UniProtKB - P00860 (DCOR_MOUSE)

>sp|P00860|DCOR_MOUSE Ornithine decarboxylase OS=Mus musculus OX=10090 GN=Odc1 PE=1 SV=2
MSSFTKDEFDCHILDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP
RVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQI
KYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLL
LERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPG
SEDTKLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKTVWKEQ
PGSDDEDESNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSIWGPTC
DGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYVMSRPMWQLMKQI
QSHGFPPEVEEQDDGTLPMSCAQESGMDRHPAACASARINV

Entry version 181 (02 Jun 2021)
Sequence version 2 (27 Jul 2011)
Previous versions | rss

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Protein

Ornithine decarboxylase

Gene

Odc1

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

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.

2 Publications

Catalytic activityⁱ

H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-ornithine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
CO₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
putrescine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P11926 (DCOR_HUMAN)
EC:
4.1.1.17
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P11926 (DCOR_HUMAN)
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H⁺
+
L-ornithine
zoom
=
CO₂
+
putrescine
zoom

Cofactorⁱ

pyridoxal 5'-phosphate2 Publications

Activity regulationⁱ

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.By similarity

Pathwayⁱ: putrescine biosynthesis via L-ornithine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine. This subpathway is part of the pathway putrescine biosynthesis via L-ornithine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from L-ornithine, the pathway putrescine biosynthesis via L-ornithine pathway and in Amine and polyamine biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	197	Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates1 Publication	1
Binding siteⁱ	200	Pyridoxal phosphateBy similarity	1
Binding siteⁱ	237	Pyridoxal phosphate; via amino nitrogen1 Publication	1
Active siteⁱ	360	Proton donor; shared with dimeric partner3 Publications	1
Binding siteⁱ	361	Substrate; shared with dimeric partnerBy similarity	1
Binding siteⁱ	389	Pyridoxal phosphate1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Decarboxylase, Lyase
Biological process	Polyamine biosynthesis
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

BRENDAⁱ	4.1.1.17, 3474
Reactomeⁱ	R-MMU-350562, Regulation of ornithine decarboxylase (ODC) R-MMU-351202, Metabolism of polyamines
UniPathwayⁱ	UPA00535;UER00288

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Ornithine decarboxylase (EC:4.1.1.17) Short name: ODC
Gene namesⁱ	Name:Odc1 Synonyms:Odc
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 12

Organism-specific databases

MGIⁱ	MGI:97402, Odc1

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	387	G → A: Partial loss of activity. 1 Publication		1
Mutagenesisⁱ	387	G → C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Loss of activity. 1 Publication		1

Chemistry databases

ChEMBLⁱ	CHEMBL2840

ChEMBLⁱ

CHEMBL2840

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000149892	1 – 461	Ornithine decarboxylaseAdd BLAST		461

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	69	N6-(pyridoxal phosphate)lysineCombined sources2 Publications	1
Modified residueⁱ	303	Phosphoserine; by CK21 Publication	1
Modified residueⁱ	360	S-nitrosocysteineBy similarity	1

Keywords - PTMⁱ

Phosphoprotein, S-nitrosylation

Proteomic databases

EPDⁱ	P00860
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P00860
PaxDbⁱ	P00860
PRIDEⁱ	P00860
ProteomicsDBⁱ	279314

PTM databases

iPTMnetⁱ	P00860
PhosphoSitePlusⁱ	P00860

Expressionⁱ

Tissue specificityⁱ

Expressed during testis development in the outer part of the seminiferous tubules.1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000011179, Expressed in spermatid and 139 other tissues
ExpressionAtlasⁱ	P00860, baseline and differential
Genevisibleⁱ	P00860, MM

Interactionⁱ

Subunit structureⁱ

Homodimer. Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (PubMed:8106349, PubMed:10378276). Does not form a heterodimer with AZIN2 (PubMed:24967154).

