CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013354
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
53QAQRRVMKGVDDLDFacetylation[1]
244DLVKEFNKYDTDGSKacetylation[1]
251KYDTDGSKWIKQYTGacetylation[1]
254TDGSKWIKQYTGVNAacetylation[1]
348RTVDARLKLSEELSGacetylation[1]
361SGGRLKPKPIDVQVIacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 (By similarity). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 16 16 Phosphotyrosine (By similarity).
 MOD_RES 202 202 Phosphotyrosine (By similarity).
 MOD_RES 231 231 Phosphotyrosine (By similarity).
 MOD_RES 240 240 N6-acetyllysine (By similarity).
 MOD_RES 244 244 N6-acetyllysine (By similarity).
 MOD_RES 251 251 N6-acetyllysine (By similarity).
 MOD_RES 254 254 N6-acetyllysine (By similarity).
 MOD_RES 418 418 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; ATP-binding; Cell projection; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Nucleotide-binding; Phosphoprotein; Polymorphism; 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 KWIKQYTGVN 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; IEA:InterPro.
 GO:0060076; C:excitatory synapse; IDA:RGD.
 GO:0000139; C:Golgi membrane; IDA:RGD.
 GO:0030056; C:hemidesmosome; IDA:RGD.
 GO:0030027; C:lamellipodium; IDA:RGD.
 GO:0002102; C:podosome; IDA:RGD.
 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:0060271; P:cilium morphogenesis; ISS:UniProtKB.
 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:0030838; P:positive regulation of actin filament polymerization; IMP:RGD.
 GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
 GO:0051491; P:positive regulation of filopodium assembly; IMP:RGD.
 GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
 GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
 GO:0043519; P:regulation of myosin II filament organization; IMP:RGD.
 GO:0046677; P:response to antibiotic; IEP:RGD.
 GO:0009743; P:response to carbohydrate stimulus; IEP:RGD.
 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