| UniProt ID | UBX2B_HUMAN | |
|---|---|---|
| UniProt AC | Q14CS0 | |
| Protein Name | UBX domain-containing protein 2B | |
| Gene Name | UBXN2B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 331 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytosol . Endoplasmic reticulum . Golgi apparatus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to centrosome during mitotic prophase and metaphase. | |
| Protein Description | Adapter protein required for Golgi and endoplasmic reticulum biogenesis. [PubMed: 17141156 Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis] | |
| Protein Sequence | MAEGGGPEPGEQERRSSGPRPPSARDLQLALAELYEDEVKCKSSKSNRPKATVFKSPRTPPQRFYSSEHEYSGLNIVRPSTGKIVNELFKEAREHGAVPLNEATRASGDDKSKSFTGGGYRLGSSFCKRSEYIYGENQLQDVQILLKLWSNGFSLDDGELRPYNEPTNAQFLESVKRGEIPLELQRLVHGGQVNLDMEDHQDQEYIKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAVVLIDDSVPTTKIQIRLADGSRLIQRFNSTHRILDVRNFIVQSRPEFAALDFILVTSFPNKELTDESLTLLEADILNTVLLQQLK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAEGGGPEP ------CCCCCCCCC | 24.92 | 22814378 | |
| 16 | Phosphorylation | PGEQERRSSGPRPPS CCHHCCCCCCCCCCC | 45.96 | 20873877 | |
| 17 | Phosphorylation | GEQERRSSGPRPPSA CHHCCCCCCCCCCCH | 51.51 | 25159151 | |
| 23 | Phosphorylation | SSGPRPPSARDLQLA CCCCCCCCHHHHHHH | 38.32 | 24670416 | |
| 35 | Phosphorylation | QLALAELYEDEVKCK HHHHHHHHHCHHHCC | 16.91 | 28796482 | |
| 40 | Ubiquitination | ELYEDEVKCKSSKSN HHHHCHHHCCCCCCC | 33.62 | - | |
| 46 | Phosphorylation | VKCKSSKSNRPKATV HHCCCCCCCCCCCEE | 39.76 | - | |
| 50 | Ubiquitination | SSKSNRPKATVFKSP CCCCCCCCCEEECCC | 54.15 | - | |
| 52 | Phosphorylation | KSNRPKATVFKSPRT CCCCCCCEEECCCCC | 32.38 | 29449344 | |
| 55 | Ubiquitination | RPKATVFKSPRTPPQ CCCCEEECCCCCCCH | 56.04 | - | |
| 55 | Methylation | RPKATVFKSPRTPPQ CCCCEEECCCCCCCH | 56.04 | 115978971 | |
| 56 | Phosphorylation | PKATVFKSPRTPPQR CCCEEECCCCCCCHH | 14.24 | 25159151 | |
| 59 | Phosphorylation | TVFKSPRTPPQRFYS EEECCCCCCCHHCCC | 42.58 | 25159151 | |
| 65 | Phosphorylation | RTPPQRFYSSEHEYS CCCCHHCCCCCCCCC | 17.30 | 28450419 | |
| 66 | Phosphorylation | TPPQRFYSSEHEYSG CCCHHCCCCCCCCCC | 26.91 | 27273156 | |
| 67 | Phosphorylation | PPQRFYSSEHEYSGL CCHHCCCCCCCCCCC | 31.43 | 26657352 | |
| 71 | Phosphorylation | FYSSEHEYSGLNIVR CCCCCCCCCCCCEEC | 15.22 | 23927012 | |
| 72 | Phosphorylation | YSSEHEYSGLNIVRP CCCCCCCCCCCEECC | 33.54 | 28450419 | |
| 80 | Phosphorylation | GLNIVRPSTGKIVNE CCCEECCCCHHHHHH | 38.95 | 27251275 | |
| 81 | Phosphorylation | LNIVRPSTGKIVNEL CCEECCCCHHHHHHH | 45.22 | 27251275 | |
| 83 | Ubiquitination | IVRPSTGKIVNELFK EECCCCHHHHHHHHH | 43.50 | - | |
| 90 | Ubiquitination | KIVNELFKEAREHGA HHHHHHHHHHHHHCC | 64.19 | - | |
| 104 | Phosphorylation | AVPLNEATRASGDDK CEECCHHHHHCCCCC | 22.16 | 28555341 | |
| 107 | Phosphorylation | LNEATRASGDDKSKS CCHHHHHCCCCCCCC | 39.19 | - | |
| 112 | Phosphorylation | RASGDDKSKSFTGGG HHCCCCCCCCCCCCC | 40.29 | - | |
| 113 | Ubiquitination | ASGDDKSKSFTGGGY HCCCCCCCCCCCCCC | 56.16 | - | |
| 114 | Phosphorylation | SGDDKSKSFTGGGYR CCCCCCCCCCCCCCC | 34.82 | - | |
| 125 | Phosphorylation | GGYRLGSSFCKRSEY CCCCCCCCHHCCHHC | 32.63 | 27251275 | |
| 128 | Ubiquitination | RLGSSFCKRSEYIYG CCCCCHHCCHHCCCC | 57.88 | - | |
| 132 | Phosphorylation | SFCKRSEYIYGENQL CHHCCHHCCCCCCHH | 10.73 | 29978859 | |
| 134 | Phosphorylation | CKRSEYIYGENQLQD HCCHHCCCCCCHHHH | 19.93 | 29978859 | |
| 154 | Phosphorylation | KLWSNGFSLDDGELR HHHHCCCCCCCCCCC | 32.08 | 28348404 | |
| 163 | Phosphorylation | DDGELRPYNEPTNAQ CCCCCCCCCCCCCHH | 26.23 | 28348404 | |
| 167 | Phosphorylation | LRPYNEPTNAQFLES CCCCCCCCCHHHHHH | 36.69 | 28348404 | |
| 176 | Ubiquitination | AQFLESVKRGEIPLE HHHHHHHHCCCCCHH | 65.06 | 21906983 | |
| 205 | Phosphorylation | EDHQDQEYIKPRLRF CCCCCHHHCCCCEEE | 14.49 | 29978859 | |
| 207 | Ubiquitination | HQDQEYIKPRLRFKA CCCHHHCCCCEEEEE | 24.15 | - | |
| 213 | Ubiquitination | IKPRLRFKAFSGEGQ CCCCEEEEEECCCCC | 41.93 | - | |
| 216 | Phosphorylation | RLRFKAFSGEGQKLG CEEEEEECCCCCCCC | 40.57 | 29978859 | |
| 221 | Ubiquitination | AFSGEGQKLGSLTPE EECCCCCCCCCCCCC | 66.72 | - | |
| 224 | Phosphorylation | GEGQKLGSLTPEIVS CCCCCCCCCCCCHHC | 39.23 | 30278072 | |
| 226 | Phosphorylation | GQKLGSLTPEIVSTP CCCCCCCCCCHHCCC | 22.14 | 30278072 | |
| 231 | Phosphorylation | SLTPEIVSTPSSPEE CCCCCHHCCCCCHHH | 40.02 | 30278072 | |
| 232 | Phosphorylation | LTPEIVSTPSSPEEE CCCCHHCCCCCHHHH | 19.12 | 30278072 | |
| 234 | Phosphorylation | PEIVSTPSSPEEEDK CCHHCCCCCHHHHCC | 59.62 | 29255136 | |
| 235 | Phosphorylation | EIVSTPSSPEEEDKS CHHCCCCCHHHHCCH | 37.22 | 29255136 | |
| 242 | Phosphorylation | SPEEEDKSILNAVVL CHHHHCCHHHEEEEE | 44.63 | 26657352 | |
| 276 | Phosphorylation | LIQRFNSTHRILDVR HHHHHHCCCCEEHHH | 19.11 | 24719451 | |
| 302 | Phosphorylation | ALDFILVTSFPNKEL CCCEEEEECCCCCCC | 22.62 | 28450419 | |
| 303 | Phosphorylation | LDFILVTSFPNKELT CCEEEEECCCCCCCC | 31.09 | 28450419 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBX2B_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 UBX2B_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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-235, ANDMASS SPECTROMETRY. | |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232; SER-234 ANDSER-235, AND MASS SPECTROMETRY. | |
| "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-56 AND THR-59, AND MASSSPECTROMETRY. | |