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Protein Page:
coronin 2B (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
coronin 2B May play a role in the reorganization of neuronal actin structure. Belongs to the WD repeat coronin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Actin binding protein; Cytoskeletal protein
Cellular Component: membrane; cytoplasm; actin cytoskeleton
Molecular Function: actin filament binding; actin binding
Biological Process: actin cytoskeleton organization and biogenesis
Reference #:  Q9UQ03 (UniProtKB)
Alt. Names/Synonyms: clipin C; Clipin-C; CLIPINC; COR2B; CORO2B; coronin 2B; coronin, actin binding protein, 2B; coronin, actin-binding protein, 2B; coronin, actin-binding, 2B; Coronin-2B; Coronin-like protein C; KIAA0925; Protein FC96
Gene Symbols: CORO2B
Molecular weight: 54,953 Da
Basal Isoelectric point: 8.53  Predict pI for various phosphorylation states
Select Structure to View Below

coronin 2B
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 K123 EIPEGGLKRNMtEAL
0 1 T127-p GGLKRNMtEALLELH
0 3 K221-u VLQEANCkNHRVNRV
0 2 K235 VVFLGNMKRLLTTGV
0 1 Y364-p VPRRSDSyQEDIyPM
0 1 Y369-p DSyQEDIyPMTPGTE
0 1 K402-a MSLKEGYkkSSkMVF
0 1 K403-a SLKEGYkkSSkMVFk
0 1 K406-a EGYkkSSkMVFkAPI
0 1 K410-a kSSkMVFkAPIKEkK
0 1 K416-a FkAPIKEkKsVVVNG
0 1 S418-p APIKEkKsVVVNGID
0 1 K453 QDEIRRLKEELAQKD
  mouse

 
K123-u EIPDGGLkRNMTEAL
T127 GGLkRNMTEALLELH
K221-u VLQEANCkNHRVNRV
K235 VVFLGNMKRLLTTGV
Y364-p VPRRSDSyQEDIYPM
Y369 DSyQEDIYPMTPGTE
K402 MSLKEGYKKSSKVVF
K403 SLKEGYKKSSKVVFK
K406 EGYKKSSKVVFKAPI
K410 KSSKVVFKAPIREKK
K416 FKAPIREKKSVVVNG
S418 APIREKKSVVVNGID
K453-m1 QDEIRRLkEELAQKD
  rat

 
K118 EIPEGGLKRNMTEAL
T122 GGLKRNMTEALLELH
K216 VLQEANCKNHRVNRV
K230-u VVFLGNMkRLLTTGV
Y359 VPRRSDSYQEDIYPM
Y364 DSYQEDIYPMTPGTE
K397 MSLKEGYKKSSKVVF
K398 SLKEGYKKSSKVVFK
K401 EGYKKSSKVVFKAPI
K405 KSSKVVFKAPIREKK
K411 FKAPIREKKSVVVNG
S413 APIREKKSVVVNGID
K448 QDEIRRLKEELAQKD
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