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Protein Page:
Arp3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Arp3 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. 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. Belongs to the actin family. ARP3 subfamily. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis
Cellular Component: Golgi membrane; Arp2/3 protein complex; hemidesmosome; lamellipodium; excitatory synapse; podosome; cytosol; actin cytoskeleton
Molecular Function: protein binding; actin binding; ATP binding
Biological Process: response to antibiotic; positive regulation of filopodium formation; positive regulation of actin filament polymerization; asymmetric cell division; regulation of myosin II filament assembly or disassembly; establishment and/or maintenance of cell polarity; innate immune response; cytokinesis after meiosis; positive regulation of dendrite morphogenesis; positive regulation of neuron differentiation; cell motility; response to carbohydrate stimulus; spindle localization
Reference #:  P61158 (UniProtKB)
Alt. Names/Synonyms: Actin-like protein 3; Actin-related protein 3; ACTR3; ARP3; ARP3 actin-related protein 3 homolog (yeast)
Gene Symbols: ACTR3
Molecular weight: 47,371 Da
Basal Isoelectric point: 5.61  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Arp3

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 89 Y16-p VVDCGTGyTKLGYAG
0 4 K42-u IAIKESAkVGDQAQR
0 7 K53-u QAQRRVMkGVDDLDF
0 17 K69-u IGDEAIEkPTYATkW
0 1 T71 DEAIEkPTYATkWPI
0 1 Y72 EAIEkPTYATkWPIR
0 1 T74 IEkPTYATkWPIRHG
0 8 K75-u EkPTYATkWPIRHGI
0 8 K99-u FMEQVIFkyLRAEPE
0 6 Y100-p MEQVIFkyLRAEPED
0 36 Y109-p RAEPEDHyFLLTEPP
0 2 Y184-p VIPVAEGyVIGSCIk
0 3 K191-u yVIGSCIkHIPIAGR
0 1 T201-p PIAGRDItyFIQQLL
0 228 Y202-p IAGRDItyFIQQLLR
0 1 K225-u EQSLETAkAVKERyS
0 11 Y231-p AkAVKERySyVCPDL
0 2 Y233-p AVKERySyVCPDLVk
0 1 K240-a yVCPDLVkEFNkYDT
0 3 K240-u yVCPDLVkEFNkYDT
0 6 K244-a DLVkEFNkYDTDGSk
0 1 K244-u DLVkEFNkYDTDGSk
0 1 K251-a kYDTDGSkWIkQYTG
0 11 K251-u kYDTDGSkWIkQYTG
0 1 K254-a TDGSkWIkQYTGINA
0 5 K254-u TDGSkWIkQYTGINA
1 1 T257 SkWIkQYTGINAISK
0 1 K264 TGINAISKkEFSIDV
0 3 K265-u GINAISKkEFSIDVG
0 3 K317-u DVRRPLYkNIVLSGG
0 1 T326-p IVLSGGStMFRDFGR
0 20 K348-u RTVDARLkLSEELSG
0 1 K359-u ELSGGRLkPkPIDVQ
0 4 K361-u SGGRLkPkPIDVQVI
0 1 K398 YQVCHTKKDYEEIGP
0 8 S418-p NPVFGVMs_______
  mouse

 
Y16-p VVDCGTGyTKLGYAG
K42 IAIKESAKVGDQAQR
K53-u QAQRRVMkGVDDLDF
K69-u IGDEAIEkPtyAtkW
T71-p DEAIEkPtyAtkWPI
Y72-p EAIEkPtyAtkWPIR
T74-p IEkPtyAtkWPIRHG
K75-u EkPtyAtkWPIRHGI
K99-u FMEQVIFkyLRAEPE
Y100-p MEQVIFkyLRAEPED
Y109-p RAEPEDHyFLLTEPP
Y184 VIPVAEGYVIGSCIk
K191-u YVIGSCIkHIPIAGR
T201 PIAGRDITyFIQQLL
Y202-p IAGRDITyFIQQLLR
K225 EQSLETAKAVKERyS
Y231-p AKAVKERySYVCPDL
Y233 AVKERySYVCPDLVk
K240 YVCPDLVKEFNKYDT
K240-u YVCPDLVkEFNKYDT
K244 DLVkEFNKYDTDGSk
K244 DLVkEFNKYDTDGSk
K251 KYDTDGSKWIkQYTG
K251-u KYDTDGSkWIkQYTG
K254 TDGSkWIKQYTGVNA
K254-u TDGSkWIkQYTGVNA
T257 SkWIkQYTGVNAISk
K264-u TGVNAISkkEFSIDV
K265-u GVNAISkkEFSIDVG
K317-u DVRRPLYkNIVLSGG
T326 IVLSGGSTMFRDFGR
K348-u RTVDARLkLSEELSG
K359 ELSGGRLKPkPIDVQ
K361-u SGGRLKPkPIDVQVI
K398-u YQVCHTKkDYEEIGP
S418-p NPVFGVMs_______
  rat

