wanglab/gogpt-training-data huggingface dataset:
Protein: Tryprostatin B 6-hydroxylase (EC 1.14.14.118) (Cytochrome P450 monooxygenase ftmP450-1) (Fumitremorgin biosynthesis protein C) (Q4WAW5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 6-hydroxytryprostatin B O-methyltransferase
- Tryprostatin B synthase ftmPT1
- Fumitremorgin C monooxygenase
Sequence:
MKPSHSDTPLMMPSVMKCGYLATAGLIGICTHLSYFRYGEHHLYPWRYVRFHLCLTMGVAALLYAKKPPQYTLCSMDLVKDVSLLMATYLVGLFASLLLYRTLFHPLRQIRGPWAAKISSFWLSFRLRRGPSFRILHELHEEYGPVVRVGPSEVSIIHPEAVRMIYGPNSRCSKNTFYDNGHPMMSLHSYRDRIAHDQRRRVWSAGFGDRALRGYEQRMRVYRQKLFQRLEARAVAESAINISQWFNFYSYDTMGDLAFARSFDMLDASRNHWAVDMLMHGMIGYRYLFPSWFFRLLATMPSLSSDWHKFIGFATDTMLRRVGEQVDVPDIFASLLAPLNGREPTEDERNMLMGDAMLIITAGSDTTATSLTSIVYELARHLDEVDKLRAELDPIEADSDGEYQHDTLAKLPHLNGFINETLRLHPPIPGVIPRKTPPEGIHVKDVFIPGNMTVFSPQWSMGRSEAAYIDPEIFNPERWYKHMDLVKDPSAFAPFSIGPYSCIGKPLALMNIRTTVARLIMSFDVRFPEGEDGIRWMDAADEHFAMGIHQMPVVLTRRH
Protein: Ras-related protein Rap-1 (EC 3.6.5.2) (Q18246)
Organism: Caenorhabditis elegans
Function: Required in the hypodermis for proper formation of the cuticle.
Interaction partners:
- Ras guanyl-releasing protein 3
- cAMP-dependent protein kinase catalytic subunit
- Raf homolog serine/threonine-protein kinase
- Rap guanine nucleotide exchange factor 1
- Abnormal cell migration protein 10
- Rap-GAP domain-containing protein
- Protein shank
- TNF Receptor Associated Factor
- MATH domain-containing protein
- Rap-GAP domain-containing protein
Sequence:
MREYKIVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYSITAQSTFNDLMDLRDQILRVKDTDEVPMILVGNKCDLEDERVVGKDQGQNLARQFGSAFLETSAKAKINVSEVFYDLVRQINRRYPESGRRQGQSNKQCCSCVIM
Protein: Protein argonaute 1 (O04379)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Requires DRB1 for directional loading of the small RNA duplex (guide stand and passenger strand) onto RISC for passenger strand degradation. Unlike animal RISC that associates in high molecular weight complex, Arabidopsis RISC is probably composed only of the AGO1 protein and associated RNA without any other proteins. Associates mainly with miRNAs of 21 nucleotide in length and preferentially recruits small RNAs with a 5' terminal uridine. Associates with 22 nucleotide miRNAs to trigger RDR6-dependent secondary siRNAs biogenesis. This pathway amplifies silencing by using the target RNA as substrate to generate secondary siRNAs. Binds to miR168 which targets its own mRNA for repression, establishing a homeostatic regulatory loop. Involved in antiviral RNA silencing by contributing to viral RNA clearance. Is capable of targeting viral RNAs with more compact structures than AGO7 which favors less structured RNA targets. May not associate with 24 nucleotide siRNAs involved in chromatin silencing. Essential for multiple processes in development. Essential for proper development of leaves and floral organs, and formation of axillary meristems. Like AGO10, required for stem cell function and organ polarity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28463111}.
