wanglab/gogpt-training-data huggingface dataset:
Protein: Forkhead box protein C1-A (FoxC1) (Fork head domain-related protein 11) (XFD-11) (Q9PVZ3)
Organism: Xenopus laevis (African clawed frog)
Function: DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development. Acts either as a transcriptional activator or repressor. Binds to the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon DNA-binding, promotes DNA bending. Required for cell viability and resistance to oxidative stress in the eye. Promotes cell growth inhibition by stopping the cell cycle in the G1 phase through TGFB1-mediated signals. Involved in epithelial-mesenchymal transition (EMT) induction by increasing cell proliferation, migration and invasion. Involved in chemokine-induced endothelial cell migration. Plays a role in epidermal keratinocyte terminal differentiation. Essential developmental transcriptional factor required for mesoderm-derived tissues formation, such as the somites, skin, bone and cartilage. Plays a role in the development and maintenance of mesenchymal niches for haematopoietic stem and progenitor cells (HSPC). Plays a role in corneal transparency by preventing both blood vessel and lymphatic vessel growth during embryonic development in a VEGF-dependent manner (By similarity). Plays a role at the gastrula stage for expression of several mesodermal and endodermal genes. At the late neurula stage, regulates expression of adhesion genes to maintain cell adhesion in the mesodermal germ layer.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q61572}.
Interaction partners:
Sequence:
MQARYSVSSPNSLGVVPYLSGEQSYYRAAAAAAAAGGGYTGMAAPMSMYSHPAHEQYQAGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMERFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKDATKEDKERLLKEHHGSQSAAAQQQRQQQQSQAQAEQDSNSQPVRIQDIKTENGTSSPPQSMSPALSAVPKIESPDSSSSMSSGSPHSIPSNRSMSLEAAESHHPHHQQHSQGFSVDNIMTSLRGSPQGSAELPSPLISSSRTGIAPSLSLSYSPGQGSIYSSPCSQGTSSGGGAGTYHCNMQAMSLYSGDRSGHLTPANTPAATTVEETLPDYSISTTSAQSHGNQEHPHQGRLPSWYLNQTGELGHLAGATYPGQQQNFHSVREMFESQRLALNSSPVNGNSSCQMSFPPSQSLYRTSGAFVYDCSKF
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (F1M4Q5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Cofilin 2
- Cofilin-1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase
- Calcineurin subunit B type 2
- Protein phosphatase Slingshot homolog 3
- Protein phosphatase Slingshot homolog 1
- Calcineurin subunit B type 1
Sequence:
MTLSTLADERKAPPASTCSLGGPDMIPYFSANAVISQNAINQLISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARMHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIPTERERTERLIKTKLREIMMQKDLENITSKEIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYEYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKEMTTSADQITEVKTVESLAAMPPVFMEHVVPQDVNQKGLRTKERVICLEFSSQEFHAGQIEDELNLNDINGCSSGCCLSESKFPLDNCHASKALLQPGQAPDIANKFPDLAVEDLETDALKADVRVHLLPMEELTSRLKDLPMSPDLESPSPQAGCQAAISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRIEELGGGRSEGCRLSVMEMAPSEMVTDDQRSSSLSDTPHASEESSVDEDQPKAVSELVSPDIIMQSHSENAISVKEIVTEIESISQGVGQVQLKGDILSNPCHTPKKNIIHELPLERVQGPENKPGHLEQDESFCSVQLELARDSGKCAPEEGCLATLSSTGDLEEEEPVEGEHDWGPGTHPGAKWCPGSVRRATLEFEERLRQEQENHGTASPGPTLSNRKNSKNDSSVADLMPKWKSDETASEHSLSPKEAEPGKGKGKCSGSEAGPLSHCEHNPAAAAPQLLEHHPSPAPQDCLGSESRSEKQEEDLRKQRTVVSNQECETQAALLPLPKKIEIIEYTPTVTSLDHTEPGGETTPSKESEKQELRKVKMERSITMFCTLDENLNRTLDPSQVSLRPQVLPLPHSSSEYDRLTDPTPMLSSPQDKGDSPSTPFKTPARLVGCSTQGASVSLDCSHRHSVLHLEGCTEQSSTTDSRLSSEHMNWEDSQGDFLSSSTGMAHTSSPLTNEDLSLINKLGDSVGVLPKKLDPSPEACRIPHSSSSENIRDLSHGPGVVKEHAKEIEPRVIFQAAFSKTSQMRRSASLAKLGYLDLCKDYLPDRELGSSESPHLKLLQPFLRTDSGMHALMVHEPSESPGAHPNPQPTKYFVEQLKTTECVVQSKPVERPHVQYAKEFGFSQQCLLPKARPELTSSEGGLPLLQTQGLQYPGPSPGLAVAPRQQHGRTHPLRRLKRANDKKRTTNPFYNTM
Protein: MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 1 (MA3 domain-containing protein 6) (Q94BR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in target of rapamycin (TOR)-regulated translation control, especially under energy-deficient conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytosol {ECO:0000269|PubMed:29084871}.
Interaction partners:
- F-box protein At5g18160
- Cytochrome P450, family 705, subfamily A, polypeptide 18
- Probable protein phosphatase 2C 23
- Probable histone H2A.3
Sequence:
MASGEGILTDGQWKKLEIATHNSGSLSSSPKSHTLFADLNIKSPTGGKGPVAGIPNRHVRRTHSGKHIRVKKEGAGGKGTWGKLLDTDDGDSCIDKNDPNYDSGEDAYDGLVDSPVSDPLNDYKKSVVSIIDEYFSTGDVKVAASDLRELGSSEYHPYFTKRLVSMAMDRHDKEKEMASVLLSALYADVILPDQIRDGFIRLLRSVDDLAVDILDAVNVLALFIARAIVDEILPPVFLVRSKKILPESCKGFQVIVTAEKSYLSAPHHAELVEKKWGGSTHTTVEETKKKISEILKEYVENGDTYEACRCIRELGVSFFHHEVVKRALVLAMDSPTAESLVLKLLKETAEEGLISSSQMVKGFFRVAESLDDLALDIPSAKKLFDSIVPKAISGGWLDDSFKITSDQDGEKSSQDGKLRQYKKDTVNIIQEYFLSDDIPELIRSLQDLGAPEYNPVFLKRLITLALDRKNREKEMASVLLSALHMELFSTEDFINGFIMLLESAEDTALDIMDASNELALFLARAVIDDVLAPLNLEDISTKLPPKSTGTETVRSARSLISARHAGERLLRSWGGGTGWIVEDAKDKISKLLEEYETGGVTSEACQCIRDLGMPFFNHEVVKKALVMAMEKQNDRLLNLLEECFGEGLITTNQMTKGFGRVNDSLDDLSLDIPNAKEKFELYASHAMDNGWILPEFGISATQ
Protein: Xylulose kinase (Xylulokinase) (EC 2.7.1.17) (O75191)
Organism: Homo sapiens (Human)
Function: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis.
Interaction partners:
- Sorbitol dehydrogenase
- Ribulose-phosphate 3-epimerase
- Solute carrier family 22 member 14
- Ribulose-phosphate 3-epimerase-like protein 1
- Fucose mutarotase
- Solute carrier family 22 member 13
- Transketolase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Transketolase-like protein 2
- Transketolase-like protein 1
Sequence:
MAEHAPRRCCLGWDFSTQQVKVVAVDAELNVFYEESVHFDRDLPEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSIYWKAGAQQALTSLSPDLRLHQQLQDCFSISDCPVWMDSSTTAQCRQLEAAVGGAQALSCLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPIDYSDGSGMNLLQIQDKVWSQACLGACAPHLEEKLSPPVPSCSVVGAISSYYVQRYGFPPGCKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFYFDVMEITPEIIGRHRFNTENHKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLAPNPRLAATPSPGASQVYEALLPQYAKLEQRILSQTRGPPE
Protein: Cycloviolacin-O2 (P58434)
Organism: Viola odorata (Sweet violet)
Function: Probably participates in a plant defense mechanism. Has strong cytotoxic activity against a variety of drug-resistant and drug-sensitive human tumor cell lines, and against primary chronic lymphocytic leukemia and ovarian carcinoma cells. Has weaker cytotoxic activity against normal lymphocytes. Has hemolytic activity.
Interaction partners:
Sequence:
GIPCGESCVWIPCISSAIGCSCKSKVCYRN
Protein: Zinc finger protein ham-2 (HSN abnormal migration protein 2) (H2KYH4)
Organism: Caenorhabditis elegans
Function: Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:10049362}.
