| UniProt ID | TGON2_HUMAN | |
|---|---|---|
| UniProt AC | O43493 | |
| Protein Name | Trans-Golgi network integral membrane protein 2 | |
| Gene Name | TGOLN2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 479 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane Single-pass type I membrane protein. Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endoso |
|
| Protein Description | May be involved in regulating membrane traffic to and from trans-Golgi network.. | |
| Protein Sequence | MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKYVLILNVFPAPPKRSFFPVLTEWYIPLEKDERHQWIVLLSFQL | |
| 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 |
|---|---|---|---|---|---|
| 23 | O-linked_Glycosylation | GAVPLLATESVKQEE CCCCCCCCCCHHHHH | 28.85 | OGP | |
| 36 | O-linked_Glycosylation | EEAGVRPSAGNVSTH HHCCCCCCCCCCCCC | 37.94 | 55833463 | |
| 39 | N-linked_Glycosylation | GVRPSAGNVSTHPSL CCCCCCCCCCCCCCH | 25.04 | UniProtKB CARBOHYD | |
| 41 | O-linked_Glycosylation | RPSAGNVSTHPSLSQ CCCCCCCCCCCCHHC | 25.62 | 55833467 | |
| 42 | O-linked_Glycosylation | PSAGNVSTHPSLSQR CCCCCCCCCCCHHCC | 33.26 | 55833471 | |
| 45 | O-linked_Glycosylation | GNVSTHPSLSQRPGG CCCCCCCCHHCCCCC | 32.80 | 55833475 | |
| 47 | O-linked_Glycosylation | VSTHPSLSQRPGGST CCCCCCHHCCCCCCC | 28.60 | 55833479 | |
| 53 | O-linked_Glycosylation | LSQRPGGSTKSHPEP HHCCCCCCCCCCCCC | 38.28 | 55833483 | |
| 54 | O-linked_Glycosylation | SQRPGGSTKSHPEPQ HCCCCCCCCCCCCCC | 39.58 | 55833487 | |
| 56 | O-linked_Glycosylation | RPGGSTKSHPEPQTP CCCCCCCCCCCCCCC | 44.34 | 55824035 | |
| 62 | O-linked_Glycosylation | KSHPEPQTPKDSPSK CCCCCCCCCCCCCCC | 42.92 | 55824039 | |
| 62 | Phosphorylation | KSHPEPQTPKDSPSK CCCCCCCCCCCCCCC | 42.92 | 26091039 | |
| 66 | Phosphorylation | EPQTPKDSPSKSSAE CCCCCCCCCCCCCCC | 36.88 | 29255136 | |
| 68 | O-linked_Glycosylation | QTPKDSPSKSSAEAQ CCCCCCCCCCCCCCC | 49.47 | OGP | |
| 68 | Phosphorylation | QTPKDSPSKSSAEAQ CCCCCCCCCCCCCCC | 49.47 | 29255136 | |
| 70 | O-linked_Glycosylation | PKDSPSKSSAEAQTP CCCCCCCCCCCCCCC | 38.83 | OGP | |
| 70 | Phosphorylation | PKDSPSKSSAEAQTP CCCCCCCCCCCCCCC | 38.83 | 29255136 | |
| 71 | O-linked_Glycosylation | KDSPSKSSAEAQTPE CCCCCCCCCCCCCCC | 33.59 | OGP | |
| 71 | Phosphorylation | KDSPSKSSAEAQTPE CCCCCCCCCCCCCCC | 33.59 | 29255136 | |
| 76 | O-linked_Glycosylation | KSSAEAQTPEDTPNK CCCCCCCCCCCCCCC | 35.38 | OGP | |
