| UniProt ID | AGR2_HUMAN | |
|---|---|---|
| UniProt AC | O95994 | |
| Protein Name | Anterior gradient protein 2 homolog | |
| Gene Name | AGR2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 175 | |
| Subcellular Localization | Secreted . Endoplasmic reticulum. | |
| Protein Description | Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion. [PubMed: 23274113] | |
| Protein Sequence | MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL | |
| 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 |
|---|---|---|---|---|---|
| 36 | Phosphorylation | AKKDTKDSRPKLPQT CCCCCCCCCCCCCHH | 52.63 | 50564017 | |
| 55 | Phosphorylation | WGDQLIWTQTYEEAL CCCEEEEEEHHHHHH | 12.21 | 26657352 | |
| 95 | 2-Hydroxyisobutyrylation | KKVFAENKEIQKLAE HHHHHCCHHHHHHHH | 47.93 | - | |
| 111 | Phosphorylation | FVLLNLVYETTDKHL HHHHHHHHHCCCCCC | 15.66 | 6947735 | |
| 113 | Phosphorylation | LLNLVYETTDKHLSP HHHHHHHCCCCCCCC | 23.70 | 46160571 | |
| 114 | Phosphorylation | LNLVYETTDKHLSPD HHHHHHCCCCCCCCC | 30.98 | 46160577 | |
| 116 | Acetylation | LVYETTDKHLSPDGQ HHHHCCCCCCCCCCC | 44.33 | 25825284 | |
| 119 | Phosphorylation | ETTDKHLSPDGQYVP HCCCCCCCCCCCEEC | 22.21 | 23312004 | |
| 124 | Phosphorylation | HLSPDGQYVPRIMFV CCCCCCCEECEEEEE | 20.25 | 11896147 | |
| 134 | Phosphorylation | RIMFVDPSLTVRADI EEEEECCCCEEEEEE | 32.01 | 28348404 | |
| 136 | Phosphorylation | MFVDPSLTVRADITG EEECCCCEEEEEECC | 16.57 | 28348404 | |
| 145 | Phosphorylation | RADITGRYSNRLYAY EEEECCCCCCCEEEE | 16.19 | 22210691 | |
| 146 | Phosphorylation | ADITGRYSNRLYAYE EEECCCCCCCEEEEC | 17.70 | 22210691 | |
| 150 | Phosphorylation | GRYSNRLYAYEPADT CCCCCCEEEECCCCH | 12.14 | 76972927 | |
| 152 | Phosphorylation | YSNRLYAYEPADTAL CCCCEEEECCCCHHH | 14.64 | 76972933 | |
| 157 | Phosphorylation | YAYEPADTALLLDNM EEECCCCHHHHHHHH | 22.70 | 110738527 | |
| 165 | Acetylation | ALLLDNMKKALKLLK HHHHHHHHHHHHHHH | 40.94 | 155405 | |
| 166 | Acetylation | LLLDNMKKALKLLKT HHHHHHHHHHHHHHH | 48.46 | 156175 | |
| 172 | Acetylation | KKALKLLKTEL---- HHHHHHHHHCC---- | 50.84 | 25825284 | |
| 173 | Phosphorylation | KALKLLKTEL----- HHHHHHHHCC----- | 42.35 | 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 AGR2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AGR2_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 AGR2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| BRD7_HUMAN | BRD7 | physical | 16169070 | |
| CC90B_HUMAN | CCDC90B | physical | 16169070 | |
| MED31_HUMAN | MED31 | physical | 16169070 | |
| DPYL1_HUMAN | CRMP1 | physical | 16169070 | |
| DAG1_HUMAN | DAG1 | physical | 12592373 | |
| LYPD3_HUMAN | LYPD3 | physical | 12592373 | |
| A4_HUMAN | APP | physical | 21832049 | |
| UBQL1_HUMAN | UBQLN1 | physical | 25416956 | |
| N62CL_HUMAN | NUP62CL | physical | 25416956 | |
| CTSR1_HUMAN | CATSPER1 | physical | 25416956 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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