Interaction partners:
- Putative protein tag-53
- Zwei Ig domain protein zig-6
- SWI/SNF chromatin-remodeling accessory subunit 1
Sequence:
MPYRAELKRPDLKGSFPCSICQKVFCHSSSLSRHRMQAHFKSYTCTTCNNEIPSNDTLRSHMYRVHNITRMFMCRCCNWAFPDKTSLHIHMQSMLKNGTPGEAAVLAKSSDVVDSTSESGSPRQSPPFSPDLLMQKRMLQVAANNNNIGSIFPTLLKSPDSKSMFPLDLSNMGPSQFLSAWLANNPINTAALNLAAQQTPSKDSIQSSNISDYDDLEVQTTEEDIKFEVESSDVSPRSVIVKTEPTFKRELEHDADIDVEGDDGEPPLKMTIDDKNIHISHDQPSPTVSDSHISGGSSSHSGESLKCFDCQVARGKLVAVEDKCRAYEKTIRELQVQVDFLRKIQPNPMPPVMLPPPMMPMPSPGPNNLFQNPAMRMLLNNLIHMNRPSVVP
Protein: Probable E3 ubiquitin-protein ligase ipaH4.5 (EC 2.3.2.27) (Probable RING-type E3 ubiquitin transferase ipaH4.5) (P18009)
Organism: Shigella flexneri
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway.
Subcellular location: Secreted. Host cytoplasm {ECO:0000305}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000305}.
Interaction partners:
- Conserved hypothetical protein.
- Hypothetical protein.
- Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF
Sequence:
MKPINNHSFFRSLCGLSCISRLSVEEQCTRDYHRIWDDWAREGTTTENRIQAVRLLKICLDTREPVLNLSLLKLRSLPPLPLHIRELNISNNELISLPENSPLLTELHVNGNNLNILPTLPSQLIKLNISFNRNLSCLPSLPPYLQSLSARFNSLETLPELPSTLTILRIEGNRLTVLPELPHRLQELFVSGNRLQELPEFPQSLKYLKVGENQLRRLSRLPQELLALDVSNNLLTSLPENIITLPICTNVNISGNPLSTHVLQSLQRLTSSPDYHGPQIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLA
Protein: Quinoprotein glucose dehydrogenase (EC 1.1.5.2) (Glucose dehydrogenase [pyrroloquinoline-quinone]) (P15877)
Organism: Escherichia coli (strain K12)
Function: GDH is probably involved in energy conservation rather than in sugar metabolism.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Periplasmic side {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}.
Interaction partners:
- Glucokinase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase
- Enolase
- Glyceraldehyde-3-phosphate dehydrogenase A
- Triosephosphate isomerase
- Pyruvate kinase II
- Pyruvate kinase I
- Fructose-bisphosphate aldolase class 1
- Phosphoenolpyruvate synthase
Sequence:
MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRSKRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGAVAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRFSPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALDAASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLIAINAENGKLCETFANKGVLNLQSNMPDTKPGLYEPTSPPIITDKTIVMAGSVTDNFSTRETSGVIRGFDVNTGELLWAFDPGAKDPNAIPSDEHTFTFNSPNSWAPAAYDAKLDLVYLPMGVTTPDIWGGNRTPEQERYASSILALNATTGKLAWSYQTVHHDLWDMDLPAQPTLADITVNGQKVPVIYAPAKTGNIFVLDRRNGELVVPAPEKPVPQGAAKGDYVTPTQPFSELSFRPTKDLSGADMWGATMFDQLVCRVMFHQMRYEGIFTPPSEQGTLVFPGNLGMFEWGGISVDPNREVAIANPMALPFVSKLIPRGPGNPMEQPKDAKGTGTESGIQPQYGVPYGVTLNPFLSPFGLPCKQPAWGYISALDLKTNEVVWKKRIGTPQDSMPFPMPVPVPFNMGMPMLGGPISTAGNVLFIAATADNYLRAYNMSNGEKLWQGRLPAGGQATPMTYEVNGKQYVVISAGGHGSFGTKMGDYIVAYALPDDVK
Protein: Ion-translocating oxidoreductase complex subunit D (EC 7.-.-.-) (Rsx electron transport complex subunit D) (P76182)
Organism: Escherichia coli (strain K12)
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00462}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00462}.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit C
- Ion-translocating oxidoreductase complex subunit E
- Ion-translocating oxidoreductase complex subunit A
- Ion-translocating oxidoreductase complex subunit G
- Ion-translocating oxidoreductase complex subunit B
- FAD:protein FMN transferase
- Endonuclease III lyase)
- Probable pyruvate-flavodoxin oxidoreductase
- UPF0125 protein RatB
Sequence:
MVFRIASSPYTHNQRQTSRIMLLVLLAAVPGIAAQLWFFGWGTLVQILLASVSALLAEALVLKLRKQSVAATLKDNSALLTGLLLAVSIPPLAPWWMVVLGTVFAVIIAKQLYGGLGQNPFNPAMIGYVVLLISFPVQMTSWLPPHEIAVNIPGFIDAIQVIFSGHTASGGDMNTLRLGIDGISQATPLDTFKTSVRAGHSVEQIMQYPIYSGILAGAGWQWVNLAWLAGGVWLLWQKAIRWHIPLSFLVTLALCAMLGWLFSPETLAAPQIHLLSGATMLGAFFILTDPVTASTTNRGRLIFGALAGLLVWLIRSFGGYPDGVAFAVLLANITVPLIDYYTRPRVYGHRKG
Protein: BOS complex subunit TMEM147 (Transmembrane protein 147) (Q6DGL7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:I6VSD2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- BOS complex subunit ncln
- BOS complex subunit NOMO1
- PAT complex subunit CCDC47
- Calcium load-activated calcium channel
- Zgc:109965.
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L32
- Large ribosomal subunit protein uL2
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha-like 2
Sequence:
MTLFHFGNCFSLAYFPYFITYKCSGLSEYNAFWRCVQAGATYLFVRLCKMLFLATFFPTWEGGAGVYDFVGEFMKATVDMADLLGLHLVMSRNAGKGEYKIMVAAMGWATAELIMSRCIPLWVGARGIEFDWKYIQMSFDSNISLVHYIAMAAVVWMFTRYDLPKSFRLPVAILLGLCVYKGFLMELFVHVFLLGSWTALLVKAVLTGAISLCSLFLFVTLVHSN
Protein: Beta-elicitin cryptogein (CRY) (P15570)
Organism: Phytophthora cryptogea
Function: Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNFTALLAAVAAALVGSANATACTATQQTAAYKTLVSILSDASFNQCSTDSGYSMLTAKALPTTAQYKLMCASTACNTMIKKIVTLNPPNCDLTVPTSGLVLNVYSYANGFSNKCSSL
Protein: Uncharacterized MFS-type transporter YhhS (P37621)
Organism: Escherichia coli (strain K12)
Function: Confers high-level resistance to glyphosate when overexpressed. Overexpression has no effect on intracellular arabinose concentrations.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01118, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01118, ECO:0000305|PubMed:15919996}.
Interaction partners:
Sequence:
MPEPVAEPALNGLRLNLRIVSIVMFNFASYLTIGLPLAVLPGYVHDVMGFSAFWAGLVISLQYFATLLSRPHAGRYADSLGPKKIVVFGLCGCFLSGLGYLTAGLTASLPVISLLLLCLGRVILGIGQSFAGTGSTLWGVGVVGSLHIGRVISWNGIVTYGAMAMGAPLGVVFYHWGGLQALALIIMGVALVAILLAIPRPTVKASKGKPLPFRAVLGRVWLYGMALALASAGFGVIATFITLFYDAKGWDGAAFALTLFSCAFVGTRLLFPNGINRIGGLNVAMICFSVEIIGLLLVGVATMPWMAKIGVLLAGAGFSLVFPALGVVAVKAVPQQNQGAALATYTVFMDLSLGVTGPLAGLVMSWAGVPVIYLAAAGLVAIALLLTWRLKKRPPEHVPEAASSS
Protein: Cell wall mannoprotein 1 (Q9HFP8)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Constitutive protein of the cell wall. Antigen target of host humoral immune response.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:11682494}. Note=Associated with the entire thickness of the hyphal cell walls, hyphal septa, and walls of conidiospores. {ECO:0000269|PubMed:11682494}.
