wanglab/gogpt-training-data huggingface dataset:
Protein: Putative erythrocyte binding protein EBL-1 (Q9U4X0)
Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Interaction partners:
Sequence:
MNVPLNIKFLFFLFCLHCVSSKDQTSEKVKSQKENDSLQVHKKKSGELNNNKSGILRSTYKRIVGYTQKKLEDLFHVNGEYIKKEEDEKEKVDQNKDMLKSGLMIIDQNKDGEELENLIDPIKSIKDSNNLENYYDDNYNNIKFDVGNKSNHLKYMKTRNSDSDERFSNYYFIDNNLFLRDNKEQDENVFLSKSIIRNKDVDISIKDFEKNKFIDTYSLYECGKKIKEMKWICTDNQFKSNNLCAPIRRIQLCIVNIILFSENENEYIYKNDSINNKFKENILKAVKLESNLLVQKHNNEYNSKLCDDIRWSFLDYGDIIIGRDLIYKNNTDYIKEQFKKIFNNEYNNNELNDELNNELNDEKNIKLRKEWWEKYKEDIWEEMTKEHNDKFIEKCKYFAKDEPQIVRWIEEWSKQFLDEKNYMLFTLRNTYNEMNIIHENNCKQYNKWVQNRKKEWTFLSNEFNKIFPERNVQTHISNIFKEYKENNVDIIFGTLNYEYNNFCKEKPELVSAAKYNLKAPNAKSPRIYKSKEHEESSVFGCKTKISKVKKKWNCYSNNKVTKPEGVCGPPRRQQLCLGYIFLIRDGNEEGLKDHINKAANYEAMHLKEKYENAGGDKICNAILGSYADIGDIVRGLDVWRDINTNKLSEKFQKIFMGGGNSRKKQNDNNERNKWWEKQRNLIWSSMVKHIPKGKTCKRHNNFEKIPQFLRWLKEWGDEFCEEMGTEVKQLEKICENKNCSEKKCKNACSSYEKWIKERKNEYNLQSKRFDSDKKLNKKNNLYNKFEDSKAYLRSESKQCSNIEFNDETFTFPNKYKEACMVCENPSSSKALKPIKTDVFPIEETKKSELSSLTDKSKNTPNSSGGGNYGDRQISKRDDVHHDGPKEVKSGEKEVPKIDAAVKTENEFTSNRNDIEGKEKSKGDHSSPVHSKDIKNEEPQRVVSENLPKIEEKMESSDSIPITHIEAEKGQSSNSSDNDPAVVSGRESKDVNLHTSERIKENEEGVIKTDDSSKSIEISKIPSDQNNHSDLSQNANEDSNQGNKETINPPSTEKNLKEIHYKTSDSDDHGSKIKSEIEPKELTEESPLTDKKTESAAIGDKNHESVKSADIFQSEIHNSDNRDRIVSESVVQDSSGSSMSTESIRTDNKDFKTSEDIAPSINGHEKIGSSADDRGSEDKSIIDKDSENFENNKSSHSDIKQSDNEGSTDYESLTEESPKGDLESVSPSSIDMDLKPNKSSPVTSFDHVDSPNISELQSASQNADSYQGEKPSKNILRTDGDVSEKEKISVSPPNVSVTYDEGDKRQGISDDSSIHHEIDPEKNLHYESFISEGGLEEGDIEKEKGKEDGSLIPISPEKINDFGKRENIVDPSVSERVDDNRSDISNVVSEEQESSIISSRNGTEGINNSEELKSEEHTSVDVNNRDEHNKQENLVSSSTQQESEREKREKKENADSSHESELSSISEVGETIRRNDAEASENDKGEDILQSEEQQIVTEKTKLIEPTVNILQPSTPLGEIHKEKSEEIDDKDNTGGEVTHTDANTFQYRSSESVEVITNKPDEMEMTTKPPSQYIEKEIGEIDSTKNQDNDEQSNSIIPLINKNNEEDGVSIPSTRNVMESGSFVSRNEQIIEEKDDKHITDDTTINPSENGLKGYGEMPNDSIKSVTITESPLRDVEQMIEPIDGKGNEKNNIIGEPQESTTEIRKQMDGPISNVNIPEELHPVAEGSKLEEAKERSMDDADKGTITEDITVVEDPNGIGEHQNLKEVHEQASELNTYNSLDGRTNVEVKERLDENPGSIPNDRITTEHIELDKEKEIHEPNELDAHNGEQEEMIRNEVSDNRMDEQISRDNETRQLNQDHESDSKDEIIDKREMENLEENPNSSSDSLENPEGKEKGKIEHTHSSEELDSVRDETYKYKGIENQITETEIESVEQQDTNIPGNSKETEVDNSRADMEEEKDVKIKQIITEESEEELEISKDTTTSHSEKPSIEEQSVNIVDSKNEINVQIEKNVQNEQNEGDPIILLEEQNKNIAILENQKNEYNNPSQLSHKERTLLEVDDLEGSMDTNCLTSELNKNKCDSIQIIPEASNTDNKLNKDITENKDDFSEIEKSVGEIHENGKDLLNKESAESDDVPVQNKIEHDSENAGVIDQYEYRTDYEENEKVNFVGLPGKPEEERSDVTRGSVPGSVDAFEKKLHEPLDSNEKNKEELNVSKEIEYPVGLDILGIDSESSDSVTIYKRPTDTFVENVHVLSRDIKSLFENEKTVGLNEQKKETEKNIAGGMIDVLNNKNIDDDQSVRLSTSLYHKGLDDDQSGRLSTALYDKGLDDDQHYLHDNSYNNNINNIKNEVQCKENCGRNENVSSFVDTTTLRDVKQNKEHTEETKLIENTKIDNTEVDDGVDITSDNRSSFISVDNYDEKKKETIINEKKNDPKPSRKEEKDVKHDDSENDNNNLSSNIKIKERIENIYNYIKKLFNLTDINNYTEKKDMPRYNLNNFINTKSYTLFENSKESEYHGNELLQSENIPEHHNKSNNIKVSSNLDNNYYRYVNKILEDIINLSKKKKKSINDTSFEYCESILRHSISSSSIYKDELKYLCFSILYYCLIYFDNTSEYYNCITNEFNNTLYIMFQTDMTSMIYNIYK
Protein: Cell adhesion molecule L1-like (A0A8I5YCG7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MELPLGGRGLILSLIFLLLKLSTAEIPLSVHQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPKFSWTKDDKPFDLSDPRIIAFNNSGTFRIPNEGHISHFQGKYRCFASNRLGTAISEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGHPPLHIYWMNIELEHIEQDERVYMSQKGDLYFANVEEKDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQIGSASSKTVLKGDTLLLECFAEGLPTPQIEWSKLGSELPKGRATIEIHEKTLKIENVSYQDRGNYRCTANNLLGKASHDFHVIVEEPPRWKKKPQSAVYSTGSNGILLCEAEGEPQPTIKWRVNGLPIENHPFPGDVMFPREISFTNLQPNHTAVYQCEASNIHGTILANANIDVVDVVPLIQTKNEENYETVVGYSAFLHCEYFASPKATVVWEVADETHPLEGGRYHTHENGTLEIERTTEEDAGSYSCWVDNTMGKAVITANLDIRNATKLRVFPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGANLTISNISGEDQGIYSCSAQTALDSTSGKTQLVHGLASEYIVEFEGNREEPGKWEELTRVRGEETDVVLPLAPYVRYQFRVTAVNEVGKSHSSQPSDHHETPPAAPDKNPHNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYRVSWKPQGAPEEWEEETVTNHTLRVMTPTVYAPYDVQVQAINQLGSGPEPQPVTLYSGEDYPSTAPVIHRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLEPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNATTKYKFYLKACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKSHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTVCFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein (Cnt-b) (Centaurin-beta) (Q6NXL5)
Organism: Mus musculus (Mouse)
Subcellular location: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}.