3 Publications

GO - Molecular functionⁱ

protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.17
  "Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2."
  Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M., Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.
  FEBS Open Bio 4:510-521(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBUNIT.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	201896, 1 interactor
IntActⁱ	P00860, 1 interactor
STRINGⁱ	10090.ENSMUSP00000128661

Miscellaneous databases

RNActⁱ	P00860, protein

RNActⁱ

P00860, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 6	Combined sources	4
Beta strandⁱ	9 – 14	Combined sources	6
Helixⁱ	20 – 28	Combined sources	9
Beta strandⁱ	40 – 44	Combined sources	5
Helixⁱ	45 – 58	Combined sources	14
Beta strandⁱ	62 – 67	Combined sources	6
Helixⁱ	68 – 70	Combined sources	3
Helixⁱ	74 – 83	Combined sources	10
Beta strandⁱ	86 – 89	Combined sources	4
Helixⁱ	92 – 100	Combined sources	9
Helixⁱ	105 – 107	Combined sources	3
Beta strandⁱ	108 – 110	Combined sources	3
Helixⁱ	117 – 125	Combined sources	9
Beta strandⁱ	130 – 133	Combined sources	4
Helixⁱ	136 – 145	Combined sources	10
Beta strandⁱ	150 – 155	Combined sources	6
Helixⁱ	174 – 186	Combined sources	13
Beta strandⁱ	190 – 195	Combined sources	6
Helixⁱ	206 – 225	Combined sources	20
Beta strandⁱ	231 – 233	Combined sources	3
Beta strandⁱ	241 – 246	Combined sources	6
Helixⁱ	248 – 262	Combined sources	15
Helixⁱ	265 – 267	Combined sources	3
Beta strandⁱ	270 – 273	Combined sources	4
Helixⁱ	277 – 280	Combined sources	4
Helixⁱ	281 – 283	Combined sources	3
Beta strandⁱ	284 – 296	Combined sources	13
Beta strandⁱ	313 – 319	Combined sources	7
Turnⁱ	322 – 326	Combined sources	5
Helixⁱ	327 – 331	Combined sources	5
Beta strandⁱ	339 – 342	Combined sources	4
Beta strandⁱ	350 – 356	Combined sources	7
Beta strandⁱ	358 – 360	Combined sources	3
Beta strandⁱ	365 – 373	Combined sources	9
Beta strandⁱ	380 – 383	Combined sources	4
Beta strandⁱ	388 – 390	Combined sources	3
Helixⁱ	391 – 393	Combined sources	3
Helixⁱ	397 – 399	Combined sources	3
Beta strandⁱ	404 – 410	Combined sources	7
Helixⁱ	411 – 417	Combined sources	7

Show more details

3D structure databases

SMRⁱ	P00860
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P00860

EvolutionaryTraceⁱ

P00860

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	274 – 277	Pyridoxal phosphate binding1 Publication		4
Regionⁱ	331 – 332	Substrate bindingBy similarity		2

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG0622, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00950000182995
HOGENOMⁱ	CLU_026444_1_1_1
InParanoidⁱ	P00860
OMAⁱ	VVGYICE
Database of Orthologous Groups More...OrthoDBⁱ	725914at2759
TreeFamⁱ	TF300760

Family and domain databases

Gene3Dⁱ	2.40.37.10, 1 hit 3.20.20.10, 1 hit
InterProⁱ	View protein in InterPro 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
PANTHERⁱ	PTHR11482, PTHR11482, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02784, Orn_Arg_deC_N, 1 hit PF00278, Orn_DAP_Arg_deC, 1 hit
PRINTSⁱ	PR01179, ODADCRBXLASE PR01182, ORNDCRBXLASE
SUPFAMⁱ	SSF50621, SSF50621, 1 hit SSF51419, SSF51419, 1 hit
PROSITEⁱ	View protein in PROSITE PS00878, ODR_DC_2_1, 1 hit PS00879, ODR_DC_2_2, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

P00860-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK 
        60         70         80         90        100
KHLRWLKALP RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG 
       110        120        130        140        150
LGVPAERVIY ANPCKQVSQI KYAASNGVQM MTFDSEIELM KVARAHPKAK 
       160        170        180        190        200
LVLRIATDDS KAVCRLSVKF GATLKTSRLL LERAKELNID VIGVSFHVGS 
       210        220        230        240        250
GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG SEDTKLKFEE 
       260        270        280        290        300
ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ 
       310        320        330        340        350
PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY 
       360        370        380        390        400
YSSSIWGPTC DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF 
       410        420        430        440        450
QRPNIYYVMS RPMWQLMKQI QSHGFPPEVE EQDDGTLPMS CAQESGMDRH 
       460 
PAACASARIN V

Length:461

Mass (Da):51,177

Last modified:July 27, 2011 - v2

Checksum:ⁱB581753F57AC0A30

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A1Y7VJC5	A0A1Y7VJC5_MOUSE	Ornithine decarboxylase Ornithine decarboxylase	Odc1	197	Annotation score:
A0A1Y7VMF9	A0A1Y7VMF9_MOUSE	Ornithine decarboxylase Ornithine decarboxylase	Odc1	42	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	178	R → W in AAA39846 (PubMed:3456155).Curated	1
Sequence conflictⁱ	206	E → D in AAA51638 (PubMed:2982844).Curated	1
Sequence conflictⁱ	206	E → D in AAA39845 (PubMed:3856848).Curated	1
Sequence conflictⁱ	206	E → D in CAA30301 (PubMed:3362685).Curated	1
Sequence conflictⁱ	206	E → D in AAA39849 (PubMed:3372502).Curated	1
Sequence conflictⁱ	206	E → D in AAB27809 (PubMed:8350350).Curated	1
Sequence conflictⁱ	350	Y → H in AAA39848 (PubMed:3456155).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20617 mRNA Translation: AAA51638.1 M10624 mRNA Translation: AAA39845.1 X07392 Genomic DNA Translation: CAA30301.1 J03733 Genomic DNA Translation: AAA39849.1 S64539 mRNA Translation: AAB27809.1 EU684749 mRNA Translation: ACD81645.1 AK139610 mRNA Translation: BAE24082.1 CH466582 Genomic DNA Translation: EDK98494.1 BC059826 mRNA Translation: AAH59826.1 BC083122 mRNA Translation: AAH83122.1 M12330 mRNA Translation: AAA39846.1 M12331 mRNA Translation: AAA39848.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS25829.1
PIRⁱ	A01077, DCMSO I56477
NCBI Reference Sequences More...RefSeqⁱ	NP_038642.2, NM_013614.2 XP_017170479.1, XM_017314990.1

Genome annotation databases

Ensemblⁱ	ENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179
GeneIDⁱ	18263
KEGGⁱ	mmu:18263
UCSC genome browser More...UCSCⁱ	uc007ncv.1, mouse

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P00860	Ornithine decarboxylase		CRIGR		455	UniRef90_P00860
ornithine decarboxylase		MUSCR		463
ornithine decarboxylase		PERMB		462
ornithine decarboxylase		MESAU		461
ornithine decarboxylase isoform X1		SAPAP		461
+8

Protein	Similar proteins		Species	Score	Length	Source
P00860	Ornithine decarboxylase		CRIGR		455	UniRef50_P00860
Antizyme inhibitor 2		XENLA		456
ornithine decarboxylase		MUSCR		463
ornithine decarboxylase		PERMB		462
ornithine decarboxylase		MESAU		461
+441

