wanglab/gogpt-training-data huggingface dataset:
Protein: Probable acyl-CoA dehydrogenase FadE2 (EC 1.3.99.-) (P96831)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible acyl-CoA dehydrogenase FadE36
- propanoyl-CoA C-acyltransferase
- Probable fatty oxidation protein FadB
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase beta1 subunit
- Triple specificity protein phosphatase PtpB
- Acyl-CoA dehydrogenase FadE7
- Probable enoyl-CoA hydratase EchA3
- Possible enoyl-CoA hydratase EchA21
- Probable enoyl-CoA hydratase EchA8
- Enoyl-CoA hydratase EchA19
Sequence:
MDFAMSAKAIDYRTRLSDFMTEHVFGAEADYDDYRRAAGPADHTAPPIIEELKTKAKDRGLWNLFLSAESGLTNLEYAPLAEMTGWSMEIAPEALNCAAPDTGNMEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAVASSDARNIETTISRDGADYVINGRKWWTSGAADPRCKILIVMGRTNPDAAAHQQQSMVLVPIDTPGVTIVRSTPVFGWQDRHGHCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQHGNKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELSREKSTFAAAVT
Protein: Ectonucleoside triphosphate diphosphohydrolase 7 (NTPDase 7) (EC 3.6.1.15) (Lysosomal apyrase-like protein 1) (Q3TCT4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. Preferentially hydrolyzes nucleoside 5'-triphosphates, with substrate preference for UTP > GTP > CTP. Hydrolyzes nucleoside diphosphates only to a minor extent (By similarity). In contrast to its human ortholog is able to hydrolyze ATP. In the epithelial cells of small intestine controls luminal ATP levels, therefore regulating Th17-cell development.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9NQZ7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MARISFSYLCPASWYFTVPTVSPFLRQRVAFLGLFFIPCVLLLLLIMDLRHWATSLPRDRQYERYLARVGDLEATNTEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKKHRETPLYILCTAGMRLLPERQQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDSDTSVDSAAGRRRTVGILDMGGASLQIAYEVPTSASDLPPKQEEAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGGNFARQRYEDLVLNETLNKNRLLGQKTGLSPDNPFLDPCLPVGLTDMVKRNNQVLHFRGKGDWASCRTLLSPLLARSNTSQASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGHYHGPTFAKAAQDYCGMAWPVLAQRFKNGLFSSHADEHRLKYQCFKSAWMYEVLHEGFHFPYDYPNLQTAQLVYDREVQWTLGAILYKTRFLPLRDLRQGQGGVRPAHGSWLRLSFVYNHYLFFACTLVVLLAIVLYLLRIHRIHRRQTRASAPLDLLWIEQVVPMIGVQVGP
