| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 9 (in isoform 3) | Phosphorylation | - | 4.27 | 25849741 | |
| 9 (in isoform 2) | Phosphorylation | - | 4.27 | 25849741 | |
| 20 | Phosphorylation | QEQRSRLSRIWLEKT HHHHHHHHHHHHHHH | 22.17 | 28348404 | |
| 27 | Phosphorylation | SRIWLEKTRVFLEGS HHHHHHHHEEECCCC | 23.77 | 28348404 | |
| 99 | Phosphorylation | GREGRTMTSRASELS CCCCCCCCCCHHHCC | 17.91 | 22167270 | |
| 100 | Phosphorylation | REGRTMTSRASELSP CCCCCCCCCHHHCCC | 18.28 | 22167270 | |
| 103 | Phosphorylation | RTMTSRASELSPGRS CCCCCCHHHCCCCCC | 37.65 | 22167270 | |
| 106 | Phosphorylation | TSRASELSPGRSVTA CCCHHHCCCCCCEEE | 22.66 | 29255136 | |
| 110 | Phosphorylation | SELSPGRSVTAGIII HHCCCCCCEEEEEEE | 29.72 | 24247654 | |
| 111 | Ubiquitination | ELSPGRSVTAGIIIV HCCCCCCEEEEEEEE | 4.02 | 29967540 | |
| 113 | Ubiquitination | SPGRSVTAGIIIVGD CCCCCEEEEEEEECC | 12.67 | 29967540 | |
| 120 | Ubiquitination | AGIIIVGDEILKGHT EEEEEECCHHHCCCC | 28.95 | 27667366 | |
| 122 | Ubiquitination | IIIVGDEILKGHTQD EEEECCHHHCCCCCC | 5.99 | 27667366 | |
| 141 | Phosphorylation | FLCRTLRSLGVQVCR HHHHHHHHCCCEEEE | 32.37 | 20068231 | |
| 210 | Ubiquitination | PKLEAATKALGGEGW HHHHHHHHHHCCCCH | 36.57 | 29967540 | |
| 219 | Ubiquitination | LGGEGWEKLSLVPSS HCCCCHHHEEECCCC | 36.55 | 27667366 | |
| 247 | Phosphorylation | PFRFPLVSVRNVYLF CEEECEEEEECEEEC | 24.04 | 24719451 | |
| 281 | Ubiquitination | NPAVQFHSKELYVAA CCHHEECCCEEEEEE | 29.16 | 29967540 | |
| 285 (in isoform 5) | Phosphorylation | - | 6.80 | 25072903 | |
| 288 (in isoform 5) | Phosphorylation | - | 12.72 | 25072903 | |
| 291 (in isoform 5) | Phosphorylation | - | 13.54 | 25072903 | |
| 294 (in isoform 5) | Phosphorylation | - | 5.21 | 25072903 | |
| 296 (in isoform 5) | Phosphorylation | - | 4.15 | 25072903 | |
| 299 (in isoform 5) | Phosphorylation | - | 37.56 | 25072903 | |
| 301 (in isoform 5) | Phosphorylation | - | 27.20 | 25072903 | |
| 372 | Phosphorylation | AVYKLAESGSSLGKK HHHHHHHHCCHHHHH | 38.07 | 22985185 | |
| 378 | Succinylation | ESGSSLGKKVAGALQ HHCCHHHHHHHHHHH | 49.74 | - | |
| 378 | Ubiquitination | ESGSSLGKKVAGALQ HHCCHHHHHHHHHHH | 49.74 | 29967540 | |
| 378 | 2-Hydroxyisobutyrylation | ESGSSLGKKVAGALQ HHCCHHHHHHHHHHH | 49.74 | - | |
| 378 | Acetylation | ESGSSLGKKVAGALQ HHCCHHHHHHHHHHH | 49.74 | - | |
| 378 | Succinylation | ESGSSLGKKVAGALQ HHCCHHHHHHHHHHH | 49.74 | - | |
| 440 | Phosphorylation | ILYIRSISPFPELEQ EEEEEECCCCHHHHH | 23.02 | - | |
| 466 | Phosphorylation | QMLEAEGSMKQALGE HHHHHCCHHHHHHHH | 17.82 | 18691976 | |
| 553 | Phosphorylation | SLGSRENTVRNPALK CCCCCCCCCCCCHHH | 18.98 | 26074081 | |
| 563 | Phosphorylation | NPALKCLSPGGHPTY CCHHHCCCCCCCCCC | 30.85 | 22167270 | |
| 569 | Phosphorylation | LSPGGHPTYRPAYLL CCCCCCCCCCCHHHC | 26.87 | 28450419 | |
| 570 | Phosphorylation | SPGGHPTYRPAYLLE CCCCCCCCCCHHHCC | 21.03 | 28450419 | |
| 574 | Phosphorylation | HPTYRPAYLLENEEE CCCCCCHHHCCCHHH | 17.95 | 28450419 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FAD1_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| FAD1_HUMAN | FLAD1 | physical | 16189514 | |
| GEMI4_HUMAN | GEMIN4 | physical | 21988832 | |
| FAD1_HUMAN | FLAD1 | physical | 25416956 | |
| PUR4_HUMAN | PFAS | physical | 26344197 |
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |