FAD1_HUMAN - dbPTM
FAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAD1_HUMAN
UniProt AC Q8NFF5
Protein Name FAD synthase
Gene Name FLAD1
Organism Homo sapiens (Human).
Sequence Length 587
Subcellular Localization Isoform 1: Mitochondrion matrix .
Isoform 2: Cytoplasm.
Protein Description Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme..
Protein Sequence MGWDLGTRLFQRQEQRSRLSRIWLEKTRVFLEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQPFRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEAQAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVEQASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
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
9 (in isoform 3)Phosphorylation-4.2725849741
9 (in isoform 2)Phosphorylation-4.2725849741
20PhosphorylationQEQRSRLSRIWLEKT
HHHHHHHHHHHHHHH
22.1728348404
27PhosphorylationSRIWLEKTRVFLEGS
HHHHHHHHEEECCCC
23.7728348404
99PhosphorylationGREGRTMTSRASELS
CCCCCCCCCCHHHCC
17.9122167270
100PhosphorylationREGRTMTSRASELSP
CCCCCCCCCHHHCCC
18.2822167270
103PhosphorylationRTMTSRASELSPGRS
CCCCCCHHHCCCCCC
37.6522167270
106PhosphorylationTSRASELSPGRSVTA
CCCHHHCCCCCCEEE
22.6629255136
110PhosphorylationSELSPGRSVTAGIII
HHCCCCCCEEEEEEE
29.7224247654
111UbiquitinationELSPGRSVTAGIIIV
HCCCCCCEEEEEEEE
4.0229967540
113UbiquitinationSPGRSVTAGIIIVGD
CCCCCEEEEEEEECC
12.6729967540
120UbiquitinationAGIIIVGDEILKGHT
EEEEEECCHHHCCCC
28.9527667366
122UbiquitinationIIIVGDEILKGHTQD
EEEECCHHHCCCCCC
5.9927667366
141PhosphorylationFLCRTLRSLGVQVCR
HHHHHHHHCCCEEEE
32.3720068231
210UbiquitinationPKLEAATKALGGEGW
HHHHHHHHHHCCCCH
36.5729967540
219UbiquitinationLGGEGWEKLSLVPSS
HCCCCHHHEEECCCC
36.5527667366
247PhosphorylationPFRFPLVSVRNVYLF
CEEECEEEEECEEEC
24.0424719451
281UbiquitinationNPAVQFHSKELYVAA
CCHHEECCCEEEEEE
29.1629967540
285 (in isoform 5)Phosphorylation-6.8025072903
288 (in isoform 5)Phosphorylation-12.7225072903
291 (in isoform 5)Phosphorylation-13.5425072903
294 (in isoform 5)Phosphorylation-5.2125072903
296 (in isoform 5)Phosphorylation-4.1525072903
299 (in isoform 5)Phosphorylation-37.5625072903
301 (in isoform 5)Phosphorylation-27.2025072903
372PhosphorylationAVYKLAESGSSLGKK
HHHHHHHHCCHHHHH
38.0722985185
378SuccinylationESGSSLGKKVAGALQ
HHCCHHHHHHHHHHH
49.74-
378UbiquitinationESGSSLGKKVAGALQ
HHCCHHHHHHHHHHH
49.7429967540
3782-HydroxyisobutyrylationESGSSLGKKVAGALQ
HHCCHHHHHHHHHHH
49.74-
378AcetylationESGSSLGKKVAGALQ
HHCCHHHHHHHHHHH
49.74-
378SuccinylationESGSSLGKKVAGALQ
HHCCHHHHHHHHHHH
49.74-
440PhosphorylationILYIRSISPFPELEQ
EEEEEECCCCHHHHH
23.02-
466PhosphorylationQMLEAEGSMKQALGE
HHHHHCCHHHHHHHH
17.8218691976
553PhosphorylationSLGSRENTVRNPALK
CCCCCCCCCCCCHHH
18.9826074081
563PhosphorylationNPALKCLSPGGHPTY
CCHHHCCCCCCCCCC
30.8522167270
569PhosphorylationLSPGGHPTYRPAYLL
CCCCCCCCCCCHHHC
26.8728450419
570PhosphorylationSPGGHPTYRPAYLLE
CCCCCCCCCCHHHCC
21.0328450419
574PhosphorylationHPTYRPAYLLENEEE
CCCCCCHHHCCCHHH
17.9528450419

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 FAD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAD1_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 FAD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAD1_HUMANFLAD1physical
16189514
GEMI4_HUMANGEMIN4physical
21988832
FAD1_HUMANFLAD1physical
25416956
PUR4_HUMANPFASphysical
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
There are no disease associations of PTM sites.
Regulatory Network of FAD1_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-106 AND SER-563, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.

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