Interaction partners:
- Endoribonuclease Dicer homolog 1
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 2
- Endoribonuclease Dicer homolog 3
- Double-stranded RNA-binding protein 1
- RNA-dependent RNA polymerase 6
- Protein SUPPRESSOR OF GENE SILENCING 3
- RNA-dependent RNA polymerase 2
- Small RNA 2'-O-methyltransferase
- Protein DCL homolog, chloroplastic
Sequence:
MVRKRRTDAPSEGGEGSGSREAGPVSGGGRGSQRGGFQQGGGQHQGGRGYTPQPQQGGRGGRGYGQPPQQQQQYGGPQEYQGRGRGGPPHQGGRGGYGGGRGGGPSSGPPQRQSVPELHQATSPTYQAVSSQPTLSEVSPTQVPEPTVLAQQFEQLSVEQGAPSQAIQPIPSSSKAFKFPMRPGKGQSGKRCIVKANHFFAELPDKDLHHYDVTITPEVTSRGVNRAVMKQLVDNYRDSHLGSRLPAYDGRKSLYTAGPLPFNSKEFRINLLDEEVGAGGQRREREFKVVIKLVARADLHHLGMFLEGKQSDAPQEALQVLDIVLRELPTSRYIPVGRSFYSPDIGKKQSLGDGLESWRGFYQSIRPTQMGLSLNIDMSSTAFIEANPVIQFVCDLLNRDISSRPLSDADRVKIKKALRGVKVEVTHRGNMRRKYRISGLTAVATRELTFPVDERNTQKSVVEYFHETYGFRIQHTQLPCLQVGNSNRPNYLPMEVCKIVEGQRYSKRLNERQITALLKVTCQRPIDREKDILQTVQLNDYAKDNYAQEFGIKISTSLASVEARILPPPWLKYHESGREGTCLPQVGQWNMMNKKMINGGTVNNWICINFSRQVQDNLARTFCQELAQMCYVSGMAFNPEPVLPPVSARPEQVEKVLKTRYHDATSKLSQGKEIDLLIVILPDNNGSLYGDLKRICETELGIVSQCCLTKHVFKMSKQYMANVALKINVKVGGRNTVLVDALSRRIPLVSDRPTIIFGADVTHPHPGEDSSPSIAAVVASQDWPEITKYAGLVCAQAHRQELIQDLFKEWKDPQKGVVTGGMIKELLIAFRRSTGHKPLRIIFYRDGVSEGQFYQVLLYELDAIRKACASLEAGYQPPVTFVVVQKRHHTRLFAQNHNDRHSVDRSGNILPGTVVDSKICHPTEFDFYLCSHAGIQGTSRPAHYHVLWDENNFTADGLQSLTNNLCYTYARCTRSVSIVPPAYYAHLAAFRARFYMEPETSDSGSMASGSMARGGGMAGRSTRGPNVNAAVRPLPALKENVKRVMFYC
Protein: Propionate--CoA ligase (EC 6.2.1.1) (EC 6.2.1.17) (G3V9U0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Citrate synthase, mitochondrial
- Acetyl-CoA carboxylase 1
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-coenzyme A thioesterase
- Peroxisomal acyl-coenzyme A oxidase 1
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Acetyl-CoA acetyltransferase, cytosolic
Sequence:
MPRARPLASGSALTRGPASRVDLFSPPRHPQRPQRRPRCSELDVMGLPEERRKSGSGSRAREETGAEGRVRGWSPPPEVRRSAHVPSLQRYRELHRRSVEEPREFWGNIAKEFYWKTPCPGPFLQYNFDVTKGKIFTEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTKITYRELLVQVCQFSNVLRKQGVQKGDRVAIYMPMILELVVAMLACARLGALHSIVFAGFSAESLCERILDSSCCLLITTDAFYRGEKLVNLKELADESLEKCREKGFPVRCCIVVKHLGRAELGMNDSPSQSPPVKRPCPDVQISWNEGVDLWWHELMQQAGDEFEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHPEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDEGRLWSIVDKYKVTKFYTAPTAIRMLMKFGDDPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGSQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSASFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHTRFETTYFKKFPGYYVTGDGCRRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPTLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDTSTVADPSVINHLFSHRCLTTQ
Protein: Ergothioneine biosynthesis protein 1 (Meiotically up-regulated gene 158 protein) [Includes: L-histidine N(alpha)-methyltransferase (EC 2.1.1.44); Hercynylcysteine S-oxide synthase (EC 1.21.3.10)] (O94632)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine and subsequent conjugation with cysteine and oxygen to form hercynylcysteine sulfoxide, the first two steps in the biosynthesis pathway of ergothioneine. May play a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Hercynylcysteine sulfoxide lyase
- Histidinol dehydrogenase
- Uncharacterized protein C11D3.10
- Uncharacterized aminotransferase C777.03c
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS7
Sequence:
MTEIENIGALEVLFSPESIEQSLKRCQLPSTLLYDEKGLRLFDEITNLKEYYLYESELDILKKFSDSIANQLLSPDLPNTVIELGCGNMRKTKLLLDAFEKKGCDVHFYALDLNEAELQKGLQELRQTTNYQHVKVSGICGCFERLLQCLDRFRSEPNSRISMLYLGASIGNFDRKSAASFLRSFASRLNIHDNLLISFDHRNKAELVQLAYDDPYRITEKFEKNILASVNAVFGENLFDENDWEYKSVYDEDLGVHRAYLQAKNEVTVIKGPMFFQFKPSHLILIEESWKNSDQECRQIIEKGDFKLVSKYESTIADYSTYVITKQFPAMLQLPLQPCPSLAEWDALRKVWLFITNKLLNKDNMYTAWIPLRHPPIFYIGHVPVFNDIYLTKIVKNKATANKKHFWEWFQRGIDPDIEDPSKCHWHSEVPESWPSPDQLREYEKESWEYHIVKLCKAMDELSTSEKRILWLCYEHVAMHVETTLYIYVQSFQNANQTVSICGSLPEPAEKLTKAPLWVNVPETEIAVGMPLTTQYTSVGSNLQSSDLSAHENTDELFYFAWDNEKPMRKKLVSSFSIANRPISNGEYLDFINKKSKTERVYPKQWAEIDGTLYIRTMYGLLPLDDYLGWPVMTSYDDLNNYASSQGCRLPTEDELNCFYDRVLERTDEPYVSTEGKATGFQQLHPLALSDNSSNQIFTGAWEWTSTVLEKHEDFEPEELYPDYTRDFFDGKHNVVLGGSFATATRISNRRSFRNFYQAGYKYAWIGARLVKN
Protein: NAD(P)(+)--arginine ADP-ribosyltransferase 2 (EC 2.4.2.31) (Mono(ADP-ribosyl)transferase 2) (AT2) (P55807)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted, extracellular space. Note=The mature enzyme is probably secreted from granulocytes into the extracellular space.
Interaction partners:
- Type-1 angiotensin II receptor
- Uncharacterized protein.
- Ig-like domain-containing protein.
Sequence:
MELLALRWVLLAGTLLSTSAASSALQEGDLGSITVIMDMAPNSFDDQYVGCAHVMWANLQKLKCTEFARNYAYAVGWRKAAAEWQKRWGYLAHPMQLRPEQAIALLAYSAASNLYQQFNAATRQGGCSHQYYVHFYHFKTLHFLLTQALFALRASQPRCYYVYRGVRGIRFMTQRGKSVRFGQFTSTSLRKDVAVNFGQDTFFVVKTCYGVPIKQFSFYPSEDEVLIPPFEVFEVTNFCTGNGRIQIYLRSKGKMSRHNCELLKPRGGQWGRGHQEVGLGLSPGLALPVLPCSNCSCWGSGHRAGDPIPAAV
Protein: DNA-directed RNA polymerase subunit Rpo11 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit L) (B8YB62)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00261, ECO:0000269|PubMed:22848102}.