Protein: Plexin-B (Q9V4A7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transmembrane receptor that binds the molecular guidance cue Sema2a, to regulate axon guidance and possibly salivary gland positioning in embryos. Acts as a receptor for Sema2a and seems to transduce signal by suppressing Rac activity and enhancing Rho activity. As transmembrane receptor for Sema2a, involved in peripheral and central nervous system axon guidance. During embryogenesis, plays an important role in correct salivary gland positioning.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Semaphorin-2A
- Semaphorin-2A
- Semaphorin-1A
- MIP07328p
- Semaphorin 5c
- Plexin A, isoform A
- Ras-related protein Rac1
- Ras-like GTP-binding protein Rho1
- E3 ubiquitin-protein ligase CBL
- Epidermal growth factor receptor
Sequence:
MLRKELYCANIIHVLHVLCIIIILGSQHYCVNCIEELPAQALSPLNDIVAQFNLPSIPVQSTASSYGNRSIGNNIESVRDSQSKNYFTHMSFDFMHNVLFAGATNKILKLNENLRVLAEAVTGPLHDSPQCHAGGCPEDIETSLVNNFNKILVVSYAHDGILIACGSIRQGACEIYSLPRFPATPQFFAVPLAANDENASTYAFVGPARYAWKEEDILYVGTTFTNVGDYRHDVPAISSRRLDDLNYAEFSIQQSIINIDVKYRDHFLVDYIYGFNSSEYAYFIIVQKKSHLADEAGYVTRLARICITDPNYDSYTEITVQCTATENNVDYNIVRDAKVTPASHKLAQKMGIKKDDHVLVTVFSPSREISNQPESKSAMCIYSIKDIEDMFIENIHLCFNGTTKDRNLGYISGTINDGRCPIVGSLGNIYNFCSVGLKISGVSPITAHALFHFDNVSVTSVTATSTTDQQHSLAFLGTNMGVIKKVLLSGQSPGEYEEIVVDAGNRILPNTMMSPKKDFLYVLSQRKITKLRIEHCSVYTNCSACLESRDPFCGWCSLEKRCTVRSTCQRDTSASRWLSLGSGQQCIEFESIIPEKIPISELSHLHLIIRTLPEPFNAKYRCVFGNSTPIDAEILENGLGCATPPLDERPLIPTNTDHILVPLSVRSSETNKDFVSRNFAFFDCSHHGNCQECLQSSWGCNWCIFDNKCVHKSLQCRNIENAVSTVGHCPHLKKNRPEILLPVRVPIEIRLEIENLPKPKSAHAGFLCTIHIEAAQMLLPAHVESNKIVVCEKTPYFYEINTHEYQAKVVVTWNFQHYVDTAIVTLYKCDVLGSHREHPDCSLCVTRDPKYKCAWCSNSCVYNETCIADKNSISSGSKSAIENECPLPRIDIIKPLSGPVEGGTLITIEGSNLGIREEDVRGKIFIGSVPCELENYQISVKIECRTGASLYEMSAPIKVANDAGFTESSVQFHFKNVLLTGLYPTIGPRSGGTQLSLIGKFLNIGSTMRAFLDEYECHIDVTQASSSQVSCTTSEATQPEPIRSLHLVIDGANRTLECQISTPSITNTNPTRSNFGSYQLRSLPRQPCSIFNYTQDPRIMQIKPLRSFKSGGRVLTVHGIYLNSIQKPELEVFYDNERVNKTSCVVINSNQMECPSPPVNYKFETFKKTNRKMDTELHLQNSSFQTETRYKNEYDRKKRRADFGDTFRLYTNAGSSANYFVNNNMDVTTFVKVHETQLNLQLSFVMDNVQLVRNLNKYFHDIRSTIVYLADPKYLPFPNDGVKLYKGDSLVIEGELLNLAADEYDVNVTIGTSQCNITSLALNQLLCIPPEQQPLPTDENGVDQSTDLPLVVVKVGRNLRFVIGYLKYDLNKPYVFSHALLVGILTVALLVVVFVIVLIIFRRKSTQAEREYKRIQIQMITLESNVRSECKQAFAELQTDMTDLTADLESTGIPTLDHVNYIMKVFFPGVSDHPILNSPKFREGSPQTNYDAAMVQFEQLIGNKYFLLMFIETLEAQRSSFSIRDRVNVASLIMVVLMNKMEYATEILKSLLLRLIDKSLASKHPQLMLRRTESVVEKMLTNYLAICMYDYLKEYAGSNLFLLFKAIKHQIEKGLVDAITNDARYSLSEERLLHEQVTHSVVILHILQDDLDEKVQCRVNDWDTISQVKLKILDAIFKNTPFSMRPSVNEVDLEWRHGRGGHLTLQDEDLTTKTVNGWKRLNTLAHYGVKESAVMSLIARQNDNYHIPYSKNQNSAPYHNFYFINNSQSHIIINNDIESGLQQPRVYHLVKPNIPDHYMNIKNSVLSGGSPAFQSHVVNNCNDRVNKTIPEVYLTRLLATKGTIQKFVDDFFSIILTVNEELPPAVKWLFDLLDEAARRHDIADTDIVHAWKSNCLPLRFWVNFIKNPDFIFDVNKTYSVDSCLSVIAQTFMDACSTSEHRLGKDSPSNKLLFAKDIPNYRIMVKEFYRDVSRLPQISDQEMSTAMQQLSVRQNEEFDTISALKELYIYITKYKDQIMESLETDINCRKMHLSRKLGNVAATLDGDCTSNC
Protein: Protein-cysteine N-palmitoyltransferase Rasp (EC 2.3.1.-) (Protein central missing) (Protein sightless) (Protein skinny hedgehog) (Q9VZU2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required in hedgehog (hh) expressing cells for production of appropriate signaling activity in embryos and in the imaginal precursors of adult tissues. Acts within the secretory pathway to catalyze N-terminal palmitoylation of Hh; this lipid modification is required for the embryonic and larval patterning activities of the Hh signal. Not required for Wg signaling.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Protein hedgehog
- Beta-alanine-activating enzyme
- Beta-alanyl-bioamine nonribosomal peptide synthetase ebony
Sequence:
MSRLPDRSLLTRCEIFVYFGVYIAYIVVGLYKIYGLRDHIVKEAKFQFPEGWSLYPFSQRRRDDSNDELENFGDFIVSFWPFYLLHVAVQGFIRWKRPRLQCLGFIGVCALALSVNLDWSSMVLLVTLIASYYIVSLLSLKFLVWLLSAGWILCINVMQKNVWWTDRVGYTEYVLVIVTMSWSVLRGCSYSLSKIGAKQEDLTRYSLVQYLGYAMYFPCLTYGPIISYQRFAARREDEVQNWLGFVGGVLRSAIWWLVMQCALHYFYIHYMSRDVRMVEMMDSVFWQHSAGYFMGQFFFLYYVVTYGLGIAFAVQDGIPAPNRPRCIGRIHFYSDMWKYFDEGLYEFLFQNIYAELCGKRSSAAAKFGATALTFAFVFVWHGCYTYVLIWSILNFLCLAAEKVFKTFTAMPEYQRWTQRHLGAVGAQRLYAMLATQLFIPAAFSNVYFIGGQEIGDFLMRGAYLSGVGNYVALCFCSYCFFQCSELLLTKSDGRSKTKTF
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (EC 1.3.8.4) (Q9I296)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Methylcrotonyl-CoA carboxylase, beta-subunit
- Biotin carboxylase
- Regulator of liu genes
- Fatty acid oxidation complex subunit alpha
- Probable 3-hydroxyacyl-CoA dehydrogenase
- 3-methylglutaconyl-CoA hydratase
- Probable enoyl-CoA hydratase/isomerase
- Probable enoyl-CoA hydratase/isomerase
- Probable enoyl-CoA hydratase/isomerase