| 76 | Phosphorylation | KSSAEAQTPEDTPNK CCCCCCCCCCCCCCC | 35.38 | 29255136 | |
| 80 | Phosphorylation | EAQTPEDTPNKSGAE CCCCCCCCCCCCHHH | 27.40 | 23927012 | |
| 82 | N-linked_Glycosylation | QTPEDTPNKSGAEAK CCCCCCCCCCHHHHH | 53.90 | UniProtKB CARBOHYD | |
| 84 | Phosphorylation | PEDTPNKSGAEAKTQ CCCCCCCCHHHHHHC | 50.29 | 22798277 | |
| 94 | Phosphorylation | EAKTQKDSSNKSGAE HHHHCCCCCCCCCHH | 42.73 | 17287340 | |
| 95 | Phosphorylation | AKTQKDSSNKSGAEA HHHCCCCCCCCCHHH | 59.41 | 21601212 | |
| 96 | N-linked_Glycosylation | KTQKDSSNKSGAEAK HHCCCCCCCCCHHHH | 46.60 | UniProtKB CARBOHYD | |
| 98 | Phosphorylation | QKDSSNKSGAEAKTQ CCCCCCCCCHHHHHC | 47.70 | 17287340 | |
| 114 | Phosphorylation | GSTSKSGSEAQTTKD CCCCCCCCCCCCCCC | 36.53 | - | |
| 118 | O-linked_Glycosylation | KSGSEAQTTKDSTSK CCCCCCCCCCCCCCC | 42.75 | 55829725 | |
| 118 | Phosphorylation | KSGSEAQTTKDSTSK CCCCCCCCCCCCCCC | 42.75 | - | |
| 119 | O-linked_Glycosylation | SGSEAQTTKDSTSKS CCCCCCCCCCCCCCC | 22.30 | 55829731 | |
| 119 | Phosphorylation | SGSEAQTTKDSTSKS CCCCCCCCCCCCCCC | 22.30 | - | |
| 122 | O-linked_Glycosylation | EAQTTKDSTSKSHPE CCCCCCCCCCCCCCC | 35.82 | 55829737 | |
| 123 | O-linked_Glycosylation | AQTTKDSTSKSHPEL CCCCCCCCCCCCCCC | 50.75 | 55829741 | |
| 123 | Phosphorylation | AQTTKDSTSKSHPEL CCCCCCCCCCCCCCC | 50.75 | 24275569 | |
| 124 | O-linked_Glycosylation | QTTKDSTSKSHPELQ CCCCCCCCCCCCCCC | 35.79 | 55829745 | |
| 126 | O-linked_Glycosylation | TKDSTSKSHPELQTP CCCCCCCCCCCCCCC | 44.00 | 55823947 | |
| 126 | Phosphorylation | TKDSTSKSHPELQTP CCCCCCCCCCCCCCC | 44.00 | - | |
| 132 | O-linked_Glycosylation | KSHPELQTPKDSTGK CCCCCCCCCCCCCCC | 44.95 | 36033481 | |
| 132 | Phosphorylation | KSHPELQTPKDSTGK CCCCCCCCCCCCCCC | 44.95 | 20068231 | |
| 136 | O-linked_Glycosylation | ELQTPKDSTGKSGAE CCCCCCCCCCCCCCC | 45.23 | 55833185 | |
| 136 | Phosphorylation | ELQTPKDSTGKSGAE CCCCCCCCCCCCCCC | 45.23 | - | |
| 137 | O-linked_Glycosylation | LQTPKDSTGKSGAEA CCCCCCCCCCCCCCC | 59.78 | 55833189 | |
| 137 | Phosphorylation | LQTPKDSTGKSGAEA CCCCCCCCCCCCCCC | 59.78 | - | |
| 140 | Phosphorylation | PKDSTGKSGAEAQTP CCCCCCCCCCCCCCC | 44.58 | 22798277 | |
| 146 | O-linked_Glycosylation | KSGAEAQTPEDSPNR CCCCCCCCCCCCCCC | 35.38 | OGP | |
| 146 | Phosphorylation | KSGAEAQTPEDSPNR CCCCCCCCCCCCCCC | 35.38 | 26699800 | |
| 147 (in isoform 6) | Phosphorylation | - | 31.17 | 24275569 | |
| 150 | Phosphorylation | EAQTPEDSPNRSGAE CCCCCCCCCCCCHHH | 23.55 | 21815630 | |
| 150 (in isoform 6) | Phosphorylation | - | 23.55 | 26699800 | |
| 152 | N-linked_Glycosylation | QTPEDSPNRSGAEAK CCCCCCCCCCHHHCC | 55.49 | UniProtKB CARBOHYD | |
| 154 | Phosphorylation | PEDSPNRSGAEAKTQ CCCCCCCCHHHCCCC | 49.33 | 28192239 | |
| 158 (in isoform 6) | Phosphorylation | - | 21.47 | 25849741 | |
| 159 (in isoform 6) | Phosphorylation | - | 42.89 | 26699800 | |
| 160 | Phosphorylation | RSGAEAKTQKDSPSK CCHHHCCCCCCCCCC | 48.15 | 23312004 | |
| 162 (in isoform 6) | Phosphorylation | - | 66.46 | 26699800 | |
| 164 | Phosphorylation | EAKTQKDSPSKSGSE HCCCCCCCCCCCCCC | 37.80 | 23312004 | |
| 166 | Phosphorylation | KTQKDSPSKSGSEAQ CCCCCCCCCCCCCCC | 43.32 | 23312004 | |
| 168 | Phosphorylation | QKDSPSKSGSEAQTT CCCCCCCCCCCCCCC | 52.46 | 23312004 | |
| 170 | Phosphorylation | DSPSKSGSEAQTTKD CCCCCCCCCCCCCCC | 36.53 | 24505115 | |
| 174 | O-linked_Glycosylation | KSGSEAQTTKDVPNK CCCCCCCCCCCCCCC | 42.75 | OGP | |
| 175 | O-linked_Glycosylation | SGSEAQTTKDVPNKS CCCCCCCCCCCCCCC | 17.11 | OGP | |
| 180 | N-linked_Glycosylation | QTTKDVPNKSGADGQ CCCCCCCCCCCCCCC | 51.48 | UniProtKB CARBOHYD | |
| 182 | O-linked_Glycosylation | TKDVPNKSGADGQTP CCCCCCCCCCCCCCC | 45.94 | OGP | |
| 188 | O-linked_Glycosylation | KSGADGQTPKDGSSK CCCCCCCCCCCCCCC | 37.52 | OGP | |
| 194 | O-linked_Glycosylation | QTPKDGSSKSGAEDQ CCCCCCCCCCCCCCC | 36.05 | OGP | |
| 196 | Phosphorylation | PKDGSSKSGAEDQTP CCCCCCCCCCCCCCC | 45.22 | 28102081 | |
| 202 | O-linked_Glycosylation | KSGAEDQTPKDVPNK CCCCCCCCCCCCCCC | 44.63 | 55829345 | |
| 202 | Phosphorylation | KSGAEDQTPKDVPNK CCCCCCCCCCCCCCC | 44.63 | 28102081 | |
| 208 | N-linked_Glycosylation | QTPKDVPNKSGAEKQ CCCCCCCCCCCCCCC | 51.48 | UniProtKB CARBOHYD | |
| 210 | Phosphorylation | PKDVPNKSGAEKQTP CCCCCCCCCCCCCCC | 50.29 | 28857561 | |
| 221 | Phosphorylation | KQTPKDGSNKSGAEE CCCCCCCCCCCCCHH | 51.74 | 29255136 | |
| 222 | N-linked_Glycosylation | QTPKDGSNKSGAEEQ CCCCCCCCCCCCHHC | 48.30 | UniProtKB CARBOHYD | |
| 224 | O-linked_Glycosylation | PKDGSNKSGAEEQGP CCCCCCCCCCHHCCC | 47.70 | OGP | |
| 224 | Phosphorylation | PKDGSNKSGAEEQGP CCCCCCCCCCHHCCC | 47.70 | 29255136 | |
| 236 | O-linked_Glycosylation | QGPIDGPSKSGAEEQ CCCCCCCCCCCCCCC | 45.01 | 55832785 | |
| 236 | Phosphorylation | QGPIDGPSKSGAEEQ CCCCCCCCCCCCCCC | 45.01 | 28355574 | |
