| UniProt ID | GPAT3_HUMAN | |
|---|---|---|
| UniProt AC | Q53EU6 | |
| Protein Name | Glycerol-3-phosphate acyltransferase 3 {ECO:0000312|HGNC:HGNC:28157} | |
| Gene Name | GPAT3 {ECO:0000312|HGNC:HGNC:28157} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 434 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA).. | |
| Protein Sequence | MEGAELAGKILSTWLTLVLGFILLPSVFGVSLGISEIYMKILVKTLEWATIRIEKGTPKESILKNSASVGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEELVSWNLLTRTNVNFQYISLRLTMVWVLGVIVRYCVLLPLRVTLAFIGISLLVIGTTLVGQLPDSSLKNWLSELVHLTCCRICVRALSGTIHYHNKQYRPQKGGICVANHTSPIDVLILTTDGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEMKDRHLVTKRLKEHIADKKKLPILIFPEGTCINNTSVMMFKKGSFEIGGTIHPVAIKYNPQFGDAFWNSSKYNMVSYLLRMMTSWAIVCDVWYMPPMTREEGEDAVQFANRVKSAIAIQGGLTELPWDGGLKRAKVKDIFKEEQQKNYSKMIVGNGSLS | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | ELAGKILSTWLTLVL HHHHHHHHHHHHHHH | 22.47 | 20860994 | |
| 13 | Phosphorylation | LAGKILSTWLTLVLG HHHHHHHHHHHHHHH | 22.50 | 20860994 | |
| 16 | Phosphorylation | KILSTWLTLVLGFIL HHHHHHHHHHHHHHH | 13.33 | 20860994 | |
| 26 | Phosphorylation | LGFILLPSVFGVSLG HHHHHHHHHHCCCCC | 30.01 | 20860994 | |
| 59 | Ubiquitination | RIEKGTPKESILKNS EECCCCCHHHHHHCC | 65.02 | - | |
| 61 | Phosphorylation | EKGTPKESILKNSAS CCCCCHHHHHHCCCE | 39.07 | 24719451 | |
| 64 | Ubiquitination | TPKESILKNSASVGI CCHHHHHHCCCEEEE | 47.38 | 21890473 | |
| 66 | Phosphorylation | KESILKNSASVGIIQ HHHHHHCCCEEEEEE | 21.97 | 30266825 | |
| 68 | Phosphorylation | SILKNSASVGIIQRD HHHHCCCEEEEEECC | 22.24 | 25159151 | |
| 77 | Phosphorylation | GIIQRDESPMEKGLS EEEECCCCHHHHCCC | 33.56 | 29255136 | |
| 81 | Ubiquitination | RDESPMEKGLSGLRG CCCCHHHHCCCCCCC | 59.92 | 21890473 | |
| 84 | Phosphorylation | SPMEKGLSGLRGRDF CHHHHCCCCCCCCCC | 44.44 | 24719451 | |
| 101 | Ubiquitination | SDVFYFSKKGLEAIV HHEEEEECCCHHHHH | 40.75 | - | |
| 102 | Ubiquitination | DVFYFSKKGLEAIVE HEEEEECCCHHHHHC | 68.48 | 21890473 | |
| 123 | Phosphorylation | FSSEELVSWNLLTRT CCCHHHHHCCCCCCC | 23.91 | 26074081 | |
| 264 | Ubiquitination | IIQRAMVKACPHVWF HHHHHHHHHCCCEEE | 31.05 | - | |
| 283 | Phosphorylation | MKDRHLVTKRLKEHI CCHHHHHHHHHHHHH | 19.46 | 24719451 | |
| 284 | Acetylation | KDRHLVTKRLKEHIA CHHHHHHHHHHHHHC | 48.53 | 19828349 | |
| 316 | Acetylation | NTSVMMFKKGSFEIG CCEEEEEECCEEECC | 38.03 | 26051181 | |
| 347 | Phosphorylation | AFWNSSKYNMVSYLL CCCCCCHHHHHHHHH | 15.50 | 11027811 | |
| 352 | Phosphorylation | SKYNMVSYLLRMMTS CHHHHHHHHHHHHHH | 9.80 | 11027823 | |
| 368 | Phosphorylation | AIVCDVWYMPPMTRE HHHEEEEECCCCCHH | 10.29 | 22210691 | |
| 373 | Phosphorylation | VWYMPPMTREEGEDA EEECCCCCHHCCHHH | 40.48 | 22210691 | |
| 388 | Ubiquitination | VQFANRVKSAIAIQG HHHHHHHHHHHHHCC | 30.82 | 21890473 | |
| 407 | Acetylation | LPWDGGLKRAKVKDI CCCCCCCCHHHHHHH | 54.29 | 24431325 | |
| 407 | Ubiquitination | LPWDGGLKRAKVKDI CCCCCCCCHHHHHHH | 54.29 | 21890473 | |
| 434 | Phosphorylation | IVGNGSLS------- ECCCCCCC------- | 39.61 | 25159151 |
| 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 GPAT3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPAT3_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 GPAT3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GPAT3_HUMAN !! | ||||
| 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 |
| "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-68 AND SER-77, AND MASSSPECTROMETRY. | |
| "Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY. | |