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Entry version 181 (13 Feb 2019)
Sequence version 2 (01 Oct 1996)
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Protein

Endochitinase

Gene

CTS1

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

Chitinase is required for cell separation during growth of S.cerevisiae.

Miscellaneous

Present with 6350 molecules/cell in log phase SD medium.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

  • Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. EC:3.2.1.14

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 sitei157Proton donorPROSITE-ProRule annotation1

<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

  • chitinase activity Source: GO_Central
  • chitin binding Source: UniProtKB-KW
  • endochitinase activity Source: SGD

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • chitin catabolic process Source: SGD
  • polysaccharide catabolic process Source: UniProtKB-KW
  • septum digestion after cytokinesis Source: SGD

<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, Cell wall biogenesis/degradation, Chitin degradation, Polysaccharide degradation
LigandChitin-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YLR286C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.14 984

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM19 Carbohydrate-Binding Module Family 19
GH18 Glycoside Hydrolase Family 18

<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:
Endochitinase (EC:3.2.1.14)
Alternative name(s):
Soluble cell wall protein 2
<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:CTS1
Synonyms:SCW2
Ordered Locus Names:YLR286C
ORF Names:L8003.13
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR286C

Saccharomyces Genome Database

More...
SGDi
S000004276 CTS1

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell wall, Secreted

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1293195

<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 – 202 PublicationsAdd BLAST20
<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_000001193621 – 562EndochitinaseAdd BLAST542

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>Glycosylationi553N-linked (GlcNAc...) asparagineSequence analysis1

<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

Extensively glycosylated with a series of short O-linked mannose oligosaccharides ranging in size from Man2 to Man5.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P29029

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

More...
PaxDbi
P29029

PRoteomics IDEntifications database

More...
PRIDEi
P29029

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31551, 83 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YLR286C

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P29029

<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

1562
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
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P29029

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

More...
SMRi
P29029

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
P29029

<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>Regioni21 – 327CatalyticAdd BLAST307
Regioni481 – 562Chitin-binding, high affinityAdd BLAST82

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi328 – 480Ser/Thr-richAdd BLAST153

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160027

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P29029

KEGG Orthology (KO)

More...
KOi
K01183

Identification of Orthologs from Complete Genome Data

More...
OMAi
CDHSAWV

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005089 CBM_fam19
IPR001223 Glyco_hydro18_cat
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03427 CBM_19, 1 hit
PF00704 Glyco_hydro_18, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01095 CHITINASE_18, 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.

P29029-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLLYIILLF TQFLLLPTDA FDRSANTNIA VYWGQNSAGT QESLATYCES
60 70 80 90 100
SDADIFLLSF LNQFPTLGLN FANACSDTFS DGLLHCTQIA EDIETCQSLG
110 120 130 140 150
KKVLLSLGGA SGSYLFSDDS QAETFAQTLW DTFGEGTGAS ERPFDSAVVD
160 170 180 190 200
GFDFDIENNN EVGYSALATK LRTLFAEGTK QYYLSAAPQC PYPDASVGDL
210 220 230 240 250
LENADIDFAF IQFYNNYCSV SGQFNWDTWL TYAQTVSPNK NIKLFLGLPG
260 270 280 290 300
SASAAGSGYI SDTSLLESTI ADIASSSSFG GIALWDASQA FSNELNGEPY
310 320 330 340 350
VEILKNLLTS ASQTATTTVA TSKTSAASTS SASTSSASTS QKKTTQSTTS
360 370 380 390 400
TQSKSKVTLS PTASSAIKTS ITQTTKTLTS STKTKSSLGT TTTESTLNSV
410 420 430 440 450
AITSMKTTLS SQITSAALVT PQTTTTSIVS SAPIQTAITS TLSPATKSSS
460 470 480 490 500
VVSLQTATTS TLSPTTTSTS SGSTSSGSTS SDSTARTLAK ELNAQYAAGK
510 520 530 540 550
LNGKSTCTEG EIACSADGKF AVCDHSAWVY MECASGTTCY AYDSGDSVYT
560
QCNFSYLESN YF
Length:562
Mass (Da):59,015
Last modified:October 1, 1996 - 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:i0ABCEFBF448E1E19
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 conflicti168A → R in AAA34539 (PubMed:1918080).Curated1
Sequence conflicti168A → R in AAA34538 (PubMed:1918080).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 varianti16L → P in strain: DBY939. 1
Natural varianti23R → S in strain: DBY939 and SEY6210. 1
Natural varianti321T → S in strain: DBY939. 1
Natural varianti336 – 340Missing in strain: DBY939. 5
Natural varianti399S → A in strain: DBY939. 1
Natural varianti433 – 434PI → SL in strain: DBY939. 2
Natural varianti461T → K in strain: DBY939. 1
Natural varianti477 – 481Missing in strain: DBY939. 5

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M74070 Genomic DNA Translation: AAA34539.1
M74069 Genomic DNA Translation: AAA34538.1
U17243 Genomic DNA Translation: AAB67331.1
AY693040 Genomic DNA Translation: AAT93059.1
BK006945 Genomic DNA Translation: DAA09597.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41035
B41035
S50371

NCBI Reference Sequences

More...
RefSeqi
NP_013388.1, NM_001182173.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR286C_mRNA; YLR286C_mRNA; YLR286C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850992

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR286C

<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
M74070 Genomic DNA Translation: AAA34539.1
M74069 Genomic DNA Translation: AAA34538.1
U17243 Genomic DNA Translation: AAB67331.1
AY693040 Genomic DNA Translation: AAT93059.1
BK006945 Genomic DNA Translation: DAA09597.1
PIRiA41035
B41035
S50371
RefSeqiNP_013388.1, NM_001182173.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UY2X-ray1.60A22-315[»]
2UY3X-ray1.90A22-315[»]
2UY4X-ray1.75A22-315[»]
2UY5X-ray1.60A22-315[»]
4TXEX-ray1.80A22-315[»]
ProteinModelPortaliP29029
SMRiP29029
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31551, 83 interactors
STRINGi4932.YLR286C

Chemistry databases

BindingDBiP29029
ChEMBLiCHEMBL1293195

Protein family/group databases

CAZyiCBM19 Carbohydrate-Binding Module Family 19
GH18 Glycoside Hydrolase Family 18

Proteomic databases

MaxQBiP29029
PaxDbiP29029
PRIDEiP29029

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR286C_mRNA; YLR286C_mRNA; YLR286C
GeneIDi850992
KEGGisce:YLR286C

Organism-specific databases

EuPathDBiFungiDB:YLR286C
SGDiS000004276 CTS1

Phylogenomic databases

HOGENOMiHOG000160027
InParanoidiP29029
KOiK01183
OMAiCDHSAWV

Enzyme and pathway databases

BioCyciYEAST:YLR286C-MONOMER
BRENDAi3.2.1.14 984

Miscellaneous databases

EvolutionaryTraceiP29029

Protein Ontology

More...
PROi
PR:P29029

Family and domain databases

InterProiView protein in InterPro
IPR005089 CBM_fam19
IPR001223 Glyco_hydro18_cat
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF03427 CBM_19, 1 hit
PF00704 Glyco_hydro_18, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS01095 CHITINASE_18, 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 nameiCHIT_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: P29029
Secondary accession number(s): D6VYT1, P29028
<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 1, 1992
Last sequence update: October 1, 1996
Last modified: February 13, 2019
This is version 181 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
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