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Q16853

- AOC3_HUMAN

UniProt

Q16853 - AOC3_HUMAN

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Protein

Membrane primary amine oxidase

Gene

AOC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis.4 Publications

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • L-topaquinoneNote: Contains 1 topaquinone per subunit.

Kineticsi

  1. KM=1.94 mM for 2-phenylethylamine1 Publication
  2. KM=0.67 mM for methylamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei386 – 3861Proton acceptorBy similarity
Active sitei471 – 4711Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi520 – 5201Copper1 Publication
Metal bindingi522 – 5221Copper1 Publication
Metal bindingi529 – 5291Calcium 1
Metal bindingi530 – 5301Calcium 1; via carbonyl oxygen
Metal bindingi531 – 5311Calcium 1
Metal bindingi572 – 5721Calcium 2
Metal bindingi638 – 6381Calcium 2
Metal bindingi663 – 6631Calcium 2; via carbonyl oxygen
Metal bindingi665 – 6651Calcium 2
Metal bindingi667 – 6671Calcium 2
Metal bindingi673 – 6731Calcium 1
Metal bindingi674 – 6741Calcium 1; via carbonyl oxygen
Metal bindingi684 – 6841Copper1 Publication

GO - Molecular functioni

  1. aliphatic-amine oxidase activity Source: UniProtKB-EC
  2. aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
  3. calcium ion binding Source: UniProtKB
  4. cation channel activity Source: UniProtKB
  5. copper ion binding Source: UniProtKB
  6. phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
  7. primary amine oxidase activity Source: UniProtKB
  8. protein heterodimerization activity Source: UniProtKB
  9. protein homodimerization activity Source: UniProtKB
  10. quinone binding Source: UniProtKB
  11. tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

GO - Biological processi

  1. amine metabolic process Source: UniProtKB
  2. cation transmembrane transport Source: GOC
  3. cation transport Source: GOC
  4. cell adhesion Source: UniProtKB
  5. inflammatory response Source: UniProtKB
  6. response to antibiotic Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

SABIO-RKQ16853.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane primary amine oxidase (EC:1.4.3.21)
Alternative name(s):
Copper amine oxidase
HPAO
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
Vascular adhesion protein 1
Short name:
VAP-1
Gene namesi
Name:AOC3
Synonyms:VAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:550. AOC3.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 54CytoplasmicSequence Analysis
Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 763737ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. integral component of membrane Source: UniProtKB
  4. microvillus Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2111M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. 1 Publication
Mutagenesisi394 – 3941Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. 1 Publication
Mutagenesisi469 – 4691L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. 1 Publication

Organism-specific databases

PharmGKBiPA24840.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 763762Membrane primary amine oxidasePRO_0000064102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi137 – 1371N-linked (GlcNAc...)2 Publications
Disulfide bondi198 ↔ 1991 Publication
Glycosylationi212 – 2121O-linked (GalNAc...)1 Publication
Glycosylationi232 – 2321N-linked (GlcNAc...)1 Publication
Glycosylationi294 – 2941N-linked (GlcNAc...)2 Publications
Modified residuei471 – 47112',4',5'-topaquinone
Glycosylationi592 – 5921N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi618 – 6181N-linked (GlcNAc...)3 Publications
Glycosylationi666 – 6661N-linked (GlcNAc...)3 Publications
Disulfide bondi734 ↔ 7411 Publication
Disulfide bondi748 – 748Interchain1 Publication

Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
N- and O-glycosylated.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiQ16853.
PeptideAtlasiQ16853.
PRIDEiQ16853.

Expressioni

Tissue specificityi

Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung.3 Publications

Inductioni

Up-regulated during in vitro adipocyte differentiation.1 Publication

Gene expression databases

BgeeiQ16853.
CleanExiHS_AOC3.
ExpressionAtlasiQ16853. baseline and differential.
GenevestigatoriQ16853.

Organism-specific databases

HPAiCAB025797.
HPA000980.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Can heterodimerize with isoform 2 leading to reduced surface expression. Forms a heterodimer with AOC2.3 Publications

Protein-protein interaction databases

BioGridi114192. 2 interactions.
IntActiQ16853. 2 interactions.
STRINGi9606.ENSP00000312326.

Structurei

Secondary structure

1
763
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 7814Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 883Combined sources
Beta strandi93 – 10210Combined sources
Helixi106 – 11510Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi137 – 1448Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi151 – 1544Combined sources
Helixi156 – 1605Combined sources
Helixi166 – 1683Combined sources
Helixi173 – 18513Combined sources
Helixi188 – 1914Combined sources
Helixi192 – 1998Combined sources
Turni203 – 2064Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi234 – 2363Combined sources
Helixi238 – 2403Combined sources
Beta strandi242 – 2509Combined sources
Beta strandi253 – 2553Combined sources
Helixi256 – 2583Combined sources
Beta strandi260 – 2667Combined sources
Beta strandi269 – 2724Combined sources
Helixi274 – 2829Combined sources
Turni283 – 2853Combined sources
Turni298 – 3003Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi329 – 34214Combined sources
Turni343 – 3453Combined sources
Beta strandi346 – 3549Combined sources
Beta strandi357 – 37216Combined sources
Helixi377 – 3804Combined sources
Beta strandi383 – 3853Combined sources
Helixi386 – 3883Combined sources
Turni391 – 3944Combined sources
Turni400 – 4023Combined sources
Beta strandi408 – 42114Combined sources
Beta strandi423 – 44523Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 46818Combined sources
Beta strandi471 – 4799Combined sources
Turni481 – 4833Combined sources
Beta strandi485 – 4939Combined sources
Beta strandi497 – 4993Combined sources
Beta strandi506 – 5127Combined sources
Beta strandi515 – 5184Combined sources
Beta strandi520 – 53011Combined sources
Beta strandi534 – 55118Combined sources
Beta strandi554 – 56916Combined sources
Helixi572 – 5754Combined sources
Beta strandi577 – 5815Combined sources
Beta strandi585 – 59410Combined sources
Beta strandi600 – 6089Combined sources
Beta strandi617 – 6193Combined sources
Helixi622 – 6298Combined sources
Beta strandi630 – 6367Combined sources
Turni647 – 6515Combined sources
Beta strandi653 – 6553Combined sources
Helixi660 – 6634Combined sources
Beta strandi670 – 68415Combined sources
Helixi688 – 6903Combined sources
Beta strandi700 – 71314Combined sources
Helixi715 – 7184Combined sources
Beta strandi723 – 7297Combined sources
Turni734 – 7363Combined sources
Helixi738 – 7414Combined sources
Helixi742 – 7454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PU4X-ray3.20A/B1-763[»]
1US1X-ray2.90A/B1-763[»]
2C10X-ray2.50A/B/C/D29-763[»]
2C11X-ray2.90A/B/C/D29-763[»]
2Y73X-ray2.60A/B1-763[»]
2Y74X-ray2.95A/B1-763[»]
3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
4BTWX-ray2.80A/B27-763[»]
4BTXX-ray2.78A/B27-763[»]
4BTYX-ray3.10A/B27-763[»]
ProteinModelPortaliQ16853.
SMRiQ16853. Positions 58-761.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16853.

Family & Domainsi

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3733.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ16853.
KOiK00276.
OMAiSWERYQL.
OrthoDBiEOG7353W8.
PhylomeDBiQ16853.
TreeFamiTF314750.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSiPR00766. CUDAOXIDASE.
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16853-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' 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
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP
60 70 80 90 100
WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE
110 120 130 140 150
LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS
160 170 180 190 200
YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF
210 220 230 240 250
YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN
260 270 280 290 300
HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW
310 320 330 340 350
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF
360 370 380 390 400
DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR
410 420 430 440 450
GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH
460 470 480 490 500
YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL
510 520 530 540 550
FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA
560 570 580 590 600
VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP
610 620 630 640 650
RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ
660 670 680 690 700
NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG
710 720 730 740 750
VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP
760
DLPAFSHGGF SHN
Length:763
Mass (Da):84,622
Last modified:January 23, 2007 - v3
Checksum:i58AD55605EC9D228
GO
Isoform 2 (identifier: Q16853-2) [UniParc]FASTAAdd to Basket

Also known as: VAP-1Delta3

The sequence of this isoform differs from the canonical sequence as follows:
     630-634: YQLAV → IWWPG
     635-763: Missing.

Note: Devoid of the semicarbazide-sensitive amine oxidase (SSAO) activity.

Show »
Length:634
Mass (Da):70,675
Checksum:i3275AE7C61775C99
GO
Isoform 3 (identifier: Q16853-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-543: Missing.

Note: No experimental confirmation available.

Show »
Length:220
Mass (Da):24,533
Checksum:i37CB1D564AC233E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51T → R.1 Publication
Corresponds to variant rs33954211 [ dbSNP | Ensembl ].
VAR_025035
Natural varianti78 – 781R → Q.
Corresponds to variant rs402680 [ dbSNP | Ensembl ].
VAR_052603
Natural varianti167 – 1671H → Y.1 Publication
Corresponds to variant rs2228470 [ dbSNP | Ensembl ].
VAR_025027
Natural varianti171 – 1711V → M.
Corresponds to variant rs408038 [ dbSNP | Ensembl ].
VAR_052604
Natural varianti203 – 2031H → R.
Corresponds to variant rs630079 [ dbSNP | Ensembl ].
VAR_052605
Natural varianti317 – 3171Y → H.
Corresponds to variant rs438287 [ dbSNP | Ensembl ].
VAR_012064
Natural varianti329 – 3291R → Q.
Corresponds to variant rs2229595 [ dbSNP | Ensembl ].
VAR_024343
Natural varianti371 – 3711I → T.1 Publication
Corresponds to variant rs35097308 [ dbSNP | Ensembl ].
VAR_025028
Natural varianti408 – 4081A → S.1 Publication
Corresponds to variant rs35643019 [ dbSNP | Ensembl ].
VAR_025029
Natural varianti426 – 4261R → H.1 Publication
Corresponds to variant rs33986943 [ dbSNP | Ensembl ].
VAR_025030
Natural varianti441 – 4411R → W.1 Publication
Corresponds to variant rs2229596 [ dbSNP | Ensembl ].
VAR_025031
Natural varianti582 – 5821A → T.1 Publication
Corresponds to variant rs34987927 [ dbSNP | Ensembl ].
VAR_025032
Natural varianti700 – 7001G → S.1 Publication
Corresponds to variant rs477207 [ dbSNP | Ensembl ].
VAR_025033
Natural varianti749 – 7491A → V.1 Publication
Corresponds to variant rs34012919 [ dbSNP | Ensembl ].
VAR_025034

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 543543Missing in isoform 3. 1 PublicationVSP_055201Add
BLAST
Alternative sequencei630 – 6345YQLAV → IWWPG in isoform 2. 1 PublicationVSP_053751
Alternative sequencei635 – 763129Missing in isoform 2. 1 PublicationVSP_053752Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39447 mRNA. Translation: AAC50919.1.
AF067406 mRNA. Translation: AAC25170.1.
AB050502 Genomic DNA. Translation: BAB18866.1.
JX020506 mRNA. Translation: AGB67480.1.
AK025727 mRNA. No translation available.
AK315129 mRNA. Translation: BAG37582.1.
DQ143944 Genomic DNA. Translation: AAZ38716.1.
AC016889 Genomic DNA. No translation available.
BC050549 mRNA. Translation: AAH50549.1.
CCDSiCCDS11444.1. [Q16853-1]
CCDS62198.1. [Q16853-3]
CCDS74071.1. [Q16853-2]
PIRiJC5234.
RefSeqiNP_001264660.1. NM_001277731.1. [Q16853-2]
NP_001264661.1. NM_001277732.1. [Q16853-3]
NP_003725.1. NM_003734.3. [Q16853-1]
UniGeneiHs.198241.

Genome annotation databases

EnsembliENST00000308423; ENSP00000312326; ENSG00000131471. [Q16853-1]
ENST00000591562; ENSP00000468632; ENSG00000131471. [Q16853-3]
ENST00000613571; ENSP00000484312; ENSG00000131471. [Q16853-2]
ENST00000617500; ENSP00000477686; ENSG00000131471. [Q16853-3]
GeneIDi8639.
KEGGihsa:8639.
UCSCiuc002ibv.4. human. [Q16853-1]

Polymorphism databases

DMDMi2501336.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39447 mRNA. Translation: AAC50919.1 .
AF067406 mRNA. Translation: AAC25170.1 .
AB050502 Genomic DNA. Translation: BAB18866.1 .
JX020506 mRNA. Translation: AGB67480.1 .
AK025727 mRNA. No translation available.
AK315129 mRNA. Translation: BAG37582.1 .
DQ143944 Genomic DNA. Translation: AAZ38716.1 .
AC016889 Genomic DNA. No translation available.
BC050549 mRNA. Translation: AAH50549.1 .
CCDSi CCDS11444.1. [Q16853-1 ]
CCDS62198.1. [Q16853-3 ]
CCDS74071.1. [Q16853-2 ]
PIRi JC5234.
RefSeqi NP_001264660.1. NM_001277731.1. [Q16853-2 ]
NP_001264661.1. NM_001277732.1. [Q16853-3 ]
NP_003725.1. NM_003734.3. [Q16853-1 ]
UniGenei Hs.198241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PU4 X-ray 3.20 A/B 1-763 [» ]
1US1 X-ray 2.90 A/B 1-763 [» ]
2C10 X-ray 2.50 A/B/C/D 29-763 [» ]
2C11 X-ray 2.90 A/B/C/D 29-763 [» ]
2Y73 X-ray 2.60 A/B 1-763 [» ]
2Y74 X-ray 2.95 A/B 1-763 [» ]
3ALA X-ray 2.90 A/B/C/D/E/F/G 33-763 [» ]
4BTW X-ray 2.80 A/B 27-763 [» ]
4BTX X-ray 2.78 A/B 27-763 [» ]
4BTY X-ray 3.10 A/B 27-763 [» ]
ProteinModelPortali Q16853.
SMRi Q16853. Positions 58-761.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114192. 2 interactions.
IntActi Q16853. 2 interactions.
STRINGi 9606.ENSP00000312326.

