| UniProt ID | UGDH_HUMAN | |
|---|---|---|
| UniProt AC | O60701 | |
| Protein Name | UDP-glucose 6-dehydrogenase | |
| Gene Name | UGDH | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 494 | |
| Subcellular Localization | ||
| Protein Description | Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.. | |
| Protein Sequence | MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV | |
| 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 |
|---|---|---|---|---|---|
| 6 | Malonylation | --MFEIKKICCIGAG --CCCCEEEEEECCC | 46.79 | 26320211 | |
| 10 | Ubiquitination | EIKKICCIGAGYVGG CCEEEEEECCCCCCC | 3.53 | 23000965 | |
| 10 | Acetylation | EIKKICCIGAGYVGG CCEEEEEECCCCCCC | 3.53 | 19608861 | |
| 27 | Ubiquitination | CSVIAHMCPEIRVTV HHHHHHHCCCCEEEE | 1.64 | 33845483 | |
| 32 | Ubiquitination | HMCPEIRVTVVDVNE HHCCCCEEEEEECCH | 6.14 | 33845483 | |
| 40 | Phosphorylation | TVVDVNESRINAWNS EEEECCHHHCCCCCC | 33.00 | 21712546 | |
| 47 | Phosphorylation | SRINAWNSPTLPIYE HHCCCCCCCCCCCCC | 14.46 | 22199227 | |
| 49 | Phosphorylation | INAWNSPTLPIYEPG CCCCCCCCCCCCCCC | 45.01 | 22199227 | |
| 52 | Ubiquitination | WNSPTLPIYEPGLKE CCCCCCCCCCCCHHH | 7.37 | 22817900 | |
| 53 | Phosphorylation | NSPTLPIYEPGLKEV CCCCCCCCCCCHHHH | 17.71 | 27259358 | |
| 63 | O-linked_Glycosylation | GLKEVVESCRGKNLF CHHHHHHHCCCCCCE | 9.48 | 26853435 | |
| 67 | Ubiquitination | VVESCRGKNLFFSTN HHHHCCCCCCEEECC | 31.00 | 33845483 | |
| 67 | 2-Hydroxyisobutyrylation | VVESCRGKNLFFSTN HHHHCCCCCCEEECC | 31.00 | - | |
| 73 | Ubiquitination | GKNLFFSTNIDDAIK CCCCEEECCHHHHHH | 30.91 | 33845483 | |
| 76 | Ubiquitination | LFFSTNIDDAIKEAD CEEECCHHHHHHHCC | 41.16 | 33845483 | |
| 76 | Acetylation | LFFSTNIDDAIKEAD CEEECCHHHHHHHCC | 41.16 | 19608861 | |
| 80 | Ubiquitination | TNIDDAIKEADLVFI CCHHHHHHHCCEEEE | 48.87 | 22817900 | |
| 88 | Phosphorylation | EADLVFISVNTPTKT HCCEEEEECCCCCCC | 9.61 | 23663014 | |
| 91 | Phosphorylation | LVFISVNTPTKTYGM EEEEECCCCCCCCCC | 30.13 | 30266825 | |
| 93 | Phosphorylation | FISVNTPTKTYGMGK EEECCCCCCCCCCCC | 33.70 | 23663014 | |
| 93 | Ubiquitination | FISVNTPTKTYGMGK EEECCCCCCCCCCCC | 33.70 | 22817900 | |
| 94 | Ubiquitination | ISVNTPTKTYGMGKG EECCCCCCCCCCCCC | 40.74 | 33845483 | |
| 95 | Phosphorylation | SVNTPTKTYGMGKGR ECCCCCCCCCCCCCC | 27.99 | 23532336 | |
| 96 | Phosphorylation | VNTPTKTYGMGKGRA CCCCCCCCCCCCCCH | 13.48 | 23532336 | |
| 100 | Ubiquitination | TKTYGMGKGRAADLK CCCCCCCCCCHHHHH | 36.01 | 29967540 | |
| 100 | 2-Hydroxyisobutyrylation | TKTYGMGKGRAADLK CCCCCCCCCCHHHHH | 36.01 | - | |
| 103 | Ubiquitination | YGMGKGRAADLKYIE CCCCCCCHHHHHHHH | 17.62 | 22817900 | |
| 106 | Ubiquitination | GKGRAADLKYIEACA CCCCHHHHHHHHHHH | 3.78 | 33845483 | |
| 106 | Acetylation | GKGRAADLKYIEACA CCCCHHHHHHHHHHH | 3.78 | 19608861 | |
| 107 | Acetylation | KGRAADLKYIEACAR CCCHHHHHHHHHHHH | 44.74 | 19608861 | |
| 107 | Ubiquitination | KGRAADLKYIEACAR CCCHHHHHHHHHHHH | 44.74 | 23000965 | |
| 107 | 2-Hydroxyisobutyrylation | KGRAADLKYIEACAR CCCHHHHHHHHHHHH | 44.74 | - | |
| 107 | Malonylation | KGRAADLKYIEACAR CCCHHHHHHHHHHHH | 44.74 | 32601280 | |
| 108 | Phosphorylation | GRAADLKYIEACARR CCHHHHHHHHHHHHH | 15.99 | - | |
| 110 | Ubiquitination | AADLKYIEACARRIV HHHHHHHHHHHHHHH | 34.31 | 29967540 | |
| 120 | Ubiquitination | ARRIVQNSNGYKIVT HHHHHHCCCCCEEEE | 17.97 | 23000965 | |
| 124 | Ubiquitination | VQNSNGYKIVTEKST HHCCCCCEEEECCCC | 31.90 | 33845483 | |
| 129 | Ubiquitination | GYKIVTEKSTVPVRA CCEEEECCCCCCHHH | 41.90 | 33845483 | |
| 129 | 2-Hydroxyisobutyrylation | GYKIVTEKSTVPVRA CCEEEECCCCCCHHH | 41.90 | - | |
| 130 | Phosphorylation | YKIVTEKSTVPVRAA CEEEECCCCCCHHHH | 28.53 | 23403867 | |
| 131 | Phosphorylation | KIVTEKSTVPVRAAE EEEECCCCCCHHHHH | 39.64 | 23403867 | |
| 140 | Ubiquitination | PVRAAESIRRIFDAN CHHHHHHHHHHHCCC | 2.30 | 29967540 | |
| 142 | Ubiquitination | RAAESIRRIFDANTK HHHHHHHHHHCCCCC | 32.05 | 27667366 | |
| 149 | Ubiquitination | RIFDANTKPNLNLQV HHHCCCCCCCCCEEE | 31.54 | 22817900 | |
| 162 | Ubiquitination | QVLSNPEFLAEGTAI EECCCHHHHHCCCCH | 9.15 | 22817900 | |
| 167 | Ubiquitination | PEFLAEGTAIKDLKN HHHHHCCCCHHCCCC | 19.40 | 33845483 | |
| 170 | Ubiquitination | LAEGTAIKDLKNPDR HHCCCCHHCCCCCCC | 55.32 | 33845483 | |
| 173 | Acetylation | GTAIKDLKNPDRVLI CCCHHCCCCCCCEEE | 76.26 | 19608861 | |
| 173 | Ubiquitination | GTAIKDLKNPDRVLI CCCHHCCCCCCCEEE | 76.26 | 22817900 | |
| 173 | 2-Hydroxyisobutyrylation | GTAIKDLKNPDRVLI CCCHHCCCCCCCEEE | 76.26 | - | |
| 183 | Ubiquitination | DRVLIGGDETPEGQR CCEEECCCCCHHHHH | 51.92 | 22817900 | |
| 185 | Phosphorylation | VLIGGDETPEGQRAV EEECCCCCHHHHHHH | 31.23 | 21815630 | |
| 186 | Ubiquitination | LIGGDETPEGQRAVQ EECCCCCHHHHHHHH | 41.49 | 22817900 | |
| 197 | Ubiquitination | RAVQALCAVYEHWVP HHHHHHHHHHHHCCC | 14.05 | 33845483 | |
| 199 | Phosphorylation | VQALCAVYEHWVPRE HHHHHHHHHHCCCHH | 5.42 | 27642862 | |
| 200 | Ubiquitination | QALCAVYEHWVPREK HHHHHHHHHCCCHHH | 25.36 | 33845483 | |
| 207 | Ubiquitination | EHWVPREKILTTNTW HHCCCHHHCCCCCCC | 44.27 | 29967540 | |
| 207 | 2-Hydroxyisobutyrylation | EHWVPREKILTTNTW HHCCCHHHCCCCCCC | 44.27 | - | |
| 232 | Ubiquitination | AFLAQRISSINSISA HHHHHHHHHHHHHHH | 27.62 | 33845483 | |
| 233 | Ubiquitination | FLAQRISSINSISAL HHHHHHHHHHHHHHH | 24.34 | 33845483 | |
| 242 | Ubiquitination | NSISALCEATGADVE HHHHHHHHHHCCCHH | 50.55 | 33845483 | |
| 257 | Sulfoxidation | EVATAIGMDQRIGNK HHHHHHCCCHHHCCH | 3.03 | 30846556 | |
| 262 | Ubiquitination | IGMDQRIGNKFLKAS HCCCHHHCCHHHHHH | 33.20 | 33845483 | |
| 263 | Ubiquitination | GMDQRIGNKFLKASV CCCHHHCCHHHHHHC | 29.54 | 33845483 | |
| 264 | Ubiquitination | MDQRIGNKFLKASVG CCHHHCCHHHHHHCC | 47.03 | 33845483 | |
| 267 | Ubiquitination | RIGNKFLKASVGFGG HHCCHHHHHHCCCCC | 41.57 | 33845483 | |
| 269 | Phosphorylation | GNKFLKASVGFGGSC CCHHHHHHCCCCCCH | 22.61 | 20860994 | |
| 272 | Ubiquitination | FLKASVGFGGSCFQK HHHHHCCCCCCHHHH | 10.57 | 33845483 | |
| 273 | Ubiquitination | LKASVGFGGSCFQKD HHHHCCCCCCHHHHH | 22.60 | 29967540 | |
| 275 | Phosphorylation | ASVGFGGSCFQKDVL HHCCCCCCHHHHHHH | 16.49 | 25159151 | |
| 286 | Phosphorylation | KDVLNLVYLCEALNL HHHHHHHHHHHHCCH | 14.59 | - | |
| 303 | Ubiquitination | VARYWQQVIDMNDYQ HHHHHHHHCCCCHHH | 2.10 | 29967540 | |
| 309 | Phosphorylation | QVIDMNDYQRRRFAS HHCCCCHHHHHHHHH | 10.02 | 27259358 | |
| 316 | Phosphorylation | YQRRRFASRIIDSLF HHHHHHHHHHHHHHH | 22.69 | - | |
| 321 | Phosphorylation | FASRIIDSLFNTVTD HHHHHHHHHHHHCCC | 25.18 | - | |
| 327 | Phosphorylation | DSLFNTVTDKKIAIL HHHHHHCCCCEEEEE | 39.81 | - | |
| 329 | Ubiquitination | LFNTVTDKKIAILGF HHHHCCCCEEEEEEE | 36.39 | 33845483 | |
| 329 | 2-Hydroxyisobutyrylation | LFNTVTDKKIAILGF HHHHCCCCEEEEEEE | 36.39 | - | |
| 330 | Ubiquitination | FNTVTDKKIAILGFA HHHCCCCEEEEEEEE | 39.93 | 33845483 | |
| 330 | 2-Hydroxyisobutyrylation | FNTVTDKKIAILGFA HHHCCCCEEEEEEEE | 39.93 | - | |
| 333 | Ubiquitination | VTDKKIAILGFAFKK CCCCEEEEEEEEEEC | 4.38 | 29967540 | |
| 337 | Ubiquitination | KIAILGFAFKKDTGD EEEEEEEEEECCCCC | 17.35 | 33845483 | |
| 337 | Acetylation | KIAILGFAFKKDTGD EEEEEEEEEECCCCC | 17.35 | 19608861 | |
| 339 | Acetylation | AILGFAFKKDTGDTR EEEEEEEECCCCCCC | 46.43 | 19809299 | |
| 339 | Ubiquitination | AILGFAFKKDTGDTR EEEEEEEECCCCCCC | 46.43 | 33845483 | |
| 339 | 2-Hydroxyisobutyrylation | AILGFAFKKDTGDTR EEEEEEEECCCCCCC | 46.43 | - | |
| 348 | Phosphorylation | DTGDTRESSSIYISK CCCCCCCCCEEEEEE | 26.54 | 21406692 | |
| 349 | Phosphorylation | TGDTRESSSIYISKY CCCCCCCCEEEEEEE | 18.92 | 21406692 | |
| 350 | Phosphorylation | GDTRESSSIYISKYL CCCCCCCEEEEEEEE | 28.79 | 21406692 | |
| 352 | Phosphorylation | TRESSSIYISKYLMD CCCCCEEEEEEEECC | 10.90 | 28152594 | |
| 354 | Phosphorylation | ESSSIYISKYLMDEG CCCEEEEEEEECCCC | 9.77 | 28152594 | |
| 363 | Ubiquitination | YLMDEGAHLHIYDPK EECCCCCCEEECCCC | 28.88 | 29967540 | |
| 367 | Ubiquitination | EGAHLHIYDPKVPRE CCCCEEECCCCCCHH | 18.55 | 33845483 | |
| 367 | Acetylation | EGAHLHIYDPKVPRE CCCCEEECCCCCCHH | 18.55 | 19608861 | |
| 370 | Ubiquitination | HLHIYDPKVPREQIV CEEECCCCCCHHHEE | 63.07 | 29967540 | |
| 370 | 2-Hydroxyisobutyrylation | HLHIYDPKVPREQIV CEEECCCCCCHHHEE | 63.07 | - | |
| 379 | Phosphorylation | PREQIVVDLSHPGVS CHHHEEEECCCCCCC | 31.40 | 32142685 | |