Interaction partners:
Sequence:
MRFSALLVTLGLTGALATPTLVSREAPAVGVISDISAQTSALASAVSSYNGGDPSAVKSASEKLVSTINSGVDTVKSGPALSTADALALTSPVQDLTKQVEGVIDDLISKKDKFVAANAGGTVYEDLKAQYTAADSLAKAISAKVPESLSDIAAQLSAGITAAIQKGIDAYKDAASSTGTASSSAPATETATATETSTATGTVTETATSTPVIPTGTASGSASATPSTTATPTTGGSGSGSGSSTGTATASTSTNLLSTGAASKEHFSYSLGGAVVAAAIAVAL
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (A5XCL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLDVPHEAKVRGHQRAPSDSKEFHEVTKRDALRLLEHDVDRLLETTEKARQPALKAEMGRFADLFGRFIQEEGPALDWNKIQKLPENAVMNYSNLKSPKNEQIRNMLDKLVVIKLNGGLGTSMGCHGPKSVIPVRSDLTFLDLTVQQIEHLNKTYDANVPLVLMNSFNTDEDTEKIVRKYKGFRVQIHTFNQSCFPRISREHYLPVAKDFDVEKDMEAWYPPGHGDFYDTFRNSGLLKKFIEEGREYCFLSNIDNLGATVDLNILNKLVGEERATTPVEFVMEVTDKTRADVKGGTLIQMENKLRLLEIAQVPPEHVDDFKSVKTFKFFNTNNIWANLAAIDRVLRERTLNMEIIVNNKTLENGTRVIQLETAVGAAMKCFDGAIGINVPRSRFLPVKKSSDLLLVMSNLYTLKNGSLVMSPQRMFPTTPLVKLGENHFSKVKEFLGRFANIPDIIELDHLTVSGDVTFGRGVSLRGTVIIIANHGDRIDIPAGAILENKIVSGNMRILDH
Protein: SD04308p (Q86P82)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGHHLSKFSARANSQEKRNPTASSSPREAAALVETISLDEEELQVEEILTEATVSAATSPAEVRQIIIKIQLAKMENGNPVAAGQVESFAEVVEQEEEQQRQCADGATDDDAAALSADSLNANGQIVNVTLEGGYGEVGVVTNRTDGSSPEAPKTERQPVNNNGLAGSVGAAISTLQLHDNHGGNANCPLKADDDDDLDESLLRRRRSNSNSRSNIHHHHHHHHHQQQQQQHEAEVVEYCEVLESLPVSNMLSAGTQHSSKPVSRSNNSNSCCRSRSSKALSMGAATSSASGSASTSVSTSTSSKRRCCKCKCRDAIRGLRDMLPSSSSSVSNKKDAAAVVAMVPRKSRTADRRSTPPTLGTSSGGSQRRMQSQRIRNSVAVPDASHHHHQLIIRITSPGFVVESPNGGRVTVVTEPAPQSPQTPPRPRPLATVAPAGGAGHAGIGAARNMTVHSQIDFMHCLVPDLEKITNSSFYWGKMDRYEAEHLLEGKPEGTFLLRDSAQEEFLFSVTFRKYGRSLHARIEQSGHKFSFDCHDPCVFTAPTVTGLLEHYKDPACVMFFEPCLTIPLHRRQTFSLQQLSRATIVSNTSYDGINQMELPGRLKSYLKEYHYKQKLRVKPIDQNTPMPYYGNV
Protein: Aspartokinase 3 (EC 2.7.2.4) (Aspartate kinase 3) (Aspartokinase III) (P94417)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Interaction partners:
- Aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Diaminopimelate decarboxylase
- Homoserine kinase
- Homoserine O-acetyltransferase
- Aspartokinase 1
- Aspartokinase 2
- Threonine synthase
- Argininosuccinate synthase
- Putative aspartate aminotransferase YhdR
Sequence:
MKVVKFGGSSLASGAQLDKVFHIVTSDPARKAVVVSAPGKHYAEDTKVTDLLIACAEQYLATGSAPELAEAVVERYALIANELQLGQSIIEKIRDDLFTLLEGDKSNPEQYLDAVKASGEDNNAKLIAAYFRYKGVKAEYVNPKDAGLFVTNEPGNAQVLPESYQNLYRLRERDGLIIFPGFFGFSKDGDVITFSRSGSDITGSILANGLQADLYENFTDVDAVYSVNPSFVENPKEISELTYREMRELSYAGFSVFHDEALIPAFRAGIPVQIKNTNNPSAEGTRVVSKRDNTNGPVVGIASDTGFCSIYISKYLMNREIGFGRRALQILEEHGLTYEHVPSGIDDMTIILRQGQMDAATERSVIKRIEEDLHADEVIVEHHLALIMVVGEAMRHNVGTTARAAKALSEAQVNIEMINQGSSEVSMMFGVKEAEERKAVQALYQEFFAGVLIS
Protein: Fosmidomycin resistance protein (P52067)
