| UniProt ID | GPAT1_MOUSE | |
|---|---|---|
| UniProt AC | Q61586 | |
| Protein Name | Glycerol-3-phosphate acyltransferase 1, mitochondrial | |
| Gene Name | Gpam | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 827 | |
| Subcellular Localization |
Mitochondrion outer membrane Multi-pass membrane protein . |
|
| Protein Description | Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.. | |
| Protein Sequence | MEESSVTVGTIDVSYLPSSSEYSLGRCKHTSEDWVDCGFKPTFFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWERFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYILFVQERDVHKGMFATSVTENVLSSSRVQEAIAEVAAELNPDGSAQQQSKAIQKVKRKARKILQEMVATVSPGMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLLFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPVFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHVVELLRQQQFLEIFLEGTRSRSGKTSCARAGLLSVVVDTLSSNTIPDILVIPVGISYDRIIEGHYNGEQLGKPKKNESLWSVARGVIRMLRKNYGYVRVDFAQPFSLKEYLEGQSQKPVSAPLSLEQALLPAILPSRPNDVADEHQDLSSNESRNPADEAFRRRLIANLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIHLSTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQLLGNCVTITHTSRKDEFFITPSTTVPSVFELNFYSNGVLHVFIMEAIIACSIYAVLNKRCSGGSAGGLGNLISQEQLVRKAASLCYLLSNEGTISLPCQTFYQVCHETVGKFIQYGILTVAEQDDQEDVSPGLAEQQWDKKLPELNWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAIFVHNFSGPVPESEYLQKLHRYLITRTERNVAVYAESATYCLVKNAVKMFKDIGVFKETKQKRVSVLELSSTFLPQCNRQKLLEYILSFVVL | |
| 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 |
|---|---|---|---|---|---|
| 30 | Phosphorylation | SLGRCKHTSEDWVDC CCCCCCCCCCCCCCC | 21.21 | 23984901 | |
| 31 | Phosphorylation | LGRCKHTSEDWVDCG CCCCCCCCCCCCCCC | 33.02 | 25521595 | |
| 40 | Ubiquitination | DWVDCGFKPTFFRSA CCCCCCCCCCCCHHC | 28.56 | - | |
| 48 | Phosphorylation | PTFFRSATLKWKESL CCCCHHCCHHHHHHH | 30.07 | 23140645 | |
| 50 | Ubiquitination | FFRSATLKWKESLMS CCHHCCHHHHHHHHH | 52.44 | 27667366 | |
| 110 | Phosphorylation | GWLARRLSYILFVQE HHHHHHHHEEEEEEC | 14.33 | 23140645 | |
| 111 | Phosphorylation | WLARRLSYILFVQER HHHHHHHEEEEEECC | 13.26 | 23567750 | |
| 182 | Phosphorylation | QEMVATVSPGMIRLT HHHHHHCCHHHHHHH | 16.04 | 28285833 | |
| 288 | Malonylation | DETPDGRKDILYRAL CCCCCCCHHHHHHHH | 55.43 | 26073543 | |
| 338 | Phosphorylation | LLSVVVDTLSSNTIP HHHHHHHHCCCCCCC | 19.55 | - | |
| 371 | Acetylation | YNGEQLGKPKKNESL CCHHHCCCCCCCHHH | 63.36 | 23954790 | |
| 374 | Malonylation | EQLGKPKKNESLWSV HHCCCCCCCHHHHHH | 74.58 | 26320211 | |
| 380 | Phosphorylation | KKNESLWSVARGVIR CCCHHHHHHHHHHHH | 15.93 | - | |
| 391 | Ubiquitination | GVIRMLRKNYGYVRV HHHHHHHHHCCEEEE | 51.03 | 27667366 | |
| 448 | Phosphorylation | ADEHQDLSSNESRNP CHHCCCCCCCCCCCH | 39.13 | 30352176 | |
| 598 | S-palmitoylation | YAVLNKRCSGGSAGG HHHHCCCCCCCCCCH | 4.78 | 28526873 | |
| 657 | Phosphorylation | FIQYGILTVAEQDDQ HHHCCEEEEECCCCC | 18.75 | 23140645 | |
| 668 | Phosphorylation | QDDQEDVSPGLAEQQ CCCCCCCCCCHHHHH | 26.10 | 26643407 | |
| 687 | Phosphorylation | LPELNWRSDEEDEDS CCCCCCCCCCCCCCC | 40.77 | 25521595 | |
| 694 | Phosphorylation | SDEEDEDSDFGEEQR CCCCCCCCCCCHHHH | 32.56 | 25521595 | |
| 704 | Phosphorylation | GEEQRDCYLKVSQSK CHHHHHEEEEECCCH | 17.53 | 23140645 | |
| 779 | Malonylation | SATYCLVKNAVKMFK CHHHHHHHHHHHHHH | 26.66 | 26073543 | |
| 779 | Acetylation | SATYCLVKNAVKMFK CHHHHHHHHHHHHHH | 26.66 | 23576753 | |
| 783 | Ubiquitination | CLVKNAVKMFKDIGV HHHHHHHHHHHHHCC | 35.89 | 27667366 | |
| 783 | Malonylation | CLVKNAVKMFKDIGV HHHHHHHHHHHHHCC | 35.89 | 26320211 | |
| 783 | Acetylation | CLVKNAVKMFKDIGV HHHHHHHHHHHHHCC | 35.89 | 23576753 | |
| 786 | Malonylation | KNAVKMFKDIGVFKE HHHHHHHHHHCCCHH | 44.96 | 32601280 | |
| 786 | Acetylation | KNAVKMFKDIGVFKE HHHHHHHHHHCCCHH | 44.96 | 23954790 | |
| 800 | Phosphorylation | ETKQKRVSVLELSST HHCCCEEEEEHHHCC | 25.64 | 23140645 | |
| 812 | S-palmitoylation | SSTFLPQCNRQKLLE HCCCCCCCCHHHHHH | 4.24 | 28526873 |
| 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 GPAT1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPAT1_MOUSE !! | ||||||
* 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 GPAT1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GPAT1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND MASSSPECTROMETRY. | |
| "Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND MASSSPECTROMETRY. | |