| UniProt ID | TBA1B_MOUSE | |
|---|---|---|
| UniProt AC | P05213 | |
| Protein Name | Tubulin alpha-1B chain | |
| Gene Name | Tuba1b | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 451 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. | |
| Protein Description | Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.. | |
| Protein Sequence | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY | |
| 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 | Phosphorylation | --MRECISIHVGQAG --CCCEEEEEECCHH | 20.50 | 15345747 | |
| 40 | Acetylation | DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC | 46.51 | 2736326 | |
| 40 | Ubiquitination | DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC | 46.51 | - | |
| 40 | Methylation | DGQMPSDKTIGGGDD CCCCCCCCCCCCCCC | 46.51 | 12692561 | |
| 41 | Phosphorylation | GQMPSDKTIGGGDDS CCCCCCCCCCCCCCC | 29.82 | 25521595 | |
| 48 | Phosphorylation | TIGGGDDSFNTFFSE CCCCCCCCHHHCCCC | 25.74 | 25521595 | |
| 51 | Phosphorylation | GGDDSFNTFFSETGA CCCCCHHHCCCCCCC | 24.85 | 24925903 | |
| 54 | Phosphorylation | DSFNTFFSETGAGKH CCHHHCCCCCCCCCC | 30.02 | 25521595 | |
| 56 | Phosphorylation | FNTFFSETGAGKHVP HHHCCCCCCCCCCCC | 31.00 | 25159016 | |
| 60 | Acetylation | FSETGAGKHVPRAVF CCCCCCCCCCCEEEE | 40.68 | 19850273 | |
| 60 | Ubiquitination | FSETGAGKHVPRAVF CCCCCCCCCCCEEEE | 40.68 | - | |
| 73 | Phosphorylation | VFVDLEPTVIDEVRT EEECCCCEEEHHCCC | 22.25 | 22817900 | |
| 80 | Phosphorylation | TVIDEVRTGTYRQLF EEEHHCCCCCCHHCC | 38.77 | 22006019 | |
| 82 | Phosphorylation | IDEVRTGTYRQLFHP EHHCCCCCCHHCCCH | 18.21 | 26060331 | |
| 83 | Phosphorylation | DEVRTGTYRQLFHPE HHCCCCCCHHCCCHH | 9.56 | 26060331 | |
| 94 | Phosphorylation | FHPEQLITGKEDAAN CCHHHHCCCCHHHHH | 51.28 | 27600695 | |
| 96 | Ubiquitination | PEQLITGKEDAANNY HHHHCCCCHHHHHHC | 43.71 | 27667366 | |
| 96 | Acetylation | PEQLITGKEDAANNY HHHHCCCCHHHHHHC | 43.71 | 23201123 | |
| 103 | Phosphorylation | KEDAANNYARGHYTI CHHHHHHCCCCCCCC | 9.48 | 22817900 | |
| 108 | Phosphorylation | NNYARGHYTIGKEII HHCCCCCCCCCHHHH | 11.68 | 25195567 | |
| 109 | Phosphorylation | NYARGHYTIGKEIID HCCCCCCCCCHHHHH | 19.99 | 26824392 | |
| 112 | Ubiquitination | RGHYTIGKEIIDLVL CCCCCCCHHHHHHHH | 41.72 | - | |
| 124 | Acetylation | LVLDRIRKLADQCTG HHHHHHHHHHHHCCC | 45.73 | 156237 | |
| 140 | Ubiquitination | QGFLVFHSFGGGTGS CCEEEEEECCCCCCC | 17.70 | 27667366 | |
| 158 | Phosphorylation | SLLMERLSVDYGKKS HHHHHHHCCCCCCCC | 21.11 | 27180971 | |
| 161 | Phosphorylation | MERLSVDYGKKSKLE HHHHCCCCCCCCCEE | 28.79 | 29472430 | |
| 163 | Acetylation | RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE | 47.87 | 129189 | |
| 163 | Ubiquitination | RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE | 47.87 | 27667366 | |
| 163 | Succinylation | RLSVDYGKKSKLEFS HHCCCCCCCCCEEEE | 47.87 | 23954790 | |
| 164 | Ubiquitination | LSVDYGKKSKLEFSI HCCCCCCCCCEEEEE | 48.75 | 27667366 | |
| 165 | Phosphorylation | SVDYGKKSKLEFSIY CCCCCCCCCEEEEEE | 46.06 | - | |
| 166 | Ubiquitination | VDYGKKSKLEFSIYP CCCCCCCCEEEEEEE | 62.00 | - | |
