wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoside-triphosphatase ntp-1 (EC 3.6.1.15) (Q18411)
Organism: Caenorhabditis elegans
Function: Seems to be able to hydrolyze CTP, ATP and UTP.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Origin recognition complex subunit 6
- JmjC domain-containing protein
- SHSP domain-containing protein
- Sperm-Specific family, class Q
- Clip domain-containing protein
- Uncharacterized protein
- Protein kinase domain-containing protein
- PHD-type domain-containing protein
- UDP-glucuronosyltransferase
- Bifunctional purine biosynthesis protein ATIC
Sequence:
MRWRYTIRDQSPFEESSNCHRLTSSETANTFRWPMRTYNVYGFLLTCTCLLLILTIIPMSGGSSERVQRSVRSVVETKNNIKYGVICDAGSSGTRLFVYTLKPLSGGLTNIDTLIHESEPVVKKVTPGLSSFGDKPEQVVEYLTPLLRFAEEHIPYEQLGETDLLIFATAGMRLLPEAQKDAIIKNLQNGLKSVTALRVSDSNIRIIDGAWEGIYSWIAVNYILGRFDKENDSKVGMIDMGGASVQIAFEIANEKESYNGGNVYEINLGSIETNEDYKYKIYSTTFLGYGANEGLKKYENSLVKSGNSNDSCSPRGLNRLIGEFTVNGTGEWDVCLAQVSSLIGDKAQPSCPNPTCFLRNVIAPSVNLSTVQLYGFSEYWYTTSNFGSGGEYHYQKFTDEVRKYCQKDWNDIQDGFKRNEFPNADIERLGTNCFKAAWVTSVLHDGFNVDKTKHLFQSVLKIAGEEMQWALGAMLYHSKDLKFNLLEQLEVAQSTQQISNFFSFFVILIIVLAVALYRQLQSESTYKKYNFLRTDSKPDFLNV
Protein: Acetylene hydratase (Ahy) (EC 4.2.1.112) (Q71EW5)
Organism: Syntrophotalea acetylenica (Pelobacter acetylenicus)
Function: Catalyzes the hydration of acetylene to form acetaldehyde. Ethylene cannot act as a substrate.
Interaction partners:
- Nitrogenase molybdenum-iron protein beta chain
- Nitrogenase protein alpha chain
- Elongation factor Tu
- 4Fe-4S ferredoxin
Sequence:
MASKKHVVCQSCDINCVVEAEVKADGKIQTKSISEPHPTTPPNSICMKSVNADTIRTHKDRVLYPLKNVGSKRGEQRWERISWDQALDEIAEKLKKIIAKYGPESLGVSQTEINQQSEYGTLRRFMNLLGSPNWTSAMYMCIGNTAGVHRVTHGSYSFASFADSNCLLFIGKNLSNHNWVSQFNDLKAALKRGCKLIVLDPRRTKVAEMADIWLPLRYGTDAALFLGMINVIINEQLYDKEFVENWCVGFEELKERVQEYPLDKVAEITGCDAGEIRKAAVMFATESPASIPWAVSTDMQKNSCSAIRAQCILRAIVGSFVNGAEILGAPHSDLVPISKIQMHEALPEEKKKLQLGTETYPFLTYTGMSALEEPSERVYGVKYFHNMGAFMANPTALFTAMATEKPYPVKAFFALASNALMGYANQQNALKGLMNQDLVVCYDQFMTPTAQLADYVLPGDHWLERPVVQPNWEGIPFGNTSQQVVEPAGEAKDEYYFIRELAVRMGLEEHFPWKDRLELINYRISPTGMEWEEYQKQYTYMSKLPDYFGPEGVGVATPSGKVELYSSVFEKLGYDPLPYYHEPLQTEISDPELAKEYPLILFAGLREDSNFQSCYHQPGILRDAEPDPVALLHPKTAQSLGLPSGEWIWVETTHGRLKLLLKHDGAQPEGTIRIPHGRWCPEQEGGPETGFSGAMLHNDAMVLSDDDWNLDPEQGLPNLRGGILAKAYKC
