UniProt ID | TMX3_HUMAN | |
---|---|---|
UniProt AC | Q96JJ7 | |
Protein Name | Protein disulfide-isomerase TMX3 | |
Gene Name | TMX3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 454 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass membrane protein . |
|
Protein Description | Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase.. | |
Protein Sequence | MAAWKSWTALRLCATVVVLDMVVCKGFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEMPAVLVFKDETYFVYDEYEDGDLSSWINRERFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEHTRLKSIIQEVARDYRDLFHRDFQFGHMDGNDYINTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEAQGGDSILQRLKRIVFDAKSTIVSIFKSSPLMGCFLFGLPLGVISIMCYGIYTADTDGGYIEERYEVSKSENENQEQIEESKEQQEPSSGGSVVPTVQEPKDVLEKKKD | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | TALRLCATVVVLDMV HHHHHHHHHHHHHHH | 16.91 | 28387310 | |
58 | Ubiquitination | PWCGHCKKLEPIWNE CCCCCCCCCCCCHHH | 64.57 | - | |
71 | Ubiquitination | NEVGLEMKSIGSPVK HHHCCEEECCCCCEE | 29.55 | - | |
78 | Ubiquitination | KSIGSPVKVGKMDAT ECCCCCEEECCCCCC | 48.96 | 21906983 | |
78 (in isoform 2) | Ubiquitination | - | 48.96 | 21906983 | |
78 (in isoform 1) | Ubiquitination | - | 48.96 | 21906983 | |
81 | Ubiquitination | GSPVKVGKMDATSYS CCCEEECCCCCCCHH | 36.27 | 22817900 | |
106 | Ubiquitination | YPTIKLLKGDLAYNY CCEEEEEECCCCCCC | 61.90 | - | |
111 | Phosphorylation | LLKGDLAYNYRGPRT EEECCCCCCCCCCCC | 21.74 | - | |
119 | Ubiquitination | NYRGPRTKDDIIEFA CCCCCCCHHHHHHHH | 55.47 | 24816145 | |
126 | Ubiquitination | KDDIIEFAHRVSGAL HHHHHHHHHHHCCCC | 4.10 | 24816145 | |
148 | 2-Hydroxyisobutyrylation | QMFEHMQKRHRVFFV HHHHHHHHHCCEEEE | 42.47 | - | |
161 | Phosphorylation | FVYVGGESPLKEKYI EEEECCCCCCHHHHH | 38.52 | 24719451 | |
166 | Ubiquitination | GESPLKEKYIDAASE CCCCCHHHHHHHHHH | 46.01 | - | |
223 | Ubiquitination | DGDLSSWINRERFQN CCCHHHHHCHHHHHH | 3.63 | 22817900 | |
258 | N-linked_Glycosylation | LAVIDEKNTSVEHTR EEEECCCCCCCCHHH | 35.22 | 19159218 | |
267 | 2-Hydroxyisobutyrylation | SVEHTRLKSIIQEVA CCCHHHHHHHHHHHH | 36.00 | - | |
267 | Ubiquitination | SVEHTRLKSIIQEVA CCCHHHHHHHHHHHH | 36.00 | 24816145 | |
268 | Phosphorylation | VEHTRLKSIIQEVAR CCHHHHHHHHHHHHH | 29.52 | 22817900 | |
273 | Ubiquitination | LKSIIQEVARDYRDL HHHHHHHHHHHHHHH | 2.80 | 21963094 | |
313 | N-linked_Glycosylation | VPTVVVLNTSNQQYF CCEEEEEECCCCEEE | 29.83 | UniProtKB CARBOHYD | |
364 | Ubiquitination | KRIVFDAKSTIVSIF HHHHHCCCCHHHHHH | 50.40 | 22817900 | |
364 (in isoform 1) | Ubiquitination | - | 50.40 | 21906983 | |
369 | Phosphorylation | DAKSTIVSIFKSSPL CCCCHHHHHHCCCCC | 20.61 | 24719451 | |
387 | Ubiquitination | FLFGLPLGVISIMCY HHHCCCHHHHHHHHE | 16.87 | 33845483 | |
393 | S-palmitoylation | LGVISIMCYGIYTAD HHHHHHHHEEEEECC | 2.41 | 29575903 | |
410 | Phosphorylation | GGYIEERYEVSKSEN CCCEEEEEEECCCCC | 24.78 | 28796482 | |
413 | Phosphorylation | IEERYEVSKSENENQ EEEEEEECCCCCCCH | 20.65 | 29507054 | |
414 (in isoform 1) | Ubiquitination | - | 67.95 | 21906983 | |
414 | Ubiquitination | EERYEVSKSENENQE EEEEEECCCCCCCHH | 67.95 | 21963094 | |
415 | Phosphorylation | ERYEVSKSENENQEQ EEEEECCCCCCCHHH | 37.84 | 30576142 | |
426 | Phosphorylation | NQEQIEESKEQQEPS CHHHHHHHHHHCCCC | 28.80 | 20639409 | |
433 | Phosphorylation | SKEQQEPSSGGSVVP HHHHCCCCCCCCCCC | 40.64 | 28355574 | |
434 | Phosphorylation | KEQQEPSSGGSVVPT HHHCCCCCCCCCCCC | 58.87 | 21815630 | |
437 | Phosphorylation | QEPSSGGSVVPTVQE CCCCCCCCCCCCCCC | 24.38 | 25850435 | |
441 | Phosphorylation | SGGSVVPTVQEPKDV CCCCCCCCCCCCHHH | 24.18 | 20639409 | |
446 | Ubiquitination | VPTVQEPKDVLEKKK CCCCCCCHHHHHHCC | 60.77 | 29967540 |
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 TMX3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMX3_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 TMX3_HUMAN !! |
Kegg Disease | ||||||
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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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASSSPECTROMETRY. |