| UniProt ID | PSD2_YEAST | |
|---|---|---|
| UniProt AC | P53037 | |
| Protein Name | Phosphatidylserine decarboxylase proenzyme 2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:7890740} | |
| Gene Name | PSD2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000303|PubMed:7890739} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1138 | |
| Subcellular Localization |
Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side . Endosome membrane Peripheral membrane protein Cytoplasmic side . |
|
| Protein Description | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. [PubMed: 7890740] | |
| Protein Sequence | MRIIKGRKRGKNKKPTLILKIHVIQAENIEALKTFNCNPVCFVTTNTFYSQKTNKLKNSNTHWNQTLRIKLPRNPTSEWLRIIVYDALPTGAPPTTPSRPRTTTANTSSSTLSNSGLSSHSHSSRNLNVTSKGNQTSTSINSVSSSATPAPSHSSSSLSTTGPGSTHKNRINSYLYLGEAKISLLDLFKRKDTTTSYKFSIEAQRYHLYDMKGGKDQDSLNCNFLVGDILLGFKLECNVKRTPTFQAFNAWRNELNTYLGRIDRNKARMRSSSSLPPPLEDMLSNSSAVSGNEIRREKPYSDTDLAHDEEVNAEDEIDAEESIEDMNSSGSICTERRYDIDNDTIFDSISEVVSLNDEELDILNDFEEADHPNVPDINVHDIDEDTRISLSSMITALDEYDIVEPEDVAKLPAVSENDITSVDDEESENQQESDEEFDIYNEDEREDSDFQSKEYIGSRLLHLQRGKHNKSYANYLYRRAKSNFFISKKEHAMGVVFMHIGAIKNLPALRNRLSKTNYEMDPFIVISFGRRVFKTSWRKHTLNPEFNEYAAFEVFPHETNFAFSIKVVDKDSFSFNDDVAKCELAWFDMLQQQQHENEWIPYEIPLDLTVEPAHAPKQPVLYSSFKYVSYPFLKKSFWKEAVDTSVNLERLDIIQVMLYLERLGSFTMADSFELFQHFNKSAWAGQSITRSQLVEGLQSWRKSTNFKRIWTCPRCMRSCKPTRNARRSKLVLENDLITHFAICTFSKEHKTLKPSYVSSAFASKRWFSKVLIKLTYGKYALGSNNANILVQDRDTGIIIEEKISAHVKLGMRIIYNGKSPESKKFRSLLKTLSIRQGKKFDSTASAKQIEPFIKFHSLDLSQCRDKDFKTFNEFFYRKLKPGSRLPESNNKEILFSPADSRCTVFPTIQESKEIWVKGRKFSIKKLANNYNPETFNDNNCSIGIFRLAPQDYHRFHSPCNGTIGKPVYVDGEYYTVNPMAVRSELDVFGENIRVIIPIDSPQFGKLLYIPIGAMMVGSILLTCKENDVVESGQELGYFKFGGSTIIIIIPHNNFMFDSDLVKNSSERIETLVKVGMSIGHTSNVNELKRIRIKVDDPKKIERIKRTISVSDENAKSTGNVTWEYHTLREMMNKDFAGL | |
| 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 |
|---|---|---|---|---|---|
| 85 | Phosphorylation | EWLRIIVYDALPTGA CCEEEEEEECCCCCC | 5.77 | 27017623 | |
| 95 | Phosphorylation | LPTGAPPTTPSRPRT CCCCCCCCCCCCCCC | 50.72 | 27017623 | |
| 98 | Phosphorylation | GAPPTTPSRPRTTTA CCCCCCCCCCCCCCC | 53.47 | 27017623 | |
| 102 | Phosphorylation | TTPSRPRTTTANTSS CCCCCCCCCCCCCCC | 31.05 | 22369663 | |
| 103 | Phosphorylation | TPSRPRTTTANTSSS CCCCCCCCCCCCCCC | 25.78 | 22369663 | |
| 104 | Phosphorylation | PSRPRTTTANTSSST CCCCCCCCCCCCCCC | 19.80 | 22369663 | |
| 107 | Phosphorylation | PRTTTANTSSSTLSN CCCCCCCCCCCCCCC | 27.76 | 22369663 | |
| 108 | Phosphorylation | RTTTANTSSSTLSNS CCCCCCCCCCCCCCC | 23.30 | 22369663 | |
| 109 | Phosphorylation | TTTANTSSSTLSNSG CCCCCCCCCCCCCCC | 25.88 | 22369663 | |