Protein: E3 ubiquitin ligase complex SCF subunit sconC (Sulfur controller C) (Sulfur metabolite repression control protein C) (Q4WTT8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
Interaction partners:
- Probable E3 ubiquitin ligase complex SCF subunit sconB
- SCF ubiquitin ligase complex subunit CulA, putative
- JmjC domain-containing histone demethylation protein 1
- Ubiquitin ligase subunit HrtA, putative
- Probable E3 ubiquitin ligase complex SCF subunit sconB
- Ubiquitin ligase complex F-box protein GRR1, putative
- Probable E3 ubiquitin ligase complex SCF subunit sconB
- Leucine Rich Repeat domain protein
- Protein phosphatase PP2A regulatory subunit B
- Protein kinase, putative
Sequence:
MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE
Protein: Membrane protein (A0A0H2UQD6)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKKRSNIAPIAIFFATMLVIHFLSSLIFNLFPFPIKPTIVHIPVIIASIIYGPRVGVTLGFLMGLLSLTVNTITILPTSYLFSPFVPNGNIYSAIIAIVPRILIGLTPYLVYKLMKNKTGLILAGALGSLTNTIFVLGGIFFLFGNVYNGNIQLLLATVISTNSIAELVISAILTLAIVPRLQTLKK
Protein: Cytokine induced apoptosis inhibitor 1 (H3BV90)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA
Protein: Rifin (Q8IEU6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHCSKILLFLLPLNILVTSLSNVHSKNKPYITSRHTATTISRVLSECDIRSSIYDNDEDIKSVKECFDRQTSQRFEEYEERIQEKRQKRKEERDKNIKKIIEKDKMDKSLAEKVEKGCLRCGCALGGVAASVGLFGGLGIYGWKTAALATAIAEGAAKGAVAAEAARIAEGIKAVIKGIETKFGVSTDGLQGFKSFFTANTYNNVKNIARAINNQYEPSSCPITVPVDSKPICTWVRANFFAAKDSPGNFTSTYEVVETAVTSIVSDAEPVATAAAQQATEEAIKASTDAVESAYAACQTAIIASVVAILVIVLVMIIIYLVLRYRRKKKMKKKAQYTKLLNE
Protein: Transcription factor zip-11 (BZIP transcription factor family zip-11) (Q9N5A8)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Involved in modulating innate immune response pathways, acting to promote resistance against infection by Gram-negative bacterium P.aeruginosa strain PA14. May act as part of a feedback regulatory loop with the pmk-1/p38 MAPK pathway. May also function in concert with CCAAT/enhancer-binding protein cebp-2 to mediate immune responses, independently of the pmk-1/p38 MAPK pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:34804026}.
