CDV3_HUMAN - dbPTM
CDV3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDV3_HUMAN
UniProt AC Q9UKY7
Protein Name Protein CDV3 homolog
Gene Name CDV3
Organism Homo sapiens (Human).
Sequence Length 258
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MAETEERSLDNFFAKRDKKKKKERSNRAASAAGAAGSAGGSSGAAGAAGGGAGAGTRPGDGGTASAGAAGPGAATKAVTKDEDEWKELEQKEVDYSGLRVQAMQISSEKEEDDNEKRQDPGDNWEEGGGGGGGMEKSSGPWNKTAPVQAPPAPVIVTETPEPAMTSGVYRPPGARLTTTRKTPQGPPEIYSDTQFPSLQSTAKHVESRKDKEMEKSFEVVRHKNRGRDEVSKNQALKLQLDNQYAVLENQKSSHSQYN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAETEERSL
------CCCHHHHHH		32.2119413330
4 (in isoform 3)Phosphorylation-33.3425056879
4Phosphorylation----MAETEERSLDN
----CCCHHHHHHHH		33.3425159151
5 (in isoform 3)Phosphorylation-42.8125159151
8PhosphorylationMAETEERSLDNFFAK
CCCHHHHHHHHHHHH		43.2729255136
15AcetylationSLDNFFAKRDKKKKK
HHHHHHHHHHHHHHH		56.8423236377
15UbiquitinationSLDNFFAKRDKKKKK
HHHHHHHHHHHHHHH		56.8419608861
24DimethylationDKKKKKERSNRAASA
HHHHHHHHHHHHHHH		48.38-
25PhosphorylationKKKKKERSNRAASAA
HHHHHHHHHHHHHHH		31.5922817900
30PhosphorylationERSNRAASAAGAAGS
HHHHHHHHHHHHHHH		20.0523401153
37PhosphorylationSAAGAAGSAGGSSGA
HHHHHHHHCCCCCCC		21.0029255136
41PhosphorylationAAGSAGGSSGAAGAA
HHHHCCCCCCCCCCC		25.3629255136
42PhosphorylationAGSAGGSSGAAGAAG
HHHCCCCCCCCCCCC		35.4129255136
56PhosphorylationGGGAGAGTRPGDGGT
CCCCCCCCCCCCCCC		32.9120068231
56O-linked_GlycosylationGGGAGAGTRPGDGGT
CCCCCCCCCCCCCCC		32.9131373491
63PhosphorylationTRPGDGGTASAGAAG
CCCCCCCCCCCCCCC		23.9825159151
65PhosphorylationPGDGGTASAGAAGPG
CCCCCCCCCCCCCCC		27.3720068231
75PhosphorylationAAGPGAATKAVTKDE
CCCCCCCCCCCCCCH		20.9920068231
76AcetylationAGPGAATKAVTKDED
CCCCCCCCCCCCCHH		35.8127452117
79PhosphorylationGAATKAVTKDEDEWK
CCCCCCCCCCHHHHH		37.3230624053
80AcetylationAATKAVTKDEDEWKE
CCCCCCCCCHHHHHH		53.1523749302
91UbiquitinationEWKELEQKEVDYSGL
HHHHHHHCCCCCCHH		50.78-
91AcetylationEWKELEQKEVDYSGL
HHHHHHHCCCCCCHH		50.7823236377
95PhosphorylationLEQKEVDYSGLRVQA
HHHCCCCCCHHHEEE		15.1525159151
95NitrationLEQKEVDYSGLRVQA
HHHCCCCCCHHHEEE		15.15-
96PhosphorylationEQKEVDYSGLRVQAM
HHCCCCCCHHHEEEE		27.2125159151
103SulfoxidationSGLRVQAMQISSEKE
CHHHEEEEECCCCCC		1.7128465586
106PhosphorylationRVQAMQISSEKEEDD
HEEEEECCCCCCCCC		18.6229255136
107PhosphorylationVQAMQISSEKEEDDN
EEEEECCCCCCCCCC		55.0829255136
109AcetylationAMQISSEKEEDDNEK
EEECCCCCCCCCCCC		69.2423236377
134SulfoxidationGGGGGGGMEKSSGPW
CCCCCCCCCCCCCCC		7.1130846556
136UbiquitinationGGGGGMEKSSGPWNK
CCCCCCCCCCCCCCC		40.82-
137PhosphorylationGGGGMEKSSGPWNKT
CCCCCCCCCCCCCCC		27.5028985074
137O-linked_GlycosylationGGGGMEKSSGPWNKT
CCCCCCCCCCCCCCC		27.5031373491
144PhosphorylationSSGPWNKTAPVQAPP
CCCCCCCCCCCCCCC		32.7421945579
157PhosphorylationPPAPVIVTETPEPAM
CCCCEEEECCCCCCC		24.0221945579
159PhosphorylationAPVIVTETPEPAMTS
CCEEEECCCCCCCCC		24.4821945579
164SulfoxidationTETPEPAMTSGVYRP
ECCCCCCCCCCCCCC		4.4830846556
165PhosphorylationETPEPAMTSGVYRPP
CCCCCCCCCCCCCCC		25.1621945579
166PhosphorylationTPEPAMTSGVYRPPG
CCCCCCCCCCCCCCC		17.1221945579
169PhosphorylationPAMTSGVYRPPGARL
CCCCCCCCCCCCCEE		22.4121945579
177PhosphorylationRPPGARLTTTRKTPQ
