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Entry version 132 (18 Sep 2019)
Sequence version 1 (01 Mar 2003)
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Protein

Glycerol-3-phosphate phosphatase

Gene

Pgp

Organism
Mus musculus (Mouse)
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

Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:26755581, PubMed:24338473). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473).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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by orthovanadate, beryllium trifluoride, Ca2+ and EDTA.1 Publication

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

Kcat is 0.1 sec(-1) with glycerol-3-phosphate.1 Publication
  1. KM=0.42 mM for ADP1 Publication
  2. KM=1.23 mM for ATP1 Publication
  3. KM=1.48 mM for GDP1 Publication
  4. KM=1.47 mM for GTP1 Publication
  5. KM=1.29 mM for glycerol-3-phosphate1 Publication
  1. Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei34Nucleophile1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi34MagnesiumBy similarity1
Active sitei36Proton donorCurated1
Metal bindingi36Magnesium; via carbonyl oxygenBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei204Important for substrate specificity1 Publication1
Metal bindingi260MagnesiumBy similarity1

<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 functionHydrolase, Protein phosphatase
Biological processCarbohydrate metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.74 3474

<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:
Glycerol-3-phosphate phosphataseCurated (EC:3.1.3.211 Publication)
Short name:
G3PP1 Publication
Alternative name(s):
Aspartate-based ubiquitous Mg(2+)-dependent phosphatase1 Publication (EC:3.1.3.481 Publication)
Short name:
AUM1 Publication
Phosphoglycolate phosphatase1 Publication
Short name:
PGP1 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:PgpImported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1914328 Pgp

<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

<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>Mutagenesisi34D → N: Abolishes phosphatase activity. 1 Publication1
Mutagenesisi41R → N: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with R-44 and I-45. 1 Publication1
Mutagenesisi44T → R: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and I-45. 1 Publication1
Mutagenesisi45A → I: Slightly increases phosphatase activity with p-nitrophenylphosphate; when associated with N-41 and R-44. 1 Publication1
Mutagenesisi67T → S: Strongly reduces phosphatase activity; when associated with R-71; R-72 and A-73. Abolishes phosphatase activity; when associated with R-72 and A-73. 1 Publication1
Mutagenesisi71S → R: Mildly reduces phosphatase activity; when associated with R-72 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-72 and A-73. 1 Publication1
Mutagenesisi72K → R: Mildly reduces phosphatase activity; when associated with R-71 and A-73. Strongly reduces phosphatase activity; when associated with S-67; R-71 and A-73. Abolishes phosphatase activity; when associated with S-67 and A-73. 1 Publication1
Mutagenesisi73T → A: Abolishes phosphatase activity. Abolishes phosphatase activity; when associated with S-67 and R-72. Strongly reduces phosphatase activity; when associated with S-67; R-71 and R-72. Mildly reduces phosphatase activity; when associated with R-71 and R-72. 1 Publication1
Mutagenesisi204L → H: Strongly increases activity with pyridoxal phosphate. 1 Publication1

<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_00003168891 – 321Glycerol-3-phosphate phosphataseAdd BLAST321

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3609

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8CHP8

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q8CHP8

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8CHP8

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

More...
PaxDbi
Q8CHP8

PeptideAtlas

More...
PeptideAtlasi
Q8CHP8

PRoteomics IDEntifications database

More...
PRIDEi
Q8CHP8

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00380195
Q8CHP8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8CHP8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8CHP8

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed with higher expression in testis, heart, skeletal muscle and islet tissue (at protein level).2 Publications

<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

Up-regulated in white adipose tissue and down-regulated in brown adipose tissue upon fasting.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000043445 Expressed in 267 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8CHP8 MM

<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

Homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000052866

<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

1321
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
Q8CHP8

Database of comparative protein structure models

More...
ModBasei
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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2882 Eukaryota
COG0647 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160577

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000068104

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8CHP8

KEGG Orthology (KO)

More...
KOi
K19269

Identification of Orthologs from Complete Genome Data

More...
OMAi
VFGTAYC

Database of Orthologous Groups

More...
OrthoDBi
982374at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8CHP8

TreeFam database of animal gene trees

More...
TreeFami
TF314344

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1000, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036412 HAD-like_sf
IPR006357 HAD-SF_hydro_IIA
IPR023214 HAD_sf
IPR006349 PGP_euk

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13344 Hydrolase_6, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000915 PGP-type_phosphatase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56784 SSF56784, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01460 HAD-SF-IIA, 1 hit
TIGR01452 PGP_euk, 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>. 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.

Q8CHP8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEAEAGGDE ARCVRLSAER AKLLLAEVDT LLFDCDGVLW RGETAVPGAP
60 70 80 90 100
ETLRALRARG KRLGFITNNS SKTRTAYAEK LRRLGFGGPV GPEAGLEVFG
110 120 130 140 150
TAYCSALYLR QRLAGVPDPK AYVLGSPALA AELEAVGVTS VGVGPDVLHG
160 170 180 190 200
DGPSDWLAVP LEPDVRAVVV GFDPHFSYMK LTKAVRYLQQ PDCLLVGTNM
210 220 230 240 250
DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI FDCVSQEYGI
260 270 280 290 300
NPERTVMVGD RLDTDILLGS TCSLKTILTL TGVSSLEDVK SNQESDCMFK
310 320
KKMVPDFYVD SIADLLPALQ G
Length:321
Mass (Da):34,541
Last modified:March 1, 2003 - 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:iF083ED0432327A83
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
BC040100 mRNA Translation: AAH40100.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS28482.1

NCBI Reference Sequences

More...
RefSeqi
NP_080230.2, NM_025954.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
67078

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:67078

UCSC genome browser

More...
UCSCi
uc008awe.1 mouse

<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
BC040100 mRNA Translation: AAH40100.1
CCDSiCCDS28482.1
RefSeqiNP_080230.2, NM_025954.3

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
4BKMX-ray2.65A/B/C/D114-233[»]
SMRiQ8CHP8
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052866

PTM databases

iPTMnetiQ8CHP8
PhosphoSitePlusiQ8CHP8

2D gel databases

REPRODUCTION-2DPAGEiIPI00380195
Q8CHP8

Proteomic databases

CPTACinon-CPTAC-3609
EPDiQ8CHP8
jPOSTiQ8CHP8
MaxQBiQ8CHP8
PaxDbiQ8CHP8
PeptideAtlasiQ8CHP8
PRIDEiQ8CHP8

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
67078
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445
GeneIDi67078
KEGGimmu:67078
UCSCiuc008awe.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
283871
MGIiMGI:1914328 Pgp

Phylogenomic databases

eggNOGiKOG2882 Eukaryota
COG0647 LUCA
GeneTreeiENSGT00940000160577
HOGENOMiHOG000068104
InParanoidiQ8CHP8
KOiK19269
OMAiVFGTAYC
OrthoDBi982374at2759
PhylomeDBiQ8CHP8
TreeFamiTF314344

Enzyme and pathway databases

BRENDAi3.1.3.74 3474

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Pgp mouse

Protein Ontology

More...
PROi
PR:Q8CHP8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000043445 Expressed in 267 organ(s), highest expression level in testis
GenevisibleiQ8CHP8 MM

Family and domain databases

Gene3Di3.40.50.1000, 2 hits
InterProiView protein in InterPro
IPR036412 HAD-like_sf
IPR006357 HAD-SF_hydro_IIA
IPR023214 HAD_sf
IPR006349 PGP_euk
PfamiView protein in Pfam
PF13344 Hydrolase_6, 1 hit
PIRSFiPIRSF000915 PGP-type_phosphatase, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
TIGRFAMsiTIGR01460 HAD-SF-IIA, 1 hit
TIGR01452 PGP_euk, 1 hit

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 nameiPGP_MOUSE
<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: Q8CHP8
<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: February 5, 2008
Last sequence update: March 1, 2003
Last modified: September 18, 2019
This is version 132 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 programChordata 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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