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Protein Page:
ARP2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Motility/polarity/chemotaxis; Cytoskeletal protein; Actin binding protein
Cellular Component: Arp2/3 protein complex; cell projection; cytosol; actin cap; actin cytoskeleton
Molecular Function: actin binding; ATP binding
Biological Process: asymmetric cell division; establishment and/or maintenance of cell polarity; innate immune response; cytokinesis after meiosis; cell motility; actin cytoskeleton organization and biogenesis; cytoplasmic transport; spindle localization
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:  Actin Dynamics  |  Adherens Junction 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-ub PIIRSTtkVGNIEIk
0 4 K53-ub kVGNIEIkDLMVGDE
0 1 S62-p LMVGDEAsELRSMLE
0 5 Y72-p RSMLEVNyPMENGIV
0 1 K86 VRNWDDMKHLWDyTF
0 1 K86-ub VRNWDDMkHLWDyTF
0 8 Y91-p DMkHLWDyTFGPEkL
0 1 K97 DyTFGPEKLNIDTRN
0 6 K97-ub DyTFGPEkLNIDTRN
0 5 K106-ub NIDTRNCkILLTEPP
0 1 T110 RNCkILLTEPPMNPt
0 4 T117-p TEPPMNPtkNREKIV
0 17 K118-ub EPPMNPtkNREKIVE
0 5 K195-ub DITRYLIkLLLLRGY
0 1 K219 TVRMIKEKLCYVGYN
0 2 Y225 EKLCYVGYNIEQEQK
0 2 K253-ub LPDGRIIkVGGERFE
0 11 K299-ac DTRSEFYkHIVLSGG
0 4 K299-ub DTRSEFYkHIVLSGG
0 2 K322-ac SRLERELkQLYLERV
0 2 K322-ub SRLERELkQLYLERV
0 2 K331-ub LYLERVLkGDVEkLS
0 1 K331-sc LYLERVLkGDVEkLS
0 1 K336-ub VLkGDVEkLSKFKIR
0 3 K368-ub LADIMKDkDNFWMtR
0 1 T374-p DkDNFWMtRQEyQEk
0 1 Y378-p FWMtRQEyQEkGVRV
0 1 K381-ub tRQEyQEkGVRVLEk
0 11 K388-ub kGVRVLEkLGVTVR_
  mouse

 
K7-ub _MDSQGRkVVVCDNG
Y22 TGFVKCGYAGSNFPE
T45 RPIIRSTTkVGNIEI
K46-ub PIIRSTTkVGNIEIk
K53-ub kVGNIEIkDLMVGDE
S62 LMVGDEASELRSMLE
Y72-p RSMLEVNyPMENGIV
K86-ac VRNWDDMkHLWDyTF
K86 VRNWDDMKHLWDyTF
Y91-p DMkHLWDyTFGPEkL
K97-ac DyTFGPEkLNIDTRN
K97-ub DyTFGPEkLNIDTRN
K106 NIDTRNCKILLtEPP
T110-p RNCKILLtEPPMNPt
T117-p tEPPMNPtkNREKIV
K118-ub EPPMNPtkNREKIVE
K195 DITRYLIKLLLLRGY
K219-ub TVRMIKEkLCYVGYN
Y225 EkLCYVGYNIEQEQK
K253 LPDGRIIKVGGERFE
K299-ac DTRSEFYkHIVLSGG
K299-ub DTRSEFYkHIVLSGG
K322-ac SRLERELkQLYLERV
K322 SRLERELKQLYLERV
K331 LYLERVLKGDVEKLS
K331 LYLERVLKGDVEKLS
K336 VLKGDVEKLSKFKIR
K368-ub LADIMKDkDNFWMTR
T374 DkDNFWMTRQEYQEK
Y378 FWMTRQEYQEKGVRV
K381 TRQEYQEKGVRVLEk
K388-ub KGVRVLEkLGVTVR_
  rat

 
K7 _MDSQGRKVVVCDNG
Y22 TGFVKCGYAGSNFPE
T45 RPIIRSTTKVGNIEI
K46 PIIRSTTKVGNIEIK
K53 KVGNIEIKDLMVGDE
S62 LMVGDEASELRSMLE
Y72 RSMLEVNYPMENGIV
K86 VRNWDDMKHLWDYTF
K86 VRNWDDMKHLWDYTF
Y91 DMKHLWDYTFGPEKL
K97 DYTFGPEKLNIDTRS
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
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 KIGDIEVKDLHVDDL
S67 LMVGDEASQLRSLLE
Y77 RSLLEVSYPMENGVV
C91 VRNWDDMCHVWDYTF
C91 VRNWDDMCHVWDYTF
Y96 DMCHVWDYTFGPKKM
K102 DYTFGPKKMDIDPTN
K102 DYTFGPKKMDIDPTN
K111 DIDPTNTKILLTEPP
T115 TNTKILLTEPPMNPT
T122 TEPPMNPTKNREKMI
K123 EPPMNPTKNREKMIE
K200 DITRYLIKLLLLRGY
K224 TVRIMKEKLCYIGYD
Y230 EKLCYIGYDIEMEQR
K258 LPDGRVIKVGGERFE
K304 DIRPELYKHIVLSGG
K304 DIRPELYKHIVLSGG
K327 SRLEREIKQLYLERV
K327 SRLEREIKQLYLERV
K336 LYLERVLKNDTEKLA
K336 LYLERVLKNDTEKLA
K341 VLKNDTEKLAKFKIR
R373 LAEVTKDRDGFWMSK
S379 DRDGFWMSKQEYQEQ
Y383 FWMSKQEYQEQGLKV
Q386 SKQEYQEQGLKVLQK
K393 QGLKVLQKLQKISH_
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