- Probable enoyl CoA-hydratase/isomerase
Sequence:
MTYPSLNFALGETIDMLRDQVRGFVAAELQPRAAQIDQDNQFPMDMWRKFGEMGLLGITVDEEYGGSALGYLAHAVVMEEISRASASVALSYGAHSNLCVNQIKRNGNAEQKARYLPALVSGEHIGALAMSEPNAGSDVVSMKLRADRVGDRFVLNGSKMWITNGPDAHTYVIYAKTDADKGAHGITAFIVERDWKGFSRGPKLDKLGMRGSNTCELIFQDVEVPEENVLGAVNGGVKVLMSGLDYERVVLSGGPVGIMQACMDVVVPYIHDRRQFGQSIGEFQLVQGKVADMYTALNASRAYLYAVAAACDRGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR
Protein: Protein LIKE COV 1 (Q8VY49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MANRERDRELLIPVADFGDKDDGSSSKPSSSSSASSSHQSGHETLSLFIRGWASKKFMTGCVILLPIAVTFYTTWWFIHFVDGFFSPIYALLGINIFGFGFLTSIAFIFLVGVFMSSWLGASVLNLGEWFIKRMPFVRHIYNASKQISTAISPDQNTQAFKEVAIIRHPRVGEYAFGFITSTVVLQNYPTEEELCCVYVPTNHLYIGDILLVNSNDVIRPNLSVREGIEIVVSGGMSMPQILSTLDKPLASIGNES
Protein: Isocitrate dehydrogenase [NAD] catalytic subunit 5, mitochondrial (EC 1.1.1.41) (IDH-V) (Isocitric dehydrogenase 5) (NAD(+)-specific ICDH 5) (Q945K7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Performs an essential role in the oxidative function of the citric acid cycle.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Peroxisomal isocitrate dehydrogenase
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 1, mitochondrial
- Aconitate hydratase 3, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 2, mitochondrial
- Cytosolic isocitrate dehydrogenase
- Isocitrate dehydrogenase, chloroplastic/mitochondrial
- Aconitate hydratase 1
- Aconitate hydratase 2, mitochondrial
Sequence:
MTMAANLARRLIGNRSTQILGAVNSSSGAASSVARAFCSSTTPITATLFPGDGIGPEIAESVKKVFTTAGVPIEWEEHYVGTEIDPRTQSFLTWESLESVRRNKVGLKGPMATPIGKGHRSLNLTLRKELNLYANVRPCYSLPGYKTRYDDVDLITIRENTEGEYSGLEHQVVRGVVESLKIITRQASLRVAEYAFLYAKTHGRERVSAIHKANIMQKTDGLFLKCCREVAEKYPEITYEEVVIDNCCMMLVKNPALFDVLVMPNLYGDIISDLCAGLVGGLGLTPSCNIGEDGVALAEAVHGSAPDIAGKNLANPTALLLSGVMMLRHLKFNEQAEQIHSAIINTIAEGKYRTADLGGSSTTTEFTKAICDHL
Protein: Cysteine-rich secretory protein 4 (E9PVG4)
Organism: Mus musculus (Mouse)
Interaction partners:
- Phospholipase B1, membrane-associated
Sequence:
MDVDIQPLSRPEDRCPPSPGALCLSISSGHLGSRTPPSVFCTGMAVKFILLLFVAAFVPVVTIRPLKLDRALYNKLITESQTEPQEEIVNTHNAFRRKVSPPARNMLKVSWSSAAAENARILARYCDKSDSDSLERRLPNTFCGENMLMEHYPSSWSKVIEIWFNESKYFKYGEWPSTDDDIETDHYTQMVWASTYLVGCDVAACRRQKAATYLYVCHYCHEGNHQDTLNMPYKEGSPCDDCPNNCEDGLCTNPCIYYDEYNNCDTQVKLYGCSHPAVQPFCKASCLCTTEIK
