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P11926

- DCOR_HUMAN

UniProt

P11926 - DCOR_HUMAN

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Protein
Ornithine decarboxylase
Gene
ODC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-ornithine = putrescine + CO2.

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

Inhibited by S-nitrosylation.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei360 – 3601Proton donor; shared with dimeric partner

GO - Molecular functioni

  1. ornithine decarboxylase activity Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. kidney development Source: Ensembl
  3. polyamine metabolic process Source: Reactome
  4. positive regulation of cell proliferation Source: Ensembl
  5. putrescine biosynthetic process from ornithine Source: UniProtKB-UniPathway
  6. regulation of cellular amino acid metabolic process Source: Reactome
  7. response to virus Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS03935-MONOMER.
ReactomeiREACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_14820. Metabolism of polyamines.
SABIO-RKP11926.
UniPathwayiUPA00535; UER00288.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.17)
Short name:
ODC
Gene namesi
Name:ODC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:8109. ODC1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi360 – 3601C → A: 25% decrease of in vitro nitrosylation level. 1 Publication

Organism-specific databases

PharmGKBiPA31897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ornithine decarboxylase
PRO_0000149891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-(pyridoxal phosphate)lysine
Modified residuei303 – 3031Phosphoserine; by CK2 By similarity
Modified residuei360 – 3601S-nitrosocysteine; in inhibited form Inferred

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP11926.
PaxDbiP11926.
PRIDEiP11926.

PTM databases

PhosphoSiteiP11926.

Expressioni

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

ArrayExpressiP11926.
BgeeiP11926.
CleanExiHS_ODC1.
GenevestigatoriP11926.

Organism-specific databases

HPAiCAB035996.
HPA001536.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi111007. 9 interactions.
IntActiP11926. 3 interactions.
MINTiMINT-1208473.
STRINGi9606.ENSP00000234111.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 55
Turni6 – 83
Beta strandi11 – 144
Helixi20 – 3011
Turni31 – 333
Beta strandi40 – 445
Helixi45 – 5814
Beta strandi62 – 676
Helixi68 – 703
Helixi74 – 8310
Beta strandi86 – 894
Helixi92 – 1009
Helixi105 – 1073
Beta strandi108 – 1103
Helixi117 – 1259
Beta strandi130 – 1334
Helixi136 – 14510
Beta strandi150 – 1556
Beta strandi162 – 1643
Turni167 – 1693
Helixi174 – 18613
Beta strandi190 – 1956
Helixi206 – 22520
Beta strandi231 – 2333
Beta strandi240 – 2467
Helixi248 – 26215
Helixi265 – 2673
Beta strandi270 – 2734
Helixi277 – 2804
Helixi281 – 2833
Beta strandi284 – 29613
Beta strandi313 – 3197
Turni322 – 3243
Helixi325 – 3273
Helixi328 – 3314
Beta strandi339 – 3424
Beta strandi350 – 3567
Beta strandi358 – 3603
Beta strandi365 – 3739
Beta strandi380 – 3834
Beta strandi388 – 3903
Helixi391 – 3933
Helixi397 – 3993
Beta strandi404 – 4107
Helixi411 – 42010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7KX-ray2.10A/B7-427[»]
2ON3X-ray3.00A/B1-461[»]
2OO0X-ray1.90A/B1-461[»]
ProteinModelPortaliP11926.
SMRiP11926. Positions 7-427.

Miscellaneous databases

EvolutionaryTraceiP11926.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0019.
HOGENOMiHOG000274133.
HOVERGENiHBG005456.
InParanoidiP11926.
KOiK01581.
OMAiTIHYVMS.
OrthoDBiEOG73Z2T6.
PhylomeDBiP11926.
TreeFamiTF300760.

