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P11926 (DCOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine decarboxylase

Short name=ODC
EC=4.1.1.17
Gene names
Name:ODC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-ornithine = putrescine + CO2.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by S-nitrosylation.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.

Subunit structure

Homodimer.

Induction

Down-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.18

Post-translational modification

S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues.

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Ornithine decarboxylase
PRO_0000149891

Sites

Active site3601Proton donor; shared with dimeric partner

Amino acid modifications

Modified residue691N6-(pyridoxal phosphate)lysine
Modified residue3031Phosphoserine; by CK2 By similarity
Modified residue3601S-nitrosocysteine; in inhibited form Probable

Experimental info

Mutagenesis3601C → A: 25% decrease of in vitro nitrosylation level. Ref.17

Secondary structure

............................................................................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11926 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 8CCB88CE80E823C5

FASTA46151,148
        10         20         30         40         50         60 
MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP 

        70         80         90        100        110        120 
RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI 

       130        140        150        160        170        180 
KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLRTSRLL 

       190        200        210        220        230        240 
LERAKELNID VVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG 

       250        260        270        280        290        300 
SEDVKLKFEE ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ 

       310        320        330        340        350        360 
TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC 

       370        380        390        400        410        420 
DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPAWQLMQQF 

       430        440        450        460 
QNPDFPPEVE EQDASTLPVS CAWESGMKRH RAACASASIN V 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA."
Hickok N.J., Seppaenen P.J., Gunsalus G.L., Jaenne O.A.
DNA 6:179-187(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Jaenne O.A.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 415.
[3]"Characterization and sequence analysis of the human ornithine decarboxylase gene."
Fitzgerald M.C., Flanagan M.A.
DNA 8:623-634(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Nucleotide sequence of the human ornithine decarboxylase gene."
van Steeg H., van Oostrom C.T.M., Martens J.W.M., van Kreyl C.F., Schepens J., Wieringa B.
Nucleic Acids Res. 17:8855-8856(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene."
Hickok N.J., Wahlfors J., Crozat A., Halmekytoe M., Alhonen L., Jaenne J., Jaenne O.A.
Gene 93:257-263(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Isolation and expression of a human ornithine decarboxylase gene."
Moshier J.A., Gilbert J.D., Skunca M., Dosescu J., Almodovar K.M., Luk G.D.
J. Biol. Chem. 265:4884-4892(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells."
Moshier J.A., Osborne D.L., Skunca M., Dosescu J., Gilbert J.D., Fitzgerald M.C., Polidori G., Wagner R.L., Friezner Degen S.J., Luk G.D., Flanagan M.A.
Nucleic Acids Res. 20:2581-2590(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element."
Wright P.S., Cooper J.R., Cross-Doersen D.E., Miller J.A., Chmielewski P.A., Wagner R.L., Streng K.A., Flanagan M.A.
Cell Growth Differ. 6:1097-1102(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]"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. expand/collapse author list , 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].
Tissue: Esophagus and Testis.
[10]NIEHS SNPs program
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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].
Tissue: Lymph.
[14]"Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells."
Hsieh J.T., Denning M.F., Heidel S.M., Verma A.K.
Cancer Res. 50:2239-2244(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
[15]"Cell-cycle-dependent expression of human ornithine decarboxylase."
Kaczmarek L., Calabretta B., Ferrari S., de Riel J.K.
J. Cell. Physiol. 132:545-551(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-461.
[16]"Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation."
Bauer P.M., Fukuto J.M., Buga G.M., Pegg A.E., Ignarro L.J.
Biochem. Biophys. Res. Commun. 262:355-358(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION.
[17]"Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme."
Bauer P.M., Buga G.M., Fukuto J.M., Pegg A.E., Ignarro L.J.
J. Biol. Chem. 276:34458-34464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-360, MUTAGENESIS OF CYS-360.
[18]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding."
Almrud J.J., Oliveira M.A., Kern A.D., Grishin N.V., Phillips M.A., Hackert M.L.
J. Mol. Biol. 295:7-16(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Ornithine decarboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16650 mRNA. Translation: AAA59966.2.
M31061 Genomic DNA. Translation: AAA60563.1.
X16277 Genomic DNA. Translation: CAA34353.1.
M33764 Genomic DNA. Translation: AAA60564.1.
M34158 Genomic DNA. Translation: AAA59969.1.
M81740 Genomic DNA. Translation: AAA59967.1.
X55362 mRNA. Translation: CAA39047.1.
AK292352 mRNA. Translation: BAF85041.1.
AK312766 mRNA. Translation: BAG35632.1.
AY841870 Genomic DNA. Translation: AAV88093.1.
AC007249 Genomic DNA. Translation: AAY15034.1.
CH471053 Genomic DNA. Translation: EAX00958.1.
CH471053 Genomic DNA. Translation: EAX00959.1.
BC025296 mRNA. Translation: AAH25296.1.
X53271 mRNA. Translation: CAA37369.1.
M20372 mRNA. Translation: AAA59968.1.
PIRDCHUO. S06900.
RefSeqNP_001274118.1. NM_001287189.1.
NP_001274119.1. NM_001287190.1.
NP_002530.1. NM_002539.2.
UniGeneHs.467701.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7KX-ray2.10A/B7-427[»]
2ON3X-ray3.00A/B1-461[»]
2OO0X-ray1.90A/B1-461[»]
ProteinModelPortalP11926.
SMRP11926. Positions 7-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111007. 9 interactions.
IntActP11926. 3 interactions.
MINTMINT-1208473.
STRING9606.ENSP00000234111.

Chemistry

BindingDBP11926.
ChEMBLCHEMBL1869.
DrugBankDB00114. Pyridoxal Phosphate.
DB00127. Spermine.
GuidetoPHARMACOLOGY1276.

PTM databases

PhosphoSiteP11926.

Polymorphism databases

DMDM118377.

Proteomic databases

PaxDbP11926.
PRIDEP11926.

Protocols and materials databases

DNASU4953.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234111; ENSP00000234111; ENSG00000115758.
ENST00000405333; ENSP00000385333; ENSG00000115758.
GeneID4953.
KEGGhsa:4953.
UCSCuc002rao.1. human.

Organism-specific databases

CTD4953.
GeneCardsGC02M010580.
HGNCHGNC:8109. ODC1.
HPACAB035996.
HPA001536.
MIM165640. gene.
neXtProtNX_P11926.
PharmGKBPA31897.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000274133.
HOVERGENHBG005456.
InParanoidP11926.
KOK01581.
OMACDGLDCV.
OrthoDBEOG73Z2T6.
PhylomeDBP11926.
TreeFamTF300760.

Enzyme and pathway databases

BioCycMetaCyc:HS03935-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP11926.
UniPathwayUPA00535; UER00288.

Gene expression databases

ArrayExpressP11926.
BgeeP11926.
CleanExHS_ODC1.
GenevestigatorP11926.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR002433. Orn_de-COase.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSODC1. human.
EvolutionaryTraceP11926.
GeneWikiODC1.
GenomeRNAi4953.
NextBio19080.
PROP11926.
SOURCESearch...

Entry information

Entry nameDCOR_HUMAN
AccessionPrimary (citable) accession number: P11926
Secondary accession number(s): Q53TU3, Q6LDS9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM