KT3K_HUMAN - dbPTM
KT3K_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KT3K_HUMAN
UniProt AC Q9HA64
Protein Name Ketosamine-3-kinase
Gene Name FN3KRP
Organism Homo sapiens (Human).
Sequence Length 309
Subcellular Localization
Protein Description Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein-bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation..
Protein Sequence MEELLRRELGCSSVRATGHSGGGCISQGRSYDTDQGRVFVKVNPKAEARRMFEGEMASLTAILKTNTVKVPKPIKVLDAPGGGSVLVMEHMDMRHLSSHAAKLGAQLADLHLDNKKLGEMRLKEAGTVGRGGGQEERPFVARFGFDVVTCCGYLPQVNDWQEDWVVFYARQRIQPQMDMVEKESGDREALQLWSALQLKIPDLFRDLEIIPALLHGDLWGGNVAEDSSGPVIFDPASFYGHSEYELAIAGMFGGFSSSFYSAYHGKIPKAPGFEKRLQLYQLFHYLNHWNHFGSGYRGSSLNIMRNLVK
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
6Methylation--MEELLRRELGCSS
--CHHHHHHHHCCCC
42.52-
20PhosphorylationSVRATGHSGGGCISQ
CCCCCCCCCCCCCCC
40.2422817900
26PhosphorylationHSGGGCISQGRSYDT
CCCCCCCCCCCCEEC
30.56-
41UbiquitinationDQGRVFVKVNPKAEA
CCCEEEEEECCHHHH
25.48-
45UbiquitinationVFVKVNPKAEARRMF
EEEEECCHHHHHHHH
54.3721890473
58PhosphorylationMFEGEMASLTAILKT
HHCCCHHHHHHHHHC
25.5830177828
60PhosphorylationEGEMASLTAILKTNT
CCCHHHHHHHHHCCC
14.7930177828
64UbiquitinationASLTAILKTNTVKVP
HHHHHHHHCCCCCCC
33.3521890473
69UbiquitinationILKTNTVKVPKPIKV
HHHCCCCCCCCCEEE
51.2721890473
84PhosphorylationLDAPGGGSVLVMEHM
EECCCCCEEEEEECC
18.62-
97PhosphorylationHMDMRHLSSHAAKLG
CCCHHHHHHHHHHHH
17.6027135362
98PhosphorylationMDMRHLSSHAAKLGA
CCHHHHHHHHHHHHH
24.4127135362
102UbiquitinationHLSSHAAKLGAQLAD
HHHHHHHHHHHHHHH
48.51-
115UbiquitinationADLHLDNKKLGEMRL
HHCCCCCCHHHCEEH
49.3821890473
123UbiquitinationKLGEMRLKEAGTVGR
HHHCEEHHHCCCCCC
34.84-
127PhosphorylationMRLKEAGTVGRGGGQ
EEHHHCCCCCCCCCC
27.1718212344
130MethylationKEAGTVGRGGGQEER
HHCCCCCCCCCCCCC
35.93-
194PhosphorylationREALQLWSALQLKIP
HHHHHHHHHHHCCCC
27.9124719451
285PhosphorylationQLYQLFHYLNHWNHF
HHHHHHHHHCCCCCC
11.23-
294PhosphorylationNHWNHFGSGYRGSSL
CCCCCCCCCCCCHHH
31.5425106551
296PhosphorylationWNHFGSGYRGSSLNI
CCCCCCCCCCHHHHH
17.31-
300PhosphorylationGSGYRGSSLNIMRNL
CCCCCCHHHHHHHHH
28.41-

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 KT3K_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KT3K_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 KT3K_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TRFL_HUMANLTFphysical
26186194
LACRT_HUMANLACRTphysical
26186194
PIGR_HUMANPIGRphysical
26186194
TRFL_HUMANLTFphysical
28514442
LACRT_HUMANLACRTphysical
28514442
DOHH_HUMANDOHHphysical
28514442

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 KT3K_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.

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