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Protein Page:
ARP2 (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
ARP2 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. 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. Belongs to the actin family. ARP2 subfamily. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis; Actin binding protein
Cellular Component: Arp2/3 protein complex; cell projection; cytoplasm; actin cytoskeleton
Molecular Function: actin binding; ATP binding
Biological Process: cell motility
Reference #:  P61160 (UniProtKB)
Alt. Names/Synonyms: Actin-like protein 2; Actin-related protein 2; ACTR2; ARP2; ARP2 actin-related protein 2 homolog (yeast)
Gene Symbols: ACTR2
Molecular weight: 44,761 Da
Basal Isoelectric point: 6.29  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  Regulation of Actin Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ARP2
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 1 K7 _MDSQGRKVVVCDNG
0 2 Y22-p TGFVKCGyAGSNFPE
0 1 T45-p RPIIRSTtkVGNIEI
0 47 K46-u PIIRSTtkVGNIEIk
0 4 K53-u kVGNIEIkDLMVGDE
0 5 Y72-p RSMLEVNyPMENGIV
0 1 K86-u VRNWDDMkHLWDyTF
0 8 Y91-p DMkHLWDyTFGPEkL
0 6 K97-u DyTFGPEkLNIDTRN
0 5 K106-u NIDTRNCkILLTEPP
0 1 T110 RNCkILLTEPPMNPt
0 3 T117-p TEPPMNPtkNREKIV
0 17 K118-u EPPMNPtkNREKIVE
0 5 K195-u DITRYLIkLLLLRGY
0 1 K219 TVRMIKEKLCYVGYN
0 2 Y225 EKLCYVGYNIEQEQK
0 2 K253-u LPDGRIIkVGGERFE
0 10 K299-a DTRSEFYkHIVLSGG
0 4 K299-u DTRSEFYkHIVLSGG
0 1 K322-a SRLERELkQLYLERV
0 2 K322-u SRLERELkQLYLERV
0 2 K331-u LYLERVLkGDVEkLS
0 1 K336-u VLkGDVEkLSKFKIR
0 3 K368-u LADIMKDkDNFWMtR
0 1 T374-p DkDNFWMtRQEyQEk
0 1 Y378-p FWMtRQEyQEkGVRV
0 1 K381-u tRQEyQEkGVRVLEk
0 11 K388-u kGVRVLEkLGVTVR_
  mouse

 
K7-u _MDSQGRkVVVCDNG
Y22 TGFVKCGYAGSNFPE
T45 RPIIRSTTkVGNIEI
K46-u PIIRSTTkVGNIEIk
K53-u kVGNIEIkDLMVGDE
Y72-p RSMLEVNyPMENGIV
K86 VRNWDDMKHLWDyTF
Y91-p DMKHLWDyTFGPEkL
K97-u DyTFGPEkLNIDTRN
K106 NIDTRNCKILLtEPP
T110-p RNCKILLtEPPMNPt
T117-p tEPPMNPtkNREKIV
K118-u EPPMNPtkNREKIVE
K195 DITRYLIKLLLLRGY
K219-u TVRMIKEkLCYVGYN
Y225 EkLCYVGYNIEQEQK
K253 LPDGRIIKVGGERFE
K299-a DTRSEFYkHIVLSGG
K299-u DTRSEFYkHIVLSGG
K322 SRLERELKQLYLERV
K322 SRLERELKQLYLERV
K331 LYLERVLKGDVEKLS
K336 VLKGDVEKLSKFKIR
K368-u LADIMKDkDNFWMTR
T374 DkDNFWMTRQEYQEK
Y378 FWMTRQEYQEKGVRV
K381 TRQEYQEKGVRVLEk
K388-u KGVRVLEkLGVTVR_
  rat

 
K7 _MDSQGRKVVVCDNG
Y22 TGFVKCGYAGSNFPE
T45 RPIIRSTTKVGNIEI
K46 PIIRSTTKVGNIEIK
K53 KVGNIEIKDLMVGDE
Y72 RSMLEVNYPMENGIV
K86 VRNWDDMKHLWDYTF
Y91 DMKHLWDYTFGPEKL
K97 DYTFGPEKLNIDTRS
K106 NIDTRSCKILLTEPP
T110 RSCKILLTEPPMNPT
T117 TEPPMNPTKNREKIV
K118 EPPMNPTKNREKIVE
K195 DITRYLIKLLLLRGY
K219 TVRMIKEKLCYVGyN
Y225-p EKLCYVGyNIEQEQK
K253 LPDGRIIKVGGERFE
K299 DTRSEFYKHIVLSGG
K299 DTRSEFYKHIVLSGG
K322 SRLERELKQLYLERV
K322 SRLERELKQLYLERV
K331 LYLERVLKGDVEKLS
K336 VLKGDVEKLSKFKIR
K368 LADIMKDKDNFWMTR
T374 DKDNFWMTRQEYQEK
Y378 FWMTRQEYQEKGVRV
K381 TRQEYQEKGVRVLEK
K388 KGVRVLEKLGVTVR_
  fruit fly

 
N7 _MDSKGRNVIVCDNG
Y22 TGFVKCGYAGSNFPT
N45 RPMIRAVNKIGDIEV
K46 PMIRAVNKIGDIEVK
K53 KIGDIEVKDLMVGDE
Y72 RSLLEVSYPMENGVV
C86 VRNWDDMCHVWDYTF
Y91 DMCHVWDYTFGPKKM
K97 DYTFGPKKMDIDPTN
K106 DIDPTNTKILLTEPP
T110 TNTKILLTEPPMNPT
T117 TEPPMNPTKNREKMI
K118 EPPMNPTKNREKMIE
K195 DITRYLIKLLLLRGY
K219 TVRIMKEKLCYIGYD
Y225 EKLCYIGYDIEMEQR
K253 LPDGRVIKVGGERFE
K299 DIRPELYKHIVLSGG
K299 DIRPELYKHIVLSGG
K322 SRLEREIKQLYLERV
K322 SRLEREIKQLYLERV
K331 LYLERVLKNDTEKLA
K336 VLKNDTEKLAKFKIR
R368 LAEVTKDRDGFWMSK
S374 DRDGFWMSKQEYQEQ
Y378 FWMSKQEYQEQGLKV
Q381 SKQEYQEQGLKVLQK
K388 QGLKVLQKLQKISH_
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