Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 179 (25 May 2022)
Sequence version 2 (24 Jan 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Retina-specific copper amine oxidase

Gene

AOC2

Organism
Homo sapiens (Human)
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

Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina.

2 Publications

<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:

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.056 mM for tryptamine1 Publication
  2. KM=0.077 mM for 2-phenylethylamine1 Publication
  3. KM=0.167 mM for benzylamine1 Publication
  4. KM=0.178 mM for p-tyramine1 Publication
  5. KM=1.7 mM for methylamine1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei380Proton acceptorBy similarity1
Active sitei465Schiff-base intermediate with substrate; via topaquinoneBy similarity1
<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 bindingi516Copper; via tele nitrogenBy similarity1
Metal bindingi518Copper; via tele nitrogenBy similarity1
Metal bindingi525Calcium 1By similarity1
Metal bindingi526Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi527Calcium 1By similarity1
Metal bindingi568Calcium 2By similarity1
Metal bindingi659Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi661Calcium 2By similarity1
Metal bindingi663Calcium 2By similarity1
Metal bindingi669Calcium 1By similarity1
Metal bindingi670Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi680Copper; via pros nitrogenBy similarity1

<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

GO - Biological processi

<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
Biological processCatecholamine metabolism
LigandCalcium, Copper, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.3.21, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O75106

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-211945, Phase I - Functionalization of compounds

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O75106

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
O75106

<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:
Retina-specific copper amine oxidase (EC:1.4.3.21By similarity)
Short name:
RAO
Alternative name(s):
Amine oxidase [copper-containing]
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
<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:AOC2
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 17

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:549, AOC2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602268, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O75106

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000131480

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<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

Organism-specific databases

DisGeNET

More...
DisGeNETi
314

Open Targets

More...
OpenTargetsi
ENSG00000131480

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24839

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O75106, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4112

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AOC2

<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 – 32Sequence analysisAdd BLAST32
<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_000003567133 – 756Retina-specific copper amine oxidaseAdd BLAST724

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>Glycosylationi133N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi226N-linked (GlcNAc...) asparagineBy 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 bondi398 ↔ 424By similarity
<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 residuei4652',4',5'-topaquinoneBy similarity1
Glycosylationi588N-linked (GlcNAc...) (complex) asparagineBy similarity1
Glycosylationi662N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi730 ↔ 737By similarity
Disulfide bondi744InterchainBy 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

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O75106

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O75106

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

More...
PaxDbi
O75106

PeptideAtlas

More...
PeptideAtlasi
O75106

PRoteomics IDEntifications database

More...
PRIDEi
O75106

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
49761 [O75106-1]
49762 [O75106-2]

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1714, 2 N-Linked glycans (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
O75106, 5 sites, 2 N-linked glycans (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O75106

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

More...
PhosphoSitePlusi
O75106

<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 many tissues with much higher expression in retina. Isoform 1 and isoform 2 are expressed in adipose tissue, whereas isoform 1 only seems to be present in thymus, and isoform 2 only in testis.3 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated during in vitro adipocyte differentiation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000131480, Expressed in blood and 122 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O75106, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000131480, Low tissue specificity

<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

Homodimer; disulfide-linked (By similarity).

Forms a heterodimer with AOC3, in vitro.

By similarity1 Publication

<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
106811, 22 interactors

Protein interaction database and analysis system

More...
IntActi
O75106, 5 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000253799

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O75106

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O75106, 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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
O75106

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

More...
SMRi
O75106

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>Regioni378 – 388Substrate bindingBy similarityAdd BLAST11
Regioni462 – 467Substrate bindingBy similarity6
Regioni574 – 581Heparin-bindingBy similarity8

<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 copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1186, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183207

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015739_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O75106

Identification of Orthologs from Complete Genome Data

More...
OMAi
QDFSKFF

Database of Orthologous Groups

More...
OrthoDBi
1320015at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O75106

TreeFam database of animal gene trees

More...
TreeFami
TF314750

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.98.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032952, AOC2
IPR000269, Cu_amine_oxidase
IPR015798, Cu_amine_oxidase_C
IPR036460, Cu_amine_oxidase_C_sf
IPR016182, Cu_amine_oxidase_N-reg
IPR015800, Cu_amine_oxidase_N2
IPR015802, Cu_amine_oxidase_N3

