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Protein Page:
CALCOCO2 (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
CALCOCO2 May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion. Part of a complex consisting of CALCOCO2, TAX1BP1 and MYO6. Interacts with GEMIN4. Expressed in all tissues tested with highest expression in skeletal muscle and lowest in brain. Note: This description may include information from UniProtKB.
Protein type: Calcium-binding protein
Cellular Component: Golgi apparatus; cytoskeleton; intracellular membrane-bound organelle; perinuclear region of cytoplasm; cytoplasm; nucleus
Molecular Function: protein binding; protein homodimerization activity
Biological Process: viral reproduction
Reference #:  Q13137 (UniProtKB)
Alt. Names/Synonyms: Antigen nuclear dot 52 kDa protein; CACO2; calcium binding and coiled-coil domain 2; Calcium-binding and coiled-coil domain-containing protein 2; CALCOCO2; MGC17318; NDP52; Nuclear domain 10 protein 52; Nuclear domain 10 protein NDP52; Nuclear dot protein 52
Gene Symbols: CALCOCO2
Molecular weight: 52,254 Da
Basal Isoelectric point: 4.94  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CALCOCO2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
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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 K87-ub DLNNKSAkQQEVQFK
0 1 Y96-p QEVQFKAyYLPKDDE
0 1 Y104-p YLPKDDEyyQFCYVD
0 1 Y105-p LPKDDEyyQFCYVDE
0 9 Y204-p KVKEQKDyWETELLQ
0 1 K242-ub AQLSTQEkEMEKLVQ
0 5 K281-ub EQRKDQKkLEQTVEQ
0 3 K299-ub NETTAMKkQQELMDE
0 9 K312-ub DENFDLSkRLsENEI
0 1 S315-p FDLSkRLsENEIICN
0 28 K339-ub EGENDLLkRENSRLL
0 1 S347-p RENSRLLsYMGLDFN
0 9 S355-p YMGLDFNsLPyQVPT
0 5 Y358-p LDFNsLPyQVPTSDE
0 1 Y376-p RQNPGLAyGNPySGI
0 1 Y380-p GLAyGNPySGIQESS
0 36 K395-ub SPSPLSIkkCPICKA
0 4 K396-ub PSPLSIkkCPICKAD
0 1 S445-p EDHVFCHsL______
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