RIFK_HUMAN - dbPTM
RIFK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIFK_HUMAN
UniProt AC Q969G6
Protein Name Riboflavin kinase
Gene Name RFK
Organism Homo sapiens (Human).
Sequence Length 155
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase..
Protein Sequence MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH
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
60AcetylationVGSGDVHKMVVSIGW
ECCCCEEEEEEEECC
32.9920167786
70PhosphorylationVSIGWNPYYKNTKKS
EEECCCCCCCCCHHH
24.69-
71PhosphorylationSIGWNPYYKNTKKSM
EECCCCCCCCCHHHH
10.06-
76AcetylationPYYKNTKKSMETHIM
CCCCCCHHHHHHHHH
53.667493363
85PhosphorylationMETHIMHTFKEDFYG
HHHHHHHHHHHHHHH
21.01-
127UbiquitinationQGDIEEAKKRLELPE
HCCHHHHHHHCCCCH
41.53-
137UbiquitinationLELPEHLKIKEDNFF
CCCCHHHCCCCCCCE
54.35-
139UbiquitinationLPEHLKIKEDNFFQV
CCHHHCCCCCCCEEE
58.38-
148UbiquitinationDNFFQVSKSKIMNGH
CCCEEECHHHHCCCC
57.84-

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 RIFK_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIFK_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 RIFK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRHPR_HUMANGRHPRphysical
26344197
MEMO1_HUMANMEMO1physical
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
DB00140Riboflavin
Regulatory Network of RIFK_HUMAN

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Related Literatures of Post-Translational Modification

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