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UniProtKB - P28301 (LYOX_MOUSE)

Entry version 169 (10 Feb 2021)
Sequence version 1 (01 Dec 1992)
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Protein

Protein-lysine 6-oxidase

Gene

Lox

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (PubMed:27432961).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi286CopperSequence analysis1
Metal bindingi288CopperSequence analysis1
Metal bindingi290CopperSequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1566948, Elastic fibre formation
R-MMU-2243919, Crosslinking of collagen fibrils

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein-lysine 6-oxidase (EC:1.4.3.131 Publication)
Alternative name(s):
Lysyl oxidase
Ras excision protein
Cleaved into the following 2 chains:
Protein-lysine 6-oxidase, long formBy similarity
Protein-lysine 6-oxidase, short formBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Lox
Synonyms:Rrg
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:96817, Lox

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi292M → R: Homozygous mice display tortuous vessels aneurysm, loss of oxidase activity and die perinatally of aortic aneurysm and dissection. Heterozygous mice display thicker arterial wall with discontinuous elastic lamellae. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21By similarityAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000001852222 – 162Removed by BMP1By similarityAdd BLAST141
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000018523163 – 411Protein-lysine 6-oxidase, long formBy similarityAdd BLAST249
ChainiPRO_0000447886213 – 411Protein-lysine 6-oxidase, short formBy similarityAdd BLAST199

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi91N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei181SulfotyrosineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi232 ↔ 238By similarity
Disulfide bondi285 ↔ 334By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki314 ↔ 349Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi318 ↔ 324By similarity
Disulfide bondi345 ↔ 355By similarity
Modified residuei3492',4',5'-topaquinoneBy similarity1
Disulfide bondi392 ↔ 406By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.By similarity
Proteolytically cleaved by BMP1 which removes the propeptide (PubMed:20181949). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (By similarity). The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (PubMed:16251195). Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (By similarity). Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (By similarity).By similarity2 Publications
Sulfated at Tyr-181 and also at either Tyr-177 or Tyr-178 which enhances binding to collagen.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei212 – 213Cleavage; by ADAMTS2 and ADAMTS14By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, Sulfation, TPQ

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P28301

PeptideAtlas

More...PeptideAtlasi		P28301

PRoteomics IDEntifications database

More...PRIDEi		P28301

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P28301, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P28301

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P28301

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in aorta (at protein level). Expressed in embryonic, juvenil and adult aorta.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000024529, Expressed in stroma of bone marrow and 222 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P28301, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P28301, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with MFAP4.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		201191, 5 interactors

Protein interaction database and analysis system

More...IntActi		P28301, 16 interactors

Molecular INTeraction database

More...MINTi		P28301

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000129247

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P28301, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P28301

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni207 – 411Lysyl-oxidase likeAdd BLAST205

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QWQR, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154779

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002555_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P28301

Identification of Orthologs from Complete Genome Data

More...OMAi		IVRCDVR

Database of Orthologous Groups

More...OrthoDBi		815466at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P28301

TreeFam database of animal gene trees

More...TreeFami		TF326061

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001695, Lysyl_oxidase
IPR019828, Lysyl_oxidase_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01186, Lysyl_oxidase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00074, LYSYLOXIDASE

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00926, LYSYL_OXIDASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P28301-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRFAWAVLLL GPLQLCPLLR CAPQTPREPP AAPGAWRQTI QWENNGQVFS 
        60         70         80         90        100
LLSLGAQYQP QRRRDPSATA RRPDGDAASQ PRTPILLLRD NRTASTRART 
       110        120        130        140        150
PSPSGVAAGR PRPAARHWFQ AGFSPSGARD GASRRAANRT ASPQPPQLSN 
       160        170        180        190        200
LRPPSHIDRM VGDDPYNPYK YSDDNPYYNY YDTYERPRPG SRNRPGYGTG 
       210        220        230        240        250
YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA SSAYRADVRD 
       260        270        280        290        300
YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL 
       310        320        330        340        350
LDANTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA 
       360        370        380        390        400
ADIDCQWIDI TDVQPGNYIL KVSVNPSYLV PESDYTNNVV RCDIRYTGHH 
       410 
AYASGCTISP Y
Length:411
Mass (Da):46,701
Last modified:December 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDBC0563A9C0AEB52
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti333A → G in AAA99899 (PubMed:8100214).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M65142 mRNA Translation: AAA19032.1
M65143 mRNA Translation: AAA20185.1
L04262, L04263, L04264 Genomic DNA Translation: AAA99899.1
BC018439 mRNA Translation: AAH18439.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS50289.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47005, OXMSL

NCBI Reference Sequences

More...RefSeqi		NP_001273110.1, NM_001286181.1
NP_001273111.1, NM_001286182.1
NP_034858.2, NM_010728.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000025409; ENSMUSP00000025409; ENSMUSG00000024529
ENSMUST00000171470; ENSMUSP00000129247; ENSMUSG00000024529

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16948

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16948

UCSC genome browser

More...UCSCi		uc008exe.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65142 mRNA Translation: AAA19032.1
M65143 mRNA Translation: AAA20185.1
L04262, L04263, L04264 Genomic DNA Translation: AAA99899.1
BC018439 mRNA Translation: AAH18439.1
CCDSiCCDS50289.1
PIRiA47005, OXMSL
RefSeqiNP_001273110.1, NM_001286181.1
NP_001273111.1, NM_001286182.1
NP_034858.2, NM_010728.3

3D structure databases

SMRiP28301
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi201191, 5 interactors
IntActiP28301, 16 interactors
MINTiP28301
STRINGi10090.ENSMUSP00000129247

PTM databases

GlyGeniP28301, 2 sites
iPTMnetiP28301
PhosphoSitePlusiP28301

Proteomic databases

PaxDbiP28301
PeptideAtlasiP28301
PRIDEiP28301

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		25606, 795 antibodies

Genome annotation databases

EnsembliENSMUST00000025409; ENSMUSP00000025409; ENSMUSG00000024529
ENSMUST00000171470; ENSMUSP00000129247; ENSMUSG00000024529
GeneIDi16948
KEGGimmu:16948
UCSCiuc008exe.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4015
MGIiMGI:96817, Lox

Phylogenomic databases

eggNOGiENOG502QWQR, Eukaryota
GeneTreeiENSGT00940000154779
HOGENOMiCLU_002555_2_1_1
InParanoidiP28301
OMAiIVRCDVR
OrthoDBi815466at2759
PhylomeDBiP28301
TreeFamiTF326061

Enzyme and pathway databases

ReactomeiR-MMU-1566948, Elastic fibre formation
R-MMU-2243919, Crosslinking of collagen fibrils

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		16948, 1 hit in 17 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Lox, mouse

Protein Ontology

More...PROi		PR:P28301
RNActiP28301, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000024529, Expressed in stroma of bone marrow and 222 other tissues
ExpressionAtlasiP28301, baseline and differential
GenevisibleiP28301, MM

Family and domain databases

InterProiView protein in InterPro
IPR001695, Lysyl_oxidase
IPR019828, Lysyl_oxidase_CS
PfamiView protein in Pfam
PF01186, Lysyl_oxidase, 1 hit
PRINTSiPR00074, LYSYLOXIDASE
PROSITEiView protein in PROSITE
PS00926, LYSYL_OXIDASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLYOX_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28301
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: February 10, 2021
This is version 169 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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