| 384 | Ubiquitination | VVDLSHPGVSEDDQV EEECCCCCCCCCCCE | 30.11 | 33845483 | |
| 386 | Phosphorylation | DLSHPGVSEDDQVSR ECCCCCCCCCCCEEE | 41.02 | 27251275 | |
| 393 | Ubiquitination | SEDDQVSRLVTISKD CCCCCEEEEEEEECC | 34.03 | 33845483 | |
| 394 | Ubiquitination | EDDQVSRLVTISKDP CCCCEEEEEEEECCH | 2.87 | 29967540 | |
| 397 | Ubiquitination | QVSRLVTISKDPYEA CEEEEEEEECCHHHH | 3.62 | 33845483 | |
| 409 | Phosphorylation | YEACDGAHAVVICTE HHHCCCCCEEEEECC | 25.28 | 32142685 | |
| 414 | Ubiquitination | GAHAVVICTEWDMFK CCCEEEEECCHHHHH | 1.58 | 33845483 | |
| 419 | Sulfoxidation | VICTEWDMFKELDYE EEECCHHHHHHCCHH | 5.61 | 30846556 | |
| 423 | Ubiquitination | EWDMFKELDYERIHK CHHHHHHCCHHHHHH | 9.78 | 33845483 | |
| 424 | Ubiquitination | WDMFKELDYERIHKK HHHHHHCCHHHHHHH | 44.32 | 29967540 | |
| 430 | Ubiquitination | LDYERIHKKMLKPAF CCHHHHHHHHCCCEE | 37.19 | 29967540 | |
| 431 | Malonylation | DYERIHKKMLKPAFI CHHHHHHHHCCCEEE | 34.99 | 26320211 | |
| 434 | Acetylation | RIHKKMLKPAFIFDG HHHHHHCCCEEEECC | 30.70 | 19608861 | |
| 434 | Ubiquitination | RIHKKMLKPAFIFDG HHHHHHCCCEEEECC | 30.70 | 33845483 | |
| 461 | Phosphorylation | TIGFQIETIGKKVSS HHCEEEEECCCEECC | 36.34 | 22817900 | |
| 464 | Ubiquitination | FQIETIGKKVSSKRI EEEEECCCEECCCCC | 46.26 | 33845483 | |
| 473 | Phosphorylation | VSSKRIPYAPSGEIP ECCCCCCCCCCCCCC | 28.86 | 28152594 | |
| 476 | Phosphorylation | KRIPYAPSGEIPKFS CCCCCCCCCCCCCCC | 40.67 | 22617229 | |
| 481 | Ubiquitination | APSGEIPKFSLQDPP CCCCCCCCCCCCCCC | 53.93 | 33845483 | |
| 483 | Phosphorylation | SGEIPKFSLQDPPNK CCCCCCCCCCCCCCC | 31.11 | 28555341 | |
| 490 | Acetylation | SLQDPPNKKPKV--- CCCCCCCCCCCC--- | 75.99 | 25953088 | |
| 490 | Ubiquitination | SLQDPPNKKPKV--- CCCCCCCCCCCC--- | 75.99 | 33845483 | |
| 491 | Ubiquitination | LQDPPNKKPKV---- CCCCCCCCCCC---- | 57.63 | 29967540 | |
| 491 | Malonylation | LQDPPNKKPKV---- CCCCCCCCCCC---- | 57.63 | 26320211 | |
| 491 | Acetylation | LQDPPNKKPKV---- CCCCCCCCCCC---- | 57.63 | 25953088 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 461 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UGDH_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 UGDH_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| KAD5_HUMAN | AK5 | physical | 16169070 | |
| UD11_HUMAN | UGT1A1 | physical | 21988832 | |
| METK2_HUMAN | MAT2A | physical | 22863883 | |
| MAOX_HUMAN | ME1 | physical | 22863883 | |
| RNH2A_HUMAN | RNASEH2A | physical | 22863883 | |
| SNX1_HUMAN | SNX1 | physical | 22863883 | |
| UGDH_HUMAN | UGDH | physical | 25416956 | |
| TPPC4_HUMAN | TRAPPC4 | physical | 26344197 |
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107; LYS-173 AND LYS-434,AND MASS SPECTROMETRY. | |