wanglab/gogpt-training-data huggingface dataset:
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme A) (Q9VTK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- RE11167p
Sequence:
MTIKPVSAPPSAKRVAGNVDPDNKEAQVVVVEQSVVSQTHNHAHNHRNVVIDGQSPQRRGEVYDELARTHRCSPHKSTRSKRREHHEAHAHLYKRDRLEREKLVHPTAAAGSGAPGVSGSKCNSPPSTSTSGSSSPSAVGRNSPEHLGLGCTTVPTAQVQMSTSTAAANLLKTVEETFSGYNSGDEHHQPKERLIPVEEWQRRDLEFAKCMEQRGYELKPVEEDGACLFRSISLQIYGDEEMHDVIRQHTMDYIHENREYFGQFVTEDINSYIQRKRARDAHGNHIEIQAISEIYSRTVEVYCYQSNPINIFNSEQSQAGYPPLRLSYQRGSHYNAILDPYNATVGVGLGLAGYKPEIQTKEAVRLSEQLEIEQTMFEDKLKTTDWEATNEAIEEQIARESYLQWCRENTQRSRNSNTAAGSATSSTVTSAEALTDSDASPSKYSACGGTGSSGNPPVALTSGSGGDGAGPAFSLSPKTLNQFSHKLPQEVNELGGYDSDATDMSSTSSVGHSGGSSSPSTAASQRSGKGSKSQRRATALRKKRRHETRETTLASKSAEALEAPLRKSPKRDSAPSVARADTPEAEQRPSTSKQSSHSPQKNVDSKSPTEQSYSSFYQELLEASYANEGANESEMLQQAIQMSTRDYMEDQKRKFLFGP
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (O42866)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in biosynthesis of fatty acids in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Very-long-chain 3-oxoacyl-CoA reductase
- Fatty acid synthase subunit alpha
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
Sequence:
MRKVLITGGSSGLGKRIAQIWSQKGHQCHIVGRNEFHLKETLQSLSVAKGQQHTLTIADVQSDMKNLKSIFESVEIDTVVHAAGVLQSSLCVRTSEKEIDSIICTNLVSAIKLSKMAILEWFRNKNSERDRLILNISSRLSTYALPGTSVYAASKAGLESFTKVLAAEVASKGIRVNAISPGYVDTPMLSSQIRAIAEKKVPIGRLASTDEIVDACTFLLDNRYTTGTILPITGGL
Protein: Tight junction protein 1 (F1M4A0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}.
Interaction partners:
Sequence:
MIVTCNHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSHPDPDPVSDNEDDSYDEDVHDPRSGRGALANRRGEKSWARDRSASRDRSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSVRSHDRPPRRSQSRSPDQRSEPSDHSTQSPQQPSNGSLRSREEERMSKPGAVSTPVKHVDDHTPKAVEEVTVEKHEKQTPTLPEPKPVYAQVGQPDVDLPVSPSDGVLPNSTHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIVPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDHRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQAIHRIDSPGLKTASQQKAEASSPVPYLSPETNPASSASAVKHNVNLTNVNLEEPTPAPPTSHVSQADCLGAPSPEAPHTMLRDEGVSLPSHVDPAKVYRKEPYPEEMMRQNHILKQPALGHPGQRLDKEPNPAYDPQLPYVEKQASRDLEQPPYRYESSSYTDQFSRNYDHRLRFEDRVPTYEDQWSYYDDKQPYPTRPFDTQHPRDLDSRQHPEEASERGYFQRFEEPAPLPYDSRPRYEQLPRTSTLRHEEQPTSGYEVHNRYRPEAQPYAPAGPKSSEPKQYFDQYPRSYEQVPPPGFTSKTGHYEPLHGAAVVPPLIPSSQHKPEVLPSATKPQPPPPALTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDVNDTASFKPPEVASKPPSASLVGPKPVSQTQFSEHDKTLYRLPEPQKPQAKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESKPPAHIPAGHHSEPAKPVHSQSQPNFSSYSSKGKPETDAMDRSFSEKRYDPTQAMPPPPPLPSQYSQPVPPLSNSSLHIHSKAAQSEGNSVSLDFQNSYISKPDPPPSQSKPATFRPPTREDPPQTFYPQKSFPDKASVNGAEQTQKTITPAYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETVHKPELSSKPPPSPKTLMKAHSSTQPPEFDSGVETFSVHTDKPKYQINNISTMPKAVPVSPSAVEEDEDEDGHTVVATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGIEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCDPKTWQNKCLPGDPNYLVGANCVSVLIDHF
Protein: A disintegrin and metalloproteinase with thrombospondin motifs adt-2 (ADAMTS adt-2) (EC 3.4.24.-) (Q19204)
Organism: Caenorhabditis elegans
Function: Regulates body size probably independently of the TGF beta-like dbl-1 pathway. However, may regulate some dbl-1-mediated transcription. Plays a role in cuticle collagen fibril organization. Required for embryonic development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- SMAll.
- Male abnormal protein mab-31
- RGS domain-containing protein
Sequence:
MLLPLLISGLLFRNADAFLPFFNEDDLKYTFGVDTHAEVPNHEEIDPVPYYHQNGSLHKLEFMAFNKKYNLSLEPTLAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHYGEKVYAAISNCDGRIKGTVIDDGEIIVVHPFPDHHAHRSKRATENGAHVVYKRETLAGEPKDFCGLDNVVTEESLVEDESAIFEDVFVTGQRLTQQSDLIVELAVFVDENLWRHFSSKHGGMADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAGYLHNHGNAQMYLDRFCRYQRNLAVRDWDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELGHSVGMRHDEPYCQSKHIMSSSLGPGKVTWSTCSLRDYHQFLQRLDGRGKNCLRVSNMPNKLEISSNVKPGQIYDANLQCELMHGNGYQQVTPRQDSYDGICYMMWCGQSSFGRIITSHPALEGTFCGPSKWCQLGRCVPWTGTNEIQPTVQHVAPVVTTLPSRIDGSWSGWGATICSQCTCNGILGSVGLAIARRTCSAPYPANGGSDCVGSTSRAVLCSRQCGRASKSVDEYISDKCMEQKRLKNDRELTGKGSQLNRFPQRACKVFCDVQQHYGSQRNYRFFGDNLPDGTSCGYDRYCLDGECLALNCNNNALISRDQSCPTDTCPITDQSSSVYRGQWGTWSLWTSCTATCGGGYRKRNRACSITGQCEGNEDETEVCSSESCPSVLRVGNEWSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAFDCPEKNIEVRSCDNGPCNAIGVWGTWGGWSTCSTSCGPGTLVRQRTCNREPCDGSAHERRSCNVATCQNDGIWSLWNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQQFCNEQACASSSANDWGTWSGWSQCSVSCGAGVKRRTRTCRTGNCPGNYKESAICNDRDCENKNAAWGGWGYWSSCSETCGDGVRKRVRKCYGSGNCDGQQYEKQYCNLRVCDFRRKF
Protein: Superoxide dismutase 1 copper chaperone (Q10357)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Copper chaperone for superoxide dismutase 1 (sod1). Binds copper ions and delivers them specifically to sod1. Also has a role in cell protection against copper ion toxicity during conditions of copper excess. The C-terminal region is thought to act specifically in this sequestration role.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15107426}.
