOVERGEN | HBG003771. |
| InParanoid | P61158. |
| OMA | DNVIQNC. |
| OrthoDB | EOG4XKV6W. |
| PhylomeDB | P61158. |
Gene expression databases | |
| ArrayExpress | P61158. |
| Bgee | P61158. |
| CleanEx | HS_ACTR3. |
| Genevestigator | P61158. |
| GermOnline | ENSG00000115091. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004000. Actin-like. IPR020902. Actin/actin-like_CS. IPR015623. Arp3. [Graphical view] |
| PANTHER | PTHR11937. Actin_like. 1 hit. PTHR11937:SF31. Arp3. 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 | |
| NextBio | 38185. |
| PMAP-CutDB | P61158. |
| SOURCE | Search... |
Entry information
| Entry name | ARP3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P61158 Secondary accession number(s): P32391 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with