 
Y16 VVDCGTGYTKLGYAG
K42 IAIKESAKVGDQAQR
K53 QAQRRVMKGVDDLDF
K69 IGDEAIEKPTYATKW
T71 DEAIEKPTYATKWPI
Y72 EAIEKPTYATKWPIR
T74 IEKPTYATKWPIRHG
K75 EKPTYATKWPIRHGI
K99 FMEQVIFKYLRAEPE
Y100 MEQVIFKYLRAEPED
Y109 RAEPEDHYFLLTEPP
Y184 VIPVAEGYVIGSCIK
K191 YVIGSCIKHIPIAGR
T201-p PIAGRDItyFIQQLL
Y202-p IAGRDItyFIQQLLR
K225 EQSLETAKAVKERYS
Y231 AKAVKERYSYVCPDL
Y233 AVKERYSYVCPDLVK
K240 YVCPDLVKEFNKYDT
K240 YVCPDLVKEFNKYDT
K244 DLVKEFNKYDTDGSK
K244 DLVKEFNKYDTDGSK
K251 KYDTDGSKWIKQYtG
K251 KYDTDGSKWIKQYtG
K254 TDGSKWIKQYtGVNA
K254 TDGSKWIKQYtGVNA
T257-p SKWIKQYtGVNAISK
K264 tGVNAISKKEFSIDV
K265 GVNAISKKEFSIDVG
K317 DVRRPLYKNIVLSGG
T326 IVLSGGSTMFRDFGR
K348 RTVDARLKLSEELSG
K359 ELSGGRLKPKPIDVQ
K361 SGGRLKPKPIDVQVI
K398 YQVCHTKKDYEEIGP
S418 NPVFGVMS_______
  cow

 
Y16 VVDCGTGYTKLGYAG
K42 IAIKESAKVGDQAQR
K53 QAQRRVMKGVDDLDF
K69 IGDEAIEKPTYATKW
T71 DEAIEKPTYATKWPI
Y72 EAIEKPTYATKWPIR
T74 IEKPTYATKWPIRHG
K75 EKPTYATKWPIRHGI
K99 FMEQVIFKYLRAEPE
Y100 MEQVIFKYLRAEPED
Y109 RAEPEDHYFLLTEPP
Y184 VIPVAEGYVIGSCIK
K191 YVIGSCIKHIPIAGR
T201 PIAGRDITYFIQQLL
Y202 IAGRDITYFIQQLLR
K225 EQSLETAKAVKERYS
Y231 AKAVKERYSYVCPDL
Y233 AVKERYSYVCPDLVK
K240 YVCPDLVKEFNKYDT
K240 YVCPDLVKEFNKYDT
K244 DLVKEFNKYDTDGSK
K244 DLVKEFNKYDTDGSK
K251 KYDTDGSKWIKQYTG
K251 KYDTDGSKWIKQYTG
K254 TDGSKWIKQYTGINA
K254 TDGSKWIKQYTGINA
T257 SKWIKQYTGINAISK
K264 TGINAISKKEFSIDV
K265 GINAISKKEFSIDVG
K317 DVRRPLYKNIVLSGG
T326 IVLSGGSTMFRDFGR
K348 RTVDARLKLSEELSG
K359 ELSGGRLKPKPIDVQ
K361 SGGRLKPKPIDVQVI
K398 YQVCHTKKDYEEIGP
S418 NPVFGVMS_______
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