Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P81446 (ML1_VISAL)

Protein

Beta-galactoside-specific lectin 1

Gene
N/A
Organism
Viscum album (European mistletoe)
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

The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.3 Publications

Miscellaneous

Several isoforms exist.

<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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei198By 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.2.2.22 6669

Protein family/group databases

Carbohydrate-Active enZymes

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

UniLectin database of carbohydrate-binding proteins

More...UniLectini		P81446

<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:
Beta-galactoside-specific lectin 1
Alternative name(s):
Beta-galactoside-specific lectin I
Viscumin
Cleaved into the following 2 chains:
Beta-galactoside-specific lectin 1 chain A isoform 1 (EC:3.2.2.22)
Alternative name(s):
Beta-galactoside-specific lectin I chain A isoform 1
ML-I A
Short name:
MLA
rRNA N-glycosidase
Beta-galactoside-specific lectin 1 chain B
Alternative name(s):
Beta-galactoside-specific lectin I chain B
ML-I B
Short name:
MLB
<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>OrganismiViscum album (European mistletoe)
<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 identifieri3972 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Gunneridae › Pentapetalae › Santalales › Viscaceae › Viscum

<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 protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

Due to its immunomodulative effects it is being studied in clinical trials in cancer patients as it may slow the growth of cancer cells and be an effective treatment for solid tumors.

<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 – 333 PublicationsAdd BLAST33
<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_000003074934 – 287Beta-galactoside-specific lectin 1 chain A isoform 1Add BLAST254
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000030750288 – 301Connecting peptide1 PublicationAdd BLAST14
ChainiPRO_0000030751302 – 564Beta-galactoside-specific lectin 1 chain BAdd BLAST263

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>Glycosylationi145N-linked (GlcNAc...) asparagine1 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 bondi280 ↔ 306Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication
Glycosylationi362N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi365 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi397N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi437N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi453 ↔ 466PROSITE-ProRule annotation1 Publication
Disulfide bondi492 ↔ 509PROSITE-ProRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The A chain of variant MLA' is not glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P81446

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P81446

<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.3 Publications

<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

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P81446

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

More...SMRi		P81446

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		P81446

<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>Domaini309 – 436Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Domaini440 – 564Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125

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>Regioni324 – 326Galactose binding3
Regioni536 – 538Galactose binding3

<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

Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated

Keywords - Domaini

Repeat, Signal

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
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

<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.

P81446-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY 
        60         70         80         90        100
FRFITLLRDY VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT 
       110        120        130        140        150
AAIDVTNLYV VAYQAGDQSY FLRDAPRGAE THLFTGTTRS SLPFNGSYPD 
       160        170        180        190        200
LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG STRTQARSIL ILIQMISEAA 
       210        220        230        240        250
RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ QSTDGVFNNP 
       260        270        280        290        300
IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI 
       310        320        330        340        350
ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL 
       360        370        380        390        400
WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI 
       410        420        430        440        450
INPRSNLVLA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFR 
       460        470        480        490        500
DLCMESNGGS VWVETCVISQ QNQRWALYGD GSIRPKQNQD QCLTCGRDSV 
       510        520        530        540        550
STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA NPKLRRIIIY 
       560 
PATGKPNQMW LPVP
Length:564
Mass (Da):62,628
Last modified:April 17, 2007 - v3
<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:i8BC06110DD458A6E
GO