Protein: Aryl hydrocarbon receptor nuclear translocator (rtARNT) (P79832)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14961334, ECO:0000269|PubMed:8940073}.
Interaction partners:
Sequence:
MDSSIPDIPDDSLGLGAGGAQASSSACCAKRVNKRRAAPDFDDDDDGSKLFRCDDDGGGGDKERFARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGSGNTAADGTYKPSFLTDQELKHLILEAADGFLFVVSCESGRVVYVSDSLTPVLNQSQSDWLGSSLYDQLHPDDGDKLREQLSTAESNNTGRMLDLKTGTVKKEGQQSSVRMCMGARRSFICRMRCGSCPVEPMSMNRLNFLRSRNRNGLGPPKDGEPQYVVVHCTGYIKSWPPTGVNLTDEEADNILGSRYCLVAIGRLQVTSCPSDTDMNSISVPVEFISRHNCQGLFTFVDHRCMATVGYQPQELLGKNILELAHPEDQELLRDSFQQVVKLKGQVLSVMFRFLSKTRDWLWIRTSSFTFQNPFSEEIEYIICTNANVKQLQQQQAELGGGGRDGLYEAGQVTLPQMPVQAVTAAGTDHSKTMDKAEMHPSMYPNPDQAKFLPSTSAPGVPIYPQDNNNYTTANRSNDTYSRSVGMAPQMVQPSHSAGQVLAQMSRQNGAPPSNSSPLQGGAAVSWPGPAAGARPPFNNQQVVPQAGKALSPQFAMGSFVGGSSSSFGAMPTTAAPTPTMGANYPNINPRATLNTNGYDGLGSGQQFPSRAVEAVWPQWQGQQQAQNRAEQHPHTQNNQPDIFPDVLAMLDQPANFNNDDFEIPIYPSFNE
Protein: Coagulation factor XI (LRRGT00086) (Q6TUF8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEIPRIKLTSLLLVPRQRGNLLTRTKLGSLPMCPSVDKCIKQMLEVRTKFRPCTSCPGYWLSDLYYNQSAVRQRWNISLVACWQYGLFGQNRFACILKDSLTETLPMVHMTGAVSGYSFKQCPQQLSACSKNVYVNLDMKGMNYNSSAVKNARECQERCTNDAHCQFFTYATGHFPSVDHRFSHRTACIRDIFPNTVLADLNIDSVLAPDAFVCRRICTHHPTCLFFTFFTQAWPKESQRHLCLLKTSESGFPSTRITKSNALSGFSLQHCRHSIPVFCHPNFYNDTDFLGEELDIVDVKGKESCQKMCSDNVRCQFFTYYPSRGSCSERNMHNQNQAQGVRRSCVCSRRVAMAGDPAHHPGTPVWRLHHWKPVDIDSGSLFLWVSINDIRLGSSSPSTETPKTLRVYGGIVNQSEINEDTTFFRVQEMIIHDQYTSAESGFDIALLKLEPAMNYTDEVQSTLQKAKVPLVSNEECQTRYRKHKITNKVICAGYKEGGKDTCKGDSGGPLSCKHNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKTQSE
Protein: GH13094p (Kairos, isoform A) (Kairos, isoform B) (Q9VWW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Amine oxidase domain-containing protein
Sequence:
MDALRFRGSPFARFTGQSTGPGHPRPPPHPQHPQRPQAAGTHGISAPEPLIVVEESNLPEEQEDSSEPTVSNRGSLDIDSPVNPYLLSPWRDPREARKHSLPSQQVTDGITASQVRRLSERGGEGSGPTPKEAAFLATLSQAPAPTGRRHSVVTISKVPTTLFGRSRRESVAAYPNSNGSSRVLNSRRESNTGPPSTDPIGSIHNLQLDIMDDIYLQSRKARLKLWTSSNEKVCEVQTVDEAGSGQPGRRFTNRRYSECPQPGLASSFRRASELPPSQQQQQQAQSQSSTRASTRRKKSGSGTGLLGSRTDIAGIFSSLTSSAMDMHRPEPEGRDGSSSASSSATATASSPFLSQTFQAAARGRATSATPTPTTHSGSLAVGGGGGVGGGGSGTTGGLLDPNAGRSTRSNSFDVSLLNNAKQLVSDVQDNGSATLSGWFAKRHTPLARKKSVRSKSSAVALSKDVLERLQKKDPLGGDSGKPKLKPRSKQKTWAESTKATVDATILGTAIEGFLRKSSNASMGGSGAGSSGGGASTSAASRGATPKAGKDSGSASGSPAHGARRSRPSASSSAQSQAGRAVRSTLNWFGKADEDDSKDTCDASLCATLKDLFVK
Protein: DUF927 domain-containing protein (SCCmec staphylococcal cassette region, isolate CMFT246) (SCCmec staphylococcal cassette region, isolate CMFT454) (SCCmec staphylococcal cassette region, isolate CMFT503) (Q0WXP6)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
MSYTLFEIGPFALDSFGWKETIPPKKDGDSEKVVRMASPIIVNARFSDPITGVEKLIITNNNGKKDIFESDILTTRNLPSLIKYGYSINEKYIRSLSYALQLMRDRLPLSELYEGVGILETPFGYLISLDKVLKSIQFNQSSPSYPIVDSAYDLTPKGTFDNWFNMYIDEVKGHLLLELAVIFGISALVTSFLKHKHEIEFAGILFSFTGQSSTGKSTAAALAVSVAGNPTKGNETLFRSWNATRNALEGYLSNNYGIPIVFDELSSTTLRDTTGLLYSIAEGQGRQRSNVHGEVKTPKNWGTSVISTSEYSIFNDSAQNDGLRVRTIEINEQFTTNATNADNIKKAVALNYGHVLPLVAKYLINREDEVIQWFYKEVDWFEAKLKDETNNTGIRMFKRYAVITTSAKILGRVLSTDIDIANIRDYFIDYHTHTVSERSLADKAIDVIIQFVAQNRGKFSDEGALKNMFENYGLISLKDDHIEVKIIANVFKQMLNNHQFQDVNNVVNALRDKGFILADRGRQTTKRSVKDNSGKKQSLVFYHLKLDVEFASILGLTKDKSLLQNWTPSNDNKAAKELFKSANEGIGPSGVHEDF
Protein: Interferon gamma (Q1WDD9)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
KGGPLFSEILKNWKEESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNAALRN
Protein: ADP-ribosylhydrolase ARH1 (EC 3.2.2.19) (ADP-ribose-L-arginine cleaving enzyme) ([Protein ADP-ribosylarginine] hydrolase) (ADP-ribosylarginine hydrolase) (Q02589)
Organism: Rattus norvegicus (Rat)
Function: Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins.
Interaction partners:
Sequence:
MGGGLIERYVAAMVLSAAGDTLGYFNGKWEFLRDGEKIHRQLAQMGDLEAIDVAQWRVSDDTIMHLATAEALMEAGSSPDLPQLYSLLAKHYRDCMGDMDGRAPGGACMQNAMQLDPDRADGWRIPFNSHEGGCGAAMRAMCIGLRFPHPSQLDTLIQVSIESGRMTHHHPTGYLGSLASALFTAYAVNGKSPRQWGKGLMEVLPEAKAYVTQSGYFVKENLQHWSYFEKEWEKYLELRGILDGKSAPVFPKPFGVKERDQFYIEVSYSGWGGSSGHDAPMIAYDALLAAGDSWKELAHRAFFHGGDSDSTATIAGCWWGVMHGFKGVNPSNYEKLEYRQRLEEAGRALYSLGSKEDTILGP
Protein: Alpha-copaene synthase (EC 4.2.3.133) (Alpha-humulene synthase) (EC 4.2.3.104) (Alpha-muurolene synthase) (EC 4.2.3.125) (Delta-cadinene synthase) (HaCS) (Terpene synthase 2) (HaTPS2) (Q4U3F6)
Organism: Helianthus annuus (Common sunflower)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Catalyzes the cyclization of farnesyl diphosphate to alpha-copaene, delta-cadinene, alpha-muurolene, beta-caryophyllene and alpha-humulene.
