Inactive tyrosine-protein kinase PRAG1

<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

Caution

<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

• identical protein binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.7

    "Dimerization of the Pragmin pseudo-kinase regulates protein tyrosine phosphorylation."
    Lecointre C., Simon V., Kerneur C., Allemand F., Fournet A., Montarras I., Pons J.L., Gelin M., Brignatz C., Urbach S., Labesse G., Roche S.
    Structure 26:545-554(2018) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 906-1368, MUTAGENESIS OF TYR-391; LEU-939; ASP-978; TYR-981; LYS-997; GLN-1021; ALA-1329; TYR-1349 AND LEU-1362, SUBUNIT, INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391, DOMAIN, LACK OF ATP-BINDING, FUNCTION.
• protein kinase activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell migration Source: Ensembl
• negative regulation of neuron projection development Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.3

    "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity."
    Tanaka H., Katoh H., Negishi M.
    J. Biol. Chem. 281:10355-10364(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH RND2.
• positive regulation of Rho protein signal transduction Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.3

    "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity."
    Tanaka H., Katoh H., Negishi M.
    J. Biol. Chem. 281:10355-10364(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH RND2.
• protein phosphorylation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of cell motility Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin creates a feed-forward C-terminal Src kinase activation loop that promotes cell motility."
    Senda Y., Murata-Kamiya N., Hatakeyama M.
    Cancer Sci. 107:972-980(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391; TYR-238 AND TYR-343, SUBCELLULAR LOCATION, FUNCTION.
• regulation of cell shape Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.5

    "C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin creates a feed-forward C-terminal Src kinase activation loop that promotes cell motility."
    Senda Y., Murata-Kamiya N., Hatakeyama M.
    Cancer Sci. 107:972-980(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391; TYR-238 AND TYR-343, SUBCELLULAR LOCATION, FUNCTION.
• regulation of Notch signaling pathway Source: UniProtKB

<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

Organism-specific databases

<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>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>Keywords - Cellular componentⁱ

<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

<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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

Gene expression databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• identical protein binding Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Dimerization of the Pragmin pseudo-kinase regulates protein tyrosine phosphorylation."
    Lecointre C., Simon V., Kerneur C., Allemand F., Fournet A., Montarras I., Pons J.L., Gelin M., Brignatz C., Urbach S., Labesse G., Roche S.
    Structure 26:545-554(2018) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 906-1368, MUTAGENESIS OF TYR-391; LEU-939; ASP-978; TYR-981; LYS-997; GLN-1021; ALA-1329; TYR-1349 AND LEU-1362, SUBUNIT, INTERACTION WITH CSK, PHOSPHORYLATION AT TYR-391, DOMAIN, LACK OF ATP-BINDING, FUNCTION.

Protein-protein interaction databases

<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

3D structure databases

<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

Region

Compositional bias

<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

<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

Family and domain databases

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

        10         20         30         40         50
MSACSDFVEH IWKPGSCKNC FCLRSDHQLT AGHPKARASS LPAGARLPAR 
        60         70         80         90        100
PEICRLEDEG VNGLAYSKPT IAVKPTMMTS ETADLWTEAS LSAEVPKVNW 
       110        120        130        140        150
RRTPGKLLLQ KQEDGPIVYL GSFRGMQKAA GPLACTDSNS RCPPAYTMVG 
       160        170        180        190        200
LHNLEARVDR NTALQPVNFQ EEKAGREELP SAQESFRQKL AAFTGMTSSC 
       210        220        230        240        250
LKGPRPCTSP QPLRESLPSE DDSDQRCSPS GDSEGGEYCS ILDCRPESRD 
       260        270        280        290        300
AVHNTEGSGR RRGDCSPICW EQGTCTRPTE EEKQALNFPR ECCGQGSTAN 
       310        320        330        340        350
PPHLGPKKPS LNSEAASSSD GLSCGSSRSG ANSPFAPHLE NDYCSLVKEP 
       360        370        380        390        400
TSVKQQDSGC HLVNSGKYVG QAVDLQPPAL PREAVQPEPI YAESAKRKKA 
       410        420        430        440        450
APVPQRPEPK KEQVSSGQVW TGDTWSQKTP SGWSQEREGP NAAPQVATTI 
       460        470        480        490        500
TVIAAHPEED HRTIYLSSPD SAVGVQWPRG SLNQDLHGSG EEPLVVQGLS 
       510        520        530        540        550
SRESHPHNMT ENSSKEKPAI PPKLSKSSPG GSPVSPAAPP LTDHSDGNTS 
       560        570        580        590        600
GSSVGSQPSS RVPTNLTSSC QTNGVAAGDP AKCPPQANSS VLDQRRPRYQ 
       610        620        630        640        650
TGAWSRQCRI EEEEEVGQEL LSQSWGRELE NGIADHSNSS TWHRLHPIDG 
       660        670        680        690        700
ASGQNGKTNS GMSKSASFAF EFPKDRGRLE SFSPPPPPPK SRHLLKMNKS 
       710        720        730        740        750
SSDLEKVSQS SAESLSPSFR GAHVSFTTGS TDSLASDSRT CSDGGPSCEA 
       760        770        780        790        800
THSPTISGKK LFAPVPFPSG STEDVSPSGP AQPPPLPQKK IVSRAASSPD 
       810        820        830        840        850
GFFWTQGSPK PRTASPKLNL SHSETNVCAH DEPPLSYSLN SGNHPHHVFS 
       860        870        880        890        900
SSEPLEKAFK GSVPWAPALG PANSKGGCGS PNLQGRAATS TSSSQLSVSS 
       910        920        930        940        950
QASTGSSQLQ LHSLLSSISS KEGTYAKLGG LYTQSLARLV TKCEDLFMGG 
       960        970        980        990       1000
LKTELRFDEN SWSLFKLICN KPCCDSGDAI YYGATCSKDP DSIYAVKICK 
      1010       1020       1030       1040       1050
TPEPKSASYC SPSVPVHFNI QQDCGHFVAS VPSSMLAFPD TSSKDPAPAA 
      1060       1070       1080       1090       1100
PSHTPAQEQD CVVVITREVP HQTASDFVRD SVASHRAEPE VYERRVCFLL 
      1110       1120       1130       1140       1150
LQLCNGLEHL KEHGIIHRDL CLENLLLVHC NPQSSPGPSA NPSVPTTTSR 
      1160       1170       1180       1190       1200
CPSAAPAATT ACQGGPGEKH LPRLIISNFL KAKQKPGGTT NLQQKKSQAR 
      1210       1220       1230       1240       1250
LAPEIVSASQ YRKFDEFQTG ILIYELLHQP NPFEVRAQLR ERDYRREDLP 
      1260       1270       1280       1290       1300
PLPTLSLYSP GLQQLAHLLL EADPIKRIRI GEAKRVLQCL LWGPRRELVE 
      1310       1320       1330       1340       1350
QPCPSEEVLC NTLHNWIDMK RALMMMKFAE KAVERRRGVE LEDWLCCQYL 
      1360 
ASAEPGALLQ SLKLLQLL                                    

Sequence databases

Genome annotation databases

<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

• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families