LYOX_HUMAN - dbPTM
LYOX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
81N-linked_GlycosylationAAVPGAANASAQQPR
CCCCCCCCCCCCCCC
33.62UniProtKB CARBOHYD
83PhosphorylationVPGAANASAQQPRTP
CCCCCCCCCCCCCCC
26.8121955146
89O-linked_GlycosylationASAQQPRTPILLIRD
CCCCCCCCCEEEEEC
22.7455825463
97N-linked_GlycosylationPILLIRDNRTAAART
CEEEEECCCCCHHHH
33.10UniProtKB CARBOHYD
113O-linked_GlycosylationTAGSSGVTAGRPRPT
CCCCCCCCCCCCCCC
27.2455825081
120O-linked_GlycosylationTAGRPRPTARHWFQA
CCCCCCCCHHHHHHC
37.2955825085
130O-linked_GlycosylationHWFQAGYSTSRAREA
HHHHCCCCHHHHHHH
20.9955826175
131O-linked_GlycosylationWFQAGYSTSRAREAG
HHHCCCCHHHHHHHH
17.4755826181
132O-linked_GlycosylationFQAGYSTSRAREAGA
HHCCCCHHHHHHHHC
20.2955826185
144N-linked_GlycosylationAGASRAENQTAPGEV
HHCCHHCCCCCCCCC
43.44UniProtKB CARBOHYD
146O-linked_GlycosylationASRAENQTAPGEVPA
CCHHCCCCCCCCCCC
46.53OGP
155PhosphorylationPGEVPALSNLRPPSR
CCCCCCHHCCCCCCC
35.6024719451
172PhosphorylationGMVGDDPYNPYKYSD
CCCCCCCCCCCCCCC
35.4530257219
175PhosphorylationGDDPYNPYKYSDDNP
CCCCCCCCCCCCCCC
20.9430257219
187SulfationDNPYYNYYDTYERPR
CCCCCCCCCCCCCCC
9.7331152061
355OtherSPGCYDTYGADIDCQ
CCCCHHCCCCCCCCE
13.86-
355"2',4',5'-topaquinone"SPGCYDTYGADIDCQ
CCCCHHCCCCCCCCE
13.86-
384PhosphorylationKVSVNPSYLVPESDY
EEEECHHHCCCHHHH
16.99-
413O-linked_GlycosylationHAYASGCTISPY---
EEEECCCEEECC---
28.1955834745

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYOX_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H11_HUMANHIST1H1Aphysical
12686141
ELN_HUMANELNphysical
12686141
H2B2E_HUMANHIST2H2BEphysical
12686141
SH3K1_HUMANSH3KBP1physical
24167568
CD2AP_HUMANCD2APphysical
24167568
CBL_HUMANCBLphysical
24167568
RAF1_HUMANRAF1physical
22438909

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYOX_HUMAN

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Related Literatures of Post-Translational Modification

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