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Protein

Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase

Gene

ALG3

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

Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin.2 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.
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

  • alpha-1,3-mannosyltransferase activity Source: SGD
  • dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity Source: SGD

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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YBL082C-MONOMER
YEAST:YBL082C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.258 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-446193 Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein

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

More...
UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT58 Glycosyltransferase Family 58

<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:
Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase (EC:2.4.1.258)
Alternative name(s):
Asparagine-linked glycosylation protein 3
Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase
Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
HM-1 killer toxin resistance protein
<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:ALG3
Synonyms:RHK1
Ordered Locus Names:YBL082C
ORF Names:YBL0720
<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 II

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000000178 ALG3

<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

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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 41LumenalSequence analysisAdd BLAST41
<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>Transmembranei42 – 62HelicalSequence analysisAdd BLAST21
Topological domaini63 – 95CytoplasmicSequence analysisAdd BLAST33
Transmembranei96 – 116HelicalSequence analysisAdd BLAST21
Topological domaini117 – 137LumenalSequence analysisAdd BLAST21
Transmembranei138 – 158HelicalSequence analysisAdd BLAST21
Topological domaini159 – 171CytoplasmicSequence analysisAdd BLAST13
Transmembranei172 – 192HelicalSequence analysisAdd BLAST21
Topological domaini193 – 216LumenalSequence analysisAdd BLAST24
Transmembranei217 – 237HelicalSequence analysisAdd BLAST21
Topological domaini238 – 242CytoplasmicSequence analysis5
Transmembranei243 – 263HelicalSequence analysisAdd BLAST21
Topological domaini264 – 302LumenalSequence analysisAdd BLAST39
Transmembranei303 – 323HelicalSequence analysisAdd BLAST21
Topological domaini324 – 345CytoplasmicSequence analysisAdd BLAST22
Transmembranei346 – 366HelicalSequence analysisAdd BLAST21
Topological domaini367 – 381LumenalSequence analysisAdd BLAST15
Transmembranei382 – 402HelicalSequence analysisAdd BLAST21
Topological domaini403 – 415CytoplasmicSequence analysisAdd BLAST13
Transmembranei416 – 436HelicalSequence analysisAdd BLAST21
Topological domaini437 – 458LumenalSequence analysisAdd BLAST22

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi275A → V in ALG3-1; leads to an underglycosylation of secretory proteins. 1

<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_00000805651 – 458Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferaseAdd BLAST458

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38179

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

More...
PaxDbi
P38179

PRoteomics IDEntifications database

More...
PRIDEi
P38179

<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
32621, 178 interactors

Database of interacting proteins

More...
DIPi
DIP-4854N

Molecular INTeraction database

More...
MINTi
P38179

STRING: functional protein association networks

More...
STRINGi
4932.YBL082C

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P38179

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

<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 58 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013904

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000237555

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38179

KEGG Orthology (KO)

More...
KOi
K03845

Identification of Orthologs from Complete Genome Data

More...
OMAi
TKKVPPY

Database of Orthologous Groups

More...
OrthoDBi
EOG092C26UZ

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007873 Glycosyltransferase_ALG3

The PANTHER Classification System

More...
PANTHERi
PTHR12646 PTHR12646, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05208 ALG3, 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.

P38179-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEGEQSPQGE KSLQRKQFVR PPLDLWQDLK DGVRYVIFDC RANLIVMPLL
60 70 80 90 100
ILFESMLCKI IIKKVAYTEI DYKAYMEQIE MIQLDGMLDY SQVSGGTGPL
110 120 130 140 150
VYPAGHVLIY KMMYWLTEGM DHVERGQVFF RYLYLLTLAL QMACYYLLHL
160 170 180 190 200
PPWCVVLACL SKRLHSIYVL RLFNDCFTTL FMVVTVLGAI VASRCHQRPK
210 220 230 240 250
LKKSLALVIS ATYSMAVSIK MNALLYFPAM MISLFILNDA NVILTLLDLV
260 270 280 290 300
AMIAWQVAVA VPFLRSFPQQ YLHCAFNFGR KFMYQWSINW QMMDEEAFND
310 320 330 340 350
KRFHLALLIS HLIALTTLFV TRYPRILPDL WSSLCHPLRK NAVLNANPAK
360 370 380 390 400
TIPFVLIASN FIGVLFSRSL HYQFLSWYHW TLPILIFWSG MPFFVGPIWY
410 420 430 440 450
VLHEWCWNSY PPNSQASTLL LALNTVLLLL LALTQLSGSV ALAKSHLRTT

SSMEKKLN
Length:458
Mass (Da):52,861
Last modified:October 1, 1994 - 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:i1C2FEAD6D459C249
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 conflicti86G → R in AAA75352 (PubMed:7754714).Curated1
Sequence conflicti187 – 198LGAIV…RCHQR → FRGYRGQQVPSA in AAA75352 (PubMed:7754714).CuratedAdd BLAST12
Sequence conflicti266S → Q in AAA75352 (PubMed:7754714).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
X79489 Genomic DNA Translation: CAA56024.1
Z35844 Genomic DNA Translation: CAA84904.1
M89908 Genomic DNA Translation: AAA75352.1
BK006936 Genomic DNA Translation: DAA07041.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S45424

NCBI Reference Sequences

More...
RefSeqi
NP_009471.1, NM_001178322.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBL082C_mRNA; YBL082C_mRNA; YBL082C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852196

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBL082C

<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
X79489 Genomic DNA Translation: CAA56024.1
Z35844 Genomic DNA Translation: CAA84904.1
M89908 Genomic DNA Translation: AAA75352.1
BK006936 Genomic DNA Translation: DAA07041.1
PIRiS45424
RefSeqiNP_009471.1, NM_001178322.1

3D structure databases

ProteinModelPortaliP38179
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32621, 178 interactors
DIPiDIP-4854N
MINTiP38179
STRINGi4932.YBL082C

Protein family/group databases

CAZyiGT58 Glycosyltransferase Family 58

Proteomic databases

MaxQBiP38179
PaxDbiP38179
PRIDEiP38179

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
852196
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL082C_mRNA; YBL082C_mRNA; YBL082C
GeneIDi852196
KEGGisce:YBL082C

Organism-specific databases

SGDiS000000178 ALG3

Phylogenomic databases

GeneTreeiENSGT00390000013904
HOGENOMiHOG000237555
InParanoidiP38179
KOiK03845
OMAiTKKVPPY
OrthoDBiEOG092C26UZ

Enzyme and pathway databases

UniPathwayi
UPA00378

BioCyciMetaCyc:YBL082C-MONOMER
YEAST:YBL082C-MONOMER
BRENDAi2.4.1.258 984
ReactomeiR-SCE-446193 Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P38179

Family and domain databases

InterProiView protein in InterPro
IPR007873 Glycosyltransferase_ALG3
PANTHERiPTHR12646 PTHR12646, 1 hit
PfamiView protein in Pfam
PF05208 ALG3, 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 nameiALG3_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: P38179
Secondary accession number(s): D6VPS1
<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: October 1, 1994
Last sequence update: October 1, 1994
Last modified: December 5, 2018
This is version 156 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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