Interaction partners:
Sequence:
MATTEANTMAQANSQTTIEPVRHLANFPPSIWGDQFLSFSLDNSQLEAYSKAMEQPKENVRRMILNPAIDTNEKLGLIYCVYRLGLTYNFSKDIDGQLDELFKQLNLQSYNEADLYTISIHFQVFRHFGYRFSCDVFNKFKDSSSGKFKEDMTRDVRGMISLYESAQLRIRGESILDEAGAFAESKLKTIEKTLDGTLAQQVKHVLERPFNRGHQMVEARKYLFLFEEEISRYDSLLMLAKVHFNYLQLLQKEELRSVSKWWKDLDLPAKTLYVRDRVPELYVWILAFFLEPYYSEVRIITTKIVLLVLVLDDTYDAYATIEESRLLTHAINRWEVSAMLQLPEYMKPLYEILLNEYDGFYKHGRTNVIETSKKAFQDLARSYHQESEWRHAKEVPSFEEYMKIGTTTSAHNVLSKTALIGMGNIVTREALAWYESYPKIVQLSELIGRLEDDVVSVEFERERAPTATSVDAYMKTYGVSENVAVKILKKLVENGWKDLNEACLKPTEVSLDLLAPIIGLTNMTDVAYRHNDGLTFPEKTLKEYITLLFCVPVPM
Protein: Ets variant 6 isoform 2 (A0A0S2Z3N6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSETPAQCSIKQERISYTPPESPVPSYASSTPLHVPVPRALRMEEDSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPRILFSPFFHPGNSIHTQPEVILHQNHEEDNCVQRTPRPSVDNVHHNPPTIELLHRSRSPITTNHRPSPDPEQRPLRSPLDNMIRRLSPAERAQGPRPHQENNHQESYPLSVSPMENNHCPASSESHPKPSSPRQESTRVIQLMPSPIMHPLILNPRHSVDFKQSRLSEDGLHREGKPINLSHREDLAYMNHIMVSVSPPEEHAMPIGRIAGL
Protein: 6-deoxyerythronolide B hydroxylase (6-DEB hydroxylase) (EC 1.14.15.35) (CYPCVIIA1) (Cytochrome P450 107A1) (Cytochrome P450eryF) (Erythromycin A biosynthesis hydroxylase) (Q00441)
Organism: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Function: Catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1732208}.
Interaction partners:
- 6-deoxyerythronolide-B synthase
- 6-deoxyerythronolide-B synthase
- 6-deoxyerythronolide-B synthase
- 6-DEB TDP-mycarosyl glycosyltransferase
- 6-deoxyerythronolide-B synthase
- 6-deoxyerythronolide-B synthase
- Non-ribosomal peptide synthetase
- Non-ribosomal peptide synthetase
- Thioesterase, erythromycin biosynthesis
- EryBIII NDP-4-keto-2,6-dideoxyhexose 3-C-methyltransferase
Sequence:
MTTVPDLESDSFHVDWYRTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAALSDLRLSSDPKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRLRKLVSQEFTVRRVEAMRPRVEQITAELLDEVGDSGVVDIVDRFAHPLPIKVICELLGVDEKYRGEFGRWSSEILVMDPERAEQRGQAAREVVNFILDLVERRRTEPGDDLLSALIRVQDDDDGRLSADELTSIALVLLLAGFEASVSLIGIGTYLLLTHPDQLALVRRDPSALPNAVEEILRYIAPPETTTRFAAEEVEIGGVAIPQYSTVLVANGAANRDPKQFPDPHRFDVTRDTRGHLSFGQGIHFCMGRPLAKLEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVRLDG
Protein: tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ALKBH8 (EC 2.1.1.229) (Alkylated DNA repair protein alkB homolog 8) (Alpha-ketoglutarate-dependent dioxygenase ALKBH8) (S-adenosyl-L-methionine-dependent tRNA methyltransferase ALKBH8) (Q80Y20)
Organism: Mus musculus (Mouse)
Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys) (By similarity). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly). Required for normal survival after DNA damage (By similarity). May inhibit apoptosis and promote cell survival and angiogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96BT7}. Nucleus {ECO:0000250|UniProtKB:Q96BT7}. Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:Q96BT7}.
