FXRD1_HUMAN - dbPTM
FXRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FXRD1_HUMAN
UniProt AC Q96CU9
Protein Name FAD-dependent oxidoreductase domain-containing protein 1 {ECO:0000312|HGNC:HGNC:26927}
Gene Name FOXRED1 {ECO:0000312|HGNC:HGNC:26927}
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein . According to a report, it is associated with the matrix face of the mitochondrial inner membrane and does not contain any transmembrane region. However, one transmembrane domain is clearly
Protein Description Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). [PubMed: 20858599]
Protein Sequence MIRRVLPHGMGRGLLTRRPGTRRGGFSLDWDGKVSEIKKKIKSILPGRSCDLLQDTSHLPPEHSDVVIVGGGVLGLSVAYWLKKLESRRGAIRVLVVERDHTYSQASTGLSVGGICQQFSLPENIQLSLFSASFLRNINEYLAVVDAPPLDLRFNPSGYLLLASEKDAAAMESNVKVQRQEGAKVSLMSPDQLRNKFPWINTEGVALASYGMEDEGWFDPWCLLQGLRRKVQSLGVLFCQGEVTRFVSSSQRMLTTDDKAVVLKRIHEVHVKMDRSLEYQPVECAIVINAAGAWSAQIAALAGVGEGPPGTLQGTKLPVEPRKRYVYVWHCPQGPGLETPLVADTSGAYFRREGLGSNYLGGRSPTEQEEPDPANLEVDHDFFQDKVWPHLALRVPAFETLKVQSAWAGYYDYNTFDQNGVVGPHPLVVNMYFATGFSGHGLQQAPGIGRAVAEMVLKGRFQTIDLSPFLFTRFYLGEKIQENNII
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
12MethylationVLPHGMGRGLLTRRP
CCCCCCCCCCCCCCC
24.56-
12DimethylationVLPHGMGRGLLTRRP
CCCCCCCCCCCCCCC
24.56-
23MethylationTRRPGTRRGGFSLDW
CCCCCCCCCCEEECC
49.80-
33UbiquitinationFSLDWDGKVSEIKKK
EEECCCCCHHHHHHH
39.8621890473
33 (in isoform 1)Ubiquitination-39.8621890473
33UbiquitinationFSLDWDGKVSEIKKK
EEECCCCCHHHHHHH
39.8621890473
42UbiquitinationSEIKKKIKSILPGRS
HHHHHHHHHHCCCCC
40.0821890473
42 (in isoform 1)Ubiquitination-40.0821890473
42UbiquitinationSEIKKKIKSILPGRS
HHHHHHHHHHCCCCC
40.0821890473
48 (in isoform 2)Ubiquitination-31.9721890473
87PhosphorylationYWLKKLESRRGAIRV
HHHHHHHHCCCCEEE
37.40-
133PhosphorylationQLSLFSASFLRNINE
EEEHHCHHHHHCHHH
24.5024719451
166UbiquitinationYLLLASEKDAAAMES
EEEEEEHHHHHHHHC
50.61-
176UbiquitinationAAMESNVKVQRQEGA
HHHHCCCEEEECCCC
36.58-
184AcetylationVQRQEGAKVSLMSPD
EEECCCCEEECCCHH
43.1219829097
189PhosphorylationGAKVSLMSPDQLRNK
CCEEECCCHHHHHHC
30.5325850435
259UbiquitinationRMLTTDDKAVVLKRI
CEECCCCCCHHHHHH
45.9821890473
259UbiquitinationRMLTTDDKAVVLKRI
CEECCCCCCHHHHHH
45.9821890473
259 (in isoform 1)Ubiquitination-45.9821890473
272AcetylationRIHEVHVKMDRSLEY
HHEEEEEEECCCCCC
21.8719608861
279PhosphorylationKMDRSLEYQPVECAI
EECCCCCCCCEEEEE
24.34-
458UbiquitinationAVAEMVLKGRFQTID
HHHHHHHCCCCCEEE
36.31-
467PhosphorylationRFQTIDLSPFLFTRF
CCCEEECCHHHHHHH
15.17-

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 FXRD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FXRD1_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 FXRD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT4I1_HUMANRTN4IP1physical
28514442
SUCHY_HUMANSUGCTphysical
28514442
COPRS_HUMANCOPRSphysical
28514442
CH60_HUMANHSPD1physical
28514442
CLPX_HUMANCLPXphysical
28514442
MCCA_HUMANMCCC1physical
28514442
IF2M_HUMANMTIF2physical
28514442
NDUF7_HUMANNDUFAF7physical
28514442
HSP7C_HUMANHSPA8physical
28514442
SYNM_HUMANNARS2physical
28514442
CPSM_HUMANCPS1physical
28514442
HCFC1_HUMANHCFC1physical
28514442
CLPP_HUMANCLPPphysical
28514442
MINP1_HUMANMINPP1physical
28514442
LONM_HUMANLONP1physical
28514442
HSP72_HUMANHSPA2physical
28514442

Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
OMIM Disease
252010Mitochondrial complex I deficiency (MT-C1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FXRD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, AND MASS SPECTROMETRY.

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