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Protein

Ornithine decarboxylase antizyme 1

Gene

OAZ1

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

Functioni

Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to and targeting ODC1 for degradation (PubMed:17900240). Stabilizes AZIN2 by interfering with its ubiquitination. Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol.2 Publications

GO - Molecular functioni

  • ornithine decarboxylase inhibitor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Polyamine biosynthesis, Transport

Enzyme and pathway databases

ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase antizyme 1
Short name:
ODC-Az
Gene namesi
Name:OAZ1
Synonyms:OAZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:8095. OAZ1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31884.

Chemistry

DrugBankiDB00129. L-Ornithine.

Polymorphism and mutation databases

BioMutaiOAZ1.
DMDMi1709427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 228227Ornithine decarboxylase antizyme 1PRO_0000220849Add
BLAST

Proteomic databases

EPDiP54368.
PaxDbiP54368.
PeptideAtlasiP54368.
PRIDEiP54368.

PTM databases

iPTMnetiP54368.

Expressioni

Gene expression databases

BgeeiP54368.
CleanExiHS_OAZ1.
ExpressionAtlasiP54368. baseline and differential.
GenevisibleiP54368. HS.

Organism-specific databases

HPAiHPA009291.

Interactioni

Subunit structurei

Forms a ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with AZIN2; the interaction stabilizes the complex by inhibiting AZIN2 ubiquitination and degradation and leads to increased ornithine decarboxylase (ODC) activity and decreased rate of ODC1 degradation.2 Publications

Protein-protein interaction databases

BioGridi111000. 21 interactions.
IntActiP54368. 17 interactions.
MINTiMINT-2861418.
STRINGi9606.ENSP00000464146.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi96 – 1005Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi128 – 1358Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi145 – 1473Combined sources
Helixi152 – 16514Combined sources
Beta strandi170 – 17910Combined sources
Helixi183 – 19311Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi211 – 2177Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZGYX-ray2.63B95-219[»]
4ZGZX-ray5.81B/D110-228[»]
5BWAX-ray3.20B69-228[»]
ProteinModelPortaliP54368.
SMRiP54368. Positions 94-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ODC antizyme family.Curated

Phylogenomic databases

eggNOGiKOG4387. Eukaryota.
ENOG4112791. LUCA.
GeneTreeiENSGT00390000009476.
HOGENOMiHOG000115253.
HOVERGENiHBG007857.
InParanoidiP54368.
KOiK16548.
OMAiAKHITWR.
PhylomeDBiP54368.
TreeFamiTF314741.

Family and domain databases

InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR029914. ODC-AZ_1.
IPR002993. ODC_AZ.
[Graphical view]
PANTHERiPTHR10279. PTHR10279. 1 hit.
PTHR10279:SF8. PTHR10279:SF8. 1 hit.
PfamiPF02100. ODC_AZ. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS01337. ODC_AZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by ribosomal frameshifting. AlignAdd to basket

Note: A ribosomal frameshift occurs between the codons for Ser-68 and Asp-69. An autoregulatory mechanism enables modulation of frameshifting according to the cellular concentration of polyamines.

Isoform 1 (identifier: P54368-1) [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
MVKSSLQRIL NSHCFAREKE GDKPSATIHA SRTMPLLSLH SRGGSSSESS
60 70 80 90 100
RVSLHCCSNP GPGPRWCSDA PHPPLKIPGG RGNSQRDHNL SANLFYSDDR
110 120 130 140 150
LNVTEELTSN DKTRILNVQS RLTDAKRINW RTVLSGGSLY IEIPGGALPE
160 170 180 190 200
GSKDSFAVLL EFAEEQLRAD HVFICFHKNR EDRAALLRTF SFLGFEIVRP
210 220
GHPLVPKRPD ACFMAYTFER ESSGEEEE
Length:228
Mass (Da):25,406
Last modified:January 23, 2007 - v3
Checksum:iDA43B74DF030BD9D
GO

Sequence cautioni

The sequence BAA11374.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691D → C in BAA13497 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321R → L.1 Publication
Corresponds to variant rs4667 [ dbSNP | Ensembl ].
VAR_022215
Natural varianti44 – 441G → D.1 Publication
Corresponds to variant rs28359762 [ dbSNP | Ensembl ].
VAR_022216
Natural varianti50 – 501S → F.1 Publication
Corresponds to variant rs28384673 [ dbSNP | Ensembl ].
VAR_022217
Natural varianti53 – 531S → F.1 Publication
Corresponds to variant rs2230749 [ dbSNP | Ensembl ].
VAR_022218
Natural varianti147 – 1471A → V.1 Publication
Corresponds to variant rs28384677 [ dbSNP | Ensembl ].
VAR_022219

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09202 mRNA. Translation: AAA82155.1. Sequence problems.
U09202 mRNA. Translation: AAA82154.1. Sequence problems.
D87914 mRNA. Translation: BAA13497.1.
D78361 mRNA. Translation: BAA11373.1.
D78361 mRNA. Translation: BAA11374.1. Different initiation.
D89870 Genomic DNA. Translation: BAA23101.1.
AY865622 Genomic DNA. Translation: AAW56074.1.
AC004152 Genomic DNA. Translation: AAC02802.1.
AC004152 Genomic DNA. Translation: AAC02803.1.
CCDSiCCDS58639.1. [P54368-1]
PIRiI38591.
RefSeqiNP_004143.1. NM_004152.3. [P54368-1]
UniGeneiHs.446427.

Genome annotation databases

EnsembliENST00000602676; ENSP00000473381; ENSG00000104904. [P54368-1]
GeneIDi4946.
KEGGihsa:4946.
UCSCiuc002lvk.4. human. [P54368-1]

Keywords - Coding sequence diversityi

Polymorphism, Ribosomal frameshifting

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09202 mRNA. Translation: AAA82155.1. Sequence problems.
U09202 mRNA. Translation: AAA82154.1. Sequence problems.
D87914 mRNA. Translation: BAA13497.1.
D78361 mRNA. Translation: BAA11373.1.
D78361 mRNA. Translation: BAA11374.1. Different initiation.
D89870 Genomic DNA. Translation: BAA23101.1.
AY865622 Genomic DNA. Translation: AAW56074.1.
AC004152 Genomic DNA. Translation: AAC02802.1.
AC004152 Genomic DNA. Translation: AAC02803.1.
CCDSiCCDS58639.1. [P54368-1]
PIRiI38591.
RefSeqiNP_004143.1. NM_004152.3. [P54368-1]
UniGeneiHs.446427.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZGYX-ray2.63B95-219[»]
4ZGZX-ray5.81B/D110-228[»]
5BWAX-ray3.20B69-228[»]
ProteinModelPortaliP54368.
SMRiP54368. Positions 94-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111000. 21 interactions.
IntActiP54368. 17 interactions.
MINTiMINT-2861418.
STRINGi9606.ENSP00000464146.

Chemistry

DrugBankiDB00129. L-Ornithine.

PTM databases

iPTMnetiP54368.

Polymorphism and mutation databases

BioMutaiOAZ1.
DMDMi1709427.

Proteomic databases

EPDiP54368.
PaxDbiP54368.
PeptideAtlasiP54368.
PRIDEiP54368.

Protocols and materials databases

DNASUi4946.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000602676; ENSP00000473381; ENSG00000104904. [P54368-1]
GeneIDi4946.
KEGGihsa:4946.
UCSCiuc002lvk.4. human. [P54368-1]

Organism-specific databases

CTDi4946.
GeneCardsiOAZ1.
H-InvDBHIX0040080.
HGNCiHGNC:8095. OAZ1.
HPAiHPA009291.
MIMi601579. gene.
neXtProtiNX_P54368.
PharmGKBiPA31884.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4387. Eukaryota.
ENOG4112791. LUCA.
GeneTreeiENSGT00390000009476.
HOGENOMiHOG000115253.
HOVERGENiHBG007857.
InParanoidiP54368.
KOiK16548.
OMAiAKHITWR.
PhylomeDBiP54368.
TreeFamiTF314741.

Enzyme and pathway databases

ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).

Miscellaneous databases

ChiTaRSiOAZ1. human.
GeneWikiiOAZ1.
GenomeRNAii4946.
PROiP54368.
SOURCEiSearch...

Gene expression databases

BgeeiP54368.
CleanExiHS_OAZ1.
ExpressionAtlasiP54368. baseline and differential.
GenevisibleiP54368. HS.

Family and domain databases

InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR029914. ODC-AZ_1.
IPR002993. ODC_AZ.
[Graphical view]
PANTHERiPTHR10279. PTHR10279. 1 hit.
PTHR10279:SF8. PTHR10279:SF8. 1 hit.
PfamiPF02100. ODC_AZ. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS01337. ODC_AZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme."
    Tewari D.S., Qian Y., Thornton R.D., Pieringer J., Taub R., Mochan E., Tewari M.
    Biochim. Biophys. Acta 1209:293-295(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  2. "Molecular cloning of human antizyme from brain library."
    Hideyama T., Nisiyama M., Hayashi S.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Molecular cloning of human antizyme cDNA."
    Yang D., Takii T., Hayashi H., Itoh S., Hayashi M., Onozaki K.
    Biochem. Mol. Biol. Int. 38:957-964(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  4. "Characterization of the human antizyme gene."
    Hayashi T., Matsufuji S., Hayashi S.
    Gene 203:131-139(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. NIEHS SNPs program
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-32; ASP-44; PHE-50; PHE-53 AND VAL-147.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs)."
    Lin Y., Martin J., Gruendler C., Farley J., Meng X., Li B.-Y., Lechleider R., Huff C., Kim R.H., Grasser W.A., Paralkar V., Wang T.
    BMC Cell Biol. 3:15-15(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH PSMB4 AND SMAD1, FUNCTION.
  8. "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase."
    Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.
    Biochem. J. 409:187-192(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AZIN2.

Entry informationi

Entry nameiOAZ1_HUMAN
AccessioniPrimary (citable) accession number: P54368
Secondary accession number(s): O43382
, Q14989, Q92595, Q9UPL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 127 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.