Interaction partners:
- Metal homeostasis factor atx1
- Cytochrome c oxidase copper chaperone
- Glutathione-independent glyoxalase DJ-1
- Copper-transporting ATPase ccc2
- Catalase
- Protein sco1
- Copper transport protein ctr5
- Copper transport protein ctr4
- Glutathione peroxidase-like peroxiredoxin gpx1
- Copper amine oxidase 1
Sequence:
MFEVEYLIKDCDDVNKNTLEQEFQDLNIEDWKWDAATGQLIVKGSVSPSKVLRRLENATSKPILIRGASNKESGVSILYEANEDITQIPKVYGLCRFIPTEEKIFLDLIATQLLPNREYTGLVTISGDISRGLKSAGDSLVTLFNANSNEQGKIVLDKEVSGSLPNWIGHCFVLKCVDDSDSATMGIISRSAGLGQNTKQICACTGKSLWTEHAELKSVNEGSSCCSKKDSSPSEKPSCCSQEKKSCCSSKKPSCCSQEKKGCCSTEKTSCCSQEKKSCCTSEKPSCCSNGKSTVCA
Protein: Bicyclo-germacrene synthase (EC 4.2.3.100) (Allo-aromadendrene synthase) (EC 4.2.3.-) (Geraniol synthase) (EC 3.1.7.11) (Limonene synthase) (EC 4.2.3.20) (Terpene synthase 4) (OvTPS4) (Terpinolene synthase) (EC 4.2.3.113) (E2E2N7)
Organism: Origanum vulgare (Wild marjoram)
Function: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is greatly favored while both alloaromadendrene and bicyclo-germacrene are produced in equivalent amounts in the presence of magnesium. Can also convert geranyl diphosphate (GPP) to terpinolene, limonene and geraniol, and this conversion is not affected by the presence of magnesium or manganese.
Interaction partners:
Sequence:
MEIYSPVVPAVKDVKRLDEIRKSAKFHPSIWGDFFLSYNSDNTQISEAEEEEVAKQKEAVRELLAQVPEGSTYKMELIDLIQRLGVNYHFEKEIHDSLNYIHENSQHNDDEVRTTALRFRLLRQQGYRVPCDVFRKFTDGEGNFATALTNDVEGLLELYEASHLATRGEEILDRAMEFSSSHLQALLNQHLVGSVSLSKRVDEALKMPIRKTLTRLGARKFISLYQEDESRNELLLNFAKLDFNMVQKMHQRELSDATRWWKKLEVAKRMPYARDRVVECFFWIVGVYFEPCYATARRILSKAINMASIVDDTYEYATLDELQILTDAIQRWDVNETLEDSPPHVQMCYKALIQAYAEIEDEVVENFGGEELYRVQYAIEHVKQSAVAFFEEAKWIYNNSIPTVEEYMKVAFVTCGYMMLSTTSLVGVGSDRVSKADFDWIVNEPLIVRASCVICRLMDDLVGDEYEEKPSSVLCYMKQYVVSKDEARARLEQQVKDAWKDMNEECIEPRPASMQILTRVLNLGRVIHLLYREGDSYTDPNRSKEWVKMVFVDPI
Protein: Probable DNA-directed RNA polymerase III subunit rpc6 (RNA polymerase III subunit C6) (DNA-directed RNA polymerase III 34 kDa polypeptide) (RNA polymerase III subunit C34) (O94553)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase III subunit rpc5
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit rpc3
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase III subunit rpc1
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerase III subunit rpc8
- DNA-directed RNA polymerase III subunit rpc31
Sequence:
MADQLRTLPKNAKVIYEHCLKQIPNSLSQQDLVEAIGASISVNDLSSALNILLSRRLLDPLRQGNVLVYRAVRLDEAKTVSTMEGDEQIVYSFIKNSGNEGIWRKTLTLRTNLHVSVVDRCLKSLESKNLVKSIKSVKNPTRKIYMLYDLVPSTELTGGPWFTDQELDVEFIENLKKVIYRYVHSKSFPPKKAAMGPDLVWGPEYNGYPTALQIHNWLRSTNITKVDLSLANVISLVDVLIYDGKVEKRSDGASYRAIRVNNENIDAFTESPCGNCPVSDICDANSRVNPITCEYLDKWLN