Interaction partners:
- MADF domain-containing protein
- Glycosyl transferase family 11
- Transmembrane protein
- Adenylate kinase isoenzyme 5
- BTB domain-containing protein
- CCAAT/enhancer-binding protein homolog 2
- BZIP domain-containing protein
- Zinc transporter ZIP3
Sequence:
MWPPNAENNHCNYSYHEHAELNPHDHYHHHHYPHSSVHHTECYQTLSCPSDLPVETSYYNSVPPSYQDLGQTDLSPQFWCAEVDCVHERCSTKEIPHEQSKIFEEISKECDHIMNSAGDCEKCQVEHENGAQEAIPINDLVDIVMQTVDNLKKEGSSNDETKLLSRKRQQNKVAAARYRDKQKAKWQDLLDQLEAEEDRNQRLKLQAGHLEKEVAEMRQAFLAKLAKK
Protein: Small ribosomal subunit protein uS2 (37 kDa laminin receptor precursor) (37LRP) (37/67 kDa laminin receptor) (LRP/LR) (40S ribosomal protein SA) (67 kDa laminin receptor) (67LR) (Laminin receptor 1) (LamR) (Laminin-binding protein precursor p40) (LBP/p40) (P38983)
Organism: Rattus norvegicus (Rat)
Function: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:15548204}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:15548204}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocalizes with PPP1R16B in the cell membrane (By similarity). {ECO:0000255|HAMAP-Rule:MF_03016}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS7
- Ubiquitin-like protein FUBI
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS1
Sequence:
MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS
Protein: Extracellular sulfatase Sulf-1 (hSulf-1) (Arylsulfatase) (EC 3.1.6.1) (N-acetylglucosamine-6-sulfatase) (EC 3.1.6.14) [Cleaved into: Extracellular sulfatase Sulf-2 secreted form] (Q8IWU6)
Organism: Homo sapiens (Human)
Function: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8VI60}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q8VI60}. Cell surface {ECO:0000269|PubMed:12368295, ECO:0000269|PubMed:12686563}.; SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted {ECO:0000269|PubMed:12368295}.
Interaction partners:
- Solute carrier organic anion transporter family member 5A1
- Sciellin
- Collagen alpha-1
Sequence:
MKYSCCALVLAVLGTELLGSLCSTVRSPRFRGRIQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFINAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMYPHRPVMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNILQRKRLQTLMSVDDSVERLYNMLVETGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDPEKPGNRFRTNKKAKIWRDTFLVERGKFLRKKEESSKNIQQSNHLPKYERVKELCQQARYQTACEQPGQKWQCIEDTSGKLRIHKCKGPSDLLTVRQSTRNLYARGFHDKDKECSCRESGYRASRSQRKSQRQFLRNQGTPKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEEELQVLQPRNIAKRHDEGHKGPRDLQASSGGNRGRMLADSSNAVGPPTTVRVTHKCFILPNDSIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECSCSKQSYYNKEKGVKKQEKLKSHLHPFKEAAQEVDSKLQLFKENNRRRKKERKEKRRQRKGEECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNTVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKNLDVGNKDGGSYDLHRGQLWDGWEG
Protein: Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5) (Q09M02)
Organism: Mus musculus (Mouse)
Function: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818, ECO:0000269|PubMed:24022482}. Nucleus {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis (By similarity). Mainly cytoplasmic. Slight accumulation in the nucleus is observed (PubMed:17244818). {ECO:0000250|UniProtKB:Q8NDL9, ECO:0000269|PubMed:17244818}.
Interaction partners:
Sequence:
MELRCGGLLFSSRFDSGNLAHVEKVETVSSDGEGVGGVATAPASGSAASPDYEFNVWTRPDCAETEYENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPSRPRWERIRERPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLSQLDQRFSENYSTHSSPLDSIYYHRELLCYSLDGLRVDLLTITSCHGLRDDREPRLEQLFPDLGTPRPFRFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNAKSPTNQQPTLHLPPEAPLSDLEKANNLHNEAHLGQSPDGENPATWPETEPAEEKTDPVWLMPQPIPELEEPAPDTIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPAFPSRYTVELFEQVGRAMAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLRHVRNSRGLTSAGNMGASKKRGARTPPKSNNSLPVSCSENALSRVRSFSTGTSTGGSSSSQQNSPQMKNSPSFPFHGSRTAGLPGLGSSTQKVSHRVLGPVREPRCSDRRRRQQPLNHRSTTSSLAPSPTLASSGPTSSRNMGSCLLPNSLSLSGSSCSFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQARPRLGRSSPPTRRGMRGSSPTSPIPQTRESSELEPGPHSATPGLPQAGPPRPRSAPAFSPISCTLSDSPSRICYSRGLLNQCEVCFVPKSPPLTISPRV
Protein: Large ribosomal subunit protein bL36B (50S ribosomal protein L36 2) (Q2EEQ2)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Large ribosomal subunit protein bL31B
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL29
Sequence:
MKVLNSLRTAKERHPDCQIVKRKGRLYVICKSNPRFKAVQGRKKKR
Protein: Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] (K0BRG7)
Organism: Human betacoronavirus 2c EMC/2012
Subcellular location: Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00034689, ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04099}. Note=Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion. {ECO:0000256|HAMAP-Rule:MF_04099}.