The PANTHER Classification System

More...
PANTHERi
PTHR10638, PTHR10638, 1 hit
PTHR10638:SF4, PTHR10638:SF4, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01179, Cu_amine_oxid, 1 hit
PF02727, Cu_amine_oxidN2, 1 hit
PF02728, Cu_amine_oxidN3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00766, CUDAOXIDASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49998, SSF49998, 1 hit
SSF54416, SSF54416, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01164, COPPER_AMINE_OXID_1, 1 hit
PS01165, COPPER_AMINE_OXID_2, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O75106-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MHLKIVLAFL ALSLITIFAL AYVLLTSPGG SSQPPHCPSV SHRAQPWPHP
60 70 80 90 100
GQSQLFADLS REELTAVMRF LTQRLGPGLV DAAQAQPSDN CIFSVELQLP
110 120 130 140 150
PKAAALAHLD RGSPPPAREA LAIVLFGGQP QPNVSELVVG PLPHPSYMRD
160 170 180 190 200
VTVERHGGPL PYHRRPVLRA EFTQMWRHLK EVELPKAPIF LSSTFNYNGS
210 220 230 240 250
TLAAVHATPR GLRSGDRATW MALYHNISGV GLFLHPVGLE LLLDHRALDP
260 270 280 290 300
AHWTVQQVFY LGHYYADLGQ LEREFKSGRL EVVRVPLPPP NGASSLRSRN
310 320 330 340 350
SPGPLPPLQF SPQGSQYSVQ GNLVVSSLWS FTFGHGVFSG LRIFDVRFQG
360 370 380 390 400
ERIAYEVSVQ ECVSIYGADS PKTMLTRYLD SSFGLGRNSR GLVRGVDCPY
410 420 430 440 450
QATMVDIHIL VGKGAVQLLP GAVCVFEEAQ GLPLRRHHNY LQNHFYGGLA
460 470 480 490 500
SSALVVRSVS SVGNYDYIWD FVLYPNGALE GRVHATGYIN TAFLKGGEEG
510 520 530 540 550
LLFGNRVGER VLGTVHTHAF HFKLDLDVAG LKNWVVAEDV VFKPVAAPWN
560 570 580 590 600
PEHWLQRPQL TRQVLGKEDL TAFSLGSPLP RYLYLASNQT NAWGHQRGYR
610 620 630 640 650
IQIHSPLGIH IPLESDMERA LSWGRYQLVV TQRKEEESQS SSIYHQNDIW
660 670 680 690 700
TPTVTFADFI NNETLLGEDL VAWVTASFLH IPHAEDIPNT VTLGNRVGFL
710 720 730 740 750
LRPYNFFDED PSIFSPGSVY FEKGQDAGLC SINPVACLPD LAACVPDLPP

FSYHGF
Length:756
Mass (Da):83,673
Last modified:January 24, 2006 - v2
<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:i10263D8D56D3BD25
GO
Isoform 2 (identifier: O75106-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     599-625: Missing.

Show »
Length:729
Mass (Da):80,516
Checksum:i5F28CCC8EE353415
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 conflicti181E → D (PubMed:9119395).Curated1
Sequence conflicti181E → D (PubMed:9722954).Curated1
Sequence conflicti215 – 218GDRA → RERT (PubMed:9119395).Curated4
Sequence conflicti215 – 218GDRA → RERT (PubMed:9722954).Curated4
Sequence conflicti221 – 222MA → IG (PubMed:9119395).Curated2
Sequence conflicti610H → Q (PubMed:9119395).Curated1
Sequence conflicti610H → Q (PubMed:9722954).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0250225I → V1 PublicationCorresponds to variant dbSNP:rs34230945Ensembl.1
Natural variantiVAR_02502322Y → C1 PublicationCorresponds to variant dbSNP:rs34435306Ensembl.1
Natural variantiVAR_025024141P → L1 PublicationCorresponds to variant dbSNP:rs35833794EnsemblClinVar.1
Natural variantiVAR_025025273R → Q1 PublicationCorresponds to variant dbSNP:rs35508987Ensembl.1
Natural variantiVAR_025026427E → D1 PublicationCorresponds to variant dbSNP:rs34351794Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006549599 – 625Missing in isoform 2. 1 PublicationAdd BLAST27

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
D88213 mRNA Translation: BAA19001.1
AB012943 Genomic DNA Translation: BAA32590.1
AB012943 Genomic DNA Translation: BAA32589.1
AF081363 mRNA Translation: AAD39345.1
DQ060035 Genomic DNA Translation: AAY43129.1
AC016889 Genomic DNA No translation available.
CH471152 Genomic DNA Translation: EAW60895.1
BC142641 mRNA Translation: AAI42642.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11443.1 [O75106-1]
CCDS45690.1 [O75106-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001149.2, NM_001158.4 [O75106-2]
NP_033720.2, NM_009590.3 [O75106-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000253799.8; ENSP00000253799.2; ENSG00000131480.9
ENST00000452774.2; ENSP00000406134.1; ENSG00000131480.9 [O75106-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
314

