| UniProt ID | PIGG_HUMAN | |
|---|---|---|
| UniProt AC | Q5H8A4 | |
| Protein Name | GPI ethanolamine phosphate transferase 2 | |
| Gene Name | PIGG | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 983 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose.. | |
| Protein Sequence | MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTLPPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIKALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGTTSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMDSVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKPGDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSKLLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLSLSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVILVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNPMHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLGDDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWLILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVSKAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKSQVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAAEITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWASHLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGMHLLITAAVCVFFTAMDQTRLTQS | |
| 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 |
|---|---|---|---|---|---|
| 66 | Phosphorylation | TLPPPLFSKVVIVLI CCCCCHHHHHHHHHH | 32.02 | 24719451 | |
| 92 | Phosphorylation | KGVKFMPYTTYLVEK CCCEECCCEEEEEEC | 10.42 | 18083107 | |
| 93 | Phosphorylation | GVKFMPYTTYLVEKG CCEECCCEEEEEECC | 11.77 | 30206219 | |
| 94 | Phosphorylation | VKFMPYTTYLVEKGA CEECCCEEEEEECCC | 14.71 | 30206219 | |
| 95 | Phosphorylation | KFMPYTTYLVEKGAS EECCCEEEEEECCCC | 10.84 | 18083107 | |
| 120 | Ubiquitination | TVTMPRIKALMTGSL CCCCHHHHHHHHCCC | 36.43 | - | |
| 139 | Phosphorylation | DVIRNLNSPALLEDS HHHHHCCCCHHHCHH | 18.08 | - | |
| 194 | N-linked_Glycosylation | DYTEVDNNVTRHLDK CCEEECCHHHHHHHH | 31.88 | UniProtKB CARBOHYD | |
| 201 | Ubiquitination | NVTRHLDKVLKRGDW HHHHHHHHHHHCCCC | 56.69 | - | |
| 238 (in isoform 3) | Ubiquitination | - | 58.40 | 21890473 | |
| 246 (in isoform 3) | Ubiquitination | - | 2.39 | 21890473 | |
| 249 | Ubiquitination | VLMKIHTSLQSKERE HHHHHHHHHHCCCCC | 15.39 | - | |
| 253 | Ubiquitination | IHTSLQSKERETPLP HHHHHHCCCCCCCCC | 48.07 | - | |
| 257 | Ubiquitination | LQSKERETPLPNLLV HHCCCCCCCCCCEEE | 36.02 | - | |
| 274 (in isoform 3) | Ubiquitination | - | 36.36 | 21890473 | |
| 285 | Ubiquitination | GASSTEEVNTPLILI CCCCCCCCCCCEEEE | 8.66 | - | |
| 312 | Phosphorylation | HPKHVQQTDVAATLA CCHHHCHHHHHHHHH | 18.49 | 19690332 | |
| 317 | Phosphorylation | QQTDVAATLAIALGL CHHHHHHHHHHHHCC | 13.64 | 19690332 | |
| 371 (in isoform 2) | Ubiquitination | - | 62.07 | 21890473 | |
| 371 (in isoform 4) | Ubiquitination | - | 62.07 | 21890473 | |
| 371 (in isoform 1) | Ubiquitination | - | 62.07 | 21890473 | |
| 371 | Ubiquitination | ENVPSYEKDPGFEQF HCCCCCCCCCCCHHH | 62.07 | 21906983 | |
| 379 (in isoform 4) | Ubiquitination | - | 41.01 | 21890473 | |
| 379 (in isoform 2) | Ubiquitination | - | 41.01 | 21890473 | |
| 379 | Ubiquitination | DPGFEQFKMSERLHG CCCCHHHHHHHHHCC | 41.01 | 21906983 | |
| 379 (in isoform 1) | Ubiquitination | - | 41.01 | 21890473 | |
| 407 (in isoform 4) | Ubiquitination | - | 43.41 | 21890473 | |
| 407 | Ubiquitination | VLFNLGSKVLRQYLD HHHHHCHHHHHHHHH | 43.41 | 21890473 | |
| 407 (in isoform 2) | Ubiquitination | - | 43.41 | 21890473 | |
| 407 (in isoform 1) | Ubiquitination | - | 43.41 | 21890473 | |
| 407 | Ubiquitination | VLFNLGSKVLRQYLD HHHHHCHHHHHHHHH | 43.41 | 21890473 | |
| 502 (in isoform 3) | Ubiquitination | - | 16.91 | 21890473 | |
| 627 (in isoform 2) | Ubiquitination | - | 26.28 | 21890473 | |
| 635 (in isoform 1) | Ubiquitination | - | 60.05 | 21890473 | |
| 635 | Ubiquitination | CDVLERDKGHGSPST CCEEECCCCCCCCCH | 60.05 | 2190698 | |
| 639 | Phosphorylation | ERDKGHGSPSTSEVL ECCCCCCCCCHHHHH | 15.25 | 25159151 | |
| 641 | Phosphorylation | DKGHGSPSTSEVLRG CCCCCCCCHHHHHCC | 46.38 | 29083192 | |
| 642 | Phosphorylation | KGHGSPSTSEVLRGR CCCCCCCHHHHHCCH | 32.08 | 21712546 | |
| 643 | Phosphorylation | GHGSPSTSEVLRGRE CCCCCCHHHHHCCHH | 30.00 | 25159151 | |
| 750 | Acetylation | FPWRPDSKDISKGII CCCCCCCCCCCHHHH | 67.47 | 88439 | |
| 754 | Acetylation | PDSKDISKGIIEARF CCCCCCCHHHHHHHH | 55.23 | 88443 | |
| 952 | Phosphorylation | LFIWSVFSPKLLYEG HHHHHHCCHHHHHHH | 20.97 | 24719451 |
| 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 PIGG_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIGG_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 PIGG_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| A4_HUMAN | APP | physical | 21832049 | |
| PIGF_MOUSE | Pigf | physical | 15632136 |
| 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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