UniProt ID | TMTC3_HUMAN | |
---|---|---|
UniProt AC | Q6ZXV5 | |
Protein Name | Transmembrane and TPR repeat-containing protein 3 | |
Gene Name | TMTC3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 915 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . Endoplasmic reticulum . In odontoblast cultures, it colocalizes with PDIA3 in the endoplasmic reticulum. |
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Protein Description | Involved in the positive regulation of proteasomal protein degradation in the endoplasmic reticulum (ER), and the control of ER stress response.. | |
Protein Sequence | MANINLKEITLIVGVVTACYWNSLFCGFVFDDVSAILDNKDLHPSTPLKTLFQNDFWGTPMSEERSHKSYRPLTVLTFRLNYLLSELKPMSYHLLNMIFHAVVSVIFLKVCKLFLDNKSSVIASLLFAVHPIHTEAVTGVVGRAELLSSIFFLAAFLSYTRSKGPDNSIIWTPIALTVFLVAVATLCKEQGITVVGICCVYEVFIAQGYTLPLLCTTAGQFLRGKGSIPFSMLQTLVKLIVLMFSTLLLVVIRVQVIQSQLPVFTRFDNPAAVSPTPTRQLTFNYLLPVNAWLLLNPSELCCDWTMGTIPLIESLLDIRNLATFTFFCFLGMLGVFSIRYSGDSSKTVLMALCLMALPFIPASNLFFPVGFVVAERVLYVPSMGFCILVAHGWQKISTKSVFKKLSWICLSMVILTHSLKTFHRNWDWESEYTLFMSALKVNKNNAKLWNNVGHALENEKNFERALKYFLQATHVQPDDIGAHMNVGRTYKNLNRTKEAEESYMMAKSLMPQIIPGKKYAARIAPNHLNVYINLANLIRANESRLEEADQLYRQAISMRPDFKQAYISRGELLLKMNKPLKAKEAYLKALELDRNNADLWYNLAIVHIELKEPNEALKKNFNRALELNPKHKLALFNSAIVMQESGEVKLRPEARKRLLSYINEEPLDANGYFNLGMLAMDDKKDNEAEIWMKKAIKLQADFRSALFNLALLYSQTAKELKALPILEELLRYYPDHIKGLILKGDILMNQKKDILGAKKCFERILEMDPSNVQGKHNLCVVYFEEKDLLKAERCLLETLALAPHEEYIQRHLNIVRDKISSSSFIEPIFPTSKISSVEGKKIPTESVKEIRGESRQTQIVKTSDNKSQSKSNKQLGKNGDEETPHKTTKDIKEIEKKRVAALKRLEEIERILNGE | |
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 |
---|---|---|---|---|---|
50 | Phosphorylation | HPSTPLKTLFQNDFW CCCCCHHHHHCCCCC | 40.25 | 24719451 | |
50 (in isoform 2) | Phosphorylation | - | 40.25 | 24719451 | |
66 (in isoform 2) | Phosphorylation | - | 38.25 | 24719451 | |
66 | Phosphorylation | TPMSEERSHKSYRPL CCCCCCCCCCCCCCC | 38.25 | 24719451 | |
117 | N-linked_Glycosylation | VCKLFLDNKSSVIAS HHHHHHCCHHHHHHH | 48.53 | UniProtKB CARBOHYD | |
227 | Phosphorylation | QFLRGKGSIPFSMLQ HHHCCCCCCCHHHHH | 30.49 | 21406692 | |
231 | Phosphorylation | GKGSIPFSMLQTLVK CCCCCCHHHHHHHHH | 17.15 | 21406692 | |
235 | Phosphorylation | IPFSMLQTLVKLIVL CCHHHHHHHHHHHHH | 29.56 | 21406692 | |
274 | Phosphorylation | FDNPAAVSPTPTRQL CCCCCCCCCCCCCCE | 20.52 | - | |
337 | O-linked_Glycosylation | LGMLGVFSIRYSGDS HHHHHHHHCCCCCCC | 12.07 | 29351928 | |
460 | Ubiquitination | GHALENEKNFERALK HHHHHCHHHHHHHHH | 77.76 | 21890473 | |
460 (in isoform 2) | Ubiquitination | - | 77.76 | 21890473 | |
460 (in isoform 1) | Ubiquitination | - | 77.76 | 21890473 | |
468 | Phosphorylation | NFERALKYFLQATHV HHHHHHHHHHHHCCC | 15.46 | 24719451 | |
473 | Phosphorylation | LKYFLQATHVQPDDI HHHHHHHCCCCCCHH | 15.04 | 24719451 | |
490 | Phosphorylation | HMNVGRTYKNLNRTK HCCCCCHHHCCCCCH | 9.12 | - | |
494 | N-linked_Glycosylation | GRTYKNLNRTKEAEE CCHHHCCCCCHHHHH | 59.99 | UniProtKB CARBOHYD | |
503 (in isoform 2) | Phosphorylation | - | 8.32 | - | |
503 | Phosphorylation | TKEAEESYMMAKSLM CHHHHHHHHHHHHHC | 8.32 | 18669648 | |
517 | 2-Hydroxyisobutyrylation | MPQIIPGKKYAARIA CCCCCCCCCHHHHHC | 36.94 | - | |
541 | N-linked_Glycosylation | LANLIRANESRLEEA HHHHHHHCHHHHHHH | 37.62 | UniProtKB CARBOHYD | |
552 | Phosphorylation | LEEADQLYRQAISMR HHHHHHHHHHHHHCC | 8.61 | 21406692 | |
563 | Acetylation | ISMRPDFKQAYISRG HHCCCCHHHHHHHHH | 41.20 | 26051181 | |
737 (in isoform 2) | Ubiquitination | - | 5.02 | 21890473 | |
738 | 2-Hydroxyisobutyrylation | RYYPDHIKGLILKGD HHCCHHHCEEEECCC | 44.22 | - | |
738 (in isoform 1) | Ubiquitination | - | 44.22 | 21890473 | |
738 | Ubiquitination | RYYPDHIKGLILKGD HHCCHHHCEEEECCC | 44.22 | 21890473 | |
743 | Acetylation | HIKGLILKGDILMNQ HHCEEEECCCHHHCC | 47.76 | 7711367 | |
782 | Phosphorylation | KHNLCVVYFEEKDLL CCEEEEEEECHHHHH | 5.72 | - | |
821 | Phosphorylation | IVRDKISSSSFIEPI HHHHHHCCCCCCCCC | 33.21 | 24114839 | |
823 | Phosphorylation | RDKISSSSFIEPIFP HHHHCCCCCCCCCCC | 31.99 | - | |
831 | O-linked_Glycosylation | FIEPIFPTSKISSVE CCCCCCCCCCCEECC | 31.72 | OGP | |
832 | Phosphorylation | IEPIFPTSKISSVEG CCCCCCCCCCEECCC | 28.38 | 24114839 | |
844 | O-linked_Glycosylation | VEGKKIPTESVKEIR CCCCCCCCHHHHHHC | 44.35 | OGP | |
857 | Phosphorylation | IRGESRQTQIVKTSD HCCCCCCEEEEECCC | 21.10 | 29083192 | |
887 | Phosphorylation | DEETPHKTTKDIKEI CCCCCCCCHHHHHHH | 35.72 | 26074081 | |
888 | Phosphorylation | EETPHKTTKDIKEIE CCCCCCCHHHHHHHH | 31.36 | 26074081 | |
896 | Acetylation | KDIKEIEKKRVAALK HHHHHHHHHHHHHHH | 52.09 | 12433699 | |
897 | Acetylation | DIKEIEKKRVAALKR HHHHHHHHHHHHHHH | 39.04 | 12433707 |
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 TMTC3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMTC3_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 TMTC3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
COTL1_HUMAN | COTL1 | physical | 26344197 |
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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Phosphorylation | |
Reference | PubMed |
"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 TYR-503, AND MASSSPECTROMETRY. |