Interaction partners:
Sequence:
MTVEFEECIKDSPRFRATIDEVETDVVEIEAKLDKLVKLCSGMIEAGKAYVTTNRLFVSGVRDLSQQCQGDTVISECLQRFGDSLQEMVNYHTILFDQAQRSVRQQLHNFVKEDVRKFKETKKQFDKVREDMELSLVRNAQAPRHRPHEVEEATGALTVTRKCFRHLALDYVLQINVLQAKKKFEILDSMLSFMHAQYSFFQQGYSLLHQLDPYMKKLAAELDQLVIDSAVEKREMERKHAAIQQRTLLQDFSYDEPKVEFDVDAPSGVVMEGYLFKRASNAFKTWNRRWFSIQNSQLVYQKKLKDALTVVVDDLRLCSVKPCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWVQAVQASIASAYRESPDSCYSERLDRTASPSTSSIDSTTDSRERGVKGESVLQRVQSVAGNSQCGDCGQPDPRWASINLGVLLCIECSGIHRSLGVHCSKVRSLTLDSWEPELLKLMCELGNSTVNQIYEAQCEGPGVRKPTASSSRQDKEAWIKDKYVEKKFLRKLTSAPAREPPRRWRAQKCQRPHSSPHAPTTRRKVRLEPVLPSVAALSSAATMERKFRRDSLFCPDELDSLFSYFDAGAAGAGPRSLSSDSGLGGSSDGSSDVLAFGTGSVVDSVTEEEGAESEESSSEVDGEAEAWSLADVRELHPGLLAHQAARTRDLPALAAALAHGAEVNWADAADEGKTPLVQAVLGGSLIVCEFLLQNGADVNQRDSLGRAPLHHATLLGRTGQVCLFLKRGADQHALDQEQQDPLTIAVQAANADIVTLLRLARMAEEMREAEAPPGQPGPLPGSSPTELQYRRCIQEFIGLHLEES
Protein: RabGAP/TBC domain-containing protein (Q75JG4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Ras-related protein Rab-11A
Sequence:
MEEIQPSSSKETESINSNENDNDNKISTTPVISISTFIKSKKSASTSTSPPKSGSLLSIQRTLKNSSETQIIKEEKEIKPTIIKVDELKYKEKEKEKENHDENDDDKLLTIKKNSIIQHIVDVKWRDKYGFVSDDFFVPELKKFEAMEEEQAQEKMNKWAQFHEQYNKVGLSSNAKQFLKLLANGIPHSSRGSLWKVYSGSFEKQRKEELSLFKQQKEEKKYSRFGTIRGLQPPTNRRSYYLHLQGIIKTSNRLSTKFQSLPEIDKDISRTFPGHPFFESDEGKRKLSRVLQAYSIRNRKVGYCQSMNIVAGFVLFVGGGNEEDAFWLLSTIVEDFCQNYYSTNLMGSQVDMSVFSILVAQYFPKLYNHMEEYDVSLSLLSTKWFMCLFVNVLPTEIVLRIWDHLFVECGIYGYHKPASDELWLQPDPETLLKNSKENGGETFRCNGLASYNLLLTGLSVLAYFEETLLNCHSTPHLLMILSTHAKGLFKAKQFFKYYQKLRNTIPEDYFNGLKRKSELVFLKELEDMRKARDLHQTLKFTRFSKNDLEKIWSGFRQLEISSRYSMGKSMILDFKMFQNVFQFILPSNIGMGTADENNTRDIIIKQLFKAFDKNKDGTLDFTELMSGLCILAKGTSEERLKLYFSFFDSNGNGFISKSDMKLMLENVYDKIELDPLAATQYSIDEYVEMIFSNYSIPEGEGLSFDMFRQAIASYPRIFRCFMLEEEEFSVDIDNFLEQQQEQTTTTNTSDGNGEIKSLKRKQTKGSRIQFQEVLIRESELENNNNNNKDSIGSCNNSNITNNDNVNNNNESKDNNNNNNTLDNDSTVEGKQNIIIKNNSEEQEDSSTSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDSDEEPTNINNKFGFAEIKKKQPTEPKGSTVNSSLLIDAIEKAKIDKPQPNIIIEMKSNNYSTTTVSYNTPSSPPQSGNPLSCCKFM
Protein: Exocyst complex component EXO70E2 (AtExo70e2) (Exocyst subunit Exo70 family protein E2) (Q9FNR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Influences the subcellular localization patterns of other exocyst complex proteins (e.g. SEC5A, SEC15A, SEC15B and EXO84B) leading to their recruitment to exocyst, well-defined large punctate structures throughout the cytosol. Essential component for the formation and the recruitment of exocyst subunits to the exocyst-positive organelle (EXPO), a secreted double membrane structure also called extracellular exosome, that acts as a sequester for cytosolic proteins to release them into the apoplast.
Subcellular location: Secreted, extracellular exosome {ECO:0000269|PubMed:21193573}. Secreted {ECO:0000269|PubMed:21193573}. Cell membrane {ECO:0000269|PubMed:21193573}. Cytoplasm {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21193573}. Endomembrane system {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21193573}. Note=Localized to well-defined large punctate structures throughout the cytosol (PubMed:19895414). Component of the secreted double membrane structure exocyst-positive organelle (EXPO). Locates to the plasma membrane as discrete punctae and secreted outside of the cells (PubMed:21193573). {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21193573}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC15B
- Exocyst complex component SEC6
- Exocyst complex component SEC10a
- Exocyst complex component EXO84B
- Exocyst complex component EXO84C
- Exocyst complex component SEC10b
- Exocyst complex component SEC15A
- Exocyst complex component SEC5A
- Exocyst complex component EXO84A
Sequence:
MAEFDSKVPVSGMNNHVFEACHHVVKALRASDNNLDANLRKLLSDLEMHLSTFGIADTKVEDAGFSEIKKRFKEAVKRIRSWETNQSTMFEAGLSEADQFFQALYDVQTVLVGFKALPMKTNQMEKDVYNQATVALDIAMLRLEKELCDVLHQHKRHVQPDYLAVSSRRKDIVYDESFVSLDDEVIVEASSHEDDEQISDFYNSDLVDPIVLPHIKAIANAMFACEYDQPFCEAFIGVQREALEEYMVTLEMERFSCVDVLRMDWEDLNGAMRKWTKVVKIITQVYLASEKQLCDQILGDFESISTACFIEISKDAILSLLNFGEAVVLRSCKPEMLERFLSMYEVSAEILVDVDNLFPDETGSSLRIAFHNLSKKLADHTTTTFLKFKDAIASDESTRPFHGGGIHHLTRYVMNYLKLLPEYTDSLNSLLQNIHVDDSIPEKTGEDVLPSTFSPMARHLRSIVTTLESSLERKAQLYADEALKSIFLMNNFRYMVQKVKGSELRRLFGDEWIRKHIASYQCNVTNYERSTWSSILALLRDNNDSVRTLRERCRLFSLAFDDVYKNQTRWSVPDSELRDDLHISTSVKVVQSYRGFLGRNAVRIGEKHIRYTCEDIENMLLDLFECLPSPRSLRSSRKR
Protein: Inositol-1-monophosphatase ImpA (I-1-Pase) (IMPase) (Inositol-1-phosphatase) (EC 3.1.3.25) (A0QX86)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the dephosphorylation of inositol 1-phosphate (I-1-P) to yield free myo-inositol, a key metabolite in mycobacteria.
Interaction partners:
- Imidazole glycerol phosphate synthase subunit HisF
- Phosphoribosyl isomerase A
- Inositol-3-phosphate synthase
- Phosphoribosyl-AMP cyclohydrolase
- Imidazole glycerol phosphate synthase subunit HisH
- Imidazoleglycerol-phosphate dehydratase
- Inositol-1-monophosphatase
- inositol-phosphate phosphatase
- Inositol 2-dehydrogenase
- Oxidoreductase YisS
Sequence:
MTVVGELDPQKLTALVATAAEILDAASVPFVAGHRADSAVRKQGNDFATEVDLAIERQVVRALTEATGIGVHGEEFGGEPIDSPLVWVLDPIDGTFNYAAGSPMAAILLGLLADGEPVAGLTWLPFTGEKYSALVGGPLYSDGKPCPPLGSPTLADSIIGIQTFNIDSRGRFPGRYRVEVLANLSRVCSRVRMHGATGVDLAYVAAGILGGAISFGHHIWDHAAGVALVRAAGGVVTDLTGAPWTVDSKSVLAAAPGVHEKMLEIVKSTGKPEDYL
Protein: MIOREX complex component 12 (Mitochondrial organization of gene expression protein 12) (P47084)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Protein-lysine N-methyltransferase EFM2
- Protein HGH1
- Regulator of rDNA transcription protein 14
- Protein arginine N-methyltransferase SFM1
- Uncharacterized protein YLR287C
- 25S rRNA
- Uncharacterized protein YCR016W
- rRNA-processing protein FCF2
Sequence:
MLRSLHSAATLSNKRFYSLISHSNRKNIIKKLLRHPSFDPIRHHLPEDITTIDPYSLSQNVIESLNKLEVPKKDAAMVHNMMIENLSDLDYGVATIHSNNLRDLDLKPSLPAIKQIIRNNPGRVQSSWELFTQYKASMENVPDELMEVVLEKIIKFDKAEKVDGKKSLTYQDLVRCLYLINHFSSNYNLPSELVEPILIYIVDNGIPNVLGSVLKYKIPLSFFDKYVSEMTQYQICELYDFYSLDNIVADPLVLHKCLTVLGENEKIQQTEEEKEIISKLEEEIDIVKSQCHDNWSLEFPNWSVRKTATSFEELFLEIQKRNIDKKDFELAHKLLRLIGAFKGKVSLFFKLYDEYLLKFKNNEDDLMFEAFLTLCCQGYKSSNEKMLQYAEAFIKEDFDSKLESKIQSVLIVANAKANIDLSLKIYNSNISTAKREKDKYTDLAESDVLTESLILAFLSRDDADFARVIFDGALGEKLISGPTAAKKIKNLLAQYGEALETKTSKQVMQTKIEHYMESI
Protein: Pentacotripeptide-repeat region of PRORP domain-containing protein (Q389W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRGNGPWHHVEVAGIAMGNRRSHATSMRAENSHDNREFSLCCCAPTNRPKSVFLLCVCVCVCFNYCSCVMLFIGLTYFTTNCSSSFSLSGYFCSSCLLSSSTTETERLPILYLSLSPAESCITTARTDPTVLEKVRVSLISVVYSKAARRCFLCFRLPSQTFCSPQRRVMAMLSQARVAGWASRWLTDELVALSKAGNWEAAISTFLQLQQANIVQSNVFHYTTVISACGRAGKWEAAMSIFDQMTKNEVKPNVYTYTAVINACASAEKADVALRMFAHMRLADVPPNVQTMTALVNACARSGEWERAIKILRDCEELFVAPNVFTYTAAMDGCRRGGVWKPAVDLLNEMRDPTRVRPNEVTYNTVINACAVASELNAALQVYATMVSDGYTPVNFTKTLLMQLFRNTALSGLADELKVRKTTWREINVPDTDPATALEAVREDSPAVEEEEEEGKG
Protein: Spire type actin nucleation factor 1 (D3YTL8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}.
Interaction partners:
Sequence:
MANTVEADGSKDEGYEAADEGPEDEDGEKRSISAIRSYQDVMKICAAHLPTESEAPNHYQAVCRALFAETMELHTFLTKIKSAKENLKKIQEMEKGDESSTDLEDLKNADWARFWVQVMRDLRNGVKLKKVQQRQYNPLPIEYQLTPYEMLMDDIRCKRYTLRKVMVNGDVPPRLKKSAHEVILDFIRSRPPLNPVSARKLKPTPPRPRSLHERILEEIKAERKLRPVSPEEIRRSRLDVTTPESPKNVGESSMVNGGLTSQTKENGLSAAQQGSAQRKRLLKAPTLAELDSSDSEEEKSLHKSTSSSSASPSLYEDPVLEAMCSRKKPPKFLPISSTPQPERRQPPQRRHSIEKETPTNVRQFLPPSRQSSRSLVPRITGVWPRTPFRPLFSTIQTASLLSSHPFEAAMFGVAGAMYYLFERAFTSRWKPSKEEFCYPVECLALTVEEVMHIRQVLVKAELEKYQQYKDVYTALKKGKLCFCCRTRRFSFFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGPSALQRGESCSRSEKPSTSHHRPLRSIARFSTKSRSVDKSDEELQFPKELMEDWSTMEVCVDCKKFISEIISSSRRSLVLANKRARLKRKTQSFYMSSAGPSEYCPSERTINEI
Protein: Uncharacterized protein C887.08 (O94293)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MDLLAIDLDFDVSESKLERNKRLKQKVSIETDGWTPRVQCFGHLSKNGVVLGEEAYILEQSKFAAEEQYYLGNYSLAKKFAFQALDVPTDSSSIEYHRLSSGEINEIEDIIRRCEMKLENKQSN
Protein: Endoribonuclease MazF4 (EC 3.1.-.-) (Toxin MazF4) (mRNA interferase MazF-mt7) (P9WII5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease (mRNA interferase) on single-strand mRNA, cleaving between the first and second bases in the sequence UCGCU. Overexpression in M.smegmatis but not E.coli inhibits growth, this effect is neutralized by coexpression with cognate toxin MazE4.
Interaction partners:
- Probable antitoxin MazE4
- Endoribonuclease MazF9
- Endoribonuclease MazF6
- Endoribonuclease MazF3
- Probable methylmalonyl-CoA mutase large subunit
- Probable GTPase Rv1496
- Probable methylmalonyl-CoA mutase small subunit
- Putative fatty-acid--CoA ligase fadD25
Sequence:
MNAPLRGQVYRCDLGYGAKPWLIVSNNARNRHTADVVAVRLTTTRRTIPTWVAMGPSDPLTGYVNADNIETLGKDELGDYLGEVTPATMNKINTALATALGLPWP
Protein: Hermaphrodite, isoform A (Hermaphrodite, isoform B) (LD32783p) (Q9VJJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSADRDSVEEEYGSCSAWKFRCSVDRCPYRTNRPYNLARHEESHIGITQSKLYGCPVCVYNTDKASNLKRHVSIKHPGCKKRPPEAQHKDRNAKLQCLVMGCRYETNRPYDLKRHLMVHNNPEKSHRTFKCSLCTYSSDRKANLKRHHELRHSGIEEAIQTAEELRQEMLLEKQMLKEHKLKYQITEKQDLKNLKLKDQKQKVQMLRDQQPKQRQKKEQLLEDQSPVLNKQLEHGNIPLKEALVGSMKYDEESLEFVYEELQEEEQPPIITISNPQILHGDIRDKHVIAVNVDGQLRWFQSIDPPPGAPTKLELPIKSTSISVQQQMDELDDELAMSLAEEDQQDEFLVPMLSGEEPVKIKQSSLTDLAWSWSTPDAVHHISPKAELKKDLKAGDADTDFPDWWDDGKYTKMQKNQTFAKHSKKPSQENVQRILRIIYDIYYKPFKEDRKQFEAFQIKDSWLCATRMTRMQIIKDMYSKQGTLSQT
Protein: B-box zinc finger protein 22 (Protein DOUBLE B-BOX 3) (Protein LIGHT-REGULATED ZINC FINGER PROTEIN 1) (Protein SALT TOLERANCE HOMOLOG 3) (Q9SYM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as positive regulator of seedling photomorphogenesis and light-regulated inhibition of hypocotyl elongation, independently and in concert with HY5 and BBX21. Acts as a positive regulator of de-etiolation and influences chloroplast biogenesis and function through regulation of genes encoding chloroplast proteins. Acts downstream of COP1 and plays an important role in early and long-term adjustment of the shade avoidance syndrome (SAS) responses in natural environments. Regulates the expression of genes responsive to light hormone signals which may contribute to optimal seedling development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18796637}.
Interaction partners:
- Transcription factor HY5
- E3 ubiquitin-protein ligase COP1
- Transcription factor HY5-like
- B-box type zinc finger family protein
- B-box zinc finger protein 32
- Transcription factor HFR1
- B-box domain protein 30
- Transcription factor LAF1
- At5g54470
- B-box domain protein 31
Sequence:
MKIQCNVCEAAEATVLCCADEAALCWACDEKIHAANKLAGKHQRVPLSASASSIPKCDICQEASGFFFCLQDRALLCRKCDVAIHTVNPHVSAHQRFLLTGIKVGLESIDTGPSTKSSPTNDDKTMETKPFVQSIPEPQKMAFDHHHHQQQQEQQEGVIPGTKVNDQTSTKLPLVSSGSTTGSIPQWQIEEIFGLTDFDQSYEYMENNGSSKADTSRRGDSDSSSMMRSAEEDGEDNNNCLGGETSWAVPQIQSPPTASGLNWPKHFHHHSVFVPDITSSTPYTGSSPNQRVGKRRRRF
Protein: E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) (A0A8I6GK47)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR006748}. Nucleus, nucleoplasm {ECO:0000256|PIRNR:PIRNR006748}. Nucleus, nucleolus {ECO:0000256|PIRNR:PIRNR006748}.
Interaction partners:
Sequence:
MCNTNMSVSTEGAAGTSQIPASEQETLVRPKPLLLKLLKSVGAQKDIYTMKEIIFYIGQYIMTKRLYDEKQQHIVYCSNDLLGDVFGVPSFSVGYKNAYSGTSPSESRCQPEGGSDLKDPVQASQEEKPSSSDVVSRPSTSSRRRAISETEENTDELPGERQRKRHRALSFDESLGLCVLREICCERSSSSEATDTPSHQDLDDGVSDHSADCLDQDSVSDQFSVEFEVESLDSEDYSLSDEGHELSDEDDEVYRVTVYQAGESDADSFEGDPEISLADYWKCTSCNEMNPPLPSHCNRCWTLRENWLPDDKGKDKVEISEKAKLESSDQAEEGLDVPDGKKVTEDDAKESSAEDSEEKVAQMLLSQESDDYSQPSTSSSIVYSSQESGKELKEDTQDKEESMESSFSLNAIEPCVICQGRPKNGCIVHGKTGHLMSCFTCAKKLKKRNKPCPVCRQPIQMIVLTYFN
Protein: Serine carboxypeptidase 1 (EC 3.4.16.-) (A0A0C3VJP4)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis).
Subcellular location: Secreted {ECO:0000269|PubMed:23662629}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23662629}.
Interaction partners:
Sequence:
MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKIDSFNIYAPLCHDSTLKNGSTGYVSNDLDPCSDYYGTAYLNRPEVQKALHAKPTNWSHCSDSINLNWKDSPITILPTIKYLIDNGIKLWIYSGDTDAVGVTISRYPINTLKLPIDSTWRPWYSGKEIGGYVVGYKGLTFVTVRGAGHLVPSWQPERALTLISSFLYGILPASVSPSN
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (P17721)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8508805}.
Interaction partners:
- Bifunctional PGK/TIM
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Enolase
- Transaldolase
- Transketolase, putative
- Glucose-6-phosphate 1-dehydrogenase
- Deoxyribose-phosphate aldolase
- D-glycerate 2-kinase
- Uridine kinase-related protein
Sequence:
MARVAINGFGRIGRLVYRIIYERKNPDIEVVAINDLTDTKTLAHLLKYDSVHKKFPGKVEYTENSLIVDGKEIKVFAEPDPSKLPWKDLGVDFVIESTGVFRNREKAELHLQAGAKKVIITAPAKGEDITVVIGCNEDQLKPEHTIISCASCTTNSIAPIVKVLHEKFGIVSGMLTTVHSYTNDQRVLDLPHKDLRRARAAAVNIIPTTTGAAKAVALVVPEVKGKLDGMAIRVPTPDGSITDLTVLVEKETTVEEVNAVMKEATEGRLKGIIGYNDEPIVSSDIIGTTFSGIFDATITNVIGGKLVKVASWYDNEYGYSNRVVDTLELLLKM
Protein: Uncharacterized protein C22H10.02 (Q10296)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MAFYYKNNLGYQNIPYGYQLNDFRASFEKARTFDMEDDLEFCPSLSDEELVSIYQSTGLSPTSSSPSLSPMTPNLYPNVLPNVHPGVSNYTHHPLSGLHQNVGSRTRKSSGIPIIDPVTRAPAVLAGAVSSSRAKQMW
Protein: SET domain binding factor, isoform B (Q7KSP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRLADYFVIVGYDSDKEKTASNVGGQPTCGKIVQRFPEKDWPDTPFIEGIEWFCQPLGWSLSYEKQEPKFFVSVLTDIDANKHYCACLSFHETVAITQTRSVDDEDETIGSSRLLGATPSSMDGITTTSTPASITHHSVMYAPKCLVLISRLDCAETFKNCLGTIYTVYIENLAYGLETLIGNILGCIQVPPAGGPQVRFSIGAGDKQSLQPPQSSSLPTTGSGVHFLFKQLGIKNVLILLCSVMTENKILFLSKCYWHLTDSCRALVALMYPFRYTHVYIPILPAPLTEVLSTPTPFIMGIHSSLQTEITDLLDVIVVDLDGGLVTIPESLTPPVPILPSPLWEQTQDLLSMILFPNLAQADLAFPTLERPSAIAKTDAQIDKELRAIFMRLFAQLLQGYRSCLTIIRIHPKPVITFHKAGFLGARDLIESEFLFRVLDSMFFTTFVNERGPPWRSSDAWDELYSSMNELLKSEAQNRNLILTHIQELGRVLYENEGTLAHISYAQKVLRPPEGAFQRIHQPAFPRISSEKVELIIQEGIRKNGVPQRFHVTRNQHRIIPMGPRLPEALDVRPNVQNSARRLEVLRICVSYIFENRITDARKLLPAVMRTLMHRDARLILCREFFGYVHGNKAVLDHQQFELVVRFMNKALQKSSGIDEYTVAAALLPMSTIFCRKLSTGVVQFAYTEIQDHAIWKNLQFWESTFFQDVQGQIKALYLLHRRQNEHQKEANCVLDEVPLEEPTALEITAEQLRKSPNIEEEKKAELAKSEESTLYSQAIHFANRMVSLLIPLDVNVDAASKPKPAFRLEENQSVSNSIMGSHSLSEHSDEGFEENNALEIGVTVGKTISRFIDCVCTEGGVTSEHIRNLHDMVPGVVHMHIESLEPVYLEAKRHPHVQKPKIQTPCLLPGEDLVTDHLRCFLMPDGREDETQCLIPAEGALFLTNYRVIFKGSPCDPLFCEQVIVRTFPIASLLKEKKISVLYLAHLDQTLTEGLQLRSSSFQLIKVAFDPEVTPEQIESFRKILSKARHPFDEFEYFAFQSYGTMLQGVAPLKTKEKYSTLKGFAKKTLLRGAKKAGFKQKQQTKRKLVSDYDYGSADAQETQSIDDELEDGDEFETQNNAMPRLLTTKDVERMRERSYVQDWKRLGFDAESQRGFRISNANTSYATCRSYPAIIVAPVQCSDAAIMHLGRCFKGQRIPLPTWRHANGALLIRGGQPNSKSVIGMLKNTTGSTTNAHHDVTHYPEQDKYFLALINTMPKLTPLALNQYSGMNLSMSSLMGHSSSDDRQPLTPELSRKHKNNLDISDGNKSSQGGKGGTMKGNPKNSLAHPFRKMRLYALGEKSQAKSNMNVDFCADFIPVDYPDIRQSRPAFKKLIRACMPSHNTNEADGQSFAKMVEQSDWLQQISSLMQLSGAVVDLIDLQESSVMLSLEDGSDVTAQLSSIAQLCLDPYYRSLDGFRVLVEKEWLAFGHRFAHRSNLKPSHANTNIAFAPTFLQFLDVVHQLQRQFPMAFEFNDFYLRFLAYHSVSCRFRTFLFDCELERSDSGIAAMEDKRGSLNAKHMFGAGGMATNGSDDECSVYPLDIRSQRAPAPLNRIGHSIFDYIERQHNKTPIFYNFLYSGDKSVTLRPQNNVAALDLWCYYTNEELAQGAPYDLEVTTVDDEIDLSETKGKRMVITAGYDNMEKCNPSAYVCLLSEVKQAETERGHLPQKWLQVWNSLEVPQLEPVARNTSLGNIFVQTHQHKRSTLEIIMKGRLAGYQDKYFHPHRFEKHPYTTPTNCNHCTKLLWGPVGYRCMDCGNSYHEKCTEHSMKNCTKYKAIDGAVGPPNVNMSQGDTASIASSAATTARTSSHHFYNQFSSNVAENRTHEGHLYKRGALLKGWKQRWFVLDSIKHQLRYYDTSEDTAPKGIIELAEVQSVTAAQPAQIGAKGVDEKGFFDLKTSKRIYNFYAINANLAQEWIEKLQACLQ
Protein: Chorion-specific transcription factor GCMa (GCM motif protein 1) (Glial cells missing homolog 1) (Q9Z288)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes. Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer. Binds to the SYDE1 promoter. Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00245}.
Interaction partners:
- Glial cells missing transcription factor 2
- Cathepsin Q
- Endogenous retrovirus group FRD member 1, envelope
- Trophoblast specific protein alpha
- Ctsq protein-like
Sequence:
MELDDFDPEDKEILSWDINDMKLPQNVKKTDWFQEWPDSYVKHIYSSDDRSAQRHLSSWAMRNTNNHNSRILKKSCLGVVVCSRDCSTEEGRKIYLRPAICDKARQKQQRKSCPNCNGPLKLIPCRGHGGFPVTNFWRHDGRFIFFQSKGEHDHPRPETKLEAEARRAMKKVHMASASSSLRMKGRPEMKGLPGEIPSQGSLPLTWSFQEGVQLPSGYSTPLIANAPQQNSLNDCLSFPKSYDLGGTTELEDPTSTLDPTKLYERYKFSSSKVYSAEDQFQPPVPGVYGDYDEAQTWNKNAVLGRSPTDDTYYPPYPLPVASWPCDYLPSQSSLEHSPQQVPLEPPAAQPGHHPLWTNPGGEPYEEKVPVDFSSYVPSVTYHSPQQDPFLLAYGSHPQQQYALPGKSNRWDFDEEMACMGLDHFNNEMLLNLCSLK
Protein: Pro-cathepsin H (Cysteine protease) [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain] (A0A072UTP9)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May play a role in proteolysis leading to mobilization of nitrogen during senescence and starvation.
Subcellular location: Vacuole {ECO:0000250|UniProtKB:Q8H166}. Lysosome {ECO:0000250|UniProtKB:P07688}.
Interaction partners:
- Em6
Sequence:
MAQWTLLIVFFCVATAAAGLSFHDSNPIRMVSDMEEQLLQVIGESRHAVSFARFANRYGKRYDTVDEMKRRFKIFSENLQLIKSTNKKRLGYTLGVNHFADWTWEEFRSHRLGAAQNCSATLKGNHRITDVVLPAEKDWRKEGIVSEVKDQGHCGSCWTFSTTGALESAYAQAFGKNISLSEQQLVDCAGAYNNFGCNGGLPSQAFEYIKYNGGLETEEAYPYTGQNGLCKFTSENVAVQVLGSVNITLGAEDELKHAVAFARPVSVAFQVVDDFRLYKKGVYTSTTCGSTPMDVNHAVLAVGYGIEDGVPYWLIKNSWGGEWGDHGYFKMEMGKNMCGVATCSSYPVVA