wanglab/gogpt-training-data huggingface dataset:
Protein: DNA (cytosine-5)-methyltransferase DRM2 (EC 2.1.1.37) (OsDRM2) (Protein DOMAINS REARRANGED METHYLASE 2) (Q10SU5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in de novo DNA methylation. Required for CpG and non-CpG methylation. Required for normal establishment and maintenance of RNA-directed DNA methylation (RdDM) mediated by small interfering RNAs (siRNAs). Regulates proper plant development in both vegetative and reproductive stages through DNA methylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:22380881, ECO:0000269|PubMed:23732981}.
Interaction partners:
- Histone-lysine N-methyltransferase CLF
- Os04g0589400 protein
- Os01g0314700 protein
- DNA
- DNA
- Histone H4
- Histone H4
Sequence:
MVDWASDSDNDKFEWDTDGEAETSSAPALRNIDAPGPSTRLPQDANGKANGSGALVAEFMGMGFPKEMILKAIKEIGDTDTEQLLELLLTYQAIGGDASVGNCSASACAPQTLEVDEEEDDTNWDEYDTAGNCDRTPHSDGSGDEDFFQEMSEKDEKMKSLVNMGFPEDEAKMAIDRCGLDAPVAVLVDSIYASQEAGNGYSANLSDYEDTEFSSFGGRKKTRFVDGSKKRKRYGSGPSGNQVPFDGSHEEPMPLPNPMVGFSLPNERLRSVHRNLPDQALGPPFFYYENVALAPKGVWTTISRFLYDIQPEFVDSKYFCAAARKRGYIHNLPIENRSPVLPMPPKTISEAFPNTKRWWPSWDPRRQFNCLQTCMASAKLTERIRCALGRFSDVPTPQVQKYVLDECRKWNLVWVGKNKVAPLEPDEMEFLLGYPRNHTRGVSRTERYRALGNSFQVDTVAYHLSVLRDLFPNGMNVLSLFSGIGGAEVALHRLGIHMKTVISVEKSEVNRTILKSWWDQTQTGTLIEIADVRHLTTERIETFIRRFGGFDLVIGGSPCNNLAGSNRHHRDGLEGEHSALFYDYIRILEHVKATMSAV
Protein: Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GST HB subunit 4) (GST class-mu 1) (GSTM1-1) (GSTM1a-1a) (GSTM1b-1b) (GTH4) (P09488)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase Mu 2
- Cytochrome P450 1A1
- Epoxide hydrolase 1
- Osteopontin
- Cytochrome P450 2E1
- Cytochrome P450 1B1
- Cytochrome P450 1A2
- Cytochrome P450 3A4)
- Cytochrome P450 2C9
- Cytochrome P450 2A6
Sequence:
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
Protein: Brother of rumpel (FI02016p) (Q9VGP3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSNIEEVLGELQRFAWPDYVAFVSMFLLCIGIGIYFGFMNKSVSEDDYMLGGRKMLVIPIAFSLVASFVSGITLLGLPTEVYSYGIQYLYVSCGVIGMGVVMGVFYLPVFHDLNITSTYEYLEVRFDRRLRLYGSVMFAIMNVAYLPIVIYVPALAFNQVTGIGVHTITPIVCIICVFYTSLGGLKAVVWTDVVQAISMLGALCLVAIKGTRDIGGAGVVLERAWSSDRLEAPDLSIDPTVRHTFWCLFFGGIVYWTQTNAVSQNMIQRYLSLPSLGDARKALCIFCVGVLILMALCGYNGLLIYATYQNCDPLTTKLAKARDQLLPLFVMKTLGELPGMTGLFIAGVFSAALSSLSTCLNSMSAVVLEDFVKPYVKKPLSSSAINWIMRLVVVGVGVLCVCLVYVVEHMGTVLQLTMSLEAITNGPLFGIFTIGLFLPWINGNSALVGGVMGVIAMSWVSLNAQWAIASGAITYKTKPLNVEQCDYSFNVTTSLANTTHLGASAEDIFPLYRISYMWYTTFGASITIFVALLGTFVFGKNNPNKVDPVLLTPCIRKFFAFGSEKHMDAFRPDIPLQHKLRNDEVAL
Protein: Faulty attraction, isoform F (Faulty attraction, isoform G) (M9PHP7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWAAKYVLCALACVAFASASPSSERKRKNVMNIPEDPKVSDSLAASLDMSCSSAKILPPEINHGRVSVFDRRRRGKKVFLVAFFVCDDNYDFENGISEMFCSNQKWVDEIPTCIPQLNFEEHDEKVGYDLEDYSDETVPNDYVENSDIDEDDDEEVSEREPPPPPPPPVVDGADSKPEPQIVIEINDDHANEVVESEPALAETETENEVLENETPLKAEVQTDVLNSSNASVKVTNDPYEPTFLDNNCGEDNGGCAHICKRLLYPDENQPINKCDCREGYTLDPNDYASCLDIDECLESNGGCSEICENLPGEYKCSCQEGYYLDESGKSCVDINECANPELSSNCQGACENLPGSYRCVEPLEENPEITEVVENPIEKTNEVPVNVSESQPAGKTCNSGFQLSADGTDCQDINECEVDGPEDLDNNAVCQQKCENTIGSFRCTCVEGYHLLEDQRSCALDSCTDLENPQLNRTRCAHECQDLPEGSYRCVCPKGYELSEDQHSCLVQESPCSTEKGVEKCSPGTCLASEDNTSFSCICPTGYRSEAFSCQDIDECAEDTHLCSHTCQNTPGGYQCQCPEGLNLVEEYTCLAENLCEVNNNGCEQICLTARGGVCACREGFRLSADGKSCEDVDECLVNNGGCQQVCRNLPGTHACACERGYELAKDKLSCLDVDECAGLLSGGCSHECINKAGTFECGCPLGYILNDDGRSCSPALVGCPPGTQRSADGCAPIECNPGYTLGSDDKCVDIDECQKQNGGCSHRCSNTEGSFKCSCPPGYELDSDQKTCQDIDECDQDKTSCITGTCINEIGGFRCEFPKFPVLPEIPTASSLPESPKIELKTPKYPDFTELSNEIPENPKKPAEFDYPEPKFPSLPKWEGLPKLPPLADIPTSKAPVPLRPEVPKSLWVNQLQPRDLCPRFQAPRNGKSHCNRYRHKQKLFYYSRCRISCNSGYILQGPEIKSCDANGIWEGPETKCVAINQPRAQSPGICPALKPAQNGVILPASCTQGPSRFGDVCRLQCNAGFVSTGSLLTACMMLQGWSFGADLNCQPFGNGLLGNQLSPMWNSPKTVTPHQIQNVEQIRPYINCPENVVILLHAGEQKAHVTLQRPQTNVKNGRLVAHPAWAGQLQGHLPAGVHKVDFRVNDPETKLTIKCHTIITVKAATPRESNPFTLFRISDYSRSSLPRPAPFATLSTGSSFSFPAFKALDATPKPVSFTKFQVFPDSESSEHSKLGSSSFFRLEPLFHESSKLISAAPASSENTRVDLGSDTSNYCPPSIEVYLKENQNLRSVVWDEPRFEGKLLKIYKSHFPGSLFKVGDHAIKYEATTTDGKTLSCTFFIYVRSAKPTPAPTEPKISFDSEPETLSDVSQTYVVCPDKEPVRVTAESVSLPVGCTLKNIRPKSRSPKELKRGKLTSLWHQYTNF
Protein: Interleukin-9 receptor (IL-9 receptor) (IL-9R) (CD antigen CD129) (Q01114)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the immune response against parasites by acting as a receptor of IL9.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Secreted.
