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 | ||
* 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 | ||||||
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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. |