CA052_HUMAN - dbPTM
CA052_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CA052_HUMAN
UniProt AC Q8N6N3
Protein Name UPF0690 protein C1orf52
Gene Name C1orf52
Organism Homo sapiens (Human).
Sequence Length 182
Subcellular Localization
Protein Description
Protein Sequence MAAEEKDPLSYFAAYGSSSSGSSDEEDNIEPEETSRRTPDPAKSAGGCRNKAEKRLPGPDELFRSVTRPAFLYNPLNKQIDWERHVVKAPEEPPKEFKIWKSNYVPPPETYTTEKKPPPPELDMAIKWSNIYEDNGDDAPQNAKKARLLPEGEETLESDDEKDEHTSKKRKVEPGEPAKKKK
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
34PhosphorylationDNIEPEETSRRTPDP
CCCCHHHHHCCCCCH
26.3526074081
35PhosphorylationNIEPEETSRRTPDPA
CCCHHHHHCCCCCHH
24.0526074081
38PhosphorylationPEETSRRTPDPAKSA
HHHHHCCCCCHHHHC
30.8226074081
44PhosphorylationRTPDPAKSAGGCRNK
CCCCHHHHCCCCCCH
33.9626074081
65PhosphorylationGPDELFRSVTRPAFL
CHHHHHHHCCCCHHH
22.1025159151
67PhosphorylationDELFRSVTRPAFLYN
HHHHHHCCCCHHHCC
31.9821712546
73PhosphorylationVTRPAFLYNPLNKQI
CCCCHHHCCCCHHCC
14.3127642862
78 (in isoform 3)Ubiquitination-57.2021890473
78 (in isoform 1)Ubiquitination-57.2021890473
78UbiquitinationFLYNPLNKQIDWERH
HHCCCCHHCCCHHHC
57.2021963094
78 (in isoform 2)Ubiquitination-57.2021890473
101UbiquitinationPKEFKIWKSNYVPPP
CCCCCCCCCCCCCCC
32.0929967540
102PhosphorylationKEFKIWKSNYVPPPE
CCCCCCCCCCCCCCC
20.56-
104PhosphorylationFKIWKSNYVPPPETY
CCCCCCCCCCCCCCC
22.79-
113PhosphorylationPPPETYTTEKKPPPP
CCCCCCCCCCCCCCC
35.08-
129PhosphorylationLDMAIKWSNIYEDNG
CCEEEEHHHHCCCCC
14.3521945579
132PhosphorylationAIKWSNIYEDNGDDA
EEEHHHHCCCCCCCC
22.8321945579
144AcetylationDDAPQNAKKARLLPE
CCCCCHHHHHCCCCC
55.2923236377
144UbiquitinationDDAPQNAKKARLLPE
CCCCCHHHHHCCCCC
55.2929967540
155PhosphorylationLLPEGEETLESDDEK
CCCCCCHHHCCCCCC
31.3625159151
158PhosphorylationEGEETLESDDEKDEH
CCCHHHCCCCCCCHH
54.1729255136
166PhosphorylationDDEKDEHTSKKRKVE
CCCCCHHCCCCCCCC
39.9522167270
167PhosphorylationDEKDEHTSKKRKVEP
CCCCHHCCCCCCCCC
37.7822167270
179AcetylationVEPGEPAKKKK----
CCCCCCCCCCC----
75.6925953088
182UbiquitinationGEPAKKKK-------
CCCCCCCC-------
74.5624816145

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 CA052_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CA052_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 CA052_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CA052_HUMAN !!

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 CA052_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, 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 SER-158, 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-158, AND MASSSPECTROMETRY.
"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 SER-158, 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-132, AND MASSSPECTROMETRY.

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