CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031386
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actin-related protein 3 
Protein Synonyms/Alias
 cDNA FLJ51148, highly similar to Actin-like protein 3; cDNA FLJ52434, highly similar to Actin-like protein 3; cDNA, FLJ79112, highly similar to Actin-like protein 3; cDNA, FLJ79295, highly similar to Actin-like protein 3 
Gene Name
 ACTR3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18IGDEAIEKPTYATKWubiquitination[1, 2, 3, 4, 5, 6]
24EKPTYATKWPIRHGIubiquitination[2, 3, 4, 5, 6]
48FMEQVIFKYLRAEPEubiquitination[2, 3, 4, 5, 6, 7]
140YVIGSCIKHIPIAGRubiquitination[4, 6]
174EQSLETAKAVKERYSubiquitination[2, 4, 6]
177LETAKAVKERYSYVCubiquitination[4, 6]
189YVCPDLVKEFNKYDTacetylation[6, 8]
189YVCPDLVKEFNKYDTubiquitination[4, 6, 7, 9]
193DLVKEFNKYDTDGSKacetylation[6, 10]
193DLVKEFNKYDTDGSKubiquitination[2, 4, 5]
200KYDTDGSKWIKQYTGacetylation[6, 8, 10]
200KYDTDGSKWIKQYTGubiquitination[1, 2, 4, 6, 7, 9]
203TDGSKWIKQYTGINAubiquitination[2, 3, 4, 5, 6, 7]
213TGINAISKKEFSIDVubiquitination[4, 6, 9]
214GINAISKKEFSIDVGubiquitination[2, 4, 6, 7]
266DVRRPLYKNIVLSGGubiquitination[4]
297RTVDARLKLSEELSGubiquitination[2, 4, 5, 6, 9, 11]
308ELSGGRLKPKPIDVQubiquitination[1, 4, 6, 7]
310SGGRLKPKPIDVQVIubiquitination[1, 4, 7]
347YQVCHTKKDYEEIGPubiquitination[4, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [11] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 367 AA 
Protein Sequence
MKGVDDLDFF IGDEAIEKPT YATKWPIRHG IVEDWDLMER FMEQVIFKYL RAEPEDHYFL 60
LTEPPLNTPE NREYTAEIMF ESFNVPGLYI AVQAVLALAA SWTSRQVGER TLTGTVIDSG 120
DGVTHVIPVA EGYVIGSCIK HIPIAGRDIT YFIQQLLRDR EVGIPPEQSL ETAKAVKERY 180
SYVCPDLVKE FNKYDTDGSK WIKQYTGINA ISKKEFSIDV GYERFLGPEI FFHPEFANPD 240
FTQPISEVVD EVIQNCPIDV RRPLYKNIVL SGGSTMFRDF GRRLQRDLKR TVDARLKLSE 300
ELSGGRLKPK PIDVQVITHH MQRYAVWFGG SMLASTPEFY QVCHTKKDYE EIGPSICRHN 360
PVFGVMS 367 
Gene Ontology
 GO:0005885; C:Arp2/3 protein complex; IEA:InterPro.
 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:InterPro.
 GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
 GO:0008356; P:asymmetric cell division; IEA:Compara.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 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