| UniProt ID | GSLG1_CAEEL | |
|---|---|---|
| UniProt AC | Q19459 | |
| Protein Name | Golgi apparatus protein 1 homolog | |
| Gene Name | F14E5.2 | |
| Organism | Caenorhabditis elegans. | |
| Sequence Length | 1149 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
| Protein Description | ||
| Protein Sequence | MWRFPLILASVCWLTTAQQQNVANDPDKKLASFDACKADIHKHCSRPDVDLTSDMSILECLQDAGFSETATLSEQCEQLVWDFKVKITQDERFVSAAKQYCEEELKGNAAMNLCTSQTQPGFALSCLMEFTKNVTETGKCHAFLARTERLAFSDFRLVGPFVTKCRAILDKFKCNVLTPDPAHKGVRVAHTQGMALECILDKVVKNAKTQADALQILGDDCKHEVLRLAEMQADDFHLDRPLFFACRLDRERYCKDVPSGEGKVFECLMMNRNDKFMDPECGNLLAERAYLMGRDYRMAHPLTKACQPELTRYKCEPQNQIESAAHFHLAWILLCLENGANQPEHKEVQPSKECAHEMITHRQMMMQHFRMAPELVLNCAQEIDKWCSPRGDIEAEGRTLHCLMEHAESRNETLKLGAQCLQAVQQVVKVADIGRNYKVDKVLYGSCRSLIDGPCAQDAVSETATLTCLMRNVDSPDMVPECEKRLLEVQYFMARDWTMDPQLYEACHQEAVSRCSALDNWHQQHNSDNTVDRGPQVLACLYRSAYDEQNPLSVKCGTQVRQLLHVRAVRVNLIPEIEDSCREALSEFCSHNVKPSEEMMCLQQNFETDNFKRKHPQCFAELTKFTEMEAKDTKLNRALSKACKPVISTHCAQFANEEIDHGDVLECLVNNKDAKEMNNKCRSYVNHFELISLRDYHFSYKFQKACASDIEQSCKGHNNDKGEIIRCLSEVRFEHKVLGSPKDLTDDCKKQLKVAYLQQEQVEFDDKEHMADADPKLSQKCEQEIKMYKCNQADTFEDTIECLRLNFEHLGPECKSMIFYREKIEAVDNSMDDELQKKCRYDIGKFCANSDSENVLECLTNTKIVRLLQRECKAIVKERMQESARDVRLRPQLLTSCRKEAEQYCPEDMKKINMPQYSQTVLDGVVVSCLRDKFRQSISDQNHIDFSPRCSAEVSRAIVEAEFDPQLDPPLYNACKSTINDHCSATIMESGGHFDNVMECLKNDFNKGLIRDKQCSEQVARRLQESLVDIHLDPVLHEACAMDIQRYCRDVPPGHSRIVMCLMDSADKQELSKECSTKLSDRNKLWMKAHSEFQMALPDSWHAFANLVMEHPERNSILGYLAGFIVFILLIGCCCGRVSKKQYIEMKNR | |
| 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 |
|---|---|---|---|---|---|
| 133 | N-linked_Glycosylation | CLMEFTKNVTETGKC HHHHHHCCCCCCCCC | 42.77 | - | |
| 411 | N-linked_Glycosylation | MEHAESRNETLKLGA HHHHHHHHHHHHHHH | 56.75 | 17761667 | |
| 830 | Phosphorylation | KIEAVDNSMDDELQK HHHHHCCCCCHHHHH | 21.08 | 28854356 | |
| 850 | Phosphorylation | IGKFCANSDSENVLE HHHHHCCCCCCCHHH | 24.80 | 30078680 | |
| 1072 | Phosphorylation | SADKQELSKECSTKL CCCHHHHHHHHHHHH | 26.17 | 19530675 | |
| 1076 | Phosphorylation | QELSKECSTKLSDRN HHHHHHHHHHHHHHH | 29.66 | 19530675 | |
| 1077 | Phosphorylation | ELSKECSTKLSDRNK HHHHHHHHHHHHHHC | 47.89 | 19530675 |
| 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 GSLG1_CAEEL !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GSLG1_CAEEL !! | ||||||
* 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 GSLG1_CAEEL !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GSLG1_CAEEL !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| N-linked Glycosylation | |
| Reference | PubMed |
| "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins."; Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.; Mol. Cell. Proteomics 6:2100-2109(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASSSPECTROMETRY. | |
| "Lectin affinity capture, isotope-coded tagging and mass spectrometryto identify N-linked glycoproteins."; Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,Kasai K., Takahashi N., Isobe T.; Nat. Biotechnol. 21:667-672(2003). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASSSPECTROMETRY. | |