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Protein Page:
ARPC2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ARPC2 Functions as actin-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 mother actin filament. Belongs to the ARPC2 family. Note: This description may include information from UniProtKB.
Protein type: Actin-binding; Cytoskeletal; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 2q36.1
Cellular Component: actin cytoskeleton; Arp2/3 protein complex; cytoplasm; cytosol; focal adhesion; Golgi apparatus
Molecular Function: actin filament binding; protein binding; structural constituent of cytoskeleton
Biological Process: cell motility; ephrin receptor signaling pathway
Reference #:  O15144 (UniProtKB)
Alt. Names/Synonyms: actin related protein 2/3 complex, subunit 2, 34kDa; Actin-related protein 2/3 complex subunit 2; ARC34; Arp2/3 complex 34 kDa subunit; ARP2/3 protein complex subunit 34; ARPC2; p34-ARC; PNAS-139; PRO2446
Gene Symbols: ARPC2
Molecular weight: 34,333 Da
Basal Isoelectric point: 6.84  Predict pI for various phosphorylation states
Select Structure to View Below

ARPC2

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 K65 SISLKFYKELQAHGA
0 2 K65‑ub SISLKFYkELQAHGA
0 2 K77 HGADELLKRVYGSFL
0 2 S108‑p NLPASKDsIVHQAGM
0 1 K117 VHQAGMLKRNCFAsV
0 2 K117‑ub VHQAGMLkRNCFAsV
0 1 K117‑sc VHQAGMLkRNCFAsV
0 1 S123‑p LkRNCFAsVFEkYFQ
0 2 K127‑ac CFAsVFEkYFQFQEE
0 2 K136 FQFQEEGKEGENRAV
0 5 K136‑ub FQFQEEGkEGENRAV
0 1 T151‑p IHYRDDEtMyVEskK
0 4 Y153‑p YRDDEtMyVEskKDR
0 1 S156‑p DEtMyVEskKDRVTV
0 1 K157‑ub EtMyVEskKDRVTVV
0 3 K186‑ac KVFMQEFkEGRRASH
0 3 K186‑ub KVFMQEFkEGRRASH
0 1 T194‑p EGRRASHtAPQVLFS
0 1 K210‑ub REPPLELkDTDAAVG
0 1 Y250‑p LIHTFRDyLHyHIkC
0 1 Y253‑p TFRDyLHyHIkCSKA
0 1 K256‑ub DyLHyHIkCSKAyIH
0 1 Y261‑p HIkCSKAyIHTRMRA
0 1 K269 IHTRMRAKTSDFLkV
0 1 K269‑ub IHTRMRAkTSDFLkV
0 4 K275‑ac AkTSDFLkVLNRARP
0 5 K275‑ub AkTSDFLkVLNRARP
0 5 K295‑ac EMKTITGktFSSR__
0 4 K295‑ub EMKTITGktFSSR__
0 1 T296‑p MKTITGktFSSR___
  mouse

 
K65 SISLKFYKELQAHGA
K65‑ub SISLKFYkELQAHGA
K77‑ac HGADELLkRVYGSFL
S108‑p NLPASKDsIVHQAGM
K117 VHQAGMLKRNCFASV
K117 VHQAGMLKRNCFASV
K117 VHQAGMLKRNCFASV
S123 LKRNCFASVFEKYFQ
K127 CFASVFEKYFQFQEE
K136‑ac FQFQEEGkEGENRAV
K136‑ub FQFQEEGkEGENRAV
T151 IHYRDDETMYVESKK
Y153 YRDDETMYVESKKDR
S156 DETMYVESKKDRVTV
K157 ETMYVESKKDRVTVV
K186‑ac KVFMQEFkEGRRASH
K186 KVFMQEFKEGRRASH
T194 EGRRASHTAPQVLFS
K210 REPPLELKDTDAAVG
Y250 LIHTFRDYLHYHIKC
Y253 TFRDYLHYHIKCSKA
K256 DYLHYHIKCSKAYIH
Y261 HIKCSKAYIHTRMRA
K269 IHTRMRAKTSDFLkV
K269 IHTRMRAKTSDFLkV
K275‑ac AKTSDFLkVLNRARP
K275‑ub AKTSDFLkVLNRARP
K295 EMKTITGKTFSSR__
K295‑ub EMKTITGkTFSSR__
T296 MKTITGkTFSSR___
  rat

 
K65‑ac SISLKFYkELQAHGA
K65 SISLKFYKELQAHGA
K77‑ac HGADELLkRVYGSFL
S108 NLPASKDSIVHQAGM
K117‑ac VHQAGMLkRNCFASV
K117 VHQAGMLKRNCFASV
K117 VHQAGMLKRNCFASV
S123 LkRNCFASVFEKYFQ
K127 CFASVFEKYFQFQEE
K136‑ac FQFQEEGkEGENRAV
K136 FQFQEEGKEGENRAV
T151 IHYRDDETMYVESKK
Y153 YRDDETMYVESKKDR
S156 DETMYVESKKDRVTV
K157 ETMYVESKKDRVTVV
K186‑ac KVFMQEFkEGRRASH
K186 KVFMQEFKEGRRASH
T194 EGRRASHTAPQVLFS
K210 REPPLELKDTDAAVG
Y250 LIHTFRDYLHYHIKC
Y253 TFRDYLHYHIKCSKA
K256 DYLHYHIKCSKAYIH
Y261 HIKCSKAYIHTRMRA
K269‑ac IHTRMRAkTSDFLkV
K269 IHTRMRAKTSDFLkV
K275‑ac AkTSDFLkVLNRARP
K275 AkTSDFLKVLNRARP
K295 EMKTITRKTFSST__
K295 EMKTITRKTFSST__
T296 MKTITRKTFSST___
  cow

 
K65 SISLKFYKELQAHGA
K65 SISLKFYKELQAHGA
K77 HGADELLKRVYGSYL
S108 NLPASKDSIVHQAGM
K117 VHQAGMLKRNCFASV
K117 VHQAGMLKRNCFASV
K117 VHQAGMLKRNCFASV
S123 LKRNCFASVFEKYFQ
K127 CFASVFEKYFQFQEE
K136 FQFQEEGKEGENRAV
K136 FQFQEEGKEGENRAV
T151 IHYRDDETMYVESKK
Y153 YRDDETMYVESKKDR
S156 DETMYVESKKDRVTV
K157 ETMYVESKKDRVTVV
K186 KVFMQEFKEGRRASH
K186 KVFMQEFKEGRRASH
T194 EGRRASHTAPQVLFS
K210 REPPLELKDTDAAVG
Y250 LIHTFRDYLHYHIKC
Y253 TFRDYLHYHIKCSKA
K256 DYLHYHIKCSKAYIH
Y261 HIKCSKAYIHTRMRA
K269 IHTRMRAKTSDFLKV
K269 IHTRMRAKTSDFLKV
K275 AKTSDFLKVLNRARP
K275 AKTSDFLKVLNRARP
K295 EMKTITGKTFSSR__
K295 EMKTITGKTFSSR__
T296 MKTITGKTFSSR___
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