Interaction partners:
- Interleukin-9
- Cytokine receptor common subunit gamma
- Tyrosine-protein kinase JAK1
- Interleukin-4
- Interleukin-7
- Interleukin-2
- Interleukin-5
- Interleukin-13
- Thymic stromal lymphopoietin
- Tyrosine-protein kinase JAK3
Sequence:
MALGRCIAEGWTLERVAVKQVSWFLIYSWVCSGVCRGVSVPEQGGGGQKAGAFTCLSNSIYRIDCHWSAPELGQESRAWLLFTSNQVTEIKHKCTFWDSMCTLVLPKEEVFLPFDNFTITLHRCIMGQEQVSLVDSQYLPRRHIKLDPPSDLQSNVSSGRCVLTWGINLALEPLITSLSYELAFKRQEEAWEARHKDRIVGVTWLILEAVELNPGSIYEARLRVQMTLESYEDKTEGEYYKSHWSEWSQPVSFPSPQRRQGLLVPRWQWSASILVVVPIFLLLTGFVHLLFKLSPRLKRIFYQNIPSPEAFFHPLYSVYHGDFQSWTGARRAGPQARQNGVSTSSAGSESSIWEAVATLTYSPACPVQFACLKWEATAPGFPGLPGSEHVLPAGCLELEGQPSAYLPQEDWAPLGSARPPPPDSDSGSSDYCMLDCCEECHLSAFPGHTESPELTLAQPVALPVSSRA
Protein: ATP-dependent 6-phosphofructokinase (EC 2.7.1.11) (Q8II80)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Glucose-6-phosphate isomerase
- Enolase
- Fructose-bisphosphate aldolase
- riboflavin kinase
- Pyruvate kinase
- pyruvate kinase
- Phosphoglycerate kinase
- Phosphoglycerate mutase
- Triosephosphate isomerase
- Triosephosphate isomerase
Sequence:
MDIENSKKHLSELQEERRRHKITLPDMFKRKVLIKEENNDTYEKNLETKNDMCYSLNRSDDEKEYLKMKFPNIINNPIIKLYTDPYYTIHMSDKKMNTTDSINTSMDMSSYNYTTNSFMKEMINMYKPHEKLNIGILFTGQQTPGGHNIICGVFDCLKKKNKKNTLYGFMNGFQGMLKYNFMELKNEYISMFRNSGGFDMIKSSDIQIINEDQKKKCFKICRQLNLNGLVIIGDVSGNKSTAILSEYFETVYKITNEKIKSQELKEKNKEETKCKQDGEKNEKEEQQNEQDDEKNKEQQKCKQDDEKNKEQQNEQRDDEQNKEQQKCKQDDEQNKEQQNEQRDDEQINMEDNNNICEILKNYVQEDKIYKPYNIIDNNKTCVSNENKSNNNIPYDNIQSYNMSYDNISTYDFTYDNISDISDEEINKKYPKKNKSFVKTSIVSAPTCVYNEMKNKYIECSLGFDTTIFSYCQYISYLITHIQTYLQGYHFIKVMGNSSSHIALECFLQTKVNIILVTEEIKKNNLTLDQIIQFIVDVIQNRYKKYHKNYGIVIIPDGILKKITQFKKLVTSIIHIKTKFIENKINILTDLQNILSKHLIKEQQEFFKTLPDFFQIQLLEEICSQQFHYARLSTELLLTHLVKKKLEERQINDLEFHTHSYGKEVTCSLPTNFDCAYSYILGFSCVEMLQHKYNGYMCVIKKLKNLLLNVNDIEILGIPLCHIMKIKKKNKNVAQINIVEQVKSAGEKKKKIEEKDNPQEIKENGKINKAEKPTKKNKTEKKDKVTKKDKTSKKDKNNTTDRVKKSSSNIQNDNVNKKDDALTNDLCEPTDSTTNNQNKNALVIRNDPFEEFFIKRTKVNLKDDAYFIKYKKYRYMYLYEDHYRVLTGIQYEHNFCIDYDDKSLKFRNKLNSTLSSNDYITIKPNNIFSKINFTISGLTKEYFNKKEHNEEKSSMTQNNILQNGVILQNNNTYKFNYCKHSSMLSEIEKMLTASAIKFNTILIRHNTRITYINNNFFNKLYTISFIHIPKIKDFYILQDNQFHLKQNYRNVTCPKNVGVVLLSHCTPGTNNILVGLHQRLSINNFKLIGFIKGLKGLLNNDICLINDNNLKTSINIGGFPLLGVHIQYEKKTNDDQILHIHDLIKENNISKIIKSCKNNNITNLVFIGDEKVITLMNILNDIFINKDVNIKIVSIPISLYNSFDKNLIECSIGYHSMVRHISDIISNVQSNCLNINTYYYFIKIHTNISSSLILSVQLQTHCNICYIGESLNNQLTSLHTVIENISLIIIERINRMKYYGVILFSSNLIYYINDFHELCKDVDENIKNVQEIDEIVKNDILPERFQKILKKESVDLLNLLTESMKDKLLRKEKRENEDIDSNFEVMLINEIKKYIQNLMEKSKQNKELYCYKKHMNTISSPINVKNIKVYSDIDYILHFQTLIKVIDREINCFFPTHFDNSLAFSHGLLAGIAVENDLLNYVTSIKHLNLNKQNWSSSLYPGIYFINNKDDKGHFNEYPSVAPVPISMKSSQMATMKHNANTWAYSDSYIFVGPVQYSVNPDNLGYSSYIF
Protein: U3 small nucleolar ribonucleoprotein protein IMP3 (U3 snoRNP protein IMP3) (Interacting with MPP10 protein 3) (P32899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10409734}.
Interaction partners:
- Pre-rRNA-processing protein PNO1
- Nucleolar protein 56
- Ribosome biogenesis protein BMS1
- rRNA biogenesis protein RRP5
- U3 small nucleolar RNA-associated protein 15
- U3 small nucleolar RNA-associated protein 11
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 21
- Protein BFR2
- U3 small nucleolar ribonucleoprotein protein LCP5
Sequence:
MVRKLKHHEQKLLKKVDFLEWKQDQGHRDTQVMRTYHIQNREDYHKYNRICGDIRRLANKLSLLPPTDPFRRKHEQLLLDKLYAMGVLTTKSKISDLENKVTVSAICRRRLPVIMHRLKMAETIQDAVKFIEQGHVRVGPNLINDPAYLVTRNMEDYVTWVDNSKIKKTLLRYRNQIDDFDFS
Protein: Chemokine (C-X-C motif) ligand 18b (Chemokine CXCL-C1c) (A9ZPF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Chemokine
- Chemokine
- C-X-C motif chemokine 11-1
- C-C motif chemokine
- Chemokine
- Chemokine
- Toll-like receptor 5b
- C-C motif chemokine
- C-C motif chemokine
- C-X-C chemokine receptor type 2
Sequence:
MAFTPKALLLLLLAVVYVQQGEVLAKIPDRCQCEESSLVNRARRDTIKEFYITPKRPNCDKVEIILTQKPENKTTASGQLCLNPQKQQGQLLQNCWTRLNINNTDSLKMSVCWQ
Protein: Emei (RE42071p) (Q9VTF5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAVLGAQLVITLVMVSVIQKLSPHYSFAKWILCRTGLYRYLHPTDDELRSRGGVPKEKPPKGGRNKQANGSGGAAGAQFHIPRSIEVELLTSPVLERDVVHLRYFTEYQWLLDFSVYTGIVYVVSELFHFYYPLRHEVNLSMVWCLLVIFFALKLLSSLTVLYFQSEESIGERSMVIVACLVYLLVAMVVLIVDERILETGLEDAYASFNASASKFLTEQGLPSSGPASKIVVKFFLAMGCGLLGSLFTFPGLRMAKMHWDSLKYCRGNRLLQVLLNLSFVLPFILVILWIRPISRDYLTVRVFQGMQQPLLKPHVFETLRLLLVIFVVVVRFALMPIYLQSYLNLAHDKIMDLRKEAGRITNVEFKQKISSIFYYLCVVTLQFAAPLILCLYLTLMYKSLGGFSWSGIFRESVVLQHECAASETEGAGVAVSQGDGDFNIIESAQSLQASFSSLKNVFSTEVYKGFLGFATWWSYFTLFATSSLGIVYQSYFNKT
Protein: Putative dolichyl-P-Man:GDP-ManGlcNAc2-PP-dolichyl beta-1,4-mannosyltransferase (EC 2.4.1.83) (Q4QDV2)
Organism: Leishmania major
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Alpha-1,3/1,6-mannosyltransferase ALG2
- UDP-N-acetylglucosamine transferase subunit ALG13
- mannose-1-phosphate guanylyltransferase
- Cytoplasmic tRNA 2-thiolation protein 2
- Probable methyltransferase BMT2 homolog
Sequence:
MFQYEDLMWLISFPLVCAIMLWFSLDLAVLVRVGGGRRRRANARRAIERLIMSSPVLTTASVVPSPSPVSTPDTDRPSRRRSSSASPEHACMGGLGSSSGNEEGHGVKHRAASAGAAGTPTAGTIPCHQQRVRQVVVPAALRIATRAVVRRAVVLVGGDFARSPRMQYHAASLARSSLFDEVLLVGLDYGNQLSEDLLMSGEPKPERFVSWDDPATPKGMEHAVFDVQARLDSPDPGPGRGCIVSTQYLIAPPSPPEWLQTVFPLIHLHWVVCTLYRIVTLTGLFFFQTMCATATRINEHGQLLVTDLILIQTPPAVPFVLLVKYLVCPLAFVYNMLLYYGVVVPAAWMNPGAMRDVRQQCKLQSLHFTSATECSADGRQRALAILHGLAHASLSGKRRWVFYPAIVVDWHNFGYTILAQNQRPTAAVKVYQLLEMHMCAGHVNVTVSQAMRRALEHAYPWLRCESAITAAAGVQPHCSASAAASASLQAEGAPSVAAVLPSAVTVLYDVAPSFFRPVQRSRCVRDVLERLLRRRHRAVGPSPPLASASPLAKGTGNGAAYALVSKADLEEMGWGIAGPPAWVYADAAAESVAVSALPTPAAAPATMAAVLRRGIMVVGSTSWTEDDDYSMLIQALQRLDHRLRHEVSYRSSNGEGSLSASSGPADLWVLITGKGDTRQRFEDAVRVAKLSSHVVVSTYYAQSYQEYSLLLGAADVGLCLHFSSSGLDLPMKGVDMVGSGLPIMAMQYPAIGELIGGVTRVLATQAMRLRNGAADAQGTPRVSSGYAKAVQPTLHECERGWSFSNDADLEFLLSSFIGLPSTSESVGDGASSLSRSPPTPLSVMKQRAYEARRHAHTWEQNWRRVLLPVLKQVV
Protein: Trans-sialidase (EC 3.2.1.18) (Q57XJ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Trans-sialidase, putative
Sequence:
MEELHQQMRMPISRLLLIFTAVCHCCALTSKAAGKGTTREAFLSGGAWALRKKLSEKDGEVWWWQDGPNWKDKYDKEWERWFKEEKGPWGGSEKRSEWFARMTGGYITLGKTKILSSAIEGSDKVERTVHSFRIPSFVEVDGVLMGIGDARYLTSTDYFFTDTVAKYSADGGKTWKTEVIIENGRVDPTYSRVVDPTVVAKADSVFVLVARYNVTKGYWHNENNAAGIADWEPFMYKGVVTKGADGKTSDVRISWTKTPLKPLYDFTVAGSKGTQFIGGAGNGVVTLNGTILFPVQARNEDNAVVSMVMYSVDDGVSWHFARGETALLTSEASLTEWNGKLLMSARTDTSGVNVEGGFRKVFESNNLGATWEESLGTISRVIGNSPDRTKPSPTANYPGSSGALITVTLGDVPVMLITHPKNTKGAWSRDRLQLWMTDGNRMWLVGQISEGDDNSAYSSLLLARDGLLYCLHEQNIDEVYGLHLVHLVDELEKVNATVRKWKAQDALLAGLCSSSRKKNDPTCSGVPTDGLVGLLAGPVGASVWADVYDCVNASISDGVKVSEGVQLGGKRNSRVLWPVSEQGQDQRYYFANTHFTLLATVRFAGEPKAEAPLMGFSNAEGKTSETLSLTVGGKKWVLTYGSVRKEGPTTSMDWNQTHQIALTLRDGKVDAHVNGELIIKEVSVGASESSAHLHLSHFFIGAPVNDSGEGGNNVIVRNVLLYNRKLDEDELQLLYSNREKIQPVVSAVGIPEGMSAPRLCCLLILMYVLAI