Interaction partners:
Sequence:
MEIKILKSESNYLELEIEGEDHTLGNLIAGTLRKISGVSFASYYQPHPLTDKIIVKILTDGSIAPKDALLKAIETVRVMASHYIDEIKGLTK
Protein: Frizzled (Frizzled-1) (dFz1) (P18537)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Protein wingless
- Segment polarity protein dishevelled
- Vang-like protein
- Axin
- Protein prickle
- Protein Wnt-5
- Diego, isoform A
- Protocadherin-like wing polarity protein stan
- Wnt inhibitor of Dorsal protein
Sequence:
MWRQILFILPTLIQGVQRYDQSPLDASPYYRSGGGLMASSGTELDGLPHHNRCEPITISICKNIPYNMTIMPNLIGHTKQEEAGLEVHQFAPLVKIGCSDDLQLFLCSLYVPVCTILERPIPPCRSLCESARVCEKLMKTYNFNWPENLECSKFPVHGGEDLCVAENTTSSASTAATPTRSVAKVTTRKHQTGVESPHRNIGFVCPVQLKTPLGMGYELKVGGKDLHDCGAPCHAMFFPERERTVLRYWVGSWAAVCVASCLFTVLTFLIDSSRFRYPERAIVFLAVCYLVVGCAYVAGLGAGDSVSCREPFPPPVKLGRLQMMSTITQGHRQTTSCTVLFMALYFCCMAAFAWWSCLAFAWFLAAGLKWGHEAIENKSHLFHLVAWAVPALQTISVLALAKVEGDILSGVCFVGQLDTHSLGAFLILPLCIYLSIGALFLLAGFISLFRIRTVMKTDGKRTDKLERLMLRIGFFSGLFILPAVGLLGCLFYEYYNFDEWMIQWHRDICKPFSIPCPAARAPGSPEARPIFQIFMVKYLCSMLVGVTSSVWLYSSKTMVSWRNFVERLQGKEPRTRAQAYV
Protein: Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (SMAD family member 6) (SMAD 6) (Smad6) (hSMAD6) (O43541)
Organism: Homo sapiens (Human)
Function: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta. Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes. Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions.
Subcellular location: Nucleus {ECO:0000269|PubMed:16491121}.
Interaction partners:
- E3 ubiquitin-protein ligase SMURF1
- E3 ubiquitin-protein ligase SMURF2
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 7
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 9
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog 3
Sequence:
MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLQHAPEPDAADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNPR
Protein: Calcineurin binding protein 1 (A0A1W2P8C4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XDCSMAVQEEPKEPYVSSVLPWIILHRIIWQEEDTFRSLCHQQQLQNPTEEGIPEMPMLPSSLMLLNTAHEYLGRRSWCCNSDGALLRFYVQVLQKELAASASEDTHPYKEELETALEQCFYCLYSFPSKKSKARYLEEHSAQQVDLIWEDALFMFEYFKPKTLPEFDSYKTSTVSADLANLLKRIATIVPRTEKPALSMDKVSAYIEGTSAEAPCLPEGADPTPPVLNELYYLLADYHFKNKEQSKAIKFYMHDICICPNRFDSWAGMALARASRIQDKLNSNELKSDGPIWKHATPVLNCFRRALEIDSSNLSLWIEYGTMSYALHSFASRQLKQWRSELPPELVQQMEDRRDSMLETARHCFTSAARCEGDGDEEEWLIHYMLGKVAEKQQQPPTVYLLHYRQAGHYLHEEAARYPKKIHYHNPPELAMEALEVTLQVQGRMSGQEGPPALSPGTGAHSQSPVIPLQPHW
Protein: THO complex subunit 4B (ALYREF homolog 2) (AtALY2) (Q8L719)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Export adapter involved in nuclear export of spliced and unspliced mRNA.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:15299117}.
Interaction partners:
- THO complex subunit 4C
- THO complex subunit 4D
- THO complex subunit 2
- Protein mago nashi homolog
- RNA-binding protein Y14
- DEAD-box ATP-dependent RNA helicase 15
- Eukaryotic initiation factor 4A-1
- THO complex subunit 1
- THO complex subunit 5A
- CASC3/Barentsz eIF4AIII binding protein
Sequence:
MSGGLDMSLDDIIKSNRKPTGSRGRGGIGGGNNTGGRGGSGSNSGPSRRFANRVGARTAPYSRPIQQQQAHDAMWQNDVFATDASVAAAFGHHQTAVVGGGSSIETGTKLYISNLDYGVSNEDIKELFSEVGDLKRYGIHYDRSGRSKGTAEVVFSRRGDALAAVKRYNNVQLDGKLMKIEIVGTNLSAPALPILATAQIPFPTNGILGNFNENFNGNFNGNFNGNFRGRGRGGFMGRPRGGGFGGGNFRGGRGARGRGGRGSGGRGRDENVSAEDLDAELDKYHKEAMETS
Protein: Uncharacterized protein At5g41620 (Q66GQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Glucan endo-1,3-beta-glucosidase 9
- 3'-5' exonuclease
- NDR1/HIN1-like protein 10
Sequence:
MESKVRGEEERQKVERLVEKLKVHNNNNNRSSTPAHISFVPNSIVVSSRKLAAAFWEFHQYHYKDEEDCSYSYLSSASAKMHRGPNGFAGASSRRQRHGKAVAVKENGLDLSQFLRDPSPDHQPDSAGSLRRQIGQMLIKHHQSIDRNNHALQPVSPASYGSSLEVTTYNKAVTPSSSLEFRGRPSREPHYNLKTSTELLKVLNRIWSLEEQHVSNISLIKALKTEVAHSRVRIKELLRYQQADRHELDSVVKQLAEEKLLSKNKEVERMSSAVQSVRKALEDERKLRKRSESLHRKMARELSEVKSSLSNCVKELERGSKSNKMMELLCDEFAKGIKSYEEEIHGLKKKNLDKDWAGRGGGDQLVLHIAESWLDERMQMRLEGGDTLNGKNRSVLDKLEVEIETFLQEKRNEIPRNRRNSLESVPFNTLSAPPRDVDCEEDSGGSDSNCFELKKPAESYGDETKKPNQHNKDGSIDEKPKSPSSFQVNFEDQMAWALSSNGKKKTTRAIEDEEEEEDVKPENSNNNKKPENECATTNKNDVMGEMIRTHRRLLSETREIDEASCNFPSSRRQASPVRQWISRTVAPDLLGPSEIAIAHGVKDNTLKTKLANSSKSRLRLFKG
Protein: Uncharacterized protein (Q9VGA8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP13722p
- Chorion protein a at 7F, isoform A
- GEO10373p1
- Uncharacterized protein
- Uncharacterized protein
- Mucin related 11Da
Sequence:
MFLPIATLLLIFTGAAFAADPFNQVEEFVDFEDIDEVANTESEGVTDVPIITATPISIPTSSTKTGLTREYTADGLTTTTSTTLASISTHSSTTATTTTDSSTSHSKTNDSTTDESTTTDFATLSSTTAQASTRILKTTVSTTSSTTTTSTTSPSTSDSTTNNSTTTETTTVPTTSASTTDSRLTSLSTTDSTTSDSTTNEITTSGSTKKDETSTTTSTTADSITSSPNTSDFTTTESITESSTTTRSTSIETSTSSSPTTVSTTIGSTTNNTTTSVSTEDSPTTTTESTTTTEQPSEEEIILALLAENAGALDRFNTQLDAVSAINWKIDAELDNQAEYLDAIEVTEELLRNQTQELLLWEVELLRGVVTSFQNLDIFANRSIEAVSDLTRLQEQNKDRVRNLVDKLNVTQGQILRRTKGLDDRLNFVNQLLLGYIEPKVNSLEDSFDNLNKSQINSLIELKNVPEVRNLTKTSIRKLSFLDNQLALFNQTQENRYYSVEAVIKAWTPTNLKEINDLTHALSISQKRTDLAIAISGSAEYNTETYPTRFISYKGIEDINQSRKTRTPQILGAEDNALESSWNVVAPA
Protein: Serine/threonine-protein kinase sepA (EC 2.7.11.1) (Septase A) (Q8T2I8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19479821}.
Interaction partners:
Sequence:
MSKKEPEEIKKNVTVGNYNLGVVIGKGGFGTVYQGLDIEDGDFVAIKQINLTKIPKDQLQGIMNEIDLLKNLNHANIVKYIKYVKTKDNLYIVLEYVENGSLSGIIKKFGKFPETLVCVYIRQVLEGLVYLHEQGVVHRDIKGANILTTKEGKIKLADFGVATKFDDTSAAAVVGTPYWMAPEIIELNGATTKSDIWSVGCTVIELLTGSPPYYDLGQMPALFRIVQDDCPPLPEGISPPLKDWLMQCFQKDPNLRISAQKLLKHKWIQASIKKKPVENGAGGVGNGTDSLGAPANIDDIAKNITDYNERINKKPSHQRKPSIHPKSPKGKVFLPPPEEEEDEWGDDFSNTPKSIKLPDKKSPLKLTNNKPSTPLKQQPTNNTPVQQQQQQQQPPPLKLAVPKQPVIENDDDWGDDFNTVSDLSKAVGSLNFNNNKKNETPKPNIKKPTFSEDEDEDDDDDGFGSGGDDEDDDFGDIPTSIKLNPKFGSNIKGNSSGSANTTNSSSTVVQQPKLTVSNNNNNNNKKLPLSPRQPSSGNVKEGINHGSTGSKSGGVIIDQWGEDGEEDNDWGDVATVNFDPKVIRKGTVNKPDLSTRLKNRIALSETALSNSFNNNGNDDEDEDIFADDFDEDDDEDFDLDKNLMKDNYARMSSEILKLMNLLTPEQPEEVISSACTQLITMFKENSEQKTLLIRRHGVIPIMEMLEVSNIQSHVLCSILKVVNQIIDNNMEIQENLCLVGGIPAIMKFSGPEYPASVRLETASFISKMCSTSTLTLQMFIACKGLPILVDFLLSPYAESKRLVWMAVDAIVNVFELQSPTPKNDFCRLFSKCGLLKTLPIVLRDSIADGEAAATYPDRIINLFIMFSAADSVVRKTMSAVEVIRPILDTLSQLMPEQLAKVLKSIKQLSMDHNTLANLQNAGAIRFMVPFLGRRTGAFVAEIHNHVLNTMFHLCRIDPERQYQAAIDGIIPHLQYFITSHSPLNQFALPIICDLAHSKKARSELWKNNGVAFYLSLLEERYWQVNALDSLAVWITDETHKVENIIATNENIKKLIQLFTNAESQSFAGILEPLLKIIQISIPVNILLGTSNFITKIIDKLGHTNPQVRLNLLKIITSLYECHPNAKKMIQEFKLIPIIQKIADTDKSVLVQKMASKLLEAFNANTVI
Protein: Tia1 cytotoxic granule-associated RNA binding protein-like 1 (Q5BJN3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cytotoxic granule associated RNA binding protein TIA1
- ELAV-like protein 1
- Ras GTPase-activating protein-binding protein 1
- Fragile X messenger ribonucleoprotein 1
- NTF2 domain-containing protein
- Eukaryotic translation initiation factor 3 subunit B
- Heterogeneous nuclear ribonucleoproteins C1/C2-like
- Eukaryotic translation initiation factor 4E
- RCG31562, isoform CRA_c.
Sequence:
MMEDDGQPRTLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEQPDSRRVNSSVGFSVLQHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGGRQIRTNWATRKPPAPKSTQETNTKQLRFEDVVNQSSPKNCTVYCGGIASGLTDQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYWGKESPDMTKNFQQVDYSQWGQWSQVYGNPQQYGQYMANGWQVPPYGVYGQPWNQQGFGVDQSPSAAWMGGFGAQPPQGQAPPPVIPPPNQAGYGMASFPTQ
Protein: Elastase inhibitor AFLEI (P86036)
Organism: Aspergillus flavus
Function: Elastase inhibitor. Inhibitor of A.flavus elastase with a Ki of 40 nM. Inhibitor of A.fumigatus elastase and human leukocyte elastase. Inhibits the fibrinogenase and collagenase activities of A.flavus elastase. Does not inhibit porcine pancreatic elastase, trypsin, chymotrypsin, thrombin or A.acutus AC1-proteinase.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
DPATCEKEAQFVKQELIGQPYTDAVANALQSNPIRVLHPGDMITMEYIASRLNIQVNENNEIISAHCA
Protein: PHO85 cyclin CLG1 (Cyclin-like G1 protein 1) (P35190)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Has a role in cell integrity and polarized cell growth together with the other PCL1/PCL2 cyclin family members.