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M20617 mRNA Translation: AAA51638.1 M10624 mRNA Translation: AAA39845.1 X07392 Genomic DNA Translation: CAA30301.1 J03733 Genomic DNA Translation: AAA39849.1 S64539 mRNA Translation: AAB27809.1 EU684749 mRNA Translation: ACD81645.1 AK139610 mRNA Translation: BAE24082.1 CH466582 Genomic DNA Translation: EDK98494.1 BC059826 mRNA Translation: AAH59826.1 BC083122 mRNA Translation: AAH83122.1 M12330 mRNA Translation: AAA39846.1 M12331 mRNA Translation: AAA39848.1
CCDSⁱ	CCDS25829.1
PIRⁱ	A01077, DCMSO I56477
RefSeqⁱ	NP_038642.2, NM_013614.2 XP_017170479.1, XM_017314990.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	7ODC	X-ray	1.60	A	1-424	[»]
SMRⁱ	P00860
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	201896, 1 interactor
IntActⁱ	P00860, 1 interactor
STRINGⁱ	10090.ENSMUSP00000128661

Chemistry databases

ChEMBLⁱ	CHEMBL2840

ChEMBLⁱ

CHEMBL2840

PTM databases

iPTMnetⁱ	P00860
PhosphoSitePlusⁱ	P00860

Proteomic databases

EPDⁱ	P00860
MaxQBⁱ	P00860
PaxDbⁱ	P00860
PRIDEⁱ	P00860
ProteomicsDBⁱ	279314

Protocols and materials databases

Antibodypediaⁱ	781, 874 antibodies
The DNASU plasmid repository More...DNASUⁱ	18263

Genome annotation databases

Ensemblⁱ	ENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179
GeneIDⁱ	18263
KEGGⁱ	mmu:18263
UCSCⁱ	uc007ncv.1, mouse

Organism-specific databases

CTDⁱ	4953
MGIⁱ	MGI:97402, Odc1

Phylogenomic databases

eggNOGⁱ	KOG0622, Eukaryota
GeneTreeⁱ	ENSGT00950000182995
HOGENOMⁱ	CLU_026444_1_1_1
InParanoidⁱ	P00860
OMAⁱ	VVGYICE
OrthoDBⁱ	725914at2759
TreeFamⁱ	TF300760

Enzyme and pathway databases

UniPathwayⁱ	UPA00535;UER00288
BRENDAⁱ	4.1.1.17, 3474
Reactomeⁱ	R-MMU-350562, Regulation of ornithine decarboxylase (ODC) R-MMU-351202, Metabolism of polyamines

Miscellaneous databases

BioGRID-ORCSⁱ	18263, 3 hits in 52 CRISPR screens
ChiTaRSⁱ	Odc1, mouse
EvolutionaryTraceⁱ	P00860
Protein Ontology More...PROⁱ	PR:P00860
RNActⁱ	P00860, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000011179, Expressed in spermatid and 139 other tissues
ExpressionAtlasⁱ	P00860, baseline and differential
Genevisibleⁱ	P00860, MM

Family and domain databases

Gene3Dⁱ	2.40.37.10, 1 hit 3.20.20.10, 1 hit
InterProⁱ	View protein in InterPro 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
PANTHERⁱ	PTHR11482, PTHR11482, 1 hit
Pfamⁱ	View protein in Pfam PF02784, Orn_Arg_deC_N, 1 hit PF00278, Orn_DAP_Arg_deC, 1 hit
PRINTSⁱ	PR01179, ODADCRBXLASE PR01182, ORNDCRBXLASE
SUPFAMⁱ	SSF50621, SSF50621, 1 hit SSF51419, SSF51419, 1 hit
PROSITEⁱ	View protein in PROSITE PS00878, ODR_DC_2_1, 1 hit PS00879, ODR_DC_2_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DCOR_MOUSE
Accessionⁱ	P00860Primary (citable) accession number: P00860 Secondary accession number(s): Q61997, Q61998, Q6PB87
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 27, 2011
	Last modified:	June 2, 2021
	This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - P00860 (DCOR_MOUSE)

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Ornithine decarboxylase

Odc1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: putrescine biosynthesis via L-ornithine pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: putrescine biosynthesis via L-ornithine pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