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (Q8I528)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- DNA topoisomerase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Structural maintenance of chromosomes protein 2
- BTB/POZ domain-containing protein, putative
- Structural maintenance of chromosomes protein 6, putative
- NADH-cytochrome b5 reductase, putative
Sequence:
MNVRFFKSLSLFIFFVKGVILVVQAGKGNYANIYKKNNINIFNCMKRKYDKKLSSSVVNTNDKALYESSILKYYYLLDKYKKPNRKKIYGYISNVSRFPLEEERKRKKLEHMNKRNIYPCYNYDAKDIVILEGLEAVRKRPGMYIGNTDVKGLHQILFEIIDNSVDEYNNFECNTIKVVIHKDDSVTIEDNGRGIPCDVHEKTKKSALETVLTVLHSGAKFFDDEMDDEIDNNMNNTGNTNTSEKNNRDNISNNNNNNNNNKRTKKNSKESAQKYKYSSGLHGVGLSVANALSSFMKVKVFRNNKIYSIELEKGKVTKELTITNCPINKRGTQIHYKPDSSIFKSSTKHNSDLIKNRIHQLAYLNEKLTFYFYDERSENKNSIYISKGNKSNEIIKNKKKNTSIDNENEDNKNNTSNYVSNNTLKDDVSNENENMSDNLVNKNIEITDYNNLDFYNYEIIKHEYGLNEYITNITKNKTNLFKDNDKIISISCYHKNIYIDLRMKWLSNQYNENIISFVNNVNTTDGGTHVDALKYAVSRCVNYNIKKNEMIKNFVNIPGEYIREGLTAILSVKMNNPEFEGQTKTKLGSHHLKSILESVIFEKLSEIFDFEPNLLSSIYFKALQAKLSDEEAKAARDLIRSKNNQYSSTILPGKLVDCISDDISRNEIFIVEGDSAAGSAKQARNREIQAILPLKGKILNVEKIKNNKRIFENSELKSLITALGLNVNYDNKNLKNNNILSNNKKGKNSKKKSDLKNSRFESTQNNNNILNKKKDILVDNTLRYGKVIIMTDADVDGEHIRILLLTFLYRFQKEIIENGNVYVACPPLYKITYNKFFDNSIKDIVTKQFNVTTKQSKFIIHTYSDQELNNLLKLLDKDKIASEQKNMQNKIKNKNMSSNGEPLSEYNEQSKTNDIFVNEEGSTDSFIDDNVLFNFSKKYEIQRFKGLGEMMADQLWNTTMDPTVRKLIRVTVNDAIRANDLIFSLMGEDSKLRKNFILENTNSLSE
Protein: mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase (EC 2.1.1.62) (Cap-specific adenosine methyltransferase) (CAPAM) (zCAPAM) (Phosphorylated CTD-interacting factor 1) (A0A0R4IKJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H4Z3}.
Interaction partners:
- N
- Multifunctional methyltransferase subunit TRM112-like protein
- rRNA N
Sequence:
MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEANPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT
Protein: Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) (Q16518)
Organism: Homo sapiens (Human)
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000269|PubMed:19049981}; Lipid-anchor {ECO:0000269|PubMed:19049981}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells. {ECO:0000269|PubMed:19049981, ECO:0000269|PubMed:21493626}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 5
- Retinol dehydrogenase 11
- Retinol dehydrogenase 10
- Retinol dehydrogenase 12
- Diacylglycerol O-acyltransferase 1
- Retinaldehyde-binding protein 1
- Acyl-CoA wax alcohol acyltransferase 2
- Tubby-related protein 1
- Rhodopsin
Sequence:
MSIQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNVYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYLNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKYCGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS
Protein: Pinoresinol reductase 2 (AtPrR2) ((-)-pinoresinol reductase) (EC 1.23.1.3) (Pinoresinol-lariciresinol reductase 2) (AtPLR2) (Q9SVP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reductase involved in lignan biosynthesis. Unlike conventional pinoresinol reductases that can reduce both pinoresinol and lariciresinol, PRR2 shows a strict substrate selectivity for (-)-pinoresinol. No activity with (+)-pinoresinol or lariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
Interaction partners:
- Pinoresinol reductase 1
- Cell division cycle 5-like protein
- Two-component response regulator-like APRR2
- Dirigent protein
Sequence:
MKETNFGEKTRVLVVGGTGSLGRRIVSACLAEGHETYVLQRPEIGVDIEKVQLLLSFKRLGAHLVEGSFSDHQSLVSAVKQVDVVVSAMSGVHFRTHNIPVQLKLVAAIKEAGNVKRFLPSEFGMDPSRMGHAMPPGSETFDQKMEIRNAIKAAGISHTYLVGACFAAYFGGNLSQMGTLFPPKNKVDIYGDGNVKVVFVDEDDMAKYTAKTLNDPRTLNKTVYVRPTDNILTQMELVQIWEKLTEKELEKTYVSGNDFLADIEDKEISHQAGLGHFYHIYYEGCLTDHEVGDDEEATKLYPDVKYKRMDEYLKIFV
Protein: Alpha-actinin (F-actin cross-linking protein) (allergen Der f 24) (L7UZ85)
Organism: Dermatophagoides farinae (American house dust mite)
Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
Interaction partners:
Sequence:
MTQDGYMQQEEEEWEREGLLDPAWEKQQRKTFTAWCNSHLRKAGTQIDNIEEDFRNGLKLMLLLEVISGETLGKPDRGKMRFHKIANVNKALDFIESKGVKLVSIGAEEIVDGNSKMTLGLIWTIILRFAIQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSWKDGLAFCALIHRHRPDLIDYGKLRKDNPMDNFNLAFDVAEKHLNIPRMLDAEDVVYTAKPDERAIMTYVSWYYHAFHGAQQAETAANRICKVLKVNQDNERLMEEYERLASDLLEWIRRTTPWLENRTTDNTLPGTQKKLEEFRSYRRQHKPPRVEQKANLETNFNTLQTKLRLSKRPAYMPSEGKMVSDITGAWKGLESAEKGFEEWLLSEMMRLERLDHLAQKFKHKADIHEEWTQGKEEMLVSHDFRQCKLNEIKALKKKHEAFESDLAAHQDRVEQIAAIAQELNALGYHDIASINARCQRICDQWDRLGTLTTRRRQALDEAEQILEKVDLFHLEFAKRAAPFNNWLDETREDLVDMFIVHSIEEIQQLIDAHESFKNTLGEADKEYKTIVGLAQEVQPMATQYQIPGGLENPYTTLTPEVITTKWRDVKQLVPQRDHTLQTELIRQQCNENLRRQFAEKANVVGPWIERQMDAVTAIGMGMQGTLEDQLQRLHEYDQAVVQYRPHVDDLEKIHQEVQEAMIFENRYTQYTMETLRVGWEQLLTSIHRNINEVENQILTRDSKGITQEQLNEFRTSFNHFDKKRTGRLAPEEFKSCLVSLGYNIRNDDRPEFRRILAIVDPNKTGYVHFDAFLDFMTREYTDTDTAEQMIDSFRILAGDKPYITADELRRELPPDQAEYCIRRMTPYNGQCAVPGALDYRSFSTALYGESDL