CCCCCEEECCCCCCC		22.1428450419
178PhosphorylationPPGARLTTTRKTPQG
CCCCEEECCCCCCCC		29.2428450419
179PhosphorylationPGARLTTTRKTPQGP
CCCEEECCCCCCCCC		25.5728450419
181UbiquitinationARLTTTRKTPQGPPE
CEEECCCCCCCCCCC		63.57-
182PhosphorylationRLTTTRKTPQGPPEI
EEECCCCCCCCCCCC		19.9725159151
190PhosphorylationPQGPPEIYSDTQFPS
CCCCCCCCCCCCCCH		9.9925159151
191PhosphorylationQGPPEIYSDTQFPSL
CCCCCCCCCCCCCHH		39.5821945579
193PhosphorylationPPEIYSDTQFPSLQS
CCCCCCCCCCCHHHH		26.6021945579
197PhosphorylationYSDTQFPSLQSTAKH
CCCCCCCHHHHHHHH		40.0921945579
200PhosphorylationTQFPSLQSTAKHVES
CCCCHHHHHHHHHHH		35.3121945579
201PhosphorylationQFPSLQSTAKHVESR
CCCHHHHHHHHHHHH		27.1121945579
203AcetylationPSLQSTAKHVESRKD
CHHHHHHHHHHHHCH		48.5525953088
203UbiquitinationPSLQSTAKHVESRKD
CHHHHHHHHHHHHCH		48.55-
213SulfoxidationESRKDKEMEKSFEVV
HHHCHHHHHHHHHHH		10.9430846556
2152-HydroxyisobutyrylationRKDKEMEKSFEVVRH
HCHHHHHHHHHHHHC		60.17-
216PhosphorylationKDKEMEKSFEVVRHK
CHHHHHHHHHHHHCC		17.2121712546
244PhosphorylationKLQLDNQYAVLENQK
HHHHHHHHHHHCCCC		12.6321945579
251UbiquitinationYAVLENQKSSHSQYN
HHHHCCCCCCCCCCC		66.562190698
251 (in isoform 1)Ubiquitination-66.5621906983
252PhosphorylationAVLENQKSSHSQYN-
HHHCCCCCCCCCCC-		24.4224719451
253PhosphorylationVLENQKSSHSQYN--
HHCCCCCCCCCCC--		33.91-
255PhosphorylationENQKSSHSQYN----
CCCCCCCCCCC----		35.99-
257PhosphorylationQKSSHSQYN------
CCCCCCCCC------		26.34-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CDV3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDV3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CDV3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAR4B_HUMANLARP4Bphysical
22939629
RRFM_HUMANMRRFphysical
22939629
FIS1_HUMANFIS1physical
22939629
MAN1_HUMANLEMD3physical
22939629
MYPT1_HUMANPPP1R12Aphysical
22939629
RM14_HUMANMRPL14physical
22939629
RT28_HUMANMRPS28physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
RFX5_HUMANRFX5physical
22939629
SCO2_HUMANSCO2physical
22939629
EMSA1_HUMANELMSAN1physical
22939629
VDAC3_HUMANVDAC3physical
22939629
UQCC3_HUMANUQCC3physical
22939629
GAPR1_HUMANGLIPR2physical
22939629
GNAI3_HUMANGNAI3physical
22939629
RRBP1_HUMANRRBP1physical
22939629
TIM44_HUMANTIMM44physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
GIPC1_HUMANGIPC1physical
22939629
EFTS_HUMANTSFMphysical
22939629
IDH3G_HUMANIDH3Gphysical
22939629
NDUF2_HUMANNDUFAF2physical
22939629
NDUA2_HUMANNDUFA2physical
22939629
NDUA7_HUMANNDUFA7physical
22939629
RAB31_HUMANRAB31physical
22939629
SUGP1_HUMANSUGP1physical
22939629
STX7_HUMANSTX7physical
22939629
TBL2_HUMANTBL2physical
22939629
COBL_HUMANCOBLphysical
22939629
QKI_HUMANQKIphysical
22939629
NSF1C_HUMANNSFL1Cphysical
22863883
CHM2A_HUMANCHMP2Aphysical
26344197
ILK_HUMANILKphysical
26344197
NAA50_HUMANNAA50physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
NUP50_HUMANNUP50physical
26344197
6PGD_HUMANPGDphysical
26344197
PSMD9_HUMANPSMD9physical
26344197
UBP2L_HUMANUBAP2Lphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDV3_HUMAN

loading...

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
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory