Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein CDV3 homolog  

UniProtKB / Swiss-Prot ID :  CDV3_HUMAN

Gene Name (Synonyms) : 
CDV3, H41  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). 

Protein Function :   

Protein Sequence MAETEERSLDNFFAKRDKKKKKERSNRAASAAGAAGSAGGSSGAAGAAGGGAGAGTRPGDGGTASAGAAG...
Predicted Secondary Structure  -
Protein Variant -
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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
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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.---MAETEE
---
32.21UniProtKB
Link-
4Phosphothreonine-MAETEERS
-
33.34HPRD
Link-
4Phosphothreonine-MAETEERS
-
33.34Phosphositeplus
Link-
8PhosphoserineTEERSLDNF
43.27HPRD
Link-
8PhosphoserineTEERSLDNF
43.27Phosphositeplus
Link-
8PhosphoserineTEERSLDNF
43.27SysPTM
Link-
15N6-acetyllysineNFFAKRDKK
56.84HPRD
Link-
15N6-acetyllysineNFFAKRDKK
56.84Phosphositeplus
Link-
15N6-acetyllysine.NFFAKRDKK
56.84UniProtKB
Link-
25PhosphoserineKKERSNRAA
31.59HPRD
Link-
25PhosphoserineKKERSNRAA
31.59PhosphoELM
Link-
25PhosphoserineKKERSNRAA
31.59Phosphositeplus
Link-
25Phosphoserine.KKERSNRAA
31.59UniProtKB
Link-
37PhosphoserineGAAGSAGGS
21.00HPRD
Link-
41PhosphoserineSAGGSSGAA
25.36HPRD
Link-
56PhosphothreonineAGAGTRPGD
32.91HPRD
Link-
75PhosphothreoninePGAATKAVT
20.99HPRD
Link-
95PhosphotyrosineKEVDYSGLR
15.15HPRD
Link-
95PhosphotyrosineKEVDYSGLR
15.15PhosphoELM
Link-
95PhosphotyrosineKEVDYSGLR
15.15Phosphositeplus
Link-
95PhosphotyrosineKEVDYSGLR
15.15SysPTM
Link-
95Phosphotyrosine.KEVDYSGLR
15.15UniProtKB
Link-
106PhosphoserineAMQISSEKE
18.62HPRD
Link-
106PhosphoserineAMQISSEKE
18.62Phosphositeplus
Link-
107PhosphoserineMQISSEKEE
55.08HPRD
Link-
107PhosphoserineMQISSEKEE
55.08Phosphositeplus
Link-
166PhosphoserinePAMTSGVYR
17.12HPRD
Link-
166PhosphoserinePAMTSGVYR
17.12Phosphositeplus
Link-
169PhosphotyrosineTSGVYRPPG
22.41HPRD
Link-
169PhosphotyrosineTSGVYRPPG
22.41Phosphositeplus
Link-
177PhosphothreonineGARLTTTRK
22.14HPRD
Link-
182PhosphothreonineTTRKTPQGP
19.97HPRD
Link-
182PhosphothreonineTTRKTPQGP
19.97PhosphoELM
Link-
182PhosphothreonineTTRKTPQGP
19.97Phosphositeplus
Link-
182PhosphothreonineTTRKTPQGP
19.97SysPTM
Link-
182Phosphothreonine.TTRKTPQGP
19.97UniProtKB
Link-
190PhosphotyrosinePPEIYSDTQ
9.99HPRD
Link-
190PhosphotyrosinePPEIYSDTQ
9.99PhosphoELM
Link-
190PhosphotyrosinePPEIYSDTQ
9.99Phosphositeplus
Link-
190PhosphotyrosinePPEIYSDTQ
9.99SysPTM
Link-
190Phosphotyrosine.PPEIYSDTQ
9.99UniProtKB
Link-
191PhosphoserinePEIYSDTQF
39.58HPRD
Link-
191PhosphoserinePEIYSDTQF
39.58Phosphositeplus
Link-
197PhosphoserineTQFPSLQST
40.09HPRD
Link-
197PhosphoserineTQFPSLQST
40.09PhosphoELM
Link-
197PhosphoserineTQFPSLQST
40.09Phosphositeplus
Link-
197Phosphoserine.TQFPSLQST
40.09UniProtKB
Link-
216PhosphoserineEMEKSFEVV
17.21HPRD
Link-
216PhosphoserineEMEKSFEVV
17.21PhosphoELM
Link-
216PhosphoserineEMEKSFEVV
17.21Phosphositeplus
Link-
216PhosphoserineEMEKSFEVV
17.21SysPTM
Link-
216Phosphoserine.EMEKSFEVV
17.21UniProtKB
Link-
244PhosphotyrosineLDNQYAVLE
12.63HPRD
Link-
244PhosphotyrosineLDNQYAVLE
12.63PhosphoELM
Link-
244PhosphotyrosineLDNQYAVLE
12.63Phosphositeplus
Link-
244PhosphotyrosineLDNQYAVLE
12.63SysPTM
Link-
244Phosphotyrosine.LDNQYAVLE
12.63UniProtKB
Link-
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LENQKSSHS
66.56Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
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.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-244, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND SER-216, 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-244, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-244, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-95 AND TYR-190, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-190 AND TYR-244, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-190, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; TYR-190; SER-197 ANDTYR-244, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures