UniProt ID | LYOX_HUMAN | |
---|---|---|
UniProt AC | P28300 | |
Protein Name | Protein-lysine 6-oxidase | |
Gene Name | LOX | |
Organism | Homo sapiens (Human). | |
Sequence Length | 417 | |
Subcellular Localization | Secreted . Secreted, extracellular space. | |
Protein Description | Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. [PubMed: 26838787 Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity] | |
Protein Sequence | MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY | |
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 |
---|---|---|---|---|---|
81 | N-linked_Glycosylation | AAVPGAANASAQQPR CCCCCCCCCCCCCCC | 33.62 | UniProtKB CARBOHYD | |
83 | Phosphorylation | VPGAANASAQQPRTP CCCCCCCCCCCCCCC | 26.81 | 21955146 | |
89 | O-linked_Glycosylation | ASAQQPRTPILLIRD CCCCCCCCCEEEEEC | 22.74 | 55825463 | |
97 | N-linked_Glycosylation | PILLIRDNRTAAART CEEEEECCCCCHHHH | 33.10 | UniProtKB CARBOHYD | |
113 | O-linked_Glycosylation | TAGSSGVTAGRPRPT CCCCCCCCCCCCCCC | 27.24 | 55825081 | |
120 | O-linked_Glycosylation | TAGRPRPTARHWFQA CCCCCCCCHHHHHHC | 37.29 | 55825085 | |
130 | O-linked_Glycosylation | HWFQAGYSTSRAREA HHHHCCCCHHHHHHH | 20.99 | 55826175 | |
131 | O-linked_Glycosylation | WFQAGYSTSRAREAG HHHCCCCHHHHHHHH | 17.47 | 55826181 | |
132 | O-linked_Glycosylation | FQAGYSTSRAREAGA HHCCCCHHHHHHHHC | 20.29 | 55826185 | |
144 | N-linked_Glycosylation | AGASRAENQTAPGEV HHCCHHCCCCCCCCC | 43.44 | UniProtKB CARBOHYD | |
146 | O-linked_Glycosylation | ASRAENQTAPGEVPA CCHHCCCCCCCCCCC | 46.53 | OGP | |
155 | Phosphorylation | PGEVPALSNLRPPSR CCCCCCHHCCCCCCC | 35.60 | 24719451 | |
172 | Phosphorylation | GMVGDDPYNPYKYSD CCCCCCCCCCCCCCC | 35.45 | 30257219 | |
175 | Phosphorylation | GDDPYNPYKYSDDNP CCCCCCCCCCCCCCC | 20.94 | 30257219 | |
187 | Sulfation | DNPYYNYYDTYERPR CCCCCCCCCCCCCCC | 9.73 | 31152061 | |
355 | Other | SPGCYDTYGADIDCQ CCCCHHCCCCCCCCE | 13.86 | - | |
355 | "2',4',5'-topaquinone" | SPGCYDTYGADIDCQ CCCCHHCCCCCCCCE | 13.86 | - | |
384 | Phosphorylation | KVSVNPSYLVPESDY EEEECHHHCCCHHHH | 16.99 | - | |
413 | O-linked_Glycosylation | HAYASGCTISPY--- EEEECCCEEECC--- | 28.19 | 55834745 |
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 LYOX_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LYOX_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 LYOX_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
H11_HUMAN | HIST1H1A | physical | 12686141 | |
ELN_HUMAN | ELN | physical | 12686141 | |
H2B2E_HUMAN | HIST2H2BE | physical | 12686141 | |
SH3K1_HUMAN | SH3KBP1 | physical | 24167568 | |
CD2AP_HUMAN | CD2AP | physical | 24167568 | |
CBL_HUMAN | CBL | physical | 24167568 | |
RAF1_HUMAN | RAF1 | physical | 22438909 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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