BioPerl
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t/data/interpro_short.xml view on Meta::CPAN
</example_list>
<pub_list>
<publication id="PUB00002414">
<author_list>Fujikawa K., McMullen B.A.</author_list>
<title>Primary structure of the heavy chain of human factor XIIa.</title>
<db_xref db="MEDLINE" dbkey="85182674"/>
<journal>J. Biol. Chem.</journal>
<location firstpage="5328" lastpage="5341" volume="260"/>
<year>1985</year>
</publication>
<publication id="PUB00001541">
<author_list>Patthy L., Trexler M., Vali V., Banyai L., Varadi A.</author_list>
<title>Kringles: Modules specialized for protein binding.</title>
<db_xref db="MEDLINE" dbkey="84208845"/>
<journal>FEBS Lett.</journal>
<location firstpage="131" lastpage="136" volume="171"/>
<year>1984</year>
</publication>
<publication id="PUB00003257">
<author_list>Atkinson R.A., Williams R.J.P.</author_list>
<title>Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry.</title>
<db_xref db="MEDLINE" dbkey="90219023"/>
<journal>J. Mol. Biol.</journal>
<location firstpage="541" lastpage="552" volume="212"/>
<year>1990</year>
</publication>
<publication id="PUB00003400">
<author_list>Castellino F.J., Beals J.M.</author_list>
<title>The genetic relationships between the kringle domains of human plasminogen, prothrombin, tissue plasminogen activator, urokinase, and coagulation factor XII.</title>
<db_xref db="MEDLINE" dbkey="88230478"/>
<journal>J. Mol. Evol.</journal>
<location firstpage="358" lastpage="369" volume="26"/>
<year>1987</year>
</publication>
<publication id="PUB00000803">
<author_list>Patthy L.</author_list>
<title>Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.</title>
<db_xref db="MEDLINE" dbkey="85228216"/>
<journal>Cell</journal>
<location firstpage="657" lastpage="663" volume="41"/>
<year>1985</year>
</publication>
<publication id="PUB00001620">
<author_list>Takahashi K., Ikeo K., Gojobori T.</author_list>
<title>Evolutionary origin of numerous kringles in human and simian apolipoprotein(a).</title>
<db_xref db="MEDLINE" dbkey="91348198"/>
<journal>FEBS Lett.</journal>
<location firstpage="146" lastpage="148" volume="287"/>
<year>1991</year>
</publication>
<publication id="PUB00000355">
<author_list>Friezner Degen S.J., Stuart L.A., Han S., Jamison C.S.</author_list>
<title>Characterization of the mouse cDNA and gene coding for a hepatocyte growth factor-like protein: expression during development.</title>
<db_xref db="MEDLINE" dbkey="92002017"/>
<journal>Biochemistry</journal>
<location firstpage="9781" lastpage="9791" volume="30"/>
<year>1991</year>
</publication>
<publication id="PUB00002776">
<author_list>Miyazawa K., Shimomura T., Kitamura A., Kondo J., Morimoto Y., Kitamura N.</author_list>
<title>Molecular cloning and sequence analysis of the cDNA for a human serine protease reponsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII.</title>
<db_xref db="MEDLINE" dbkey="93252878"/>
<journal>J. Biol. Chem.</journal>
<location firstpage="10024" lastpage="10028" volume="268"/>
<year>1993</year>
</publication>
</pub_list>
<member_list>
<db_xref protein_count="91" db="PRINTS" dbkey="PR00018" name="KRINGLE"/>
<db_xref protein_count="126" db="PROFILE" dbkey="PS50070" name="KRINGLE_2"/>
<db_xref protein_count="161" db="PROSITE" dbkey="PS00021" name="KRINGLE_1"/>
<db_xref protein_count="128" db="PFAM" dbkey="PF00051" name="kringle"/>
<db_xref protein_count="126" db="PRODOM" dbkey="PD000395" name="Kringle"/>
<db_xref protein_count="115" db="SMART" dbkey="SM00130" name="KR"/>
</member_list>
<external_doc_list>
<db_xref db="BLOCKS" dbkey="IPB000001"/>
<db_xref db="PDOC" dbkey="PDOC00020"/>
</external_doc_list>
</interpro>
<interpro id="IPR000002" type="Domain" short_name="Fizzy" protein_count="57">
<name>Cdc20/Fizzy</name>
<abstract>
<p>The Cdc20/Fizzy region is almost always associated with the G-protein beta WD-40 repeat (<db_xref db="INTERPRO" dbkey="IPR001680"/>). Ubiquitin-mediated proteolysis due to the anaphase-promoting complex/cyclosome
(APC/C) is essential for separation of sister chromatids, requiring degradation of the anaphase inhibitor Pds1, and for exit from mitosis, requiring inactivation of cyclin B Cdk1 kinases <cite idref="PUB00006167"/>. In <taxon tax_id="4890">yeast</t...
<p>This domain is also found in a number of, as yet, uncharacterised proteins. These include a <taxon tax_id="40674">mammalian</taxon> protein, p55CDC, that is present in dividing cells and is
associated with protein kinase activity.</p>
</abstract>
<example_list>
<example>
<db_xref dbkey="P26309" db="SWISS"/>Cell division control protein (Cdc20) from S. cerevisiae
</example>
<example>
<db_xref dbkey="Q09786" db="SWISS"/>A hypothetical protein from S. pombe
</example>
</example_list>
<pub_list>
<publication id="PUB00006167">
<author_list>Shirayama M., Toth A., Galova M., Nasmyth K.</author_list>
<title>APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5.</title>
<db_xref db="MEDLINE" dbkey="20110935"/>
<journal>Nature</journal>
<location firstpage="203" lastpage="207" volume="402" issue="6758"/>
<year>1999</year>
</publication>
</pub_list>
<member_list>
<db_xref protein_count="59" db="PREFILE" dbkey="PS50218" name="FIZZY_DOMAIN"/>
<db_xref protein_count="55" db="PRODOM" dbkey="PD004563" name="Fizzy"/>
</member_list>
<external_doc_list>
<db_xref db="QDOC" dbkey="QDOC50218"/>
</external_doc_list>
</interpro>
<interpro id="IPR000003" type="Family" short_name="RtnoidX_receptor" protein_count="75">
<name>Retinoid X receptor</name>
<abstract>
Steroid or nuclear hormone receptors (4A nuclear receptor, NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiat...
NRs are extremely important in medical research, a large number of them being implicated in diseases such as cancer, diabetes, hormone resistance syndromes, etc. While several NRs act as ligand-inducible transcription factors, many do not yet have a ...
t/data/interpro_short.xml view on Meta::CPAN
<classification id="GO:0006355" class_type="GO">
<category>Biological Process</category>
<description>regulation of transcription</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref dbkey="Q06726" db="SWISS"/>
</example>
<example>
<db_xref dbkey="P81559" db="SWISS"/>
</example>
<example>
<db_xref dbkey="Q64104" db="SWISS"/>
</example>
<example>
<db_xref dbkey="Q91766" db="SWISS"/>
</example>
<example>
<db_xref dbkey="P28701" db="SWISS"/>
</example>
<example>
<db_xref dbkey="O75454" db="SWISS"/>
</example>
</example_list>
<pub_list>
<publication id="PUB00004464">
<author_list>Nishihara T., Nishikawa J.-I., Kitaura M., Imagawa M.</author_list>
<title>Vitamin D receptor contains multiple dimerisation interfaces that are functionally different.</title>
<db_xref db="MEDLINE" dbkey="95206940"/>
<journal>Nucleic Acids Res.</journal>
<location firstpage="606" lastpage="611" volume="23"/>
<year>1995</year>
</publication>
<publication id="PUB00006168">
<author_list>Schmitt J., De Vos P., Verhoeven G., Stunnenberg H.G.</author_list>
<title>Human androgen receptor expressed in HeLa cells activates transcription in vitro.</title>
<db_xref db="MEDLINE" dbkey="94218237"/>
<journal>Nucleic Acids Res.</journal>
<location firstpage="1161" lastpage="1166" volume="22" issue="7"/>
<year>1994</year>
</publication>
</pub_list>
<parent_list>
<rel_ref ipr_ref="IPR001723"/>
</parent_list>
<contains>
<rel_ref ipr_ref="IPR000536"/>
</contains>
<member_list>
<db_xref protein_count="75" db="PRINTS" dbkey="PR00545" name="RETINOIDXR"/>
</member_list>
</interpro>
<interpro id="IPR000004" type="Domain" short_name="SapB" protein_count="135">
<name>Saposin type B</name>
<abstract>
Saposins are small lysosomal proteins that serve as activators of various
lysosomal lipid-degrading enzymes <cite idref="PUB00005747"/>. They probably act by isolating the
lipid substrate from the membrane surroundings, thus making it more
accessible to the soluble degradative enzymes. All <taxon tax_id="40674">mammalian</taxon> saposins
are synthesized as a single precursor molecule (prosaposin) which contains
four Saposin-B domains, yielding the active saposins after proteolytic
cleavage, and two Saposin-A domains that are removed in the activation
reaction.
The Saposin-B domains also occur in other
proteins, many of them active in the lysis of membranes <cite idref="PUB00005721"/>, <cite idref="PUB00005765"/>. <p>The 3D-structure of NK-lysin has recently been determined <cite idref="PUB00005798"/> and found to
be very different from the one predicted in <cite idref="PUB00005747"/>.
A group of <taxon tax_id="3193">plant</taxon> aspartic proteases related to cyprosin. These proteins
have a peculiar SAP-B domain where the two halves are 'swapped' <cite idref="PUB00005742"/>.</p>
</abstract>
<example_list>
<example>
<db_xref dbkey="P28039" db="SWISS"/>Mammalian Acyloxyacyl-hydrolase
</example>
<example>
<db_xref dbkey="P42210" db="SWISS"/>Plant aspartic proteinase
</example>
<example>
<db_xref dbkey="P17405" db="SWISS"/>Mammalian acid sphingomyelinase
</example>
<example>
<db_xref dbkey="Q07831" db="SWISS"/>Nonpathogenic pore-forming peptide from entamoeba
</example>
<example>
<db_xref dbkey="P10960" db="SWISS"/>Saposins Sap-A, Sap-B, Sap-C, Sap-D
</example>
</example_list>
<pub_list>
<publication id="PUB00005747">
<author_list>O'Hara P.J., Munford R.S., Sheppard P.O.</author_list>
<title>Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure.</title>
<db_xref db="MEDLINE" dbkey="96048294"/>
<journal>J. Lipid Res.</journal>
<location firstpage="1653" lastpage="1663" volume="36" issue="8"/>
<year>1995</year>
</publication>
<publication id="PUB00005721">
<author_list>Ponting C.P.</author_list>
<title>Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.</title>
<db_xref db="MEDLINE" dbkey="94272336"/>
<journal>Protein Sci.</journal>
<location firstpage="359" lastpage="361" volume="3" issue="2"/>
<year>1994</year>
</publication>
<publication id="PUB00005765">
<author_list>Hofmann K., Tschopp J.</author_list>
<title>Cytotoxic T cells: more weapons for new targets?</title>
<db_xref db="MEDLINE" dbkey="97021725"/>
<journal>Trends Microbiol.</journal>
<location firstpage="91" lastpage="94" volume="4" issue="3"/>
<year>1996</year>
</publication>
<publication id="PUB00005798">
<author_list>Liepinsh E., Otting G., Andersson M., Ruysschaert J.M.</author_list>
<title>Saposin fold revealed by the NMR structure of NK-lysin.</title>
<db_xref db="MEDLINE" dbkey="97475218"/>
<journal>Nat. Struct. Biol.</journal>
<location firstpage="793" lastpage="795" volume="4" issue="10"/>
<year>1997</year>
</publication>
<publication id="PUB00005742">
t/data/interpro_short.xml view on Meta::CPAN
<example>
<db_xref dbkey="P19219" db="SWISS"/>AdaA, a Bacillus subtilis bifunctional protein that acts both as a transcriptional activator of the ada operon and as a methylphosphotriester-DNA alkyltransferase.
</example>
<example>
<db_xref dbkey="P03021" db="SWISS"/>AraC, the arabinose operon regulatory protein, which activates the transcription of the araBAD genes.
</example>
<example>
<db_xref dbkey="P27246" db="SWISS"/>MarA, which may be a transcriptional activator of genes involved in the multiple antibiotic resistance (mar) phenotype.
</example>
</example_list>
<pub_list>
<publication id="PUB00004444">
<author_list>Gallegos M.-T., Michan C., Ramos J.L.</author_list>
<title>The XylS/AraC family of regulators.</title>
<db_xref db="MEDLINE" dbkey="93197143"/>
<journal>Nucleic Acids Res.</journal>
<location firstpage="807" lastpage="810" volume="21"/>
<year>1993</year>
</publication>
<publication id="PUB00003566">
<author_list>Henikoff S., Wallace J.C., Brown J.P.</author_list>
<title>Finding protein similarities with nucleotide sequence databases.</title>
<db_xref db="MEDLINE" dbkey="90190362"/>
<journal>Meth. Enzymol.</journal>
<location firstpage="111" lastpage="132" volume="183"/>
<year>1990</year>
</publication>
<publication id="PUB00001933">
<author_list>Parker L.L., Hall B.G.</author_list>
<title>Characterisation and nucleotide sequence of the cryptic cel operon of Escherichia coli K12.</title>
<db_xref db="MEDLINE" dbkey="90185127"/>
<journal>Genetics</journal>
<location firstpage="455" lastpage="471" volume="124"/>
<year>1990</year>
</publication>
<publication id="PUB00004817">
<author_list>Bustos S.A., Schleif R.F.</author_list>
<title>Functional domains of the AraC protein.</title>
<db_xref db="MEDLINE" dbkey="93296193"/>
<journal>Proc. Natl. Acad. Sci. U.S.A.</journal>
<location firstpage="5638" lastpage="5642" volume="90"/>
<year>1993</year>
</publication>
</pub_list>
<member_list>
<db_xref protein_count="478" db="PRINTS" dbkey="PR00032" name="HTHARAC"/>
<db_xref protein_count="762" db="PROFILE" dbkey="PS01124" name="HTH_ARAC_FAMILY_2"/>
<db_xref protein_count="855" db="PROSITE" dbkey="PS00041" name="HTH_ARAC_FAMILY_1"/>
<db_xref protein_count="747" db="PFAM" dbkey="PF00165" name="HTH_AraC"/>
<db_xref protein_count="683" db="SMART" dbkey="SM00342" name="HTH_ARAC"/>
</member_list>
<external_doc_list>
<db_xref db="BLOCKS" dbkey="IPB000005"/>
<db_xref db="PDOC" dbkey="PDOC00040"/>
</external_doc_list>
</interpro>
<interpro id="IPR000010" type="Family" short_name="Cystatin" protein_count="219">
<name>Cysteine proteases inhibitor</name>
<abstract>
Members of this family are inhibitors of cysteine proteases <cite idref="PUB00005324"/>, <cite idref="PUB00003412"/>, <cite idref="PUB00001614"/>, which are found in the tissues and body fluids of <taxon tax_id="33208">animals</taxon>, as well as in...
<p>Kininogen is the precursor of the active peptide bradykinin that plays a role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII. They are also inhibitors of cysteine protease...
</abstract>
<class_list>
<classification id="GO:0004869" class_type="GO">
<category>Molecular Function</category>
<description>cysteine protease inhibitor</description>
</classification>
</class_list>
<example_list>
<example>
<db_xref dbkey="P09229" db="SWISS"/>Cysteine proteinase inhibitor of rice
</example>
<example>
<db_xref dbkey="P29701" db="SWISS"/>Mammalian fetuin
</example>
<example>
<db_xref dbkey="P28325" db="SWISS"/>Type 2 cystatin
</example>
<example>
<db_xref dbkey="P37842" db="SWISS"/>Potato multicystatin, an eight-domain cysteine proteinase inhibitor
</example>
<example>
<db_xref dbkey="P01045" db="SWISS"/>Kininogen
</example>
<example>
<db_xref dbkey="Q28986" db="SWISS"/>Type 1 cystatin
</example>
<example>
<db_xref dbkey="P31727" db="SWISS"/>Sarcocystatin A from the flesh fish
</example>
</example_list>
<pub_list>
<publication id="PUB00005324">
<author_list>Barrett A.J.</author_list>
<journal>Trends Biochem. Sci.</journal>
<location firstpage="193" lastpage="196" volume="12"/>
<year>1987</year>
</publication>
<publication id="PUB00003412">
<author_list>Rawlings N.D., Barrett A.J.</author_list>
<title>Evolution of proteins of the cystatin superfamily.</title>
<db_xref db="MEDLINE" dbkey="90189177"/>
<journal>J. Mol. Evol.</journal>
<location firstpage="60" lastpage="71" volume="30"/>
<year>1990</year>
</publication>
<publication id="PUB00001614">
<author_list>Bode W., Turk V.</author_list>
<title>The cystatins: protein inhibitors of cysteine proteinases.</title>
<db_xref db="MEDLINE" dbkey="91309737"/>
<journal>FEBS Lett.</journal>
<location firstpage="213" lastpage="219" volume="285"/>
<year>1991</year>
</publication>
</pub_list>
<child_list>
<rel_ref ipr_ref="IPR001363"/>
<rel_ref ipr_ref="IPR001713"/>
<rel_ref ipr_ref="IPR003243"/>
<rel_ref ipr_ref="IPR003244"/>
</child_list>
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