ODC1
entrez
4953
canonical
uniprot
P11926
canonical
ensembl
ENSG00000115758
resolver
ensp
ENSP00000234111
resolver
ensp
ENSP00000385333
resolver
ensp
ENSP00000390691
resolver
ensp
ENSP00000514633
resolver
ensp
ENSP00000514634
resolver
ensp
ENSP00000557560
resolver
ensp
ENSP00000557561
resolver
ensp
ENSP00000557562
resolver
ensp
ENSP00000557563
resolver
ensp
ENSP00000557564
resolver
ensp
ENSP00000557565
resolver
ensp
ENSP00000557566
resolver
ensp
ENSP00000596786
resolver
ensp
ENSP00000596788
resolver
ensp
ENSP00000623480
resolver
ensp
ENSP00000623481
resolver
ensp
ENSP00000623482
resolver
ensp
ENSP00000623483
resolver
enst
ENST00000234111
resolver
enst
ENST00000405333
resolver
enst
ENST00000443218
resolver
enst
ENST00000699835
resolver
enst
ENST00000699836
resolver
enst
ENST00000887501
resolver
enst
ENST00000887502
resolver
enst
ENST00000887503
resolver
enst
ENST00000887504
resolver
enst
ENST00000887505
resolver
enst
ENST00000887506
resolver
enst
ENST00000887507
resolver
enst
ENST00000926727
resolver
enst
ENST00000926729
resolver
enst
ENST00000953421
resolver
enst
ENST00000953422
resolver
enst
ENST00000953423
resolver
enst
ENST00000953424
resolver
genesymbol
ODC1
resolver
hgnc
HGNC:8109
resolver
uniprot
B4DXF8
resolver
uniprot
Q53TU3
resolver
uniprot
Q6LDS9
resolver
uniprot_entry
B4DXF8_HUMAN
resolver
uniprot_entry
DCOR_HUMAN
resolver
uniprot_sec
Q53TU3
resolver
uniprot_sec
Q6LDS9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by S-nitrosylation (PubMed:10462479, PubMed:11461922). Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3 in response to polyamine levels. AZs inhibit the assembly of the functional homodimer by binding to ODC monomers. Additionally, OAZ1 targets ODC monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (PubMed:17900240). Inhibited by 1-amino-oxy-3-aminopropane (APA, an isosteric analog of putrescine) (PubMed:17407445). Irreversibly inhibited by alpha-difluoromethylornithine (DFMO) (PubMed:17407445). {ECO:0000269|PubMed:10462479, ECO:0000269|PubMed:11461922, ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:17900240}.
uniprot
proteins
amino_acid_sequence
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
uniprot
proteins
disease_involvement
DISEASE: Bachmann-Bupp syndrome (BABS) [MIM:619075]: An autosomal dominant disorder characterized by global developmental delay, alopecia, absolute or relative macrocephaly, and facial dysmorphism. Neuroimaging shows white matter abnormalities, prominent Virchow-Robin spaces, periventricular cysts, and abnormalities of the corpus callosum. {ECO:0000269|PubMed:30239107, ECO:0000269|PubMed:30475435}. Note=The disease is caused by variants affecting the gene represented in this entry. BABS is due to truncating variants that lead to a gain of function. This phenomenon apparently results from truncation proximal to or involving the C-terminal region of ODC1 protein, distal enough to allow escape from nonsense-mediated decay. A gain of function is corroborated by elevated plasma levels of N-acetylputrescine, with otherwise normal polyamine levels, in affected individuals. {ECO:0000269|PubMed:30475435}.
uniprot
proteins
ec_number
4.1.1.17
uniprot
proteins
function
FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. {ECO:0000269|PubMed:17900240}.
uniprot
proteins
mass_dalton
51148
uniprot
proteins
mutagenesis
MUTAGEN 360; /note="C->A: 25% decrease of in vitro nitrosylation level."; /evidence="ECO:0000269|PubMed:11461922
uniprot
proteins
pathway_participation
PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
uniprot
proteins
post_translational_modification
PTM: S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues. {ECO:0000269|PubMed:10462479, ECO:0000269|PubMed:11461922}.
uniprot
proteins
protein_family
Orn/Lys/Arg decarboxylase class-II family
uniprot
proteins
pubmed
10462479
uniprot
proteins
pubmed
10623504
uniprot
proteins
pubmed
11461922
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
1598217
uniprot
proteins
pubmed
16548883
uniprot
proteins
pubmed
17407445
uniprot
proteins
pubmed
17900240
uniprot
proteins
pubmed
2227439
uniprot
proteins
pubmed
2317811
uniprot
proteins
pubmed
2318872
uniprot
proteins
pubmed
2587220
uniprot
proteins
pubmed
26305948
uniprot
proteins
pubmed
26443277
uniprot
proteins
pubmed
2693021
uniprot
proteins
pubmed
30239107
uniprot
proteins
pubmed
30475435
uniprot
proteins
pubmed
3308908
uniprot
proteins
pubmed
3595418
uniprot
proteins
pubmed
8519686
uniprot
proteins
sequence_length
461
uniprot
proteins