Organism: Escherichia coli (strain K12)
Function: Confers the resistance against fosmidomycin.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- NAD
- Regulator of RpoS
- Multidrug resistance protein MdtH
- Flavohemoprotein
Sequence:
MAMSEQPQPVAGAAASTTKARTSFGILGAISLSHLLNDMIQSLILAIYPLLQSEFSLTFMQIGMITLTFQLASSLLQPVVGYWTDKYPMPWSLPIGMCFTLSGLVLLALAGSFGAVLLAAALVGTGSSVFHPESSRVARMASGGRHGLAQSIFQVGGNFGSSLGPLLAAVIIAPYGKGNVAWFVLAALLAIVVLAQISRWYSAQHRMNKGKPKATIINPLPRNKVVLAVSILLILIFSKYFYMASISSYYTFYLMQKFGLSIQNAQLHLFAFLFAVAAGTVIGGPVGDKIGRKYVIWGSILGVAPFTLILPYASLHWTGVLTVIIGFILASAFSAILVYAQELLPGRIGMVSGLFFGFAFGMGGLGAAVLGLIADHTSIELVYKICAFLPLLGMLTIFLPDNRHKD
Protein: Phosphoadenosine phosphosulfate reductase (EC 1.8.4.8) (3'-phosphoadenylylsulfate reductase) (PAPS reductase, thioredoxin dependent) (PAdoPS reductase) (P18408)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.
Interaction partners:
- Sulfite reductase subunit beta
- Adenylyl-sulfate kinase
- Sulfite reductase flavoprotein component
- Sulfate adenylyltransferase
- 3'
- Uroporphyrinogen-III C-methyltransferase
- Thiosulfate sulfurtransferase TUM1
- Siroheme biosynthesis protein MET8
- Transcriptional activator of sulfur metabolism MET28
- Thioredoxin-2
Sequence:
MKTYHLNNDIIVTQEQLDHWNEQLIKLETPQEIIAWSIVTFPHLFQTTAFGLTGLVTIDMLSKLSEKYYMPELLFIDTLHHFPQTLTLKNEIEKKYYQPKNQTIHVYKPDGCESEADFASKYGDFLWEKDDDKYDYLAKVEPAHRAYKELHISAVFTGRRKSQGSARSQLSIIEIDELNGILKINPLINWTFEQVKQYIDANNVPYNELLDLGYRSIGDYHSTQPVKEGEDERAGRWKGKAKTECGIHEASRFAQFLKQDA
Protein: Mitochondrial RNA binding complex 1 subunit (Q384R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial RNA binding protein
- REH2-associated factor 1
- RNA-binding protein, putative
- Mitochondrial RNA binding complex 1 subunit
Sequence:
MNGRLYCLIRRITSPPVATRLIKEELCLSMAAIARLPLRRDQLAHVTNTEAITTRAQRISHLCTPTELGMIAEGAEALSCNRFDLADALIDGAYESVRRAASSTRLSHVSAIARYSASIKTYGNETITTLLKAGASLLQKNDSVPVLKSFLGVAQSHLTDGEMRVLIDEMCAKATEEQRLCINSIGTQSLAKDAAKCGEETLTKGNEDGDETAVDDEETQAWDMLRARQWMLQLVRCGKPPTAAEAVQAMELYAHFAVRDFVLHEKIEDLVLLVLPTGNKFHLNEMHKIVLRSPNLFPRVRNTLGQDHSGVSDVHRADRGVEWSDDPASSLTTTYTTSRAYSMLLLGQRLSEDIMFDVVQEQSETIPVDVAAQAACLFAEKGDIPEGVILRLSAELEHISPQGVTAFVRAARRDSSGALLPHYAAVLNRFTERDLCDTPLETLLQMCEVFALPAPRGTSEGDNDSINESQSKFQKALIVRLFSVIQGSRDVPFLCKVAKAVRAFDANDELIQFVCSSICAQGALSECEALIAFDMIRCCDFVYEPLLDAMEPVFRRLVESVSAMLEGKSTINDVEVRRCACFATLQSEFDCPDFETLASLLVHTVEKNVTGCPVELIPSVGLLCVRTRRTSALYIVGNKLEGNMQQLSDDAIGELARLLVGTENLATKELAVEFQSVVVSRLLRQQSLPPDVVALSAVVWLRQGDKVGTIDERSVDYIIKWMYAIGSSVYTDLCLAVHLSASVESLSNALIDDLPRRLELLTTNEMANAIFGLGEVSDMGARLSHQLVAERCSDYVVDHSQEFWSGKVIARLLYGFSRMHCTKRSLYNVFATRLAHRPVFSLLDQEAISFAIAAFGRVKYLDKKLFDRFTRWILDHSKDLNAAELLLTIRGVSRVMLLNDQLYDDLGSKAAEKVKEFPIESQCVLLSSFGSLGVEHERLASRMVSSIAENREELTDATKAVDVITSLWSMNYDVEDDKHVAQLADWVVQRAEELTDESIGKLCLVLSDTNWRHVPLVRAIAEQSVRLQGQQSISPKCCREVLDVLGTFMIHHQGARENLSALGRSISKERIQLSEEEEQHLQLLLRR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (X2J946)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKKILSKFERNENSRLENPPNSSSSSSSNEKNSFVGKVFTVGRVTVTVEDVLAEGGFAMVFLARGNGGGSSSATKYALKRMYVNNEHDLNVAKREIQIASNLSGHKNIIGYVDSSITPTGNGVCEVLLLMPYCKHHMLAMMNARLHVGFTEPEVLNIFCDIAEAVSRLHYCQTPIIHRDLKVENILQTDAGNFVLCDFGSATAKTLNPQQHGVTVVQEEIQKYTTLSYRAPEMIDLYGGKSITTKADIWALGCMLYKLCFFSLPFGESTLAIQNGQFSIPDSSKYSKGMHQLIKYMLEPDMEKRPNIWQVCEVAFRLAGKDNPVQNLHKTPIPNFDLLVVPPFESEAKRISAAASKAAKAQNVSVVEAGTSVAPRSRPKGSSSVHGGNPLGLGLPPSPSPRQNITSPQPQPQPVVEQFQANFPAMPPAVPPPPQAVTPAAPAASKLFESSGYPDPFNEPAAAVIPTEFLPAAEEPNKEEVPQDLNVIAGTPTKSMLTPPKPSGGGGHRRNVSDTSAFNKTFANETSQFLAPFNNNLAAMGDGQQTLASAASNPGIYASSTANSAAVSISELMKPGQTAVEKRVEAWNPFEEEQPFSQMTEDHIFEAEFDKIRQRGSQGSITAKSASTTSTLTPTEQIPSAVVAPVTAAPGAVPPPPIAAAVSPYPSQVSEDPFGSAPFSLPPGLREKASSLRKTGESESDLNVDVDVV
Protein: Heat shock protein beta-2 (HspB2) (DMPK-binding protein) (MKBP) (Heat shock protein family B member 2) (Q16082)
Organism: Homo sapiens (Human)
Function: May regulate the kinase DMPK.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Localizes to nuclear foci.
Interaction partners:
- Cytochrome c
- Heat shock 70 kDa protein 4
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Heat shock protein beta-3
- Plectin
- Heat shock protein beta-8
- Heat shock cognate 71 kDa protein
Sequence:
MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP
Protein: Transthyretin (Prealbumin) (P50390)
Organism: Sus scrofa (Pig)
Function: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subcellular location: Secreted {ECO:0000269|PubMed:7601162}.
Interaction partners:
- Retinol-binding protein 4
- Uricase
- Vitamin D-binding protein
- Receptor for retinol uptake STRA6
- Albumin
- Alpha-1-antitrypsin
- Thyroxine-binding globulin
- Lipocalin/cytosolic fatty-acid binding domain-containing protein
- Apolipoprotein A-I
- Amyloid-beta precursor protein
Sequence:
MASYRLLLLCLAGLVFVSEAGPAGAGESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISPFHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSSPKEGAL
Protein: TRAF family member associated NFKB activator (E7ENY2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDKNIGEQLNKAYEAFRQACMDRDSAVKELQQKQTENYEQRIREQQEQLSLQQTIIDKLKSQLLLVNSTQDNNYGCVPLLEDSETRKNNLTLDQPQDKVISGIAREKLPKVRRQEVSSPRKETSARSLGSPLLHERGNIEKTFWDLKEEFHKICMLAKAQKDHLSKLNIPDTATETQCSVPIQCTDKTDK