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:314

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000253799.8; ENSP00000253799.2; NM_009590.4; NP_033720.2

UCSC genome browser

More...
UCSCi
uc002ibt.5, human [O75106-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88213 mRNA Translation: BAA19001.1
AB012943 Genomic DNA Translation: BAA32590.1
AB012943 Genomic DNA Translation: BAA32589.1
AF081363 mRNA Translation: AAD39345.1
DQ060035 Genomic DNA Translation: AAY43129.1
AC016889 Genomic DNA No translation available.
CH471152 Genomic DNA Translation: EAW60895.1
BC142641 mRNA Translation: AAI42642.1
CCDSiCCDS11443.1 [O75106-1]
CCDS45690.1 [O75106-2]
RefSeqiNP_001149.2, NM_001158.4 [O75106-2]
NP_033720.2, NM_009590.3 [O75106-1]

3D structure databases

AlphaFoldDBiO75106
SMRiO75106
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi106811, 22 interactors
IntActiO75106, 5 interactors
STRINGi9606.ENSP00000253799

Chemistry databases

BindingDBiO75106
ChEMBLiCHEMBL4112

PTM databases

GlyConnecti1714, 2 N-Linked glycans (1 site)
GlyGeniO75106, 5 sites, 2 N-linked glycans (1 site)
iPTMnetiO75106
PhosphoSitePlusiO75106

Genetic variation databases

BioMutaiAOC2

Proteomic databases

jPOSTiO75106
MassIVEiO75106
PaxDbiO75106
PeptideAtlasiO75106
PRIDEiO75106
ProteomicsDBi49761 [O75106-1]
49762 [O75106-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
17156, 81 antibodies from 17 providers

The DNASU plasmid repository

More...
DNASUi
314

Genome annotation databases

EnsembliENST00000253799.8; ENSP00000253799.2; ENSG00000131480.9
ENST00000452774.2; ENSP00000406134.1; ENSG00000131480.9 [O75106-2]
GeneIDi314
KEGGihsa:314
MANE-SelectiENST00000253799.8; ENSP00000253799.2; NM_009590.4; NP_033720.2
UCSCiuc002ibt.5, human [O75106-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
314
DisGeNETi314

GeneCards: human genes, protein and diseases

More...
GeneCardsi
AOC2
HGNCiHGNC:549, AOC2
HPAiENSG00000131480, Low tissue specificity
MIMi602268, gene
neXtProtiNX_O75106
OpenTargetsiENSG00000131480
PharmGKBiPA24839
VEuPathDBiHostDB:ENSG00000131480

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1186, Eukaryota
GeneTreeiENSGT00950000183207
HOGENOMiCLU_015739_1_0_1
InParanoidiO75106
OMAiQDFSKFF
OrthoDBi1320015at2759
PhylomeDBiO75106
TreeFamiTF314750

Enzyme and pathway databases

BRENDAi1.4.3.21, 2681
PathwayCommonsiO75106
ReactomeiR-HSA-211945, Phase I - Functionalization of compounds
SABIO-RKiO75106
SignaLinkiO75106

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
314, 13 hits in 1065 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
314
PharosiO75106, Tchem

Protein Ontology

More...
PROi
PR:O75106
RNActiO75106, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000131480, Expressed in blood and 122 other tissues
GenevisibleiO75106, HS

Family and domain databases

Gene3Di2.70.98.20, 1 hit
InterProiView protein in InterPro
IPR032952, AOC2
IPR000269, Cu_amine_oxidase
IPR015798, Cu_amine_oxidase_C
IPR036460, Cu_amine_oxidase_C_sf
IPR016182, Cu_amine_oxidase_N-reg
IPR015800, Cu_amine_oxidase_N2
IPR015802, Cu_amine_oxidase_N3
PANTHERiPTHR10638, PTHR10638, 1 hit
PTHR10638:SF4, PTHR10638:SF4, 1 hit
PfamiView protein in Pfam
PF01179, Cu_amine_oxid, 1 hit
PF02727, Cu_amine_oxidN2, 1 hit
PF02728, Cu_amine_oxidN3, 1 hit
PRINTSiPR00766, CUDAOXIDASE
SUPFAMiSSF49998, SSF49998, 1 hit
SSF54416, SSF54416, 2 hits
PROSITEiView protein in PROSITE
PS01164, COPPER_AMINE_OXID_1, 1 hit
PS01165, COPPER_AMINE_OXID_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiAOC2_HUMAN
<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: O75106
Secondary accession number(s): A5PKW2
, O00120, O75105, Q4TTW5, Q9UNY0
<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: July 15, 1999
Last sequence update: January 24, 2006
Last modified: May 25, 2022
This is version 179 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again