UniProt ID | MBOA2_HUMAN | |
---|---|---|
UniProt AC | Q6ZWT7 | |
Protein Name | Lysophospholipid acyltransferase 2 | |
Gene Name | MBOAT2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 520 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.. | |
Protein Sequence | MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAIWFRTYLHSSKTSSFIRHVVATLLGLYLALFCFGWYALHFLVQSGISYCIMIIIGVENMHNYCFVFALGYLTVCQVTRVYIFDYGQYSADFSGPMMIITQKITSLACEIHDGMFRKDEELTSSQRDLAVRRMPSLLEYLSYNCNFMGILAGPLCSYKDYITFIEGRSYHITQSGENGKEETQYERTEPSPNTAVVQKLLVCGLSLLFHLTICTTLPVEYNIDEHFQATASWPTKIIYLYISLLAARPKYYFAWTLADAINNAAGFGFRGYDENGAARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERTSFSPTIQTFILSAIWHGVYPGYYLTFLTGVLMTLAARAMRNNFRHYFIEPSQLKLFYDVITWIVTQVAISYTVVPFVLLSIKPSLTFYSSWYYCLHILGILVLLLLPVKKTQRRKNTHENIQLSQSKKFDEGENSLGQNSFSTTNNVCNQNQEIASRHSSLKQ | |
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 |
---|---|---|---|---|---|
53 | Phosphorylation | LHSSKTSSFIRHVVA HHCCCCHHHHHHHHH | 29.89 | 24719451 | |
119 | Phosphorylation | VCQVTRVYIFDYGQY HCCEEEEEEEECCCC | 7.80 | 24043423 | |
123 | Phosphorylation | TRVYIFDYGQYSADF EEEEEEECCCCCCCC | 8.72 | 24043423 | |
126 | Phosphorylation | YIFDYGQYSADFSGP EEEECCCCCCCCCCC | 11.06 | 24043423 | |
127 | Phosphorylation | IFDYGQYSADFSGPM EEECCCCCCCCCCCE | 17.30 | 24043423 | |
131 | Phosphorylation | GQYSADFSGPMMIIT CCCCCCCCCCEEEEE | 42.40 | 24043423 | |
138 | Phosphorylation | SGPMMIITQKITSLA CCCEEEEEHHHHHHH | 16.94 | 24043423 | |
160 | Phosphorylation | FRKDEELTSSQRDLA CCCCHHCCHHHHHHH | 29.61 | 29083192 | |
161 | Phosphorylation | RKDEELTSSQRDLAV CCCHHCCHHHHHHHH | 36.78 | 29083192 | |
162 | Phosphorylation | KDEELTSSQRDLAVR CCHHCCHHHHHHHHH | 24.81 | 29083192 | |
198 | Phosphorylation | PLCSYKDYITFIEGR CCCCCCCEEEEECCC | 9.56 | - | |
217 | Acetylation | TQSGENGKEETQYER EECCCCCCEECCCCC | 65.05 | 23236377 | |
217 | Ubiquitination | TQSGENGKEETQYER EECCCCCCEECCCCC | 65.05 | - | |
220 | Phosphorylation | GENGKEETQYERTEP CCCCCEECCCCCCCC | 37.23 | 28796482 | |
222 | Phosphorylation | NGKEETQYERTEPSP CCCEECCCCCCCCCC | 18.13 | 28796482 | |
276 | Phosphorylation | SWPTKIIYLYISLLA CCCHHHHHHHHHHHH | 9.27 | 22817900 | |
321 | Phosphorylation | AARWDLISNLRIQQI CCHHHHHHHHEEEEE | 36.79 | 24719451 | |
331 | Phosphorylation | RIQQIEMSTSFKMFL EEEEEEECCCHHHHH | 14.22 | 24043423 | |
332 | Phosphorylation | IQQIEMSTSFKMFLD EEEEEECCCHHHHHH | 36.55 | 24043423 | |
333 | Phosphorylation | QQIEMSTSFKMFLDN EEEEECCCHHHHHHC | 18.63 | 24043423 | |
437 | Phosphorylation | VVPFVLLSIKPSLTF HHCHHHEEECCCHHH | 25.14 | 24719451 | |
472 | Ubiquitination | VKKTQRRKNTHENIQ CCCCHHHCCCCCCHH | 69.27 | - | |
474 | Phosphorylation | KTQRRKNTHENIQLS CCHHHCCCCCCHHHH | 33.33 | 25159151 | |
481 | Phosphorylation | THENIQLSQSKKFDE CCCCHHHHHCCCCCC | 18.94 | 30266825 | |
483 | Phosphorylation | ENIQLSQSKKFDEGE CCHHHHHCCCCCCCC | 34.14 | 30266825 | |
492 | Phosphorylation | KFDEGENSLGQNSFS CCCCCCCCCCCCCCH | 29.58 | 27251275 | |
497 | Phosphorylation | ENSLGQNSFSTTNNV CCCCCCCCCHHCCCC | 16.82 | 23898821 | |
499 | Phosphorylation | SLGQNSFSTTNNVCN CCCCCCCHHCCCCHH | 33.86 | 28555341 | |
500 | Phosphorylation | LGQNSFSTTNNVCNQ CCCCCCHHCCCCHHH | 31.37 | 28348404 | |
501 | Phosphorylation | GQNSFSTTNNVCNQN CCCCCHHCCCCHHHH | 24.48 | 28348404 | |
513 | Phosphorylation | NQNQEIASRHSSLKQ HHHHHHHHHHHHCCC | 35.87 | 28348404 |
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 MBOA2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MBOA2_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 MBOA2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MBOA2_HUMAN !! |
Kegg Disease | ||||||
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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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