| 238 | O-linked_Glycosylation | PIDGPSKSGAEEQTS CCCCCCCCCCCCCCC | 47.80 | OGP | |
| 238 | Phosphorylation | PIDGPSKSGAEEQTS CCCCCCCCCCCCCCC | 47.80 | 22798277 | |
| 244 | Phosphorylation | KSGAEEQTSKDSPNK CCCCCCCCCCCCCCC | 40.81 | 24719451 | |
| 245 | O-linked_Glycosylation | SGAEEQTSKDSPNKV CCCCCCCCCCCCCCC | 33.87 | 68999563 | |
| 245 | Phosphorylation | SGAEEQTSKDSPNKV CCCCCCCCCCCCCCC | 33.87 | 22798277 | |
| 245 (in isoform 4) | Phosphorylation | - | 33.87 | 24275569 | |
| 248 (in isoform 4) | Phosphorylation | - | 33.82 | 26699800 | |
| 256 (in isoform 4) | Phosphorylation | - | 34.89 | 25849741 | |
| 257 (in isoform 4) | Phosphorylation | - | 34.14 | 26699800 | |
| 260 (in isoform 4) | Phosphorylation | - | 65.22 | 26699800 | |
| 263 | O-linked_Glycosylation | QPSRKDHSKPISNPS CCCCCCCCCCCCCCC | 50.70 | 68999757 | |
| 263 | Phosphorylation | QPSRKDHSKPISNPS CCCCCCCCCCCCCCC | 50.70 | 24275569 | |
| 267 | O-linked_Glycosylation | KDHSKPISNPSDNKE CCCCCCCCCCCCCCC | 51.74 | 55832319 | |
| 267 | Phosphorylation | KDHSKPISNPSDNKE CCCCCCCCCCCCCCC | 51.74 | - | |
| 270 | O-linked_Glycosylation | SKPISNPSDNKELPK CCCCCCCCCCCCCCC | 59.05 | 55832325 | |
| 270 | Phosphorylation | SKPISNPSDNKELPK CCCCCCCCCCCCCCC | 59.05 | - | |
| 272 (in isoform 6) | Phosphorylation | - | 44.00 | 28152594 | |
| 274 (in isoform 6) | Phosphorylation | - | 76.26 | 28152594 | |
| 290 | O-linked_Glycosylation | LADKGKLSPHAFKTE HHHHCCCCCCCEECC | 20.37 | 101661085 | |
| 290 | Phosphorylation | LADKGKLSPHAFKTE HHHHCCCCCCCEECC | 20.37 | 23927012 | |
| 296 | O-linked_Glycosylation | LSPHAFKTESGEETD CCCCCEECCCCCCCC | 29.00 | OGP | |
| 296 | Phosphorylation | LSPHAFKTESGEETD CCCCCEECCCCCCCC | 29.00 | 29255136 | |
| 298 | Phosphorylation | PHAFKTESGEETDLI CCCEECCCCCCCCCC | 57.65 | 29255136 | |
| 302 | Phosphorylation | KTESGEETDLISPPQ ECCCCCCCCCCCCCH | 31.63 | 23927012 | |
| 306 | Phosphorylation | GEETDLISPPQEEVK CCCCCCCCCCHHHHC | 37.51 | 23927012 | |
| 314 | Phosphorylation | PPQEEVKSSEPTEDV CCHHHHCCCCCCCCC | 45.14 | 25849741 | |
| 315 | O-linked_Glycosylation | PQEEVKSSEPTEDVE CHHHHCCCCCCCCCC | 41.71 | OGP | |
| 315 | Phosphorylation | PQEEVKSSEPTEDVE CHHHHCCCCCCCCCC | 41.71 | 25849741 | |
| 318 | O-linked_Glycosylation | EVKSSEPTEDVEPKE HHCCCCCCCCCCCCC | 40.54 | 55832013 | |
| 318 | Phosphorylation | EVKSSEPTEDVEPKE HHCCCCCCCCCCCCC | 40.54 | 29507054 | |