Protein: RE44586p (Transmembrane protein 63) (Q6NP91)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- FI03653p
- Myosin-2 essential light chain
- Uncharacterized protein, isoform A
Sequence:
MVMSENSNISYCQAVANRTSFFTTAYNGIPETLILNTIFWVLLILLFTVLRHQAGDFGRLALVNSNGSKKRWTEIFYSRAASVVDPQPSTSTQVSPRPSTTSQGVPDSTPLSPIQPEEGLFGWIRVTLKLRKETILLHTGPDAVHYLSFQQHLMAVMALVTIVSLVIILPVNFLNGPKENPYDVNAFGRTTMANLSPDSPWLWVHTIITILYIPLVVLIMRRASGRNAFKKAATRTIMISNISSSDRNKTVVRNYMQELFPDVTIENVSIAYNISRLYVRNAEFERVHEARLYCEHHRNRDTLMVKPEMCSCKKENAYEYYQREERKLSGDVARLRASTMNEPLDIAFITVSTVQEAQNIVTHFTPGTYRQWHLVFAPSPDDLFWENLNVNKSHWYLKFFCVNAVLFLVLFFLSTPAMVVSLLNSRPWVKETEGKISPLVADFLPTLMLWTLSALMPVIVAISDKWMRHYTRSKQNYSIMTKCFGYLLMMIMILPSLGLTSAQALLEWGFLNQTDRWQCIFLPDRGSFYVNYIITAAFIGTALELLRFPELIVYIWSLLKAKSKAETPYIRKAILIEFPFGTHYAWTTLVFTIAIVYSVACPLIMPFAMIYICLKHFVDRHNLYFAYGPSNMISRKGGKIHSTAVTMTKFSVVILVLVMAMICFFRGDNGMARFLLLIISLAITLTLFTFMSPIKRCAATRRPSIVEIAGPAPIYVPDVLKDNGIRTSSVRPSAAAFGGYGSDSVSEYDSSQYSVNSVEA
Protein: Condensin complex subunit 3 (Chromosome-associated protein G) (Condensin subunit CAP-G) (hCAP-G) (Melanoma antigen NY-MEL-3) (Non-SMC condensin I complex subunit G) (XCAP-G homolog) (Q9BPX3)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 1
- Condensin complex subunit 2
- Condensin-2 complex subunit D3
- Cyclin-dependent kinase 1
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Kinesin-like protein KIF11
- Dual specificity protein kinase TTK
- Abnormal spindle-like microcephaly-associated protein
Sequence:
MGAERRLLSIKEAFRLAQQPHQNQAKLVVALSRTYRTMDDKTVFHEEFIHYLKYVMVVYKREPAVERVIEFAAKFVTSFHQSDMEDDEEEEDGGLLNYLFTFLLKSHEANSNAVRFRVCLLINKLLGSMPENAQIDDDVFDKINKAMLIRLKDKIPNVRIQAVLALSRLQDPKDDECPVVNAYATLIENDSNPEVRRAVLSCIAPSAKTLPKIVGRTKDVKEAVRKLAYQVLAEKVHMRAMSIAQRVMLLQQGLNDRSDAVKQAMQKHLLQGWLRFSEGNILELLHRLDVENSSEVAVSVLNALFSITPLSELVGLCKNNDGRKLIPVETLTPEIALYWCALCEYLKSKGDEGEEFLEQILPEPVVYADYLLSYIQSIPVVNEEHRGDFSYIGNLMTKEFIGQQLILIIKSLDTSEEGGRKKLLAVLQEILILPTIPISLVSFLVERLLHIIIDDNKRTQIVTEIISEIRAPIVTVGVNNDPADVRKKELKMAEIKVKLIEAKEALENCITLQDFNRASELKEEIKALEDARINLLKETEQLEIKEVHIEKNDAETLQKCLILCYELLKQMSISTGLSATMNGIIESLILPGIISIHPVVRNLAVLCLGCCGLQNQDFARKHFVLLLQVLQIDDVTIKISALKAIFDQLMTFGIEPFKTKKIKTLHCEGTEINSDDEQESKEVEETATAKNVLKLLSDFLDSEVSELRTGAAEGLAKLMFSGLLVSSRILSRLILLWYNPVTEEDVQLRHCLGVFFPVFAYASRTNQECFEEAFLPTLQTLANAPASSPLAEIDITNVAELLVDLTRPSGLNPQAKTSQDYQALTVHDNLAMKICNEILTSPCSPEIRVYTKALSSLELSSHLAKDLLVLLNEILEQVKDRTCLRALEKIKIQLEKGNKEFGDQAEAAQDATLTTTTFQNEDEKNKEVYMTPLRGVKATQASKSTQLKTNRGQRKVTVSARTNRRCQTAEADSESDHEVPEPESEMKMRLPRRAKTAALEKSKLNLAQFLNEDLS