CK052_HUMAN - dbPTM
CK052_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CK052_HUMAN
UniProt AC Q96A22
Protein Name Uncharacterized protein C11orf52
Gene Name C11orf52
Organism Homo sapiens (Human).
Sequence Length 123
Subcellular Localization
Protein Description
Protein Sequence MGNRVCCGGSWSCPSTFQKKKKTGSQTRRTLKPQPQQLQQNLPKGHETTGHTYERVLQQQGSQERSPGLMSEDSNLHYADIQVCSRPHAREVKHVHLENATEYATLRFPQATPRYDSKNGTLV
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
30PhosphorylationTGSQTRRTLKPQPQQ
CCCCCCCCCCCCHHH
35.5228857561
48PhosphorylationNLPKGHETTGHTYER
HCCCCCCCCHHHHHH
32.19-
49PhosphorylationLPKGHETTGHTYERV
CCCCCCCCHHHHHHH
24.7923312004
52PhosphorylationGHETTGHTYERVLQQ
CCCCCHHHHHHHHHH
28.5523312004
53PhosphorylationHETTGHTYERVLQQQ
CCCCHHHHHHHHHHC
8.9627259358
62PhosphorylationRVLQQQGSQERSPGL
HHHHHCCCCCCCCCC
25.2423911959
66PhosphorylationQQGSQERSPGLMSED
HCCCCCCCCCCCCCC
23.6729759185
71PhosphorylationERSPGLMSEDSNLHY
CCCCCCCCCCCCCCC
43.2128152594
74PhosphorylationPGLMSEDSNLHYADI
CCCCCCCCCCCCCEE
36.9228152594
77PhosphorylationMSEDSNLHYADIQVC
CCCCCCCCCCEEEEE
21.7117016520
78PhosphorylationSEDSNLHYADIQVCS
CCCCCCCCCEEEEEC
14.7727273156
85PhosphorylationYADIQVCSRPHAREV
CCEEEEECCCCCCCC
50.4128152594
101PhosphorylationHVHLENATEYATLRF
EEECCCCCCEEEEEC
40.9027273156
103PhosphorylationHLENATEYATLRFPQ
ECCCCCCEEEEECCC
10.6727273156
105PhosphorylationENATEYATLRFPQAT
CCCCCEEEEECCCCC
19.9827273156
112PhosphorylationTLRFPQATPRYDSKN
EEECCCCCCCCCCCC
11.7528152594

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 CK052_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CK052_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 CK052_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 CK052_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-78 AND TYR-103, 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-103, AND MASSSPECTROMETRY.

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