Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Coiled-coil domain-containing protein 50  

UniProtKB / Swiss-Prot ID :  CCD50_HUMAN

Gene Name (Synonyms) : 
CCDC50, C3orf6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Note=Associated with microtubules of the cytoskeleton and mitotic apparatus (By similarity). 

Protein Function :  Involved in EGFR signaling. 

Protein Sequence MAEVSIDQSKLPGVKEVCRDFAVLEDHTLAHSLQEQEIEHHLASNVQRNRLVQHDLQVAKQLQEEDLKAQ...
Predicted Secondary Structure CCCCCCCHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
121L -> F (in dbSNP:rs35380043). VAR_050754
156M -> T (in dbSNP:rs293813). VAR_050755
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEVSI
---CCCCCC
26.37UniProtKB
Link-
129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKRKKHFPE
HHHHHCCCC
55.28Phosphositeplus
Link-
129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKRKKHFPE
HHHHHCCCC
55.28UbiProtDB
Link-
140PhosphotyrosineATRAYADSY
CCCCCCCCC
13.98HPRD
Link-
140PhosphotyrosineATRAYADSY
CCCCCCCCC
13.98HPRD
Link-
140PhosphotyrosineATRAYADSY
CCCCCCCCC
13.98Phosphositeplus
Link-
140Phosphotyrosine.ATRAYADSY
CCCCCCCCC
13.98UniProtKB
Link-
144PhosphotyrosineYADSYYYED
CCCCCCCCC
15.60HPRD
Link-
144PhosphotyrosineYADSYYYED
CCCCCCCCC
15.60HPRD
Link-
144PhosphotyrosineYADSYYYED
CCCCCCCCC
15.60Phosphositeplus
Link-
144PhosphotyrosineYADSYYYED
CCCCCCCCC
15.60SysPTM
Link-
144Phosphotyrosine.YADSYYYED
CCCCCCCCC
15.60UniProtKB
Link-
145PhosphotyrosineADSYYYEDG
CCCCCCCCC
12.34HPRD
Link-
145PhosphotyrosineADSYYYEDG
CCCCCCCCC
12.34HPRD
Link-
145PhosphotyrosineADSYYYEDG
CCCCCCCCC
12.34Phosphositeplus
Link-
145Phosphotyrosine.ADSYYYEDG
CCCCCCCCC
12.34UniProtKB
Link-
146PhosphotyrosineDSYYYEDGG
CCCCCCCCC
10.18Phosphositeplus
Link-
152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DGGMKPRVM
CCCCCCCCC
32.71Phosphositeplus
Link-
217PhosphotyrosineEKKAYKKAK
HHHHHHHHH
23.15Phosphositeplus
Link-
279PhosphotyrosineEDADYTHFT
CCCCCCCCC
12.11HPRD
Link-
279PhosphotyrosineEDADYTHFT
CCCCCCCCC
12.11Phosphositeplus
Link-
279PhosphotyrosineEDADYTHFT
CCCCCCCCC
12.11SysPTM
Link-
279Phosphotyrosine.EDADYTHFT
CCCCCCCCC
12.11UniProtKB
Link-
304PhosphotyrosineKGFHYKH
CCCCCCC
14.43Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RS3A_HUMANphysical interactionMINT-64849MINT16169070
RS3A_HUMANphysical interactionEBI-736406
intact16169070
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Disease Reference
Kegg disease
OMIM disease
607453Deafness, autosomal dominant, 44 (DFNA44)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140 AND TYR-145, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144 AND TYR-279, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144 AND TYR-279, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures