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Protein

Ricin

Gene
N/A
Organism
Ricinus communis (Castor bean)
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

Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. EC:3.2.2.22

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei50Carbohydrate; via amide nitrogen1
Binding sitei85Carbohydrate; via amide nitrogen1
<p>This subsection of the ‘Function’ 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 sitei2121
Binding sitei324Carbohydrate; via carbonyl oxygenBy similarity1
Binding sitei349Carbohydrate1
Binding sitei354Carbohydrate1
Binding sitei360Carbohydrate1
Binding sitei409CarbohydrateBy similarity1
Binding sitei449CarbohydrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi115 – 116AMP2
Nucleotide bindingi156 – 158AMP3

<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

<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 functionHydrolase, Protein synthesis inhibitor, Toxin
Biological processPlant defense
LigandLectin, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-18749

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.2.22 1204

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM13 Carbohydrate-Binding Module Family 13

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P02879

<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_and_taxonomy_section">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:
Ricin
Cleaved into the following 3 chains:
Alternative name(s):
rRNA N-glycosidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiRicinus communis (Castor bean)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri3988 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

A deglycosylated A chain may be linked to monoclonal antibodies to produce immunotoxins exploited in cancer treatment. However, a point mutation should be introduced to eliminate vascular leak syndrome, a side effect resulting from endothelial damage.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi83R → A: No effect on the toxic activity but suppresses the vascular leak syndrome. 1 Publication1
Mutagenesisi109L → A or M: No effect on the toxic activity or the vascular leak syndrome. 1 Publication1
Mutagenesisi110D → A, E or N: Suppresses the toxic activity. 1 Publication1
Mutagenesisi111V → A or M: No effect on the toxic activity or the vascular leak syndrome. 1 Publication1
Mutagenesisi132N → A: No effect on the toxic activity but Suppresses the vascular leak syndrome. 1 Publication1

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
2803 Ric c RIP

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4756

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 351 PublicationAdd BLAST35
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003074136 – 302Ricin A chainAdd BLAST267
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000030742303 – 314Linker peptide1 PublicationAdd BLAST12
ChainiPRO_0000030743315 – 576Ricin B chainAdd BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_00008045N-linked (GlcNAc...) asparagine1 Publication1
GlycosylationiCAR_000081271N-linked (GlcNAc...) asparagine; partial1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi294 ↔ 318Interchain (between A and B chains)
Disulfide bondi334 ↔ 353
Disulfide bondi377 ↔ 394
Disulfide bondi465 ↔ 478
Disulfide bondi504 ↔ 521

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
536
537

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P02879

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Disulfide-linked dimer of A and B chains.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
1022023, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-46421N

Protein interaction database and analysis system

More...
IntActi
P02879, 4 interactors

Molecular INTeraction database

More...
MINTi
P02879

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P02879

<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

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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 entryMethodResolution (Å)ChainPositionsPDBsum
1BR5X-ray2.50A36-302[»]
1BR6X-ray2.30A36-302[»]
1IFSX-ray2.00A38-298[»]
1IFTX-ray1.80A38-298[»]
1IFUX-ray2.40A38-298[»]
1IL3X-ray2.80A36-302[»]
1IL4X-ray2.60A36-302[»]
1IL5X-ray2.80A/B36-302[»]
1IL9X-ray3.10A36-302[»]
1J1MX-ray1.50A36-302[»]
1OBSX-ray2.20A36-302[»]
1OBTX-ray2.80A36-302[»]
1RTCX-ray2.30A36-302[»]
1UQ4X-ray1.90A40-302[»]
1UQ5X-ray1.40A40-302[»]
2AAIX-ray2.50A36-302[»]
B315-576[»]
2P8NX-ray1.94A36-302[»]
2PJOX-ray1.80A36-302[»]
2R2XX-ray2.40A36-302[»]
2R3DX-ray2.09A36-302[»]
2VC3X-ray1.60A36-302[»]
2VC4X-ray1.39A36-302[»]
3BJGX-ray2.14A36-302[»]
3EJ5X-ray2.50X40-296[»]
3HIOX-ray2.00A36-302[»]
3LC9X-ray2.28A36-233[»]
3MK9X-ray2.08A36-233[»]
3PX8X-ray1.29X39-296[»]
3PX9X-ray1.89X39-296[»]
3RTIX-ray2.80A36-302[»]
B315-576[»]
3RTJX-ray3.00A36-302[»]
B315-576[»]
3SRPX-ray2.14A36-302[»]
4ESIX-ray1.87A36-302[»]
4HUOX-ray1.52X36-302[»]
4HUPX-ray1.70X36-302[»]
4HV3X-ray1.54A36-302[»]
4HV7X-ray1.87X36-302[»]
4IMVX-ray2.25A36-233[»]
4KUCX-ray2.79A/I36-302[»]
4LGPX-ray2.40A/C36-296[»]
4LGRX-ray1.65A40-294[»]
4LGSX-ray2.70A39-301[»]
4LHJX-ray1.80A39-297[»]
4LHQX-ray2.30A/C39-298[»]
4MX1X-ray1.59A36-302[»]
4MX5X-ray1.52X36-302[»]
4Q2VX-ray2.20A36-302[»]
4Z9KX-ray1.50A39-296[»]
5BOZX-ray3.10A/B/C/D/E/F39-299[»]
5DDZX-ray1.50A36-302[»]
5E1HX-ray2.03A40-297[»]
5GU4X-ray1.55A/B36-302[»]
5J56X-ray1.80A36-302[»]
5J57X-ray1.70A36-302[»]
5SV3X-ray2.73B/D36-233[»]
5U4LX-ray2.50A36-302[»]
5U4MX-ray2.50A40-294[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02879

