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Entry version 168 (07 Oct 2020)
Sequence version 1 (01 Aug 1988)
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Protein

Ornithine decarboxylase

Gene

SPE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.1 Publication

Miscellaneous

Present with 688 molecules/cell in log phase SD medium.1 Publication

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by antizyme (AZ) OAZ1 in response to polyamine levels. AZ inhibits the assembly of the functional homodimer by binding to ODC monomers and targeting them for ubiquitin-independent proteolytic destruction by the 26S proteasome.1 Publication

<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

This protein is involved in step 1 of the subpathway that synthesizes putrescine from L-ornithine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Ornithine decarboxylase (SPE1)
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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei244Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediatesBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei247Pyridoxal phosphateBy similarity1
Binding sitei286Pyridoxal phosphate; via amino nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei411Proton donor; shared with dimeric partnerBy similarity1
Binding sitei412Substrate; shared with dimeric partnerBy similarity1
Binding sitei441Pyridoxal phosphateBy similarity1

<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

  • ornithine decarboxylase activity Source: SGD

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YKL184W-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-351143, Agmatine biosynthesis
R-SCE-351202, Metabolism of polyamines

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00535;UER00288

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ornithine decarboxylase (EC:4.1.1.171 Publication)
Short name:
ODC
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SPE11 Publication
Synonyms:ORD1
Ordered Locus Names:YKL184WImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL184W

Saccharomyces Genome Database

More...
SGDi
S000001667, SPE1

<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

Keywords - Cellular componenti

Cytoplasm

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001499091 – 466Ornithine decarboxylaseAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei116N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P08432

PRoteomics IDEntifications database

More...
PRIDEi
P08432

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08432

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:2669750). Only the dimer is catalytically active, as the active sites are constructed of residues from both monomers (By similarity).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33938, 505 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YKL184W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P08432, protein

<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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P08432

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni318 – 321Pyridoxal phosphate bindingBy similarity4
Regioni362 – 363Substrate bindingBy similarity2

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0622, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182995

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_026444_1_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08432

KEGG Orthology (KO)

More...
KOi
K01581

Identification of Orthologs from Complete Genome Data

More...
OMAi
CASNGEI

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.37.10, 1 hit
3.20.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01179, ODADCRBXLASE
PR01182, ORNDCRBXLASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50621, SSF50621, 1 hit
SSF51419, SSF51419, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00878, ODR_DC_2_1, 1 hit
PS00879, ODR_DC_2_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P08432-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSTQVGNAL SSSTTTLVDL SNSTVTQKKQ YYKDGETLHN LLLELKNNQD
60 70 80 90 100
LELLPHEQAH PKIFQALKAR IGRINNETCD PGEENSFFIC DLGEVKRLFN
110 120 130 140 150
NWVKELPRIK PFYAVKCNPD TKVLSLLAEL GVNFDCASKV EIDRVLSMNI
160 170 180 190 200
SPDRIVYANP CKVASFIRYA ASKNVMKSTF DNVEELHKIK KFHPESQLLL
210 220 230 240 250
RIATDDSTAQ CRLSTKYGCE MENVDVLLKA IKELGLNLAG VSFHVGSGAS
260 270 280 290 300
DFTSLYKAVR DARTVFDKAA NEYGLPPLKI LDVGGGFQFE SFKESTAVLR
310 320 330 340 350
LALEEFFPVG CGVDIIAEPG RYFVATAFTL ASHVIAKRKL SENEAMIYTN
360 370 380 390 400
DGVYGNMNCI LFDHQEPHPR TLYHNLEFHY DDFESTTAVL DSINKTRSEY
410 420 430 440 450
PYKVSIWGPT CDGLDCIAKE YYMKHDVIVG DWFYFPALGA YTSSAATQFN
460
GFEQTADIVY IDSELD
Length:466
Mass (Da):52,285
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2EBD7EE8CFAA67CD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J02777 Genomic DNA Translation: AAA34829.1
X74151 Genomic DNA Translation: CAA52254.1
Z28184 Genomic DNA Translation: CAA82027.1
BK006944 Genomic DNA Translation: DAA08982.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A28437, DCBYO

NCBI Reference Sequences

More...
RefSeqi
NP_012737.1, NM_001179750.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL184W_mRNA; YKL184W; YKL184W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853651

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL184W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02777 Genomic DNA Translation: AAA34829.1
X74151 Genomic DNA Translation: CAA52254.1
Z28184 Genomic DNA Translation: CAA82027.1
BK006944 Genomic DNA Translation: DAA08982.1
PIRiA28437, DCBYO
RefSeqiNP_012737.1, NM_001179750.1

3D structure databases

SMRiP08432
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33938, 505 interactors
STRINGi4932.YKL184W

PTM databases

iPTMnetiP08432

Proteomic databases

PaxDbiP08432
PRIDEiP08432

Genome annotation databases

EnsemblFungiiYKL184W_mRNA; YKL184W; YKL184W
GeneIDi853651
KEGGisce:YKL184W

Organism-specific databases

EuPathDBiFungiDB:YKL184W
SGDiS000001667, SPE1

Phylogenomic databases

eggNOGiKOG0622, Eukaryota
GeneTreeiENSGT00950000182995
HOGENOMiCLU_026444_1_2_1
InParanoidiP08432
KOiK01581
OMAiCASNGEI

Enzyme and pathway databases

UniPathwayiUPA00535;UER00288
BioCyciMetaCyc:YKL184W-MONOMER
ReactomeiR-SCE-351143, Agmatine biosynthesis
R-SCE-351202, Metabolism of polyamines

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P08432
RNActiP08432, protein

Family and domain databases

Gene3Di2.40.37.10, 1 hit
3.20.20.10, 1 hit
InterProiView 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
PANTHERiPTHR11482, PTHR11482, 1 hit
PfamiView protein in Pfam
PF02784, Orn_Arg_deC_N, 1 hit
PF00278, Orn_DAP_Arg_deC, 1 hit
PRINTSiPR01179, ODADCRBXLASE
PR01182, ORNDCRBXLASE
SUPFAMiSSF50621, SSF50621, 1 hit
SSF51419, SSF51419, 1 hit
PROSITEiView protein in PROSITE
PS00878, ODR_DC_2_1, 1 hit
PS00879, ODR_DC_2_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDCOR_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08432
Secondary accession number(s): D6VX16
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 7, 2020
This is version 168 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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