UniProt ID | TXND5_HUMAN | |
---|---|---|
UniProt AC | Q8NBS9 | |
Protein Name | Thioredoxin domain-containing protein 5 | |
Gene Name | TXNDC5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 432 | |
Subcellular Localization | Endoplasmic reticulum lumen . | |
Protein Description | Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity).. | |
Protein Sequence | MPARPGRLLPLLARPAALTALLLLLLGHGGGGRWGARAQEAAAAAADGPPAADGEDGQDPHSKHLYTADMFTHGIQSAAHFVMFFAPWCGHCQRLQPTWNDLGDKYNSMEDAKVYVAKVDCTAHSDVCSAQGVRGYPTLKLFKPGQEAVKYQGPRDFQTLENWMLQTLNEEPVTPEPEVEPPSAPELKQGLYELSASNFELHVAQGDHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYELCSGNQVRGYPTLLWFRDGKKVDQYKGKRDLESLREYVESQLQRTETGATETVTPSEAPVLAAEPEADKGTVLALTENNFDDTIAEGITFIKFYAPWCGHCKTLAPTWEELSKKEFPGLAGVKIAEVDCTAERNICSKYSVRGYPTLLLFRGGKKVSEHSGGRDLDSLHRFVLSQAKDEL | |
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 |
---|---|---|---|---|---|
42 | Ubiquitination | GARAQEAAAAAADGP HHHHHHHHHHHCCCC | 9.25 | 21890473 | |
72 | O-linked_Glycosylation | LYTADMFTHGIQSAA EEHHHHHHHHHHHHH | 16.74 | 55828619 | |
98 | Phosphorylation | HCQRLQPTWNDLGDK HHHHHCCCHHHHHHH | 24.76 | 24275569 | |
105 | Acetylation | TWNDLGDKYNSMEDA CHHHHHHHHCCHHHC | 44.53 | 26051181 | |
106 | Phosphorylation | WNDLGDKYNSMEDAK HHHHHHHHCCHHHCE | 19.74 | 24275569 | |
108 | Phosphorylation | DLGDKYNSMEDAKVY HHHHHHCCHHHCEEE | 22.06 | 24275569 | |
109 | Sulfoxidation | LGDKYNSMEDAKVYV HHHHHCCHHHCEEEE | 4.87 | 30846556 | |
113 | Acetylation | YNSMEDAKVYVAKVD HCCHHHCEEEEEEEE | 46.55 | 27452117 | |
113 | Ubiquitination | YNSMEDAKVYVAKVD HCCHHHCEEEEEEEE | 46.55 | 21890473 | |
113 | 2-Hydroxyisobutyrylation | YNSMEDAKVYVAKVD HCCHHHCEEEEEEEE | 46.55 | - | |
115 | Phosphorylation | SMEDAKVYVAKVDCT CHHHCEEEEEEEECC | 8.25 | 20068231 | |
118 | Acetylation | DAKVYVAKVDCTAHS HCEEEEEEEECCCCC | 28.67 | 25953088 | |
118 | Ubiquitination | DAKVYVAKVDCTAHS HCEEEEEEEECCCCC | 28.67 | 21890473 | |
122 | Phosphorylation | YVAKVDCTAHSDVCS EEEEEECCCCCHHHH | 23.96 | - | |
125 | Phosphorylation | KVDCTAHSDVCSAQG EEECCCCCHHHHCCC | 29.31 | 27251275 | |
129 | Phosphorylation | TAHSDVCSAQGVRGY CCCCHHHHCCCCCCC | 24.39 | - | |
134 | Methylation | VCSAQGVRGYPTLKL HHHCCCCCCCCEEEE | 45.83 | 115919193 | |
143 | Ubiquitination | YPTLKLFKPGQEAVK CCEEEEECCCCHHHH | 59.69 | 21890473 | |
150 | Malonylation | KPGQEAVKYQGPRDF CCCCHHHHCCCCCCH | 38.61 | 26320211 | |
150 | Acetylation | KPGQEAVKYQGPRDF CCCCHHHHCCCCCCH | 38.61 | 25953088 | |
150 | 2-Hydroxyisobutyrylation | KPGQEAVKYQGPRDF CCCCHHHHCCCCCCH | 38.61 | - | |
150 | Ubiquitination | KPGQEAVKYQGPRDF CCCCHHHHCCCCCCH | 38.61 | 21890473 | |
164 | Sulfoxidation | FQTLENWMLQTLNEE HHHHHHHHHHHCCCC | 2.75 | 30846556 | |
174 | O-linked_Glycosylation | TLNEEPVTPEPEVEP HCCCCCCCCCCCCCC | 32.42 | OGP | |
221 | Methylation | APWCGHCKALAPTWE CCCCCCCHHHHCHHH | 40.54 | - | |
241 | 2-Hydroxyisobutyrylation | LEHSETVKIGKVDCT CCCCCCEEECCEECC | 53.84 | - | |
241 | Ubiquitination | LEHSETVKIGKVDCT CCCCCCEEECCEECC | 53.84 | - | |
244 | Acetylation | SETVKIGKVDCTQHY CCCEEECCEECCCEE | 38.07 | 26051181 | |
244 | 2-Hydroxyisobutyrylation | SETVKIGKVDCTQHY CCCEEECCEECCCEE | 38.07 | - | |
244 | Ubiquitination | SETVKIGKVDCTQHY CCCEEECCEECCCEE | 38.07 | 2190698 | |
248 | Phosphorylation | KIGKVDCTQHYELCS EECCEECCCEEEECC | 17.58 | 28152594 | |
251 | Phosphorylation | KVDCTQHYELCSGNQ CEECCCEEEECCCCC | 10.77 | 28152594 | |
255 | Phosphorylation | TQHYELCSGNQVRGY CCEEEECCCCCCCCC | 54.10 | 28152594 | |
278 | 2-Hydroxyisobutyrylation | GKKVDQYKGKRDLES CCCCCCCCCCCCHHH | 52.93 | - | |
289 | Phosphorylation | DLESLREYVESQLQR CHHHHHHHHHHHHHH | 11.77 | - | |
297 | O-linked_Glycosylation | VESQLQRTETGATET HHHHHHHCCCCCCCE | 25.57 | OGP | |
302 | O-linked_Glycosylation | QRTETGATETVTPSE HHCCCCCCCEECCCC | 33.27 | OGP | |
304 | O-linked_Glycosylation | TETGATETVTPSEAP CCCCCCCEECCCCCC | 25.89 | OGP | |
306 | O-linked_Glycosylation | TGATETVTPSEAPVL CCCCCEECCCCCCEE | 28.63 | OGP | |
308 | O-linked_Glycosylation | ATETVTPSEAPVLAA CCCEECCCCCCEEEE | 36.70 | OGP | |
344 | Ubiquitination | AEGITFIKFYAPWCG HHCCEEEEEECCCCC | 28.29 | - | |
365 | 2-Hydroxyisobutyrylation | PTWEELSKKEFPGLA CCHHHHHHCCCCCCC | 69.79 | - | |
366 | 2-Hydroxyisobutyrylation | TWEELSKKEFPGLAG CHHHHHHCCCCCCCC | 62.30 | - | |
366 | Ubiquitination | TWEELSKKEFPGLAG CHHHHHHCCCCCCCC | 62.30 | - | |
381 | Glutathionylation | VKIAEVDCTAERNIC CEEEEEECCCCCCCC | 4.73 | 22555962 | |
390 | Acetylation | AERNICSKYSVRGYP CCCCCCCCCCCCCCC | 36.81 | 25953088 | |
390 | 2-Hydroxyisobutyrylation | AERNICSKYSVRGYP CCCCCCCCCCCCCCC | 36.81 | - | |
396 | Phosphorylation | SKYSVRGYPTLLLFR CCCCCCCCCEEEEEE | 5.18 | 28152594 | |
419 | Phosphorylation | SGGRDLDSLHRFVLS CCCCCHHHHHHHHHH | 33.11 | 24719451 | |
426 | Phosphorylation | SLHRFVLSQAKDEL- HHHHHHHHHHHHCC- | 23.84 | 21712546 | |
429 | Ubiquitination | RFVLSQAKDEL---- HHHHHHHHHCC---- | 44.06 | - |
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 TXND5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TXND5_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 TXND5_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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