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

More...
SMRi
P02879

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02879

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini321 – 448Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati331 – 3731-alphaAdd BLAST43
Repeati374 – 4141-betaAdd BLAST41
Repeati417 – 4491-gammaAdd BLAST33
Domaini451 – 575Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125
Repeati462 – 4972-alphaAdd BLAST36
Repeati501 – 5402-betaAdd BLAST40
Repeati543 – 5702-gammaAdd BLAST28

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>Regioni43 – 45Carbohydrate bindingBy similarity3
Regioni176 – 181Carbohydrate binding6
Regioni230 – 232Carbohydrate binding3
Regioni336 – 340Carbohydrate binding5
Regioni548 – 551Carbohydrate binding4
Regioni565 – 569Carbohydrate binding5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).

<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

In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
818458at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00161 RICIN, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.420.10, 1 hit
4.10.470.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036041 Ribosome-inact_prot_sf
IPR017989 Ribosome_inactivat_1/2
IPR001574 Ribosome_inactivat_prot
IPR017988 Ribosome_inactivat_prot_CS
IPR016138 Ribosome_inactivat_prot_sub1
IPR016139 Ribosome_inactivat_prot_sub2
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin

The PANTHER Classification System

More...
PANTHERi
PTHR33453 PTHR33453, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00652 Ricin_B_lectin, 2 hits
PF00161 RIP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00396 SHIGARICIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00458 RICIN, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50370 SSF50370, 2 hits
SSF56371 SSF56371, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50231 RICIN_B_LECTIN, 2 hits
PS00275 SHIGA_RICIN, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P02879-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFPKQ YPIINFTTAG
60 70 80 90 100
ATVQSYTNFI RAVRGRLTTG ADVRHEIPVL PNRVGLPINQ RFILVELSNH
110 120 130 140 150
AELSVTLALD VTNAYVVGYR AGNSAYFFHP DNQEDAEAIT HLFTDVQNRY
160 170 180 190 200
TFAFGGNYDR LEQLAGNLRE NIELGNGPLE EAISALYYYS TGGTQLPTLA
210 220 230 240 250
RSFIICIQMI SEAARFQYIE GEMRTRIRYN RRSAPDPSVI TLENSWGRLS
260 270 280 290 300
TAIQESNQGA FASPIQLQRR NGSKFSVYDV SILIPIIALM VYRCAPPPSS
310 320 330 340 350
QFSLLIRPVV PNFNADVCMD PEPIVRIVGR NGLCVDVRDG RFHNGNAIQL
360 370 380 390 400
WPCKSNTDAN QLWTLKRDNT IRSNGKCLTT YGYSPGVYVM IYDCNTAATD
410 420 430 440 450
ATRWQIWDNG TIINPRSSLV LAATSGNSGT TLTVQTNIYA VSQGWLPTNN
460 470 480 490 500
TQPFVTTIVG LYGLCLQANS GQVWIEDCSS EKAEQQWALY ADGSIRPQQN
510 520 530 540 550
RDNCLTSDSN IRETVVKILS CGPASSGQRW MFKNDGTILN LYSGLVLDVR
560 570
ASDPSLKQII LYPLHGDPNQ IWLPLF
Length:576
Mass (Da):64,091
Last modified:August 13, 1987 - 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:iC14C4B77A8B5470D
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence described in Ref. 4 differs from that shown. High number of conflicts with the sequence translated from DNA.Curated
The sequence described in Ref. 5 differs from that shown. High number of conflicts with the sequence translated from DNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti76E → D in CAA26230 (PubMed:3838723).Curated1
Sequence conflicti551A → R in CAA26230 (PubMed:3838723).Curated1

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
X03179 Genomic DNA Translation: CAA26939.1
X52908 Genomic DNA Translation: CAA37095.1
X02388 mRNA Translation: CAA26230.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24041 RLCSD

NCBI Reference Sequences

More...
RefSeqi
NP_001310630.1, NM_001323701.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8261245