Interaction partners:
Sequence:
MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFQKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH
Protein: Mucoricin (EC 3.2.2.22) (Ricin-like toxin) (rRNA N-glycosidase) (I1C083)
Organism: Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Function: N-glycosylase that inhibits protein synthesis in the host by depurinating ribosomal rRNA, and thus acts as a ribosomal inactivating protein (RIP). Promotes vascular permeability in the host and induces necrosis and apoptosis of host alveolar epithelial cells.
Subcellular location: Secreted {ECO:0000269|PubMed:33462434}.
Interaction partners:
Sequence:
MYFEEGRLFFIKSQFNGRVLDVEDGSTEDDANIIVYTQKYEDCLNQLWRYENGYFINAKSAKVLDIRGGEMQPESQIIQYAQKMVEEAANQRWAIDEDGYIFCEARPDLVLDIQGAEDEDCVPVILYERREGEVSANQRWELVPFEG
Protein: Uncharacterized protein, isoform D (A8DZ24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTICSLSAALSCNIAYRFPIYEMEHLDLAGYLGHTPQSWNTLGTFQDQDAVYLSSSRQMLEPILEETSEDEERARSSLIVSLDRRSTLWSSTESETGSVLRIETIKDIDAVSERDFVCPPKRPRRSHDLNSGQISEDCVQLRRPMPYDPEYHNSFERFLALEACARDSFGSQGQRSSIGSRRGGTFEDFYSDRDSSHSLSRSSSLVQFESLERQLTLQEQHQSMNSLGNSSPSLTCESGASTRARTRDSSPESRKGSAPTLSLLKRYESSDCSHLHQTYYELNNLNFEYKQQQELLSRSLREAELKSDLESSSSSSSSSDSSGHSLLSSCLVPGDAVATERGKQDGTNSRRIPPNSAENLSEDSGYCEPRTLKREKSKSIPKNFEKLCEEEEELLLLEEGAPHSRDFKDEHDLCQTEIEQTADTAALACSPSSINSSPERASSESESASPLPSPTGSASTSSAASFTWLHNSLPDIREPRGPLSVEINNSKPKTNGSVLATTRQNSGSTRSSSSADSCDGISLLGPTHSLNELQVLERRRRPRHIRPSQRNCHSNSSSEELEELDNLFVACHTPPRIRRSCSWNERARKVVGVASAGYLNASYQNLTLLNYTDNWLPAEILQKNHKRSPAEEMSKQSSNTCGNYEHMICKGNFLLDEISKVYDKNVSILTDKPVLDTKLPAPVECDLNEPIECSKVQHVQLNIKPPPRQKRLTQQPPAAMTFNGLVKTFDQDPTNLRTSYTQSLEQCHLDEQETAKPASYPPSAISQRFLPKRRFQSQTSAAKQRSLVSSTPNLAASDDGQPESEYDIYVSSAHASMHQLPQTTTLPKPLGILLPAGSRHSFGKEVSFCPVVSKYCWQEQSSEEPTEDQFHSSEGEQGPPSDDELMDPTLVHNTRENENIAALFEPEPEQAHRLREPAIAQKFTGFHTNALLSASTHAEKNLSCEESANVKNKANLATPDCRDQRTEAKTTLEPEPALSSTVSLKPCAVANSSCREETPSDAINEPASATARPLSLPILSEPPTNRAHRILYSSQQLRRYEPKASPINKMPPANELSPQAAAVARTDEKHPTSRSLFSRFTHGLRFSLRRKKKQQQQEPSQVKESPKELRQSPEESQPVDFVHIPLKPPRSSQCGRLDDTIVSETSSGHVHSWQQQEQLGKTSTLQKVTGKPPLPKMPPRSGILTHAPQETTGETVNCHRTEALPSVEREHCNQLTGQLVAKVQAQRMRDTGLSSQIVVAEETHTVNRLAGHGDATRPTVVTAVPVSVAPVAEVDKMGLIETNLDTHETVISGKTRSLMDITCNPLSMPHKRYIVKRLNVNSVAYDVDELDAEVKPSPGGMASVRRPHKSMEFLLDKENQKNILPPENELQKSHDHNPGALSEHQLRVQASLQRLNIPDWFRHYNKGPEKAADGENACTSATGGGYRPGNFTRKRAQESGRWQGLNSKTTSLSSLGSQRSDRSPLLMSPSAHSHHGGQSSYSCGSTTIHGPAPVQIGMGATRWSTSHLNSTQMSPGASQRGSFTRGAPINSSFISVASGSGLLRNSYRQPYLGWRSTEKLSQRTPHERLANSLLTQRTAPPSTRAGNETRTLHSVSTEIQSSIKEVTSAIVHFVNDQQQSQHPRSRSTSPNSRYTNGY
Protein: Terpene synthase 8 (EC 4.2.3.-) (Discodiene biosynthesis cluster protein tps8) (Q54BE5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase; part of the gene cluster that mediates the biosynthesis of the trisnorsesquiterpene discodiene which has a function during later stages of multicellular development, during the transition from fingers to Mexican hats. The terpene synthase tps8 converts its substrate farnesyl diphosphate (FDP) into the bicyclic sesquiterpene alcohol discoidol. The cytochrome P450 monooxygenase cyp521A1 then catalyzes the oxidative degradation of discoidol to form the trisnorsesquiterpene discodiene.
Interaction partners:
- Squalene synthase
Sequence:
MDYDIKFTWDKNQFLDQEIRIPKYTLPWDFKSSPFDKDFENQEMEYVKQFFQNYENAVNYVKKNEIGKIAALNFPLGEKDEYMVNSKLLDFLFILDDYIYESRNYEEDYVDNLMDRSSKSHDPFGREIWRLFDEYYRVGVKESVDLLIRDFEYWSRSAIKTNKYKSLNSSLSIEDYFNSRHGDFGMTITASSCTSTLYVENEIRESKNFKKFFKYFELCNLMINDCGSFKMEINEILLTNFVKVRAIQLGSIDLALKYCVGLLNKYIIKVDKYSTKLEQQYPNHSHLKKYIYTLKTFTAGHNKGYGHANRYN
Protein: Syntabulin (Zgc:153017) (Q08CJ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPLQTYEVKEKRNMRSRIPRFVLHPLRTKEKELSVSNMPLSEEESKDFDISSQHSKRTISPNSLSSDDTGCPSSQCASPSKTPSGSDNSSLASPGLGERKVKRVRMNVEAEWSAPTQKHKREEQQRTSIMHKGSETDFSSSSSAGSYKTRETQLSNSAGKNLSSRSRGPHIRSLPVFKPAGSPSAPRDAELYAPIRTPPKTPSFTNSSSCSNSSSSRRRTAPVRYHSCGDNHGIKPPNPEQYLTPLQQKEVAIRHLKTKLRDSENTVCDRESEIEELKSQLGRMREDWIEEECHRVEAQLALKEARKEIKQLRQVVETMKNSLMEKDKGIQKYFVDINIQNRKLESLLHSMELAQNGCNLQDEPTLDFICEAPESSTEAKMELELHCGEQAVEEMANSELLINDEMVNRVEILMSTAVDSSQDGSTKIISQPGLSCLEPSVSEKSTKEHVSSIPIGAEDKGIQTDDVIYSTDLQTLLYQLLKLQGGGFPGLLVPSPNQSHDISSAQAPKKSQKEELPEAHEQDVAISTAQIVPSDSGLGFSEPEVGPEFMEEMNSKNKAVVGKNHWSNNFFVDLVAVAAPVLPTVAWLYSQHGLVGGAPVYNIASLIRGCCVMGLHSLRHVSHGPDT
Protein: Germacrene A hydroxylase (EC 1.14.14.95) (Germacrene A oxidase) (HaGAO) (D5JBX0)
Organism: Helianthus annuus (Common sunflower)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid. Could also catalyze the three-step oxidation of non-natural substrate amorphadiene to artemisinic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:D5JBW8}.
Interaction partners:
Sequence:
MEVSLTTSIALATIVFFLYKLLTRPTSSKNRLPEPWRLPIIGHMHHLIGTMPHRGVMDLARKYGSLMHLQLGEVSAIVVSSPKWAKEILTTYDIPFANRPETLTGEIIAYHNTDIVLAPYGEYWRQLRKLCTLELLSVKKVKSFQSLREEECWNLVQEIKASGSGTPFNLSEGIFKVIATVLSRAAFGKGIKDQKQFTEIVKEILRETGGFDVADIFPSKKFLHHLSGKRGRLTSIHNKLDSLINNLVAEHTVSKSSKVNETLLDVLLRLKNSEEFPLTADNVKAIILDMFGAGTDTSSATVEWAISELIRCPRAMEKVQAELRQALNGKERIKEEEIQDLPYLNLVIRETLRLHPPLPLVMPRECRQAMNLAGYDVANKTKLIVNVFAINRDPEYWKDAESFNPERFENSNTTIMGADYEYLPFGAGRRMCPGSALGLANVQLPLANILYYFKWKLPNGASHDQLDMTESFGATVQRKTELMLVPSF
Protein: Disease resistance protein (TIR-NBS-LRR class) family (F4J3L8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDSSFLLETVAAATGFFTLLGTILFMVYRKFKDHRENKENDSSSSTQPSPSPPLSSLSLTRKYDVFPSFRGEDVRKDFLSHIQKEFQRQGITPFVDNNIKRGESIGPELIRAIRGSKIAIILLSKNYASSSWCLDELVEIIKCKEEMGQTVIVIFYKVDPSLVKKLTGDFGKVFRNTCKGKERENIERWREAFKKVATIAGYDSRKWDNESGMIEKIVSDISEMLNHSTPSRDFDDLIGMGDHMEKMKPLLDIDSDEMKTIGIWGPPGVGKTTIARSLYNQHSDKFQLSVFMESIKTAYTIPACSDDYYEKLQLQQRFLSQITNQENVQIPHLGVAQERLNDKKVLVVIDDVNQSVQVDALAKENDWLGPGSRIIITTQDRGILRAHGIEHIYEVDYPNYEEALQIFCMHAFGQKSPYDGFEELAQQVTTLSGRLPLGLKVMGSYFRGMTKQEWTMALPRVRTHLDGKIESILKLSYDALCDVDKSLFLHLACSFHNDDTELVEQQLGKKFSDLRQGLHVLAEKSLIHMDLRLIRMHVLLAQLGREIVRKQSIHEPGQRQFLVDATDIREVLTDDTGSRSVIGIDFDFNTMEKELDISEKAFRGMSNLQFIRIYGDLFSRHGVYYFGGRGHRVSLDYDSKLHFPRGLDYLPGKLSKLEKLWEGIQPLRNLEWLDLTCSRNLKELPDLSTATNLQRLSIERCSSLVKLPSSIGEATNLKKINLRECLSLVELPSSFGNLTNLQELDLRECSSLVELPTSFGNLANVESLEFYECSSLVKLPSTFGNLTNLRVLGLRECSSMVELPSSFGNLTNLQVLNLRKCSTLVELPSSFVNLTNLENLDLRDCSSLLPSSFGNVTYLKRLKFYKC
Protein: Centrin 3 (E5RK82)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGESKF
Protein: Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 (EC 1.14.11.63) (EC 3.4.-.-) (Jumonji domain containing protein 7) (Q9VU77)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:28701701}. Cytoplasm {ECO:0000269|PubMed:28701701}.