Chemistry

BindingDBi Q16853.
ChEMBLi CHEMBL3437.
DrugBanki DB01275. Hydralazine.
DB00780. Phenelzine.
GuidetoPHARMACOLOGYi 2767.

Polymorphism databases

DMDMi 2501336.

Proteomic databases

PaxDbi Q16853.
PeptideAtlasi Q16853.
PRIDEi Q16853.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308423 ; ENSP00000312326 ; ENSG00000131471 . [Q16853-1 ]
ENST00000591562 ; ENSP00000468632 ; ENSG00000131471 . [Q16853-3 ]
ENST00000613571 ; ENSP00000484312 ; ENSG00000131471 . [Q16853-2 ]
ENST00000617500 ; ENSP00000477686 ; ENSG00000131471 . [Q16853-3 ]
GeneIDi 8639.
KEGGi hsa:8639.
UCSCi uc002ibv.4. human. [Q16853-1 ]

Organism-specific databases

CTDi 8639.
GeneCardsi GC17P041003.
HGNCi HGNC:550. AOC3.
HPAi CAB025797.
HPA000980.
MIMi 603735. gene.
neXtProti NX_Q16853.
PharmGKBi PA24840.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3733.
GeneTreei ENSGT00510000046461.
HOGENOMi HOG000233919.
HOVERGENi HBG004164.
InParanoidi Q16853.
KOi K00276.
OMAi SWERYQL.
OrthoDBi EOG7353W8.
PhylomeDBi Q16853.
TreeFami TF314750.

Enzyme and pathway databases

SABIO-RK Q16853.

Miscellaneous databases

EvolutionaryTracei Q16853.
GeneWikii AOC3.
GenomeRNAii 8639.
NextBioi 32389.
PROi Q16853.
SOURCEi Search...

Gene expression databases

Bgeei Q16853.
CleanExi HS_AOC3.
ExpressionAtlasi Q16853. baseline and differential.
Genevestigatori Q16853.

Family and domain databases

Gene3Di 2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
InterProi IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view ]
PANTHERi PTHR10638. PTHR10638. 1 hit.
Pfami PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view ]
PRINTSi PR00766. CUDAOXIDASE.
SUPFAMi SSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEi PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a copper-containing, topaquinone-containing monoamine oxidase from human placenta."
    Zhang X., McIntire W.S.
    Gene 179:279-286(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule."
    Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.
    J. Exp. Med. 188:17-27(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Lung.
  3. "Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina."
    Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.
    Gene 318:45-53(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Functional modulation of vascular adhesion protein-1 by a novel splice variant."
    Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.
    PLoS ONE 8:E54151-E54151(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Placenta.
  6. NIEHS SNPs program
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-5; TYR-167; THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
  7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: PNS.
  9. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 79-90 AND 123-132.
    Tissue: Adipocyte.
  10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666.
    Tissue: Plasma.
  11. "Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes."
    Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A., Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.
    Biochimie 89:916-925(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  12. "The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase."
    Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T., Salmi M., Jalkanen S., Elima K.
    Cell. Mol. Life Sci. 66:2743-2757(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211; TYR-394 AND LEU-469.
  13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618 AND ASN-666.
    Tissue: Liver.
  14. Cited for: GLYCOSYLATION AT ASN-592.
  15. "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications."
    Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.
    Protein Sci. 14:1964-1974(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.

Entry informationi

Entry nameiAOC3_HUMAN
AccessioniPrimary (citable) accession number: Q16853
Secondary accession number(s): B2RCI5
, K7ESB3, L0L8N9, Q45F94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3