Interaction partners:
- Nucleic acid dioxygenase ALKBH1
- DNA oxidative demethylase ALKBH2
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
- Multifunctional methyltransferase subunit TRM112-like protein
- Alpha-ketoglutarate-dependent dioxygenase FTO
- RNA demethylase ALKBH5
Sequence:
MNINHKGVLKLTKMEKKFLRKQSKARHVLLKHEGIQAVSYPTQSLVIANGGLGNGVSRKQLLLTLEKCGPVEALLMPPNKPYAFVIFQTIEESKKAYFTLNGKEIIDDLGQKIFLYLNFVEKAQWKNMGLEALPPGLLVVEEIISSEEEKKLLESVNWTEDTGNQNFQRSLKHRRVKHFGYEFHYESNTVDKDKPLPGGLPEVCSSILEKLLKEGYIKHKPDQLTINQYEPGHGIPAHIDTHSAFEDEIISLSLGSAIVMDFKHPEGVTVQVMLPRRSLLVMTGESRYLWTHGITPRKFDTVQASEQFKGGIITSDIGDLTLSKRGMRTSFTFRKVRRMPCNCSYSSVCDRQRKATPPSLTESSKEALELEQKHVHQVYNEIASHFSSTRHSPWPRIVEFLKALPSGSIVADIGCGNGKYLGINKDLYMIGCDRSQNLVDICRERQFQALVCDALAVPVRSGSCDACISIAVIHHFATAERRVEALQELARLLRPGGQALIYVWAMEQEYKNQKSKYLRGKRISQGDKDELNSATSTEEFLVNQTPEGVNEDPALSVNSSSITKEEEYKSRKVPNSELPIHINRTCFHSQDVLVPWHLKRNPGKDKAIEPSGVAGCPDPSPVFHRYYHVFCDGELEASCQAVGDVSILQSYYDQGNWCVVLQKV
Protein: Ribitol-5-phosphate xylosyltransferase 1 (EC 2.4.2.61) (Transmembrane protein 5) (UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase) (Q8VDX6)
Organism: Mus musculus (Mouse)
Function: Acts as a UDP-D-xylose:ribitol-5-phosphate beta1,4-xylosyltransferase, which catalyzes the transfer of UDP-D-xylose to ribitol 5-phosphate (Rbo5P) to form the Xylbeta1-4Rbo5P linkage on O-mannosyl glycan. Participates in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y2B1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y2B1}.
Interaction partners:
- Ribitol 5-phosphate transferase FKRP
- Beta-1,4-glucuronyltransferase 1
- Ribitol-5-phosphate transferase FKTN
- Protein O-mannose kinase
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Sequence:
MRLTRTRLCSLLVALYCLFSIYAAYHVFFGRRRRPLGTTSRNSRKAAAAQAKERRGREQSALESEEWNPWEGDEKNEQRHRVKTNLQILNKSTKEKIEHRVQIWGKAAIGLYLWEHIFEGTLDPADVTAQWREGQSVVGRTHYSFITGPAVVPGYFSIDVDNVVLVLNGREKAKIFHATQWLIYAQNLMKTQKLQHLAVVLLGNEHCENDWIMQFLKRNGGFVDLLFITYDSPWINGADILQWPLGVATYRQFPVVEASWTMLHDERPYICNFLGTAYENSSRQALMNILKQDGNDKLCWVSAREQWQPQETNESLKNYQDALLHSDLTLCPVGVNTECYRIYEACSFGSIPVVEDVMTAGHCGNTTSQHSAPLQLLKAMGAPFIFIKNWKELPAILEKEKTISLQEKIQRRKVLLHWYQHFKTELKWKFTKILESSFFINNKV
Protein: TCF3 fusion partner (INO80 complex subunit F) (Protein FB1) (P0C1Z6)
Organism: Homo sapiens (Human)
Function: Appears to promote apoptosis in a p53/TP53-independent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:18922472}.
Interaction partners:
- INO80 complex subunit E
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- Actin-related protein 8
- Nuclear factor related to kappa-B-binding protein
- Actin-related protein 5
- Chromatin-remodeling ATPase INO80
- RuvB-like 2
- INO80 complex subunit C
- Microspherule protein 1
- Transcriptional repressor protein YY1
Sequence:
MELEQREGTMAAVGFEEFSAPPGSELALPPLFGGHILESELETEVEFVSGGLGGSGLRERDEEEEAARGRRRRQRELNRRKYQALGRRCREIEQVNERVLNRLHQVQRITRRLQQERRFLMRVLDSYGDDYRASQFTIVLEDEGSQGTDAPTPGNAENEPPEKETLSPPRRTPAPPEPGSPAPGEGPSGRKRRRVPRDGRRAGNALTPELAPVQIKVEEDFGFEADEALDSSWVSRGPDKLLPYPTLASPASD