Protein: Eukaryotic translation initiation factor 3 subunit 7-like protein (Q4Q6Y6)
Organism: Leishmania major
Interaction partners:
- Putative eukaryotic translation initiation factor 3 subunit 8
- Uncharacterized protein
- RRM domain-containing protein
- Putative elongation initiation factor 2 alpha subunit
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit E
- CSN8/PSMD8/EIF3K domain-containing protein
- Eukaryotic translation initiation factor 3 subunit I
- Putative translation initiation factor
- Translation initiation factor-like protein
Sequence:
MSFELPELYINPQFSWGPPEEEMKLDDGAPFELYSKADALEAVDWFTYKREADVSDSDSDDEAVAANKRKAFKQVEDNARLNALRTEREKTVMFNPRNNGPRNAKLAAGKKGGKDNRNNNQRRNRRKVTELPNTYNASAMAVVQHVMKQTDMTKLRMSALPKVIELGLYGTPPIYNTGIEAATCARPLPLDESKYDEDYFMRGLTTEDPELRKIMGETQRYPLVVVTDEILSLLMVCTRSSYPWHIRVLNYNNIWILVKGEDSNIEKQWVSETAGHEVRPSEGADNRAERISSLGEESTKVYDCFARASCAKSFAQVRTNRSPFSRKQPRMYSYRRYIMHDGTPDRYDIVVRCEVDALMPRTNDRVRCFALLEQCVVSEKDSSWRREGLLKNAASFLPIEYAHNGCKIARWTALSLLSDAKLMKIGFVTCEEKMEKGQRVFDHKQHEVLSVQTYSPASLATQFGIDVSNMWAIVDHIMRPFIEGHSICPSILMKPGDKSELIVVEEEDDDDESDEDDSEEDGDDGDDKDDE
Protein: Rho1 guanine nucleotide exchange factor TUS1 (TOR unique function suppressor protein 1) (Q06412)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Guanine nucleotide-exchange factor (GEF) for RHO1 that stimulates the exchange of RHO1 GDP-bound form into GTP-bound form. Required for signaling of cell wall defects to RHO1.
Interaction partners:
- RHO1 GEF localizing protein 1
- GTP-binding protein RHO1
- Protein kinase C-like 1
- RHO1 GDP-GTP exchange protein 1
- RHO1 GDP-GTP exchange protein 2
- GTP-binding protein RHO2
- GTP-binding protein RHO4
- Inorganic pyrophosphatase
- Rho-GTPase-activating protein LRG1
- Cytokinesis protein 2
Sequence:
MYRYNRSSPFERTPEKRVSRQESQRKSIELPKLPPLNTRNSFLDDSDNGTDNISIGWTPISDTQQFQSPVPQAFTFTSKHSARGNGTSSSESTPKSTKYVKERRPPPPPPLLYSTESIRIDSPMVSPSSQSRERSPNKLSFIGNSEERHHMEYISNHSRILKSPFANGFSPNSPKSPRDSSKQQAHFSDESDLRCHEREKALPPIPFTTTLLLSPFDDEDSEFFTKPPPPLSTSRNVSGNSRVSEALESVYSDSDYTFNNSNARQSSFNSLLGAKPLELAPSITAPTQPFSIQSIDEHKLYQCDNVYKLSAIYEWILKVYFEWFNECVFTKIDLFQIVQLLLEFQMPTNFDQDTIDSNVDNIMASFISQKAVRFDIINDEEVAVVVGGLDITGVFTELLPCYSFIDNTYGSTNSLICYSNVCTHGQSSGFRKEIKLSEIINKSVGLWTEYWHLTPDDLAEINPREVQRQSFIFDLIILEERSLNMATAAVEIYGKRFDKSLLPDEPEFKALAFDIFEPLIQLHTEFLLTPIFWKLKTRGKFIDGVGKIYSKWCGEAKNIYLNYAKAMATVHEIIMWEKKNKTKFVTWLKEIDNSVEITRSKMYHDVIFFGGFFKSLQNMPVTLRSILKNTDPSMEDYEYLKIVIKEVEKLNFEVNQVHGLAIDHRKLVRFSKQLVLSTNSSNATSYVNVGGSTNANDDDAIQDKLALGLTYPERKLVLSGTVYKKRDLWLDPTPVYIALLDNCLLITEEISKGETQKYKLIERPIPIDYLSLEKRKIPGTSKQPLRNYSQKEHKSPMHNFSTPINSMRPLLKSSGNHMSTAYGDRKTSNTEISNANPNTDEFSFKIRNTATGESFKFFTESAEVLNQWIDAIMESFKRNAENHDLNAFEFTVLSSEFAYFDKDAPVNLPVAPEGSEIDVALKAYAQKANKDSCSWSKTTRILCCEDVKFEGRIYLFVATTDGIYVKYRDDYGSGFVKILELNDVKRMEANVKLGLLFVLDNRKLCYFNISTVVSRYLAQGNTLDENCIVGTVIRDKVRFFKIADDFGNSKHLFFERKGKIVILTPEFDQLTNQVKYFKFYKEYKLPSSSNNILNNEIEDIAIFRKSFAVCTKKTVILYQDSFEDNGIVLPSFLNDKDMMAHLRHPHLNSLPFKSATDSKKRPSIESLTEEAKKDIATCKAIPVNFFQISQSSFFALVYDEAVVKINCYGEMSDWRKDILLLDFCCTGASFHGNHLILVGDNLIQIYDLKNVEQNLGELVPVQIIKGKKIKLASSERREKTILVLSHPNILNRQLLVACNPVAMADHQ
Protein: tRNA-dihydrouridine(20) synthase [NAD(P)+]-like (EC 1.3.1.91) (Dihydrouridine synthase 2) (tRNA-dihydrouridine synthase 2-like) (Q9D7B1)
Organism: Mus musculus (Mouse)
Function: Dihydrouridine synthase. Catalyzes the NADPH-dependent synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NX74}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9NX74}. Note=Mainly at the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9NX74}.
Interaction partners:
- Lysosomal amino acid transporter 1 homolog
- Bifunctional glutamate/proline--tRNA ligase
- Probable ATP-dependent RNA helicase DDX28
- tRNA
Sequence:
MIVNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMLQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQSRVVFQMGTSDAERALAVARLVENDVAGIDVNMGCPKEYSTKGGMGAALLSDPDKIEKILSTLVKGTHRPVTCKIRILPSLEDTLNLVKRIERTGISAIAVHGRNRDERPQHPVSCEVIRAIAETLSIPVIANGGSHDHIQQHVDIEDFRQATAASSVMVARAAMWNPSIFLKDGLRPLEEVMQKYIRYAVQYDNHYTNTKYCLCQMLREQLESPQGRLLHAAQSSQEICEAFGLGAFYEETIRELDARRADLLAKTPEAVEEPAEDTSGIIKMAIRFDRRAYPPQITPKMCLLEWCRREKLPQPVYETVQRTIDRMFCSVVTVAEQKYQSTLWDKSKKLAEQTAAIVCLRSQGLPEGRLGEESPSLNKRKREAPDQDPGGPRVQEPALPGEICKKPFVTLDSSEENLLEGC
Protein: Fasciclin-like arabinogalactan protein 7 (Q39777)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MEFSMIFMISFSVLILCSSLAYGQVAMSTNPTPSPSPAPAPTPAYTNIKDLLSVAGPYHKFLGYLESTKLIDTFQIQANNTVEGITIFVPKDSAFKALTKPSLSNLTDDQFKSVLLYHALPRYYALADFNDLSEKGPISTLAGGQYTLQFNDESGTVRLDSGWSKTKVTSAVHTSKPVAVYQIDKVLLPEAIFGTDIPPTPAPAPALGIGPSADTPSAAKSEETGSSSKPSFSGSSSPRIMMNSGIWTQLVLAFLGGWLVLFF
Protein: Uncharacterized protein, isoform D (EC 3.4.21.-) (X2JCP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQGLLLYCLLTAPLASIEVLAQDLNQTIDVNKLAKIVQRPGFQTRVVGGDVTTNAQLGGYLIALRYEMNFVCGGTLLHDLIVLTAAHCFLGRVKISDWLAVGGASKLNDRGIQRQVKEVIKSAEFREDDMNMDVAILRLKKPMKGKSLGQLILCKKQLMPGTELRVSGWGLTENSEFGPQKLLRTVTVPVVDKKKCRASYLPTGEWNIARQYGVNNFGNFRLGKS
Protein: O-fucosyltransferase 27 (O-FucT-27) (EC 2.4.1.-) (O-fucosyltransferase family protein) (Q8GZ81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- O-fucosyltransferase 36
- Trimethylguanosine synthase
- O-fucosyltransferase 23
- AT5g42660/MJB21_3
- Probable xyloglucan galactosyltransferase GT11
- At1g61240
- At3g26950
- At4g12700
- Transmembrane protein
- Transmembrane protein
Sequence:
MKGEGKVFLKSRMKWIGLLGLVLSAFSLLVHFLLAGFTDDSISDYSIPVTIFSWRPIFDNPRFARHTPLYRRLWGPTRHVETLLPDANPRGFHSDPPARTNGFVFVRIQGGFHEIRNSIPDVVAVSRLLNATLVIPEIQSTTSSKGISSQFKSFAYLYNEEHFMATIANDVRVVKTLPKNLKWARRKKQIPSFKVSYGSSPYYYLHHVLPVLIKHSVVELVVPHGGCLQAILPSDLEEYQRLRCRVAFHGLQFRKEVQELSTKVLQRLRPLGRPFIAYDPGMTREALAYHGCAELFQDVHTELIQHKRAWMIKRGIVKGKLSVDSAEQRLAGLCPLMPEEVGILLRAYGYSWDTIIYVAGGEVFGGQRTLIPLHGMFENVVDRTSLSTSWELAKMYGREAKHNDIKKMTPPSIEVETKHDSLKSTRQRPQPLPPPPARPKYYNIEGWWGWVAESDNEPESTVIELRTNAHKLLWEAIDYVVSVEADVFISGFDRDGKGHPSFASLVMGHRLYQSASAKTFRPDRKQIAMLLEEIRDHMYEANHTWITSVRKLLKRSILEGLMESSKRSKAFSFLSHPVPECSCITRTHPVSNATNLGVTHRCPQWVDGAVSERLKEYKNAEKEEDLDEEDLSSSGLFFGHKESGGNNNGNNETVNSEANNKEEGQLEDQEELEGSER
Protein: Dimethylnonatriene synthase (EC 1.14.14.59) (Cytochrome P450 82G1) (Protein OVIPOSITION RATE 9) (Trimethyltridecatetraene synthase) (EC 1.14.14.58) (Q9LSF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps). Catalyzes the conversion of the C20 (E,E)-geranyllinalool to C16-homoterpene 4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT) of the C15 (E)-nerolidol to C11-homoterpene (E)-4,8-dimethyl-1,3,7-nonatriene (DMNT); these volatile compounds are produced upon insect herbivore attack and emitted from flowers and vegetative tissues during herbivore feeding. Required during resistance responses to the fungus Alternaria brassicae. Prevents oviposition of the phloem-feeding insect cabbage whitefly (Aleyrodes proletella).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- 
- Ribosomal RNA-processing 7 protein
- GDSL esterase/lipase At1g06990
- Peptidyl-prolyl cis-trans isomerase CYP71
Sequence:
MTFLFSTLQLSLFSLALVIFGYIFLRKQLSRCEVDSSTIPEPLGALPLFGHLHLLRGKKLLCKKLAAMSQKHGPIFSLKLGFYRLVVASDPKTVKDCFTTNDLATATRPNIAFGRYVGYNNASLTLAPYGDYWRELRKIVTVHLFSNHSIEMLGHIRSSEVNTLIKHLYKGNGGTSIVKIDMLFEFLTFNIILRKMVGKRIGFGEVNSDEWRYKEALKHCEYLAVIPMIGDVIPWLGWLDFAKNSQMKRLFKELDSVNTKWLHEHLKKRSRNEKDQERTIMDLLLDILPEDIVISGHVRDVIVKATILALTLTGSDSTSITLTWAVSLLLNNPAALEAAQEEIDNSVGKGRWIEESDIQNLKYLQAIVKETHRLYPPAPLTGIREAREDCFVGGYRVEKGTRLLVNIWKLHRDPKIWPDPKTFKPERFMEDKSQCEKSNFEYIPFGSGRRSCPGVNLGLRVVHFVLARLLQGFELHKVSDEPLDMAEGPGLALPKINPVEVVVMPRLDPKLYSLL
Protein: Splicing factor Cactin (Renal carcinoma antigen NY-REN-24) (Q8WUQ7)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns. Required for the splicing of CDCA5/Sororin, a regulator of sister chromatid cohesion. Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways. Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli.
