BioPerl
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t/data/interpro_relationship.xml view on Meta::CPAN
<db_xref db="BLOCKS" dbkey="IPB000010"/>
<db_xref db="MEROPS" dbkey="C1"/>
<db_xref db="MEROPS" dbkey="C13"/>
<db_xref db="MEROPS" dbkey="I25"/>
<db_xref db="MEROPS" dbkey="M10"/>
<db_xref db="MEROPS" dbkey="M12"/>
<db_xref db="PROSITEDOC" dbkey="PDOC00259"/>
</external_doc_list>
<structure_db_links>
<db_xref db="PDB" dbkey="1a67"/>
<db_xref db="PDB" dbkey="1a90"/>
<db_xref db="PDB" dbkey="1cew"/>
<db_xref db="PDB" dbkey="1cyu"/>
<db_xref db="PDB" dbkey="1cyv"/>
<db_xref db="PDB" dbkey="1dvc"/>
<db_xref db="PDB" dbkey="1dvd"/>
<db_xref db="PDB" dbkey="1eqk"/>
<db_xref db="PDB" dbkey="1g96"/>
<db_xref db="PDB" dbkey="1gd3"/>
<db_xref db="PDB" dbkey="1gd4"/>
<db_xref db="PDB" dbkey="1n9j"/>
<db_xref db="PDB" dbkey="1nb3"/>
<db_xref db="PDB" dbkey="1nb5"/>
<db_xref db="PDB" dbkey="1r4c"/>
<db_xref db="PDB" dbkey="1rn7"/>
<db_xref db="PDB" dbkey="1roa"/>
<db_xref db="PDB" dbkey="1stf"/>
<db_xref db="PDB" dbkey="1tij"/>
<db_xref db="PDB" dbkey="1yvb"/>
<db_xref db="CATH" dbkey="3.10.450.10"/>
<db_xref db="SCOP" dbkey="d.17.1.2"/>
</structure_db_links>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="39"/>
<taxon_data name="Eukaryota" proteins_count="873"/>
<taxon_data name="Arabidopsis thaliana" proteins_count="11"/>
<taxon_data name="Rice spp." proteins_count="35"/>
<taxon_data name="Other Eukaryotes" proteins_count="3"/>
<taxon_data name="Other Eukaryotes" proteins_count="3"/>
<taxon_data name="Nematoda" proteins_count="3"/>
<taxon_data name="Caenorhabditis elegans" proteins_count="3"/>
<taxon_data name="Arthropoda" proteins_count="122"/>
<taxon_data name="Fruit Fly" proteins_count="6"/>
<taxon_data name="Chordata" proteins_count="376"/>
<taxon_data name="Human" proteins_count="40"/>
<taxon_data name="Mouse" proteins_count="69"/>
<taxon_data name="Virus" proteins_count="44"/>
<taxon_data name="Plastid Group" proteins_count="305"/>
<taxon_data name="Green Plants" proteins_count="305"/>
<taxon_data name="Metazoa" proteins_count="546"/>
<taxon_data name="Plastid Group" proteins_count="11"/>
<taxon_data name="Other Eukaryotes" proteins_count="4"/>
</taxonomy_distribution>
<sec_list>
<sec_ac acc="IPR001713"/>
</sec_list>
</interpro>
<interpro id="IPR000011" protein_count="359" short_name="UBQ-activ_enz_E1-like" type="Region">
<name>Ubiquitin-activating enzyme, E1-like</name>
<abstract>
<p>The post-translational attachment of ubiquitin (<db_xref db="INTERPRO" dbkey="IPR000626"/>) to proteins (ubiquitinylation) alters the function, location or trafficking of a protein, or targets it to the 26S proteasome for degradation [<cite idref=...
</abstract>
<class_list>
<classification id="GO:0006464" class_type="GO">
<category>Biological Process</category>
<description>protein modification process</description>
</classification>
<classification id="GO:0008641" class_type="GO">
<category>Molecular Function</category>
<description>small protein activating enzyme activity</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="A2VE14"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="O42939"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P22515"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="Q02053"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="Q9UBE0"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00015619">
<author_list>Burger AM, Seth AK.</author_list>
<title>The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.</title>
<db_xref db="PUBMED" dbkey="15454246"/>
<journal>Eur. J. Cancer</journal>
<location issue="15" pages="2217-29" volume="40"/>
<year>2004</year>
</publication>
<publication id="PUB00015620">
<author_list>Passmore LA, Barford D.</author_list>
<title>Getting into position: the catalytic mechanisms of protein ubiquitylation.</title>
<db_xref db="PUBMED" dbkey="14998368"/>
<journal>Biochem. J.</journal>
<location issue="Pt 3" pages="513-25" volume="379"/>
<year>2004</year>
</publication>
<publication id="PUB00015621">
<author_list>Pickart CM, Fushman D.</author_list>
<title>Polyubiquitin chains: polymeric protein signals.</title>
<db_xref db="PUBMED" dbkey="15556404"/>
<location issue="6" pages="610-6" volume="8"/>
<year>2004</year>
</publication>
<publication id="PUB00015625">
<author_list>Sun L, Chen ZJ.</author_list>
<title>The novel functions of ubiquitination in signaling.</title>
<db_xref db="PUBMED" dbkey="15196553"/>
<journal>Curr. Opin. Cell Biol.</journal>
<location issue="2" pages="119-26" volume="16"/>
<year>2004</year>
</publication>
t/data/interpro_relationship.xml view on Meta::CPAN
<pub_list>
<publication id="PUB00006449">
<author_list>Karzai AW, Susskind MM, Sauer RT.</author_list>
<title>SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA).</title>
<db_xref db="PUBMED" dbkey="10393194"/>
<journal>EMBO J.</journal>
<location issue="13" pages="3793-9" volume="18"/>
<year>1999</year>
</publication>
<publication id="PUB00045920">
<author_list>Nonin-Lecomte S, Germain-Amiot N, Gillet R, Hallier M, Ponchon L, Dardel F, Felden B.</author_list>
<title>Ribosome hijacking: a role for small protein B during trans-translation.</title>
<db_xref db="PUBMED" dbkey="19132006"/>
<journal>EMBO Rep.</journal>
<location issue="2" pages="160-5" volume="10"/>
<year>2009</year>
</publication>
</pub_list>
<contains>
<rel_ref ipr_ref="IPR020081"/>
</contains>
<member_list>
<db_xref protein_count="2032" db="PFAM" dbkey="PF01668" name="SmpB"/>
<db_xref protein_count="2014" db="PRODOM" dbkey="PD004488" name="SmpB"/>
<db_xref protein_count="2022" db="TIGRFAMs" dbkey="TIGR00086" name="smpB"/>
<db_xref protein_count="1941" db="GENE3D" dbkey="G3DSA:2.40.280.10" name="SmpB"/>
<db_xref protein_count="2040" db="SSF" dbkey="SSF74982" name="SmpB"/>
<db_xref protein_count="1894" db="HAMAP" dbkey="MF_00023" name="SmpB"/>
</member_list>
<external_doc_list>
<db_xref db="PANDIT" dbkey="PF01668"/>
<db_xref db="MSDsite" dbkey="PS01317"/>
<db_xref db="BLOCKS" dbkey="IPB000037"/>
<db_xref db="PROSITEDOC" dbkey="PDOC01021"/>
</external_doc_list>
<structure_db_links>
<db_xref db="PDB" dbkey="1j1h"/>
<db_xref db="PDB" dbkey="1k8h"/>
<db_xref db="PDB" dbkey="1p6v"/>
<db_xref db="PDB" dbkey="1wjx"/>
<db_xref db="PDB" dbkey="2czj"/>
<db_xref db="CATH" dbkey="2.40.280.10"/>
<db_xref db="SCOP" dbkey="b.111.1.1"/>
</structure_db_links>
<taxonomy_distribution>
<taxon_data name="Bacteria" proteins_count="2041"/>
<taxon_data name="Cyanobacteria" proteins_count="55"/>
<taxon_data name="Synechocystis PCC 6803" proteins_count="1"/>
<taxon_data name="Eukaryota" proteins_count="8"/>
<taxon_data name="Fungi" proteins_count="1"/>
<taxon_data name="Arthropoda" proteins_count="1"/>
<taxon_data name="Metazoa" proteins_count="3"/>
<taxon_data name="Plastid Group" proteins_count="1"/>
</taxonomy_distribution>
</interpro>
<interpro id="IPR000038" protein_count="1164" short_name="Cell_Div_GTP-bd" type="Family">
<name>Cell division/GTP binding protein</name>
<abstract>
<p>Septins constitute a eukaryotic family of guanine nucleotide-binding proteins, most of which polymerise to form filaments [<cite idref="PUB00021050"/>]. Members of the family were first identified by genetic screening for <taxon tax_id="4932">Sacc...
<p>Septins are approximately 40-50 kDa in molecular mass, and typically comprise a conserved central core domain (more than 35% sequence identity between mammalian and yeast homologues) flanked by more divergent N- and C-termini. Most septins possess...
<p>A number of septin interaction partners have been identified in yeast, many of which are components of the budding site selection machinery, kinase cascades or of the ubiquitination pathway. It has been proposed that septins may act as a scaffold ...
<p>This entry represents a variety of septins and homologous sequences involved in the cell division process.</p>
</abstract>
<class_list>
<classification id="GO:0005525" class_type="GO">
<category>Molecular Function</category>
<description>GTP binding</description>
</classification>
<classification id="GO:0007049" class_type="GO">
<category>Biological Process</category>
<description>cell cycle</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref db="SWISSPROT" dbkey="A0LY86"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P25342"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P40797"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="P42208"/>
</example>
<example>
<db_xref db="SWISSPROT" dbkey="Q14141"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00010277">
<author_list>Haarer BK, Pringle JR.</author_list>
<title>Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck.</title>
<db_xref db="PUBMED" dbkey="3316985"/>
<journal>Mol. Cell. Biol.</journal>
<location issue="10" pages="3678-87" volume="7"/>
<year>1987</year>
</publication>
<publication id="PUB00010278">
<author_list>Hartwell LH.</author_list>
<title>Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis.</title>
<db_xref db="PUBMED" dbkey="4950437"/>
<journal>Exp. Cell Res.</journal>
<location issue="2" pages="265-76" volume="69"/>
<year>1971</year>
</publication>
<publication id="PUB00010316">
<author_list>Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, Hiraoka Y, Noda M.</author_list>
<title>Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures.</title>
<db_xref db="PUBMED" dbkey="9203580"/>
<journal>Genes Dev.</journal>
<location issue="12" pages="1535-47" volume="11"/>
<year>1997</year>
</publication>
<publication id="PUB00010351">
<author_list>Field CM, Kellogg D.</author_list>
<title>Septins: cytoskeletal polymers or signalling GTPases?</title>
<db_xref db="PUBMED" dbkey="10481176"/>
<journal>Trends Cell Biol.</journal>
<location issue="10" pages="387-94" volume="9"/>
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