| 331 | Phosphorylation | KEAEDDDTGPEEGSP CCCCCCCCCCCCCCC | 62.72 | - | |
| 347 | Phosphorylation | KEEKEKMSGSASSEN HHHHHHHCCCCCCCC | 40.44 | 22617229 | |
| 349 | Phosphorylation | EKEKMSGSASSENRE HHHHHCCCCCCCCCC | 20.05 | 25159151 | |
| 351 | Phosphorylation | EKMSGSASSENREGT HHHCCCCCCCCCCCC | 39.62 | 28355574 | |
| 352 | Phosphorylation | KMSGSASSENREGTL HHCCCCCCCCCCCCC | 38.31 | 30278072 | |
| 358 | Phosphorylation | SSENREGTLSDSTGS CCCCCCCCCCCCCCC | 20.52 | 20639409 | |
| 359 | Ubiquitination | SENREGTLSDSTGSE CCCCCCCCCCCCCCC | 8.66 | 33845483 | |
| 360 | Phosphorylation | ENREGTLSDSTGSEK CCCCCCCCCCCCCCC | 29.38 | 30576142 | |
| 362 | Phosphorylation | REGTLSDSTGSEKDD CCCCCCCCCCCCCCC | 31.15 | 20639409 | |
| 363 | Phosphorylation | EGTLSDSTGSEKDDL CCCCCCCCCCCCCCC | 50.12 | 20639409 | |
| 365 | Phosphorylation | TLSDSTGSEKDDLYP CCCCCCCCCCCCCCC | 41.37 | 20639409 | |
| 368 | Ubiquitination | DSTGSEKDDLYPNGS CCCCCCCCCCCCCCC | 47.28 | 29967540 | |
| 370 (in isoform 4) | Phosphorylation | - | 12.58 | 28152594 | |
| 372 (in isoform 4) | Phosphorylation | - | 46.10 | 28152594 | |
| 373 | N-linked_Glycosylation | EKDDLYPNGSGNGSA CCCCCCCCCCCCCCH | 43.64 | UniProtKB CARBOHYD | |
| 377 | N-linked_Glycosylation | LYPNGSGNGSAESSH CCCCCCCCCCHHHHH | 42.83 | UniProtKB CARBOHYD | |
| 417 | Ubiquitination | IAFVLEGKRSKVTRR EEEEECCCCCCCCCC | 44.09 | 33845483 | |
| 419 | Phosphorylation | FVLEGKRSKVTRRPK EEECCCCCCCCCCCC | 34.66 | 29514088 | |
| 426 | Ubiquitination | SKVTRRPKASDYQRL CCCCCCCCHHHHHHC | 59.73 | 29967540 | |
| 428 | Phosphorylation | VTRRPKASDYQRLDQ CCCCCCHHHHHHCCC | 42.87 | 28152594 | |
| 428 (in isoform 2) | Phosphorylation | - | 42.87 | 28152594 | |
| 430 | Phosphorylation | RRPKASDYQRLDQKY CCCCHHHHHHCCCEE | 7.95 | 28152594 | |
| 430 (in isoform 2) | Phosphorylation | - | 7.95 | 28152594 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 71 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| 221 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| 298 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| 302 | T | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| 351 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TGON2_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 TGON2_HUMAN !! | ||||||
| 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. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-98, AND MASSSPECTROMETRY. | |