Interaction partners:
- 2-oxoglutarate and iron-dependent oxygenase JMJD4 homolog
- HSPB1 associated protein 1
Sequence:
MSEVERALDVLLQEAEELCIGSSVVELDRIPTALEFCREFYSKNQPVVIRKALNWPAIGKWTPKYLIEALGDRSVDVAITPNGYADGLATQNGQEYFVLPLETKMKLSEVVRRLDDPTGAVHYIQKQNSNLSVDLPELAADLRVSDLDFAQQSFNKPPDAVNFWLGDERAVTSMHKDPYENVYCVISGHKDFVLIPPHQLSCVPRGIYPTGVYKTSDSGQFYIEPLRDEEGSDQFTEWVSVDPLSPDLAKYPEYARAKPLKVRVHAGDILYLPNYWFHHVSQSHKCIAVNFWYDLDYDSRYCYYRMLEQMTSARSG
Protein: DH domain-containing protein (O01847)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-related protein ced-10
- Cell division control protein 42 homolog
- Ras-like GTP-binding protein rhoA
- LRRCT domain-containing protein
- Ras-related protein rac-2
- CRAL-TRIO domain-containing protein
- Clc-like protein
- Mss4 protein
- Menorin
- Leukocyte cell-derived chemotaxin-2 homolog
Sequence:
MGSRLSCSCSQAECWTNDESTLRIDAELFELSQDGQKWDKLDGRLANVRVFNAFDDSSPRLLATSSSGQVLLDTLIPMGEKVHKVSDFFVYLKTEGRTIGFNTLSSRDTSLLISQATNTTAFNMFQHSFSVSVSRIATFEGDSIQPCDEQPETSNVSLNPLNMVFNYKGSPVEIDLLECFACSSEAENCVDIAHANNIFRVIVSAHAHLFLIQALNVSSLLLARTTSNLVAINYLARQNDKIQQKLIALLETSESSENASKEDIRQMLLLKNVVVTQRLNSLQQRALPGIELIQHDISPQIDQKLLEKCRLPSLFLYHFNMNSFRIWRKPMETRDMNTMGSSMASTSQYHQIPIQIQNQNPLPSQQIQPQQQQQYHPPDHVTTHNGTTTFHTTNPTKPRLCEGSLAPGCSLAEASEQRKREMAEQKKELAGPSSAEDYFVRKTNGRLGLTIYAHNDDGVIRAEVRGVTSFAPRCAQVGDSVVAVDSELISSVRNASDVEKLLRIGKVIHLRRKTPLTPRAPSQLDATNVNKKTGCAKLAMALQELLVTEKKYVSDLREMNEVFLCMRQVRDIMNAAIRLYKMQTSFVDSIEEAIGDMSRQDISVAQIRDSVMRVCAVFINKCSDFKIYAEYAAGYHLLQHEIKNKKELLSKLEAVNSTREQHCSWESRMIKPVQRIVQYPLLLKNIADALPKDARERVQVEAALQKMQTSAEYVNEMQRLHEDYAQYMETVRKANEPMLAEKSLRLDTRELLVFAHIKWRDAPAEHYVVFVFHSLILLLPSYARKEIKMKWTRVLPINEVDINEMPNDALNLKLYHAAFEGPNGQLSHSNPNTVYNIECCQSQLKQHLIKNIKKARTLFSRESHRPLSGSSQSDGGYVSEVSKEHRNSK