Subcellular location: Nucleus {ECO:0000269|PubMed:20829348, ECO:0000269|PubMed:26363554, ECO:0000269|PubMed:28062851}. Cytoplasm, cytosol {ECO:0000269|PubMed:26363554}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with NFKBIL1 in the nucleus. {ECO:0000269|PubMed:20829348}.
Interaction partners:
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor SYF2
- Peptidyl-prolyl cis-trans isomerase-like 1
- PRKR-interacting protein 1
- ATP-dependent RNA helicase DHX8
- Crooked neck-like protein 1
- Cell division cycle 5-like protein
- Pre-mRNA-processing-splicing factor 8
- PSME3-interacting protein
Sequence:
MGRDTRSRSRSAGRRGRRRQSQSGSRSRSRSHGRRNRRRREDEGRRRRRRRSRERRSDSEEERWQRSGMRSRSPPRPKWHSRDGSSQSDSGEEQSRGQWARRRRRARSWSPSSSASSSASPGRSQSPRAAAAALSQQQSLQERLRLREERKQQEELMKAFETPEEKRARRLAKKEAKERKKREKMGWGEEYMGYTNTDNPFGDNNLLGTFIWNKALEKKGISHLEEKELKERNKRIQEDNRLELQKVKQLRLEREREKAMREQELEMLQREKEAEHFKTWEEQEDNFHLQQAKLRSKIRIRDGRAKPIDLLAKYISAEDDDLAVEMHEPYTFLNGLTVADMEDLLEDIQVYMELEQGKNADFWRDMTTITEDEISKLRKLEASGKGPGERREGVNASVSSDVQSVFKGKTYNQLQVIFQGIEGKIRAGGPNLDMGYWESLLQQLRAHMARARLRERHQDVLRQKLYKLKQEQGVESEPLFPILKQEPQSPSRSLEPEDAAPTPPGPSSEGGPAEAEVDGATPTEGDGDGDGEGEGEGEAVLMEEDLIQQSLDDYDAGRYSPRLLTAHELPLDAHVLEPDEDLQRLQLSRQQLQVTGDASESAEDIFFRRAKEGMGQDEAQFSVEMPLTGKAYLWADKYRPRKPRFFNRVHTGFEWNKYNQTHYDFDNPPPKIVQGYKFNIFYPDLIDKRSTPEYFLEACADNKDFAILRFHAGPPYEDIAFKIVNREWEYSHRHGFRCQFANGIFQLWFHFKRYRYRR
Protein: COX assembly mitochondrial protein homolog (Cmc1p) (Q7Z7K0)
Organism: Homo sapiens (Human)
Function: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18443040, ECO:0000269|PubMed:23676665}. Note=Colocalizes with MT-CO1.
Interaction partners:
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
Sequence:
MALDPADQHLRHVEKDVLIPKIMREKAKERCSEQVQDFTKCCKNSGVLMVVKCRKENSALKECLTAYYNDPAFYEECKMEYLKEREEFRKTGIPTKKRLQKLPTSM
Protein: Dual specificity protein kinase YAK1 (EC 2.7.12.1) (P14680)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2.
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles between both compartments in response to glucose.
Interaction partners:
- WD repeat-containing protein YPL247C
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Protein TEM1
- Cell cycle protein kinase DBF2
- Cell division control protein 15
- Rho-type GTPase-activating protein 2
- Rho-type GTPase-activating protein 1
- Zinc finger protein MSN2
- cAMP-dependent protein kinase type 1
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MNSSNNNDSSSSNSNMNNSLSPTLVTHSDASMGSGRASPDNSHMGRGIWNPSYVNQGSQRSPQQQHQNHHQQQQQQQQQQQQNSQFCFVNPWNEEKVTNSQQNLVYPPQYDDLNSNESLDAYRRRKSSLVVPPARAPAPNPFQYDSYPAYTSSNTSLAGNSSGQYPSGYQQQQQQVYQQGAIHPSQFGSRFVPSLYDRQDFQRRQSLAATNYSSNFSSLNSNTNQGTNSIPVMSPYRRLSAYPPSTSPPLQPPFKQLRRDEVQGQKLSIPQMQLCNSKNDLQPVLNATPKFRRASLNSKTISPLVSVTKSLITTYSLCSPEFTYQTSKNPKRVLTKPSEGKCNNGFDNINSDYILYVNDVLGVEQNRKYLVLDILGQGTFGQVVKCQNLLTKEILAVKVVKSRTEYLTQSITEAKILELLNQKIDPTNKHHFLRMYDSFVHKNHLCLVFELLSNNLYELLKQNKFHGLSIQLIRTFTTQILDSLCVLKESKLIHCDLKPENILLCAPDKPELKIIDFGSSCEEARTVYTYIQSRFYRAPEIILGIPYSTSIDMWSLGCIVAELFLGIPIFPGASEYNQLTRIIDTLGYPPSWMIDMGKNSGKFMKKLAPEESSSSTQKHRMKTIEEFCREYNIVEKPSKQYFKWRKLPDIIRNYRYPKSIQNSQELIDQEMQNRECLIHFLGGVLNLNPLERWTPQQAMLHPFITKQEFTGEWFPPGSSLPGPSEKHDDAKGQQSEYGSANDSSNNAGHNYVYNPSSATGGADSVDIGAISKRKENTSGDISNNFAVTHSVQEGPTSAFNKLHIVEE
Protein: Dihydroxy-acid dehydratase, mitochondrial (DAD) (EC 4.2.1.9) (Q10318)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P39522}.
Interaction partners:
- Probable ketol-acid reductoisomerase, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
- 2-isopropylmalate synthase
- Threonine dehydratase, mitochondrial
- Probable acetolactate synthase small subunit
- 3-isopropylmalate dehydratase
- Acetolactate synthase, mitochondrial
- Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Homocitrate synthase, mitochondrial
- Aconitate hydratase, mitochondrial
Sequence:
MMFCKLLRCQNGIASKRAALSLKGFKTSSINLVEKKLNKYSETITGPKSQGASQAMLYATGLNEEDMKKPQVGIASCWYEGNPCNMHLLDLGRRVKEGVKKAGLTGFQFNTIGVSDGISMGTTGMRYSLQSREIIADSIETVMQGQWYDANVSIPGCDKNMPGCLIAMGRFNRPSIMVYGGSIRAGHSPCQNNAPIDIVSAFQSYGEFITGKIDEPTRHDIIRHACPGGGACGGMYTANTMASCAEAMGMTLPGSSSYLAGSPEKFAECEAAGSAIKRLLVDDIKPRDIMTRSAFENAMVLTMTLGGSTNSVLHLIAIAKSVGITLTLDDFQAVSNRTPFIADMKPSGKYVMEDLFAIGGIPSVLKYLHAEGLIDGSNITVTGKTLAENLRGFKDLAEGQKIIRPLSNPIKTEGHLRVLRGSLAPEGSVAKITGKEGLNFTGKARVFDAENDFIAALERGEFKKGEKTVVIIRFEGPKGGPGMPEMLKPSSAIMGAGLGKDVALLTDGRFSGGSHGFLIGHVDPEAQVGGPIALVQDGDVIEINAVKNTLDLMVDEKEMARRRSVWKAPPLKYQQGTLLKYARNVSTASKGAVTDSLE