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Entry version 189 (11 Dec 2019)
Sequence version 2 (16 Jun 2003)
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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

PMT2

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

Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.4 Publications

Miscellaneous

Present with 6510 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

<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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YAL023C-MONOMER
YEAST:YAL023C-MONOMER

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 2Curated (EC:2.4.1.1091 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:PMT21 Publication
Synonyms:FUN251 Publication
Ordered Locus Names:YAL023CImported
<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 I

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YAL023C

Saccharomyces Genome Database

More...
SGDi
S000000021 PMT2

<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 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 domaini2 – 64CytoplasmicSequence analysisAdd BLAST63
<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>Transmembranei65 – 85HelicalSequence analysisAdd BLAST21
Topological domaini86 – 167LumenalSequence analysisAdd BLAST82
Transmembranei168 – 188HelicalSequence analysisAdd BLAST21
Topological domaini189 – 198CytoplasmicSequence analysis10
Transmembranei199 – 219HelicalSequence analysisAdd BLAST21
Topological domaini220 – 251LumenalSequence analysisAdd BLAST32
Transmembranei252 – 272HelicalSequence analysisAdd BLAST21
Topological domaini273 – 289CytoplasmicSequence analysisAdd BLAST17
Transmembranei290 – 310HelicalSequence analysisAdd BLAST21
Topological domaini311 – 609LumenalSequence analysisAdd BLAST299
Transmembranei610 – 630HelicalSequence analysisAdd BLAST21
Topological domaini631 – 647CytoplasmicSequence analysisAdd BLAST17
Transmembranei648 – 668HelicalSequence analysisAdd BLAST21
Topological domaini669 – 676LumenalSequence analysis8
Transmembranei677 – 697HelicalSequence analysisAdd BLAST21
Topological domaini698 – 710CytoplasmicSequence analysisAdd BLAST13
Transmembranei711 – 731HelicalSequence analysisAdd BLAST21
Topological domaini732 – 759LumenalSequence analysisAdd BLAST28

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

Leads to diminished in vitro and in vivo O-mannosylation activity.2 Publications

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001214922 – 759Dolichyl-phosphate-mannose--protein mannosyltransferase 2Add BLAST758

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 residuei2N-acetylserineCombined sources1
Modified residuei32PhosphoserineCombined sources1
Modified residuei38PhosphoserineCombined sources1
Modified residuei39PhosphoserineCombined sources1
<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>Glycosylationi131N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi155N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi403N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P31382

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

More...
PaxDbi
P31382

PRoteomics IDEntifications database

More...
PRIDEi
P31382

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P31382

<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. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1.

Forms also a minor complex with PMT5.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31743, 241 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3036 PMT1-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex
CPX-3038 PMT5-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex

Database of interacting proteins

More...
DIPi
DIP-6720N

Protein interaction database and analysis system

More...
IntActi
P31382, 3 interactors

Molecular INTeraction database

More...
MINTi
P31382

STRING: functional protein association networks

More...
STRINGi
4932.YAL023C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P31382 protein

<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

1759
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P31382

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Domaini339 – 394MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini407 – 463MIR 2PROSITE-ProRule annotationAdd BLAST57
Domaini471 – 529MIR 3PROSITE-ProRule annotationAdd BLAST59

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000157526

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P31382

KEGG Orthology (KO)

More...
KOi
K00728

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWAMGRV

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.

<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.

P31382-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK
60 70 80 90 100
EKPAAQSSLL RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG
110 120 130 140 150
SYYLRHEFYH DVHPPLGKML VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK
160 170 180 190 200
MRLFNASFSA LCVPLAYFTA KAIGFSLPTV WLMTVLVLFE NSYSTLGRFI
210 220 230 240 250
LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG ISLGCTISVK
260 270 280 290 300
MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI
310 320 330 340 350
FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS
360 370 380 390 400
IKNQALGGSL LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW
410 420 430 440 450
SENETDIEYL KPGTSYRLVH KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV
460 470 480 490 500
VGDNKDNWVI EIMDQRGDED PEKLHTLTTS FRIKNLEMGC YLAQTGNSLP
510 520 530 540 550
EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED FQYPKTNFLK
560 570 580 590 600
DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP
610 620 630 640 650
KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM
660 670 680 690 700
GGFYPLLAWG LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW
710 720 730 740 750
SRSKCGRIMR FVLYAGFMAL VIGCFWYFSP ISFGMEGPSS NFRYLNWFST

WDIADKQEA
Length:759
Mass (Da):86,870
Last modified:June 16, 2003 - 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:iB1E1480C2E04BE3D
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
L05146 Genomic DNA Translation: AAC04934.2
BK006935 Genomic DNA Translation: DAA06965.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S36711

NCBI Reference Sequences

More...
RefSeqi
NP_009379.2, NM_001178168.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YAL023C_mRNA; YAL023C; YAL023C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851210

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YAL023C

<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
L05146 Genomic DNA Translation: AAC04934.2
BK006935 Genomic DNA Translation: DAA06965.1
PIRiS36711
RefSeqiNP_009379.2, NM_001178168.1

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
6P25electron microscopy3.20B1-759[»]
6P28X-ray1.35A337-532[»]
6P2Relectron microscopy3.20B1-759[»]
SMRiP31382
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31743, 241 interactors
ComplexPortaliCPX-3036 PMT1-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex
CPX-3038 PMT5-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex
DIPiDIP-6720N
IntActiP31382, 3 interactors
MINTiP31382
STRINGi4932.YAL023C

Protein family/group databases

CAZyiGT39 Glycosyltransferase Family 39

PTM databases

iPTMnetiP31382

Proteomic databases

MaxQBiP31382
PaxDbiP31382
PRIDEiP31382

Genome annotation databases

EnsemblFungiiYAL023C_mRNA; YAL023C; YAL023C
GeneIDi851210
KEGGisce:YAL023C

Organism-specific databases

EuPathDBiFungiDB:YAL023C
SGDiS000000021 PMT2

Phylogenomic databases

HOGENOMiHOG000157526
InParanoidiP31382
KOiK00728
OMAiFWAMGRV

Enzyme and pathway databases

UniPathwayiUPA00378
BioCyciMetaCyc:YAL023C-MONOMER
YEAST:YAL023C-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P31382
RNActiP31382 protein

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 nameiPMT2_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: P31382
Secondary accession number(s): D6VPJ5
<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 1, 1993
Last sequence update: June 16, 2003
Last modified: December 11, 2019
This is version 189 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, Reference proteome

Documents

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