| 207 | Ubiquitination | CAFMVDNEAIYDICR EEEEECHHHHHHHHH | 31.79 | 27667366 | |
| 208 | Ubiquitination | AFMVDNEAIYDICRR EEEECHHHHHHHHHC | 16.34 | 27667366 | |
| 210 | Phosphorylation | MVDNEAIYDICRRNL EECHHHHHHHHHCCC | 13.30 | 22817900 | |
| 223 | Phosphorylation | NLDIERPTYTNLNRL CCCCCCCCHHCHHHH | 49.55 | 22817900 | |
| 224 | Phosphorylation | LDIERPTYTNLNRLI CCCCCCCHHCHHHHH | 9.05 | 22817900 | |
| 225 | Phosphorylation | DIERPTYTNLNRLIS CCCCCCHHCHHHHHH | 35.39 | 22817900 | |
| 232 | Phosphorylation | TNLNRLISQIVSSIT HCHHHHHHHHHHHHH | 20.60 | 26824392 | |
| 236 | Phosphorylation | RLISQIVSSITASLR HHHHHHHHHHHHHCC | 20.04 | 23984901 | |
| 237 | Phosphorylation | LISQIVSSITASLRF HHHHHHHHHHHHCCC | 17.05 | 23984901 | |
| 271 | Phosphorylation | RIHFPLATYAPVISA CCCCCCCCCCCCCCH | 28.09 | 25159016 | |
| 272 | Phosphorylation | IHFPLATYAPVISAE CCCCCCCCCCCCCHH | 11.87 | 25159016 | |
| 277 | Phosphorylation | ATYAPVISAEKAYHE CCCCCCCCHHHHHHH | 30.52 | 25159016 | |
| 277 | O-linked_Glycosylation | ATYAPVISAEKAYHE CCCCCCCCHHHHHHH | 30.52 | 20547045 | |
| 280 | Ubiquitination | APVISAEKAYHEQLS CCCCCHHHHHHHHCC | 54.70 | - | |
| 282 | Nitrated tyrosine | VISAEKAYHEQLSVA CCCHHHHHHHHCCHH | 19.56 | - | |
| 282 | Phosphorylation | VISAEKAYHEQLSVA CCCHHHHHHHHCCHH | 19.56 | 26745281 | |
| 282 | Nitration | VISAEKAYHEQLSVA CCCHHHHHHHHCCHH | 19.56 | - | |
| 287 | Phosphorylation | KAYHEQLSVAEITNA HHHHHHCCHHHHHHH | 20.98 | 25521595 | |
| 292 | Phosphorylation | QLSVAEITNACFEPA HCCHHHHHHHHCCCH | 14.31 | 23984901 | |
| 295 | S-nitrosocysteine | VAEITNACFEPANQM HHHHHHHHCCCHHHC | 4.27 | - | |
| 295 | S-nitrosylation | VAEITNACFEPANQM HHHHHHHHCCCHHHC | 4.27 | 19101475 | |
| 304 | Ubiquitination | EPANQMVKCDPRHGK CCHHHCCCCCCCCCC | 27.81 | - | |
| 311 | Ubiquitination | KCDPRHGKYMACCLL CCCCCCCCEEEEHHH | 26.23 | - | |
| 315 | S-nitrosocysteine | RHGKYMACCLLYRGD CCCCEEEEHHHCCCC | 0.67 | - | |
| 315 | S-nitrosylation | RHGKYMACCLLYRGD CCCCEEEEHHHCCCC | 0.67 | 20925432 | |
| 316 | S-nitrosocysteine | HGKYMACCLLYRGDV CCCEEEEHHHCCCCC | 1.81 | - | |
| 316 | S-nitrosylation | HGKYMACCLLYRGDV CCCEEEEHHHCCCCC | 1.81 | 24926564 | |
| 319 | Phosphorylation | YMACCLLYRGDVVPK EEEEHHHCCCCCCCC | 10.29 | 22817900 | |
| 326 | Ubiquitination | YRGDVVPKDVNAAIA CCCCCCCCCHHHHHH | 63.80 | 27667366 | |
| 326 | Acetylation | YRGDVVPKDVNAAIA CCCCCCCCCHHHHHH | 63.80 | 23201123 | |
| 334 | Phosphorylation | DVNAAIATIKTKRSI CHHHHHHHCCCCCEE | 19.52 | 26824392 | |
| 336 | Ubiquitination | NAAIATIKTKRSIQF HHHHHHCCCCCEEEE | 43.57 | 27667366 | |
| 337 | Phosphorylation | AAIATIKTKRSIQFV HHHHHCCCCCEEEEE | 28.04 | 26745281 | |
| 338 | Ubiquitination | AIATIKTKRSIQFVD HHHHCCCCCEEEEEE | 38.86 | - | |
| 339 | Methylation | IATIKTKRSIQFVDW HHHCCCCCEEEEEEE | 44.20 | - | |
| 340 | Phosphorylation | ATIKTKRSIQFVDWC HHCCCCCEEEEEEEC | 23.46 | 25521595 | |
| 347 | S-nitrosocysteine | SIQFVDWCPTGFKVG EEEEEEECCCCEEEE | 1.55 | - | |
| 347 | Glutathionylation | SIQFVDWCPTGFKVG EEEEEEECCCCEEEE | 1.55 | 24333276 | |
| 347 | S-nitrosylation | SIQFVDWCPTGFKVG EEEEEEECCCCEEEE | 1.55 | 22588120 | |
| 347 | S-palmitoylation | SIQFVDWCPTGFKVG EEEEEEECCCCEEEE | 1.55 | 28526873 | |
| 349 | Phosphorylation | QFVDWCPTGFKVGIN EEEEECCCCEEEEEE | 52.71 | 25159016 | |
| 352 | Acetylation | DWCPTGFKVGINYQP EECCCCEEEEEECCC | 40.68 | 69933 | |
| 352 | Ubiquitination | DWCPTGFKVGINYQP EECCCCEEEEEECCC | 40.68 | - | |
| 357 | Phosphorylation | GFKVGINYQPPTVVP CEEEEEECCCCEECC | 22.07 | 25521595 | |
| 361 | Phosphorylation | GINYQPPTVVPGGDL EEECCCCEECCCCCH | 40.60 | 25159016 | |
| 370 | Ubiquitination | VPGGDLAKVQRAVCM CCCCCHHHHHHHHHH | 46.31 | 27667366 | |
| 376 | S-nitrosocysteine | AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH | 1.90 | - | |
| 376 | S-nitrosylation | AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH | 1.90 | 20925432 | |
| 376 | S-palmitoylation | AKVQRAVCMLSNTTA HHHHHHHHHHCCHHH | 1.90 | 28526873 | |
| 379 | Phosphorylation | QRAVCMLSNTTAIAE HHHHHHHCCHHHHHH | 12.78 | 22817900 | |
| 380 | Ubiquitination | RAVCMLSNTTAIAEA HHHHHHCCHHHHHHH | 37.17 | 27667366 | |
| 381 | Phosphorylation | AVCMLSNTTAIAEAW HHHHHCCHHHHHHHH | 17.77 | 23984901 | |
| 382 | Phosphorylation | VCMLSNTTAIAEAWA HHHHCCHHHHHHHHH | 21.95 | 23984901 | |
| 394 | Ubiquitination | AWARLDHKFDLMYAK HHHHCCCCCCHHHEE | 39.99 | 27667366 | |
| 394 | Succinylation | AWARLDHKFDLMYAK HHHHCCCCCCHHHEE | 39.99 | 23954790 | |
| 399 | Phosphorylation | DHKFDLMYAKRAFVH CCCCCHHHEEEHHHH | 19.10 | 26745281 | |
| 401 | Acetylation | KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH | 27.11 | 129185 | |
| 401 | Ubiquitination | KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH | 27.11 | 27667366 | |
| 401 | Succinylation | KFDLMYAKRAFVHWY CCCHHHEEEHHHHHH | 27.11 | 23954790 | |
| 408 | Phosphorylation | KRAFVHWYVGEGMEE EEHHHHHHCCCCCCC | 5.45 | 25777480 | |
| 414 | Ubiquitination | WYVGEGMEEGEFSEA HHCCCCCCCCCHHHH | 73.95 | 27667366 | |
| 419 | Phosphorylation | GMEEGEFSEAREDMA CCCCCCHHHHHHHHH | 26.50 | 22817900 | |
| 432 | Phosphorylation | MAALEKDYEEVGVDS HHHHHHCHHHHCCCC | 25.67 | 25619855 | |
| 438 | Ubiquitination | DYEEVGVDSVEGEGE CHHHHCCCCCCCCCC | 40.82 | 27667366 | |
| 439 | Phosphorylation | YEEVGVDSVEGEGEE HHHHCCCCCCCCCCC | 21.47 | 25521595 | |
| 445 | 5-glutamyl polyglutamate | DSVEGEGEEEGEEY- CCCCCCCCCCCCCC- | 48.88 | - | |
| 445 | Ubiquitination | DSVEGEGEEEGEEY- CCCCCCCCCCCCCC- | 48.88 | 27667366 | |
| 445 | Formation of an isopeptide bond | DSVEGEGEEEGEEY- CCCCCCCCCCCCCC- | 48.88 | 1967194 | |
| 451 | Phosphorylation | GEEEGEEY------- CCCCCCCC------- | 21.39 | 25619855 | |
| 451 | Nitration | GEEEGEEY------- CCCCCCCC------- | 21.39 | - |
| 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 TBA1B_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 40 | K | Acetylation |
| 19564401 |
| 40 | K | Methylation |
| - |
* 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 TBA1B_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DNJA1_HUMAN | DNAJA1 | physical | 20360068 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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