CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actin-related protein 3 
Protein Synonyms/Alias
 Actin-like protein 3 
Gene Name
 ACTR3 
Gene Synonyms/Alias
 ARP3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38IPSCIAIKESAKVGDubiquitination[1, 2, 3]
42IAIKESAKVGDQAQRubiquitination[2, 4]
53QAQRRVMKGVDDLDFacetylation[5]
53QAQRRVMKGVDDLDFubiquitination[2, 3, 4, 6, 7]
69IGDEAIEKPTYATKWubiquitination[2, 4, 6, 7, 8]
75EKPTYATKWPIRHGIubiquitination[2, 4, 7]
99FMEQVIFKYLRAEPEubiquitination[2, 4, 6, 7]
191YVIGSCIKHIPIAGRubiquitination[2]
225EQSLETAKAVKERYSubiquitination[2, 4]
228LETAKAVKERYSYVCubiquitination[2]
240YVCPDLVKEFNKYDTacetylation[9]
240YVCPDLVKEFNKYDTubiquitination[2, 6, 10, 11]
244DLVKEFNKYDTDGSKacetylation[9]
244DLVKEFNKYDTDGSKubiquitination[2, 4, 7]
251KYDTDGSKWIKQYTGacetylation[9]
251KYDTDGSKWIKQYTGubiquitination[2, 4, 6, 8, 10, 11]
254TDGSKWIKQYTGINAacetylation[9]
254TDGSKWIKQYTGINAubiquitination[2, 4, 6, 7, 11]
264TGINAISKKEFSIDVubiquitination[2, 10]
265GINAISKKEFSIDVGubiquitination[2, 4, 6, 11]
317DVRRPLYKNIVLSGGubiquitination[2]
348RTVDARLKLSEELSGubiquitination[2, 4, 7, 10, 12]
359ELSGGRLKPKPIDVQubiquitination[2, 6, 8, 11]
361SGGRLKPKPIDVQVIubiquitination[2, 6, 8, 11]
398YQVCHTKKDYEEIGPubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [9] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [11] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
 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. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 240 240 N6-acetyllysine.
 MOD_RES 244 244 N6-acetyllysine.
 MOD_RES 251 251 N6-acetyllysine.
 MOD_RES 254 254 N6-acetyllysine.
 MOD_RES 418 418 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; ATP-binding; Cell projection; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 418 AA 
Protein Sequence
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF 60
FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP 120
ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV 180
AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK 240
EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV 300
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP 360
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS 418 
Gene Ontology
 GO:0005885; C:Arp2/3 protein complex; TAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0060076; C:excitatory synapse; IEA:Compara.
 GO:0000139; C:Golgi membrane; IEA:Compara.
 GO:0030056; C:hemidesmosome; IEA:Compara.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0002102; C:podosome; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
 GO:0008356; P:asymmetric cell division; IEA:Compara.
 GO:0006928; P:cellular component movement; TAS:UniProtKB.
 GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0051321; P:meiotic cell cycle; IEA:Compara.
 GO:0033206; P:meiotic cytokinesis; IEA:Compara.
 GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Compara.
 GO:0051491; P:positive regulation of filopodium assembly; IEA:Compara.
 GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Compara.
 GO:0045666; P:positive regulation of neuron differentiation; IEA:Compara.
 GO:0043519; P:regulation of myosin II filament organization; IEA:Compara.
 GO:0046677; P:response to antibiotic; IEA:Compara.
 GO:0009743; P:response to carbohydrate stimulus; IEA:Compara.
 GO:0051653; P:spindle localization; IEA:Compara. 
Interpro
 IPR004000; Actin-related.
 IPR020902; Actin/actin-like_CS.
 IPR015623; Arp3. 
Pfam
 PF00022; Actin 
SMART
 SM00268; ACTIN 
PROSITE
 PS01132; ACTINS_ACT_LIKE 
PRINTS