| 110 | Phosphorylation | TTANTSSSTLSNSGL CCCCCCCCCCCCCCC | 32.89 | 22369663 | |
| 111 | Phosphorylation | TANTSSSTLSNSGLS CCCCCCCCCCCCCCC | 35.83 | 22369663 | |
| 113 | Phosphorylation | NTSSSTLSNSGLSSH CCCCCCCCCCCCCCC | 29.10 | 22369663 | |
| 115 | Phosphorylation | SSSTLSNSGLSSHSH CCCCCCCCCCCCCCC | 37.42 | 22369663 | |
| 118 | Phosphorylation | TLSNSGLSSHSHSSR CCCCCCCCCCCCCCC | 29.54 | 22369663 | |
| 119 | Phosphorylation | LSNSGLSSHSHSSRN CCCCCCCCCCCCCCC | 33.77 | 22369663 | |
| 121 | Phosphorylation | NSGLSSHSHSSRNLN CCCCCCCCCCCCCCE | 27.32 | 22369663 | |
| 123 | Phosphorylation | GLSSHSHSSRNLNVT CCCCCCCCCCCCEEC | 33.73 | 23749301 | |
| 124 | Phosphorylation | LSSHSHSSRNLNVTS CCCCCCCCCCCEECC | 21.55 | 22369663 | |
| 136 | Phosphorylation | VTSKGNQTSTSINSV ECCCCCCCCCEEEEE | 37.66 | 23749301 | |
| 139 | Phosphorylation | KGNQTSTSINSVSSS CCCCCCCEEEEECCC | 21.38 | 21551504 | |
| 142 | Phosphorylation | QTSTSINSVSSSATP CCCCEEEEECCCCCC | 23.00 | 23749301 | |
| 144 | Phosphorylation | STSINSVSSSATPAP CCEEEEECCCCCCCC | 20.56 | 21551504 | |
| 157 | Phosphorylation | APSHSSSSLSTTGPG CCCCCCCCCCCCCCC | 28.43 | 21440633 | |
| 286 | Phosphorylation | LEDMLSNSSAVSGNE HHHHHCCCCCCCCCC | 19.12 | 23749301 | |
| 290 | Phosphorylation | LSNSSAVSGNEIRRE HCCCCCCCCCCCCCC | 35.30 | 23749301 | |
| 471 | Phosphorylation | QRGKHNKSYANYLYR HCCCCCHHHHHHHHH | 34.49 | 22369663 | |
| 516 | Phosphorylation | LRNRLSKTNYEMDPF HHHHHHHCCCCCCCE | 39.39 | 28889911 | |
| 518 | Phosphorylation | NRLSKTNYEMDPFIV HHHHHCCCCCCCEEE | 20.19 | 28889911 | |
| 738 | Phosphorylation | VLENDLITHFAICTF EEECCHHHEEEEEEC | 20.45 | 23749301 | |
| 744 | Phosphorylation | ITHFAICTFSKEHKT HHEEEEEECCCCCCC | 25.49 | 23749301 | |
| 753 | Ubiquitination | SKEHKTLKPSYVSSA CCCCCCCCHHHHCHH | 36.83 | 22106047 | |
| 857 | Phosphorylation | EPFIKFHSLDLSQCR HHHEEEECCCHHHHC | 27.06 | 28889911 | |
| 1043 | Pyruvate | GYFKFGGSTIIIIIP EEEEECCEEEEEEEE | 19.47 | - | |
| 1043 | Pyruvic acid (Ser) | GYFKFGGSTIIIIIP EEEEECCEEEEEEEE | 19.47 | - | |
| 1106 | Phosphorylation | KIERIKRTISVSDEN HHHHHEEEEECCCCC | 16.77 | 28152593 | |
| 1108 | Phosphorylation | ERIKRTISVSDENAK HHHEEEEECCCCCHH | 18.24 | 19823750 | |
| 1110 | Phosphorylation | IKRTISVSDENAKST HEEEEECCCCCHHCC | 32.20 | 21440633 |
| 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 PSD2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSD2_YEAST !! | ||||||
* 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 PSD2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108, AND MASSSPECTROMETRY. | |