FXRD2_HUMAN - dbPTM
FXRD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FXRD2_HUMAN
UniProt AC Q8IWF2
Protein Name FAD-dependent oxidoreductase domain-containing protein 2
Gene Name FOXRED2 {ECO:0000312|HGNC:HGNC:26264}
Organism Homo sapiens (Human).
Sequence Length 684
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation..
Protein Sequence MGLSAAAPLWGPPGLLLAIALHPALSVPPRRDYCVLGAGPAGLQMAYFLQRAGRDYAVFERAPRPGSFFTRYPRHRKLISINKRYTGKANAEFNLRHDWNSLLSHDPRLLFRHYSRAYFPDARDMVRYLGDFADTLGLRVQYNTTIAHVTLDKDRQAWNGHYFILTDQKGQVHQCSVLFVATGLSVPNQVDFPGSEYAEGYESVSVDPEDFVGQNVLILGRGNSAFETAENILGVTNFIHMLSRSRVRLSWATHYVGDLRAINNGLLDTYQLKSLDGLLESDLTDLAILKDSKGKFHVTPKFFLEEANTNQSADSITLPQDDNDNFAMRVPYDRVIRCLGWNFDFSIFNKSLRLNSGNAFGKKYPLIRASYESKGSRGLFILGTASHSVDYRKSAGGFIHGFRYTVRAVHRLLEHRHHSVTWPATELPITQLTSSIVRRVNEASGLYQMFGVLADVILLKENSTAFEYLEEFPIQMLAQLETLTGRKAKHGLFVINMEYGRNFSGPDKDVFFDDRSVGHTEDAWQSNFLHPVIYYYRYLPTEQEVRFRPAHWPLPRPTAIHHIVEDFLTDWTAPIGHILPLRRFLENCLDTDLRSFYAESCFLFALTRQKLPPFCQQGYLRMQGLVSTESLWQHRVESRLLRDYAPTGRRLEDSSQQLGDQEPLGSPLAPGPLAQSVDSNKEEL
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
33PhosphorylationSVPPRRDYCVLGAGP
CCCCCCCCEEECCCH		5.2218083107
47PhosphorylationPAGLQMAYFLQRAGR
HHHHHHHHHHHHCCC		10.2418083107
77UbiquitinationTRYPRHRKLISINKR
CCCCCCCCEEEECCC		44.01-
83UbiquitinationRKLISINKRYTGKAN
CCEEEECCCCCCCCC		45.1522817900
88UbiquitinationINKRYTGKANAEFNL
ECCCCCCCCCCEEEC		30.5721963094
101PhosphorylationNLRHDWNSLLSHDPR
ECCCCHHHHHCCCHH		26.8329449344
104PhosphorylationHDWNSLLSHDPRLLF
CCHHHHHCCCHHHHH		31.0129449344
114PhosphorylationPRLLFRHYSRAYFPD
HHHHHHHHHHHHCCC		8.8028270605
115PhosphorylationRLLFRHYSRAYFPDA
HHHHHHHHHHHCCCH		12.3328270605
118PhosphorylationFRHYSRAYFPDARDM
HHHHHHHHCCCHHHH		17.9724719451
143N-linked_GlycosylationLGLRVQYNTTIAHVT
HCCEEEECCEEEEEE		17.4119159218
153UbiquitinationIAHVTLDKDRQAWNG
EEEEEECCCCCHHCC		58.90-
181 (in isoform 2)Ubiquitination-6.6621906983
253PhosphorylationRVRLSWATHYVGDLR
CCCHHHHHHHHHHHH		13.8927251275
255PhosphorylationRLSWATHYVGDLRAI
CHHHHHHHHHHHHHH		11.1927251275
269PhosphorylationINNGLLDTYQLKSLD
HHCCCCCEEECCCCC		17.0927251275
270PhosphorylationNNGLLDTYQLKSLDG
HCCCCCEEECCCCCC		16.1227251275
272UbiquitinationGLLDTYQLKSLDGLL
CCCCEEECCCCCCHH		2.6121963094
273UbiquitinationLLDTYQLKSLDGLLE
CCCEEECCCCCCHHH		33.1922817900
290UbiquitinationLTDLAILKDSKGKFH
CCHHHHEECCCCCEE		54.5721963094
293UbiquitinationLAILKDSKGKFHVTP
HHHEECCCCCEEECC		76.0222817900
295UbiquitinationILKDSKGKFHVTPKF
HEECCCCCEEECCHH		35.7122817900
350UbiquitinationFDFSIFNKSLRLNSG
CCEEEECCHHCCCCC		39.8721963094
356PhosphorylationNKSLRLNSGNAFGKK
CCHHCCCCCCCCCCC		37.7124732914
362UbiquitinationNSGNAFGKKYPLIRA
CCCCCCCCCCCEEEE		42.5521963094
363UbiquitinationSGNAFGKKYPLIRAS
CCCCCCCCCCEEEEE		53.1022817900
374UbiquitinationIRASYESKGSRGLFI
EEEEEECCCCCEEEE		49.30-
393UbiquitinationSHSVDYRKSAGGFIH
ECCCEEHHHCCCCCC		38.13-
508UbiquitinationRNFSGPDKDVFFDDR
CCCCCCCCCCCCCCC		59.9521906983
508 (in isoform 1)Ubiquitination-59.9521906983
610UbiquitinationLFALTRQKLPPFCQQ
HHHHHHCCCCHHHHH		60.72-
666O-linked_GlycosylationGDQEPLGSPLAPGPL
CCCCCCCCCCCCCCC		25.15OGP
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 FXRD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FXRD2_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 FXRD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SE1L1_HUMANSEL1Lphysical
19706418
OS9_HUMANOS9physical
19706418
DJC10_HUMANDNAJC10physical
19706418
RPN1_HUMANRPN1physical
19706418
TXD16_HUMANTXNDC16physical
22119785
VDAC1_HUMANVDAC1physical
22119785
DPY30_HUMANDPY30physical
22119785
EMD_HUMANEMDphysical
22119785
GALK1_HUMANGALK1physical
22119785
NIPS1_HUMANNIPSNAP1physical
22119785
CSKP_HUMANCASKphysical
22119785
RL10_HUMANRPL10physical
22119785
ACTH_HUMANACTG2physical
22119785
CALX_HUMANCANXphysical
22119785
LIN7C_HUMANLIN7Cphysical
22119785
SE1L1_HUMANSEL1Lphysical
22119785
GANAB_HUMANGANABphysical
22119785
USH2A_HUMANUSH2Aphysical
22119785
VDAC2_HUMANVDAC2physical
22119785
FLNA_HUMANFLNAphysical
22119785
K1C18_HUMANKRT18physical
22119785
PRKDC_HUMANPRKDCphysical
22119785
RAB9A_HUMANRAB9Aphysical
22119785
DIC_HUMANSLC25A10physical
22119785
ACTS_HUMANACTA1physical
22119785
ERLEC_HUMANERLEC1physical
22119785
RBM45_HUMANRBM45physical
28514442
TXD16_HUMANTXNDC16physical
28514442
MIPEP_HUMANMIPEPphysical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
TOM40_HUMANTOMM40physical
28514442
SE1L1_HUMANSEL1Lphysical
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 FXRD2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-143, AND MASSSPECTROMETRY.

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