Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 129 (11 Dec 2019)
Sequence version 1 (01 Nov 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

PMT1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (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 transcript 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

Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation.6 Publications

<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 <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: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

<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 functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.109 1096

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

More...
UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT39 Glycosyltransferase Family 39

<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:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC:2.4.1.109By similarity)
Short name:
Protein mannosyltransferase 1
<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:PMT1
Ordered Locus Names:CAALFM_C702890CA
ORF Names:CaJ7.03301 Publication, CaO19.12638, CaO19.5171
<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>OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (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 identifieri237561 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
<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
  • UP000000559 <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 7

Organism-specific databases

Candida Genome Database

More...
CGDi
CAL0000192847 PMT1

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:C7_02890C_A

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Transmembranei150 – 170HelicalSequence analysisAdd BLAST21
Transmembranei196 – 216HelicalSequence analysisAdd BLAST21
Transmembranei226 – 246HelicalSequence analysisAdd BLAST21
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Transmembranei291 – 311HelicalSequence analysisAdd BLAST21
Transmembranei604 – 624HelicalSequence analysisAdd BLAST21
Transmembranei643 – 663HelicalSequence analysisAdd BLAST21
Transmembranei666 – 686HelicalSequence analysisAdd BLAST21
Transmembranei700 – 720HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Shows altered cell wall composition with a significant decrease in wall mannoproteins. Impairs biofilm formation and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE) or engineered human oral mucosa (EHOM).3 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3534

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001214981 – 877Dolichyl-phosphate-mannose--protein mannosyltransferase 1Add BLAST877

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>Glycosylationi83N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi195N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi395N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi400N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi721N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

<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

Transcript levels are increased at least twofold by tunicamycin and Congo red. Both MSB2 and CEK1 are required to down-regulate PMT1 transcript levels in cells with intact glycostructures.1 Publication

<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

PMT1 and PMT2 form a functional heterodimer.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
1224487, 3 interactors

STRING: functional protein association networks

More...
STRINGi
5476.C4YTX6

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O74189

<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>Domaini340 – 394MIR 1PROSITE-ProRule annotationAdd BLAST55
Domaini403 – 462MIR 2PROSITE-ProRule annotationAdd BLAST60
Domaini472 – 528MIR 3PROSITE-ProRule annotationAdd BLAST57

<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 glycosyltransferase 39 family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O74189

KEGG Orthology (KO)

More...
KOi
K00728

Identification of Orthologs from Complete Genome Data

More...
OMAi
NFDFKDI

Database of Orthologous Groups

More...
OrthoDBi
203029at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027005 GlyclTrfase_39-like
IPR003342 Glyco_trans_39/83
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR032421 PMT_4TMC

The PANTHER Classification System

More...
PANTHERi
PTHR10050 PTHR10050, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02815 MIR, 1 hit
PF02366 PMT, 1 hit
PF16192 PMT_4TMC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00472 MIR, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF82109 SSF82109, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50919 MIR, 3 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

O74189-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKKPVTPAS KVAAKQAAVR SRHQEDVFTL DPLIDPIFQK GELRSYLVTE
60 70 80 90 100
PSPSVLKKRS IHTKEYWMLS SLLLIAFYVR MYNLSNPNSV VFDEVHFGGF
110 120 130 140 150
ARKYILGTFF MDVHPPLAKM LFGAVGAIGG FKGDFEFKSI GDKFPDSTPY
160 170 180 190 200
IFMRQFPALL GVGTVILCYL TLRQSGVRPI IAYITTFLLI IENSNVTISR
210 220 230 240 250
YILLDSPLIF FIAAAIYAWK KFEIQIPFTF GWYRSLLATG IALGLALSSK
260 270 280 290 300
WVGLFTVAWV GFLCIYQLWF LIGDLSVSTK KIWGHFFARG IILLGVPIAL
310 320 330 340 350
YLGFFAIHFQ LLNKEGDGGA FMSSAFRAGL QGNKIPRDIT EQVGLGSVVT
360 370 380 390 400
IRHVDTQGGY LHSHEHFYQT GSKQQQITLY PHLDSNNKWL IEPYNGTIHN
410 420 430 440 450
ETFVPLINGM KIRLKHINTG RRLHSHDEKP PVSERDWQKE CSCYGYDGFA
460 470 480 490 500
GDANDDWVVE IVNYRSQKGE AQTFVKAINT IFRLRHAMTG HYLFSSEVKL
510 520 530 540 550
PEWGFGQQEV TSASQGKRAL THWYIETNEN SILPPSEAKI INYPKLSLWQ
560 570 580 590 600
KVVESHKRMW KINQGLTSHH HWQSSPSEWP LLLRGINYWN KEHKQVYLLG
610 620 630 640 650
NAVTWWAATL SIITFGTYVL VTVFRWHLGT PLSTNKHVFN FNVQTFSYVL
660 670 680 690 700
GWALHYLPFF IMGRQLFLHH YLPALYFGIL ALGHFFEIFT GYLTSRSKYF
710 720 730 740 750
QQVAFVLVGL FSILSLVFYV NYSSLIYGTP WTKASCELTK PFSGWDYNCG
760 770 780 790 800
TFFDTLGEYD IQEKSLASES EIPTETVVVE AKQTPKAEPK LAKQDDHIES
810 820 830 840 850
PAAAEPVEEK EVKEEVEQLA PPLAVDFEEE TPKVEDPQVA DVDASSNDEK
860 870
SVEEKQQQEQ QQEQEQVEDE SVHQVQQ
Length:877
Mass (Da):99,935
Last modified:November 1, 1998 - 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:i3B0F6ED9C96DCC16
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF000232 Genomic DNA Translation: AAC31119.1
AP006852 Genomic DNA Translation: BAE44795.1
CP017629 Genomic DNA Translation: AOW30636.1

NCBI Reference Sequences

More...
RefSeqi
XP_716993.1, XM_711900.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3641393

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cal:CAALFM_C702890CA

<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
AF000232 Genomic DNA Translation: AAC31119.1
AP006852 Genomic DNA Translation: BAE44795.1
CP017629 Genomic DNA Translation: AOW30636.1
RefSeqiXP_716993.1, XM_711900.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi1224487, 3 interactors
STRINGi5476.C4YTX6

Chemistry databases

BindingDBiO74189
ChEMBLiCHEMBL3534

Protein family/group databases

CAZyiGT39 Glycosyltransferase Family 39

Genome annotation databases

GeneIDi3641393
KEGGical:CAALFM_C702890CA

Organism-specific databases

CGDiCAL0000192847 PMT1
EuPathDBiFungiDB:C7_02890C_A

Phylogenomic databases

InParanoidiO74189
KOiK00728
OMAiNFDFKDI
OrthoDBi203029at2759

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.109 1096

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O74189

Family and domain databases

InterProiView protein in InterPro
IPR027005 GlyclTrfase_39-like
IPR003342 Glyco_trans_39/83
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR032421 PMT_4TMC
PANTHERiPTHR10050 PTHR10050, 1 hit
PfamiView protein in Pfam
PF02815 MIR, 1 hit
PF02366 PMT, 1 hit
PF16192 PMT_4TMC, 1 hit
SMARTiView protein in SMART
SM00472 MIR, 3 hits
SUPFAMiSSF82109 SSF82109, 1 hit
PROSITEiView protein in PROSITE
PS50919 MIR, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPMT1_CANAL
<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: O74189
Secondary accession number(s): A0A1D8PR95, Q3MP65, Q5A5A9
<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 15, 1999
Last sequence update: November 1, 1998
Last modified: December 11, 2019
This is version 129 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Candida albicans
    Candida albicans: entries and gene names
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