wanglab/gogpt-training-data huggingface dataset:
Protein: 40S ribosomal protein S4 (Q386F2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S8
- 40S ribosomal protein S16, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S26
- 60S ribosomal protein L29
- 60S ribosomal protein L19, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L39, putative
- Polyubiquitin, putative
Sequence:
MAKKHLKRLYAPKDWMLSKLTGVFAPRPRAGPHKLRECLSLLIIIRNRLKYALNALEAQMILRQGLVCVDGKPRKDGKYPAGFMDVVEIPKTGDRFRILYDVKGRFALVRVSEAESSIKMMKVVNVYTGTGRIPVAVTHDGHRIRYPDPRTSRGDTLVYDVKEKKVLDLIKIGNGKVVMVTGGANRGRIGEIVSIERHPGAFDIARLKDASGHEFATRATNIFVIGKDMSSVPVTLPKQQGLRINVIQEREEKLIAAETRRTTQAHSKRKTKV
Protein: LHFPL tetraspan subfamily member 2 protein (Lipoma HMGIC fusion partner-like 2 protein) (Q6ZUX7)
Organism: Homo sapiens (Human)
Function: Plays a role in female and male fertility. Involved in distal reproductive tract development.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MCHVIVTCRSMLWTLLSIVVAFAELIAFMSADWLIGKARSRGGVEPAGPGGGSPEPYHPTLGIYARCIRNPGVQHFQRDTLCGPYAESFGEIASGFWQATAIFLAVGIFILCMVALVSVFTMCVQSIMKKSIFNVCGLLQGIAGLFLILGLILYPAGWGCQKAIDYCGHYASAYKPGDCSLGWAFYTAIGGTVLTFICAVFSAQAEIATSSDKVQEEIEEGKNLICLL
Protein: Taste receptor type 2 member 10 (T2R10) (Taste receptor family B member 2) (TRB2) (Q9NYW0)
Organism: Homo sapiens (Human)
Function: Gustducin-coupled strychnine receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MLRVVEGIFIFVVVSESVFGVLGNGFIGLVNCIDCAKNKLSTIGFILTGLAISRIFLIWIIITDGFIQIFSPNIYASGNLIEYISYFWVIGNQSSMWFATSLSIFYFLKIANFSNYIFLWLKSRTNMVLPFMIVFLLISSLLNFAYIAKILNDYKTKNDTVWDLNMYKSEYFIKQILLNLGVIFFFTLSLITCIFLIISLWRHNRQMQSNVTGLRDSNTEAHVKAMKVLISFIILFILYFIGMAIEISCFTVRENKLLLMFGMTTTAIYPWGHSFILILGNSKLKQASLRVLQQLKCCEKRKNLRVT
Protein: RNA-binding E3 ubiquitin-protein ligase MEX3C (EC 2.3.2.27) (RING finger and KH domain-containing protein 2) (RING-type E3 ubiquitin transferase MEX3C) (Q05A36)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms, modulating levels of some mRNAs by promoting their degradation in a way involving ubiquitin ligase activity. May act as suppressor of replication stress and chromosome missegregation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly expressed in the cytoplasm and shuttles between the cytoplasm and the nucleus through the CRM1 export pathway.
Interaction partners:
- E3 ubiquitin/ISG15 ligase TRIM25
- E3 ubiquitin-protein ligase RNF135
Sequence:
MPSGSSAALALALAAAPAPLPQPPPLPPPPPAGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAAAVAAAAAAQCQARRATGLAPEEPGRLATSETAELELEVDEEEGEEAELDGELLEEEELEEAEEEDRPSLLLLSPPAATASQTQPIPGGPLGSVLLPAAGFDAREAAAAGVLYGGDDAQGMMAAMLSHAYGPGGGGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTGNYIELNEENDFHYNGTDVSFEGGTLGSAWLSSNPVPPSRARMMSNYRNDSSSSLGSGSTDSYFGSNRLADFSPTSPFSTGNFWFGDTLPSVGSEDLTVDSPAFDSLPTSAQTIWTPFEPVNPLSGFGSDPSGNMKTQRRGSQPSTPRLSPTFPESIEHPLARRVRSDPPSTGNHVGLPIYIPAFSNGTNSYSSSNGGSTSSSPPESRRKHDCVICFENEVIAALVPCGHNLFCMECANKICEKRTPSCPVCQTAVTQAIQIHS
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Q537V4)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365061}. Chromosome, telomere {ECO:0000256|RuleBase:RU365061}.
Interaction partners:
Sequence:
MERGAQPGVGVRRLRNVAREEPFAAVLGALRGCYAEATPLEAFVRRLQEGGTGEVEVLRGDDAQCYRTFVSQCVVCVPRGARAIPRPICFQQLSSQSEVITRIVQRLCEKKKKNILAYGYSLLDENSCHFRVLPSSCIYSYLSNTVTETIRISGLWEILLSRIGDDVMMYLLEHCALFMLVPPSNCYQVCGQPIYELISRNVGPSPGFVRRRYSRFKHNSLLDYVRKRLVFHRHYLSKSQWWKCRPRRRGRVSSRRKRRSHRIQSLRSGYQPSAKVNFQAGRQISTVTARLEKQSCSSLCLPARAPSLKRKRDGEQVEITAKRVKVMEKEIEEQACSIVPDVNQSSSQRHGTSWHVAPRAVGLIKEHYISERSNSEMSGPSVVRRSHPGKRPVADKSSFPQGVQGNKRIKTGAEKRAESNRRGIEMYINPIHKPNRRGIERRINPTHKPELNSVQTEPMEGASSGDRKQENPPAHLAKQLPNTLSRSTVYFEKKFLLYSRSYQEYFPKSFILSRLQGCQAGGRRLIETIFLSQNPLKEQQNQSLPQQKWRKKRLPKRYWQMREIFQKLVKNHEKCPYLVFLRKNCPVLLSEACLKKTELTLQAALPGEAKVHKHTEHGKESTEGTAPNSFLAPPSVLACGQPERGEQHPAEGSDPLLRELLRQHSSHWQVYGFVRECLERVIPAELWGSSHNKCRFFKNVKAFISMGKYