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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

Pin1

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

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (By similarity). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (By similarity). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (By similarity).By similarity1 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>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

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • GTPase activating protein binding Source: MGI
  • mitogen-activated protein kinase kinase binding Source: MGI
  • motor activity Source: ParkinsonsUK-UCL
  • peptidyl-prolyl cis-trans isomerase activity Source: MGI
  • phosphoprotein binding Source: ARUK-UCL
  • phosphoserine residue binding Source: MGI
  • phosphothreonine residue binding Source: MGI

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 functionIsomerase, Rotamase
Biological processCell cycle

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.2.1.8 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling

<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:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8)
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name:
PPIase Pin1
<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:Pin1
<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 9

Organism-specific databases

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

More...
MGIi
MGI:1346036 Pin1

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

Animals display more and larger germinal centers.1 Publication

<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_00001934361 – 165Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1Add BLAST165

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 residuei48N6-acetyllysineBy similarity1
Modified residuei73Phosphoserine; by DAPK1By similarity1
Modified residuei110PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9QUR7

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9QUR7

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

More...
PaxDbi
Q9QUR7

PRoteomics IDEntifications database

More...
PRIDEi
Q9QUR7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9QUR7

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

More...
PhosphoSitePlusi
Q9QUR7

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000032171 Expressed in 274 organ(s), highest expression level in embryo

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9QUR7 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

Interacts with STIL (PubMed:16024801). Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML and BCL-6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (By similarity). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (By similarity).By similarity2 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204839, 11 interactors

Database of interacting proteins

More...
DIPi
DIP-44280N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q9QUR7

Protein interaction database and analysis system

More...
IntActi
Q9QUR7, 7 interactors

Molecular INTeraction database

More...
MINTi
Q9QUR7

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000034689

<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
Q9QUR7

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

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SMRi
Q9QUR7

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

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>Domaini5 – 39WWPROSITE-ProRule annotationAdd BLAST35
Domaini54 – 165PpiCPROSITE-ProRule annotationAdd BLAST112

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The WW domain is required for the interaction with STIL and KIF20B.

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3259 Eukaryota
COG0760 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00640000091578

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000275331

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG002101

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9QUR7

KEGG Orthology (KO)

More...
KOi
K09578

Identification of Orthologs from Complete Genome Data

More...
OMAi
DEVQCLH

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0RO7

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9QUR7

TreeFam database of animal gene trees

More...
TreeFami
TF101101

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00201 WW, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00456 WW, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51045 SSF51045, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 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.

Q9QUR7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG
60 70 80 90 100
QGEPAKVRCS HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS
110 120 130 140 150
GEEDFESLAS QFSDCSSAKA RGDLGPFSRG QMQKPFEDAS FALRTGEMSG
160
PVFTDSGIHI ILRTE
Length:165
Mass (Da):18,370
Last modified:May 1, 2000 - 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:i188E95F009176B1F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB009691 mRNA Translation: BAA87037.1
AB009692 Genomic DNA Translation: BAA87038.1
AK002665 mRNA Translation: BAB22270.1
AK003369 mRNA Translation: BAB22743.1
AK054045 mRNA Translation: BAC35631.1
AK150652 mRNA Translation: BAE29739.1
AK160228 mRNA Translation: BAE35702.1
BC038254 mRNA Translation: AAH38254.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS22882.1

Protein sequence database of the Protein Information Resource

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PIRi
JC7136

NCBI Reference Sequences

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RefSeqi
NP_075860.1, NM_023371.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.7906

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23988

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:23988

UCSC genome browser

More...
UCSCi
uc009ojd.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
AB009691 mRNA Translation: BAA87037.1
AB009692 Genomic DNA Translation: BAA87038.1
AK002665 mRNA Translation: BAB22270.1
AK003369 mRNA Translation: BAB22743.1
AK054045 mRNA Translation: BAC35631.1
AK150652 mRNA Translation: BAE29739.1
AK160228 mRNA Translation: BAE35702.1
BC038254 mRNA Translation: AAH38254.1
CCDSiCCDS22882.1
PIRiJC7136
RefSeqiNP_075860.1, NM_023371.3
UniGeneiMm.7906

3D structure databases

ProteinModelPortaliQ9QUR7
SMRiQ9QUR7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204839, 11 interactors
DIPiDIP-44280N
ELMiQ9QUR7
IntActiQ9QUR7, 7 interactors
MINTiQ9QUR7
STRINGi10090.ENSMUSP00000034689

PTM databases

iPTMnetiQ9QUR7
PhosphoSitePlusiQ9QUR7

Proteomic databases

EPDiQ9QUR7
MaxQBiQ9QUR7
PaxDbiQ9QUR7
PRIDEiQ9QUR7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171
GeneIDi23988
KEGGimmu:23988
UCSCiuc009ojd.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5300
MGIiMGI:1346036 Pin1

Phylogenomic databases

eggNOGiKOG3259 Eukaryota
COG0760 LUCA
GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
HOVERGENiHBG002101
InParanoidiQ9QUR7
KOiK09578
OMAiDEVQCLH
OrthoDBiEOG091G0RO7
PhylomeDBiQ9QUR7
TreeFamiTF101101

Enzyme and pathway databases

BRENDAi5.2.1.8 3474
ReactomeiR-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9QUR7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000032171 Expressed in 274 organ(s), highest expression level in embryo
GenevisibleiQ9QUR7 MM

Family and domain databases

CDDicd00201 WW, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit
SMARTiView protein in SMART
SM00456 WW, 1 hit
SUPFAMiSSF51045 SSF51045, 1 hit
PROSITEiView protein in PROSITE
PS01096 PPIC_PPIASE_1, 1 hit
PS50198 PPIC_PPIASE_2, 1 hit
PS01159 WW_DOMAIN_1, 1 hit
PS50020 WW_DOMAIN_2, 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 nameiPIN1_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: Q9QUR7
Secondary accession number(s): Q543B3
<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: January 23, 2002
Last sequence update: May 1, 2000
Last modified: December 5, 2018
This is version 145 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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