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rcu:8261245

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Baneful beans - Issue 31 of February 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03179 Genomic DNA Translation: CAA26939.1
X52908 Genomic DNA Translation: CAA37095.1
X02388 mRNA Translation: CAA26230.1
PIRiA24041 RLCSD
RefSeqiNP_001310630.1, NM_001323701.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BR5X-ray2.50A36-302[»]
1BR6X-ray2.30A36-302[»]
1IFSX-ray2.00A38-298[»]
1IFTX-ray1.80A38-298[»]
1IFUX-ray2.40A38-298[»]
1IL3X-ray2.80A36-302[»]
1IL4X-ray2.60A36-302[»]
1IL5X-ray2.80A/B36-302[»]
1IL9X-ray3.10A36-302[»]
1J1MX-ray1.50A36-302[»]
1OBSX-ray2.20A36-302[»]
1OBTX-ray2.80A36-302[»]
1RTCX-ray2.30A36-302[»]
1UQ4X-ray1.90A40-302[»]
1UQ5X-ray1.40A40-302[»]
2AAIX-ray2.50A36-302[»]
B315-576[»]
2P8NX-ray1.94A36-302[»]
2PJOX-ray1.80A36-302[»]
2R2XX-ray2.40A36-302[»]
2R3DX-ray2.09A36-302[»]
2VC3X-ray1.60A36-302[»]
2VC4X-ray1.39A36-302[»]
3BJGX-ray2.14A36-302[»]
3EJ5X-ray2.50X40-296[»]
3HIOX-ray2.00A36-302[»]
3LC9X-ray2.28A36-233[»]
3MK9X-ray2.08A36-233[»]
3PX8X-ray1.29X39-296[»]
3PX9X-ray1.89X39-296[»]
3RTIX-ray2.80A36-302[»]
B315-576[»]
3RTJX-ray3.00A36-302[»]
B315-576[»]
3SRPX-ray2.14A36-302[»]
4ESIX-ray1.87A36-302[»]
4HUOX-ray1.52X36-302[»]
4HUPX-ray1.70X36-302[»]
4HV3X-ray1.54A36-302[»]
4HV7X-ray1.87X36-302[»]
4IMVX-ray2.25A36-233[»]
4KUCX-ray2.79A/I36-302[»]
4LGPX-ray2.40A/C36-296[»]
4LGRX-ray1.65A40-294[»]
4LGSX-ray2.70A39-301[»]
4LHJX-ray1.80A39-297[»]
4LHQX-ray2.30A/C39-298[»]
4MX1X-ray1.59A36-302[»]
4MX5X-ray1.52X36-302[»]
4Q2VX-ray2.20A36-302[»]
4Z9KX-ray1.50A39-296[»]
5BOZX-ray3.10A/B/C/D/E/F39-299[»]
5DDZX-ray1.50A36-302[»]
5E1HX-ray2.03A40-297[»]
5GU4X-ray1.55A/B36-302[»]
5J56X-ray1.80A36-302[»]
5J57X-ray1.70A36-302[»]
5SV3X-ray2.73B/D36-233[»]
5U4LX-ray2.50A36-302[»]
5U4MX-ray2.50A40-294[»]
ProteinModelPortaliP02879
SMRiP02879
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1022023, 2 interactors
DIPiDIP-46421N
IntActiP02879, 4 interactors
MINTiP02879

Chemistry databases

BindingDBiP02879
ChEMBLiCHEMBL4756

Protein family/group databases

Allergomei2803 Ric c RIP
CAZyiCBM13 Carbohydrate-Binding Module Family 13
UniLectiniP02879

PTM databases

GlyConnecti536
537
UniCarbKBiP02879

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8261245
KEGGircu:8261245

Phylogenomic databases

OrthoDBi818458at2759

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18749
BRENDAi3.2.2.22 1204

Miscellaneous databases

EvolutionaryTraceiP02879

Protein Ontology

More...
PROi
PR:P02879

Family and domain databases

CDDicd00161 RICIN, 2 hits
Gene3Di3.40.420.10, 1 hit
4.10.470.10, 1 hit
InterProiView protein in InterPro
IPR036041 Ribosome-inact_prot_sf
IPR017989 Ribosome_inactivat_1/2
IPR001574 Ribosome_inactivat_prot
IPR017988 Ribosome_inactivat_prot_CS
IPR016138 Ribosome_inactivat_prot_sub1
IPR016139 Ribosome_inactivat_prot_sub2
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PANTHERiPTHR33453 PTHR33453, 1 hit
PfamiView protein in Pfam
PF00652 Ricin_B_lectin, 2 hits
PF00161 RIP, 1 hit
PRINTSiPR00396 SHIGARICIN
SMARTiView protein in SMART
SM00458 RICIN, 2 hits
SUPFAMiSSF50370 SSF50370, 2 hits
SSF56371 SSF56371, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 2 hits
PS00275 SHIGA_RICIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiRICI_RICCO
<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: P02879
Secondary accession number(s): P02880
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: January 16, 2019
This is version 173 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 programPlant 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

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
UniProt is an ELIXIR core data resource
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