Family and domain databases

Gene3Di2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProiIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSiPR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11926-1 [UniParc]FASTAAdd to Basket

« Hide

MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK    50
KHLRWLKALP RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS 100
LGVPPERIIY ANPCKQVSQI KYAANNGVQM MTFDSEVELM KVARAHPKAK 150
LVLRIATDDS KAVCRLSVKF GATLRTSRLL LERAKELNID VVGVSFHVGS 200
GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG SEDVKLKFEE 250
ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ 300
TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY 350
YSSSIWGPTC DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF 400
QRPTIYYVMS GPAWQLMQQF QNPDFPPEVE EQDASTLPVS CAWESGMKRH 450
RAACASASIN V 461
Length:461
Mass (Da):51,148
Last modified:April 1, 1990 - v2
Checksum:i8CCB88CE80E823C5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1672.1.
PIRiS06900. DCHUO.
RefSeqiNP_001274118.1. NM_001287189.1.
NP_001274119.1. NM_001287190.1.
NP_002530.1. NM_002539.2.
UniGeneiHs.467701.

Genome annotation databases

EnsembliENST00000234111; ENSP00000234111; ENSG00000115758.
ENST00000405333; ENSP00000385333; ENSG00000115758.
GeneIDi4953.
KEGGihsa:4953.
UCSCiuc002rao.1. human.

Polymorphism databases

DMDMi118377.

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Ornithine decarboxylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1672.1.
PIRi S06900. DCHUO.
RefSeqi NP_001274118.1. NM_001287189.1.
NP_001274119.1. NM_001287190.1.
NP_002530.1. NM_002539.2.
UniGenei Hs.467701.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D7K X-ray 2.10 A/B 7-427 [» ]
2ON3 X-ray 3.00 A/B 1-461 [» ]
2OO0 X-ray 1.90 A/B 1-461 [» ]
ProteinModelPortali P11926.
SMRi P11926. Positions 7-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111007. 9 interactions.
IntActi P11926. 3 interactions.
MINTi MINT-1208473.
STRINGi 9606.ENSP00000234111.

Chemistry

BindingDBi P11926.
ChEMBLi CHEMBL1869.
DrugBanki DB00114. Pyridoxal Phosphate.
DB00127. Spermine.
GuidetoPHARMACOLOGYi 1276.

PTM databases

PhosphoSitei P11926.

Polymorphism databases

DMDMi 118377.

Proteomic databases

MaxQBi P11926.
PaxDbi P11926.
PRIDEi P11926.

Protocols and materials databases

DNASUi 4953.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234111 ; ENSP00000234111 ; ENSG00000115758 .
ENST00000405333 ; ENSP00000385333 ; ENSG00000115758 .
GeneIDi 4953.
KEGGi hsa:4953.
UCSCi uc002rao.1. human.

Organism-specific databases

CTDi 4953.
GeneCardsi GC02M010580.
HGNCi HGNC:8109. ODC1.
HPAi CAB035996.
HPA001536.
MIMi 165640. gene.
neXtProti NX_P11926.
PharmGKBi PA31897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0019.
HOGENOMi HOG000274133.
HOVERGENi HBG005456.
InParanoidi P11926.
KOi K01581.
OMAi TIHYVMS.
OrthoDBi EOG73Z2T6.
PhylomeDBi P11926.
TreeFami TF300760.

Enzyme and pathway databases

UniPathwayi UPA00535 ; UER00288 .
BioCyci MetaCyc:HS03935-MONOMER.
Reactomei REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_14820. Metabolism of polyamines.
SABIO-RK P11926.

Miscellaneous databases

ChiTaRSi ODC1. human.
EvolutionaryTracei P11926.
GeneWikii ODC1.
GenomeRNAii 4953.
NextBioi 19080.
PROi P11926.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11926.
Bgeei P11926.
CleanExi HS_ODC1.
Genevestigatori P11926.

Family and domain databases

Gene3Di 2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
InterProi IPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PRINTSi PR01179. ODADCRBXLASE.
PR01182. ORNDCRBXLASE.
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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).

Entry informationi

Entry nameiDCOR_HUMAN
AccessioniPrimary (citable) accession number: P11926
Secondary accession number(s): Q53TU3, Q6LDS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 159 of the entry and version 2 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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