Interaction partners:
- PHO85 cyclin-2
- PHO85 cyclin-9
- PHO85 cyclin-5
- PHO85 cyclin-1
- Cyclin-dependent protein kinase PHO85
- PHO85 cyclin-8
- PHO85 cyclin-6
- PHO85 cyclin PHO80
- PHO85 cyclin-7
- PHO85 cyclin-10
Sequence:
MANTFKYYPETMGNSSGYPISLPFPKGSATSAVNVARQLPKYLGHVPSQSVHTQLPSMASLGYFNQPSSTYYAPPAPLQQHQQPPILPPPGLMYTSNNNSNVIPPPVQMIRDGQQQPQQSNQVNGGVSENLDYDISIMSKFIMENAFVAFNANYSTDDQTTDLFFKGISSVLNATRLPSATIFLAIDYLFKYINKLSNGIHSIGGNSINIIYQNTMIAFILANKFNDDKTFTNNSWSQATGILINVINDFERQWLRIFNWELYDSAFLYFEFVKNFEIFKQNQLKPAVAVPTLLSPIVNVGDTRNVNFNLKPTSTNNLLSPVSNYETPMLMPHNMFSSPSYQSNSRSEFSSMNGYYNYYNYNQPRLNYYQQFPNIYSSPISETQFDYDFYNFSSQQQQQQQKQHSLLPAAPQLPPPHVHNQSYGHHLGWKSMDDTINHSRFERNYFPYSAVY
Protein: NK2 homeobox 2 (Q8BRS9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSLTNTKTGFSVKDILDLPDTNDEDGSVAEGPEEESEGPEPAKRAGPLGQGALDAVQSLPLKSPFYDSSDNPYTRWLASTEGLQYSLHGLAASAPPQDSSSKSPEPSADESPDNDKETQGGGGDAGKKRKRRVLFSKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKMKRARAEKAFQNRRMDARIEAAVPIVSARWSDWIRKQFQVGRLTQAWEHNLVICGFEGCLGKVHLQ
Protein: BZIP transcription factor (MetR), putative (Q4WNP9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Probable E3 ubiquitin ligase complex SCF subunit sconB
- Cytochrome c oxidase subunit 6, mitochondrial
Sequence:
MSGYNGRRAPNFSQYLEDLNAIPSPYDQALQQQQRQDTFNLDAELSLFTNTEFFDFDNLGDLNLPSFDAVNEDSAKTTDQQHGGPAAHNPDMEFLDLLGDGFGNMPDFSAANLNSINSQFPAQDTQFSTIPSIPSGLSNAPFNANPTPSQSSSSAASPAGPATSPIAAQAPSATTAAGPKRKNTQKPAPMSVEEAARIAAEEDKRRRNTAASARFRVKKKLREQALEKTVKETTEKNAALEARVTALELENQWLKNLITEKNGKSAEETKKSETDIANMFKKFLSSQKADAERSSSESKIGVGTA
Protein: 40S ribosomal protein S13, putative (Q586C2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein translation factor SUI1 homolog, putative
- 60S ribosomal protein L19, putative
- Polyubiquitin, putative
- 40S ribosomal protein S18, putative
- 60S ribosomal protein L5, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L39, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S26
- 40S ribosomal protein S16, putative
Sequence:
MVRMHGNGHGKAASALPYRRTPPTWLKSSSRDVIDAVCKLAKKGLSPSRIGMQLRDSMGIAQVKNVTGRKILRILKHKGMAPEIPEDLYCLIKRATQMRKHLERNTKDKDTKFRLILVESRIHRLARYYRRVKQLPPTWKYESSTASAMVA