CHKA_HUMAN - dbPTM
CHKA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHKA_HUMAN
UniProt AC P35790
Protein Name Choline kinase alpha
Gene Name CHKA
Organism Homo sapiens (Human).
Sequence Length 457
Subcellular Localization Cytoplasm.
Protein Description Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline..
Protein Sequence MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
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
19UbiquitinationEPSPLGLLLSCGSGS
CCCCCCEEEECCCCC		2.9121890473
68UbiquitinationPPLPLPLPLPQPPPP
CCCCCCCCCCCCCCC		39.8027667366
96UbiquitinationRRAYLWCKEFLPGAW
HHHHHHHHHHCCCCC		39.66-
114PhosphorylationREDEFHISVIRGGLS
CCCCEEEEEEECCHH		11.7024719451
177 (in isoform 2)Ubiquitination-2.3821890473
177UbiquitinationEFQGAEAMVLESVMF
CCCCHHHHHHHHHHH		2.3821890473
195UbiquitinationAERSLGPKLYGIFPQ
HHHHHCHHHEEECCC		53.1722817900
195 (in isoform 1)Ubiquitination-53.1721890473
197PhosphorylationRSLGPKLYGIFPQGR
HHHCHHHEEECCCCH		17.8221822308
206UbiquitinationIFPQGRLEQFIPSRR
ECCCCHHHHHCCCCC		41.9327667366
216PhosphorylationIPSRRLDTEELSLPD
CCCCCCCCCCCCCCH		35.6323607784
220PhosphorylationRLDTEELSLPDISAE
CCCCCCCCCCHHHHH		40.9323607784
225PhosphorylationELSLPDISAEIAEKM
CCCCCHHHHHHHHHH		27.5123607784
226UbiquitinationLSLPDISAEIAEKMA
CCCCHHHHHHHHHHH		16.7327667366
240UbiquitinationATFHGMKMPFNKEPK
HHHCCCCCCCCCCCC		3.2129967540
244UbiquitinationGMKMPFNKEPKWLFG
CCCCCCCCCCCHHHH		75.6327667366
247AcetylationMPFNKEPKWLFGTME
CCCCCCCCHHHHHHH		58.587668441
254UbiquitinationKWLFGTMEKYLKEVL
CHHHHHHHHHHHHHH		38.0929967540
258UbiquitinationGTMEKYLKEVLRIKF
HHHHHHHHHHHHCCC		42.5629967540
272UbiquitinationFTEESRIKKLHKLLS
CCCHHHHHHHHHHHH		48.4429967540
333PhosphorylationLMLIDFEYSSYNYRG
EEEEEEECCCCCCCC		11.6921822308
355UbiquitinationCEWMYDYSYEKYPFF
HHHHHCCCCCCCCHH		24.7429967540
371PhosphorylationANIRKYPTKKQQLHF
CCCCCCCCHHHHHHH		48.02-
373UbiquitinationIRKYPTKKQQLHFIS
CCCCCCHHHHHHHHH		45.8429967540
399PhosphorylationNLSTEEKSIIKEEML
CCCHHHHHHHHHHHH		32.5924719451
431PhosphorylationSIVQAKISSIEFGYM
HHHHHHHHCCCCCCC		25.2626434776
432PhosphorylationIVQAKISSIEFGYMD
HHHHHHHCCCCCCCH		29.6126434776
437PhosphorylationISSIEFGYMDYAQAR
HHCCCCCCCHHHHHH		7.6726434776
440PhosphorylationIEFGYMDYAQARFDA
CCCCCCHHHHHHHHH		5.5426434776
448PhosphorylationAQARFDAYFHQKRKL
HHHHHHHHHHHHHCC		11.9326434776
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
197YPhosphorylationKinaseSRCP12931
PSP
333YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHKA_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 CHKA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP2_HUMANSKP2physical
19270695
DPTOR_HUMANDEPTORphysical
22017875
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
DB00122Choline
Regulatory Network of CHKA_HUMAN

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Related Literatures of Post-Translational Modification

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