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Protein

Endo-1,4-beta-xylanase 2

Gene

xyn2

Organism
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
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

Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref. 5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).4 Publications

Caution

In PubMed:1369024 Figure 2, this sequence is erroneously labeled xyn1, but in the remainder of the paper and all subsequent publications, this protein is referred to as xylanase 2 (xyn2).1 Publication

<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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 68 sec(-1) with xylohexaose, 50.3 sec(-1) with xylopentaose, 0.162 sec(-1) with xylotetraose and 0.045 sec(-1) with xylotriose as substrate.1 Publication
  1. KM=0.14 mg/ml for beechwood (unsubstituted) xylan1 Publication
  2. KM=13.8 mg/ml for birchwood xylan1 Publication
  3. KM=3.0 mg/ml for acetylated glucuronoxylan1 Publication
  4. KM=3.8 mg/ml for deactetylated glucuronoxylan1 Publication
  5. KM=6.8 mg/ml for unsubstituted xylan1 Publication
  6. KM=73 µM for xylohexaose1 Publication
  7. KM=136 µM for xylopentaose1 Publication
  1. Vmax=1600 µmol/min/mg enzyme for beechwood xylan1 Publication
  2. Vmax=336 µmol/min/mg enzyme for birchwood xylan1 Publication

pH dependencei

Optimum pH is 4.5-5.5 (PubMed:1369024). Stable from pH 3.0 to 8.5 at room temperature and from pH 4.0 to 7.5 at 40 degrees Celsius (Ref. 5).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

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 sitei106Substrate1 Publication1
Binding sitei110Substrate1 Publication1
<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 sitei119Nucleophile1 Publication1 Publication1
Binding sitei121Substrate1 Publication1
Binding sitei155Substrate1 Publication1
Binding sitei159Substrate; via carbonyl oxygen1 Publication1
Binding sitei169Substrate1 Publication1
Binding sitei204Substrate1 Publication1
Active sitei210Proton donor1 Publication1 Publication1

<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 functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.8 6451

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

More...
UniPathwayi
UPA00114

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH11 Glycoside Hydrolase Family 11

mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

More...
mycoCLAPi
XYN11B_TRIRE

<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:
Endo-1,4-beta-xylanase 21 Publication (EC:3.2.1.82 Publications)
Short name:
EX 21 Publication
Short name:
Xylanase 21 Publication
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 21 Publication
Alkaline endo-beta-1,4-xylanase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:xyn21 Publication
ORF Names:M419DRAFT_124931
<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>OrganismiHypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
<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 identifieri1344414 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000024376 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unassembled WGS sequence

<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 Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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 – 19Sequence analysisAdd BLAST19
<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_000043670220 – 331 PublicationAdd BLAST14
<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_000000801434 – 223Endo-1,4-beta-xylanase 2Add BLAST190

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 residuei34Pyrrolidone carboxylic acid2 Publications1
<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>Glycosylationi71N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by D-xylose, dependent on the cellulase and xylanase regulator xyr1. Repressed by glucose through negative regulation by the crabon catabolite repressor cre1.By similarity

<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

1223
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
1ENXX-ray1.50A/B35-223[»]
1REDX-ray1.60A/B35-223[»]
1REEX-ray1.60A/B35-223[»]
1REFX-ray1.80A/B35-223[»]
1XYOX-ray1.50A/B35-223[»]
1XYPX-ray1.50A/B35-223[»]
2D97X-ray2.01A35-223[»]
2D98X-ray2.00A35-223[»]
2DFBX-ray1.11A34-223[»]
2DFCX-ray1.19A34-223[»]
3LGRX-ray1.64A35-223[»]
4HK8X-ray1.15A35-223[»]
4HK9X-ray1.55A36-223[»]
4HKLX-ray1.10A35-223[»]
4HKOX-ray1.50A35-223[»]
4HKWX-ray1.65A35-223[»]
4S2DOther1.60A35-223[»]
4S2FOther1.70A35-223[»]
4S2GOther1.60A35-223[»]
4S2HOther1.60A35-223[»]
4XPVOther1.70A35-223[»]
4XQ4X-ray1.25A/B35-223[»]
4XQDX-ray1.50A/B35-223[»]
4XQWX-ray1.50A35-223[»]
5K7Pelectron microscopy2.30A34-223[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P36217

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

More...
SMRi
P36217

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
P36217

<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>Domaini34 – 222GH11PROSITE-ProRule annotationAdd BLAST189

<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

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410JB05 Eukaryota
ENOG410YH6C LUCA

Database of Orthologous Groups

More...
OrthoDBi
1306131at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00457 Glyco_hydro_11, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00911 GLHYDRLASE11

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899 SSF49899, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 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.

P36217-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSFTSLLAG VAAISGVLAA PAAEVESVAV EKRQTIQPGT GYNNGYFYSY
60 70 80 90 100
WNDGHGGVTY TNGPGGQFSV NWSNSGNFVG GKGWQPGTKN KVINFSGSYN
110 120 130 140 150
PNGNSYLSVY GWSRNPLIEY YIVENFGTYN PSTGATKLGE VTSDGSVYDI
160 170 180 190 200
YRTQRVNQPS IIGTATFYQY WSVRRNHRSS GSVNTANHFN AWAQQGLTLG
210 220
TMDYQIVAVE GYFSSGSASI TVS
Length:223
Mass (Da):24,069
Last modified:July 6, 2016 - v2
<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:i79668149EADA22F9
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 CAA49293 differs from that shown. Reason: Frameshift at positions 10, 19 and 20.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 conflicti191A → V no nucleotide entry (PubMed:17416973).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
X69573 Genomic DNA Translation: CAA49293.1 Frameshift.
EU532196 mRNA Translation: ACB38137.1
KI911164 Genomic DNA Translation: ETR98242.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S39154

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
ETR98242; ETR98242; M419DRAFT_124931

<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
X69573 Genomic DNA Translation: CAA49293.1 Frameshift.
EU532196 mRNA Translation: ACB38137.1
KI911164 Genomic DNA Translation: ETR98242.1
PIRiS39154

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ENXX-ray1.50A/B35-223[»]
1REDX-ray1.60A/B35-223[»]
1REEX-ray1.60A/B35-223[»]
1REFX-ray1.80A/B35-223[»]
1XYOX-ray1.50A/B35-223[»]
1XYPX-ray1.50A/B35-223[»]
2D97X-ray2.01A35-223[»]
2D98X-ray2.00A35-223[»]
2DFBX-ray1.11A34-223[»]
2DFCX-ray1.19A34-223[»]
3LGRX-ray1.64A35-223[»]
4HK8X-ray1.15A35-223[»]
4HK9X-ray1.55A36-223[»]
4HKLX-ray1.10A35-223[»]
4HKOX-ray1.50A35-223[»]
4HKWX-ray1.65A35-223[»]
4S2DOther1.60A35-223[»]
4S2FOther1.70A35-223[»]
4S2GOther1.60A35-223[»]
4S2HOther1.60A35-223[»]
4XPVOther1.70A35-223[»]
4XQ4X-ray1.25A/B35-223[»]
4XQDX-ray1.50A/B35-223[»]
4XQWX-ray1.50A35-223[»]
5K7Pelectron microscopy2.30A34-223[»]
ProteinModelPortaliP36217
SMRiP36217
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11 Glycoside Hydrolase Family 11
mycoCLAPiXYN11B_TRIRE

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiETR98242; ETR98242; M419DRAFT_124931

Phylogenomic databases

eggNOGiENOG410JB05 Eukaryota
ENOG410YH6C LUCA
OrthoDBi1306131at2759

Enzyme and pathway databases

UniPathwayi
UPA00114

BRENDAi3.2.1.8 6451

Miscellaneous databases

EvolutionaryTraceiP36217

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033119 GH11_AS_2
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF00457 Glyco_hydro_11, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00776 GH11_1, 1 hit
PS00777 GH11_2, 1 hit
PS51761 GH11_3, 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 nameiXYN2_HYPJR
<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: P36217
Secondary accession number(s): A0A024RZG2, B2CNY5
<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: June 1, 1994
Last sequence update: July 6, 2016
Last modified: January 16, 2019
This is version 118 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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