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 conflicti3G → A in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti19 – 20GQ → CL in AAR25545 (PubMed:15182350).Curated2
Sequence conflicti37L → I in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti62S → G AA sequence (PubMed:1450445).Curated1
Sequence conflicti83A → T in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti92T → S in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti94E → Q in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti94E → Q AA sequence (PubMed:8980141).Curated1
Sequence conflicti94E → Q (PubMed:12823544).Curated1
Sequence conflicti96G → Q AA sequence (PubMed:8980141).Curated1
Sequence conflicti99I → V AA sequence (PubMed:8980141).Curated1
Sequence conflicti108L → A AA sequence (PubMed:8980141).Curated1
Sequence conflicti117D → N in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti141S → P in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti181S → N in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti190L → I in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti190L → I in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti193I → V in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti193I → V in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti209A → L in AAR25546 (PubMed:15182350).Curated1
Sequence conflicti209A → Y AA sequence (PubMed:8980141).Curated1
Sequence conflicti241Q → H AA sequence (PubMed:8980141).Curated1
Sequence conflicti241Q → H (PubMed:12823544).Curated1
Sequence conflicti244D → E in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti322C → R AA sequence (PubMed:9618256).Curated1
Sequence conflicti391 – 393LWE → IWQ in AAR25545 (PubMed:15182350).Curated3
Sequence conflicti391 – 393LWE → IWQ in AAL87006 (PubMed:15001393).Curated3
Sequence conflicti391 – 393LWE → IWQ AA sequence (PubMed:9618256).Curated3
Sequence conflicti396G → D AA sequence (PubMed:9618256).Curated1
Sequence conflicti408V → A in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti467V → D AA sequence (PubMed:9618256).Curated1
Sequence conflicti468I → S in AAR25545 (PubMed:15182350).Curated1
Sequence conflicti468I → S in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti468I → S AA sequence (PubMed:9618256).Curated1
Sequence conflicti471 – 474QNQR → KNQGK AA sequence (PubMed:9618256).Curated4
Sequence conflicti495C → S AA sequence (PubMed:9618256).Curated1
Sequence conflicti511 – 515AGSSG → GASGS AA sequence (PubMed:9618256).Curated5
Sequence conflicti538 – 540AQA → KGS in AAL87006 (PubMed:15001393).Curated3
Sequence conflicti546R → Q in AAL87006 (PubMed:15001393).Curated1
Sequence conflicti564P → F AA sequence (PubMed:9618256).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti48E → D in MLA'. 1 Publication1
Natural varianti145N → T in MLA'. 1 Publication1
Natural varianti149P → T in MLA'. 1 Publication1
Natural varianti166 – 167DQ → EE in MLA'. 2
Natural varianti173T → S in MLA'. 1 Publication1
Natural varianti177F → Y in MLA'. 1 Publication1
Natural varianti184T → A in MLA'. 1 Publication1
Natural varianti212Y → D in MLA'. 1 Publication1
Natural varianti217A → E in MLA'. 1 Publication1
Natural varianti223V → M in MLA'. 1 Publication1
Natural varianti251I → F in MLA'. 1 Publication1
Natural varianti256 – 257PP → ST in MLA'. 2
Natural varianti264T → S in MLA'. 1 Publication1
Natural varianti268D → S in MLA'. 1 Publication1
Natural varianti319N → S1 Publication1
Natural varianti357G → N1 Publication1
Natural varianti458G → Q1 Publication1
Natural varianti495C → V1 Publication1
Natural varianti524G → Y1 Publication1
Natural varianti531 – 533NGL → KGP. 3
Natural varianti531N → S1 Publication1
Natural varianti531N → T1 Publication1
Natural varianti532 – 535GLAM → SLMV. 4

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
AY377890 Genomic DNA Translation: AAR25545.1
AY377891 mRNA Translation: AAR25546.1
AY081149 mRNA Translation: AAL87006.1

Protein sequence database of the Protein Information Resource

More...PIRi		JW0090
PD0018
PD0019

Keywords - Coding sequence diversityi

Polymorphism

<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
AY377890 Genomic DNA Translation: AAR25545.1
AY377891 mRNA Translation: AAR25546.1
AY081149 mRNA Translation: AAL87006.1
PIRiJW0090
PD0018
PD0019

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
1M2TX-ray1.89A34-287[»]
B313-564[»]
1ONKX-ray2.10A34-287[»]
B302-563[»]
1OQLX-ray3.00A34-282[»]
B302-564[»]
1PUMX-ray2.30A34-282[»]
B302-564[»]
1PUUX-ray2.30A34-282[»]
B302-564[»]
1SZ6X-ray2.05A34-282[»]
B302-564[»]
2R9KX-ray2.70A34-287[»]
B302-564[»]
2RG9X-ray1.95A34-282[»]
B302-564[»]
3D7WX-ray2.49A34-287[»]
B302-564[»]
3O5WX-ray2.70A34-287[»]
B302-564[»]
4EB2X-ray1.94A34-282[»]
B302-564[»]
4JKXX-ray2.35A34-282[»]
B302-564[»]
6ELYX-ray2.84A34-282[»]
B302-564[»]
ProteinModelPortaliP81446
SMRiP81446
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13 Carbohydrate-Binding Module Family 13
UniLectiniP81446

PTM databases

iPTMnetiP81446

Proteomic databases

PRIDEiP81446

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.2.22 6669

Miscellaneous databases

EvolutionaryTraceiP81446

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
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

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 nameiML1_VISAL
<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: P81446
Secondary accession number(s): P81830
, Q6H270, Q6H271, Q8RXH6, Q9S7D0
<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: December 15, 1998
Last sequence update: April 17, 2007
Last modified: December 5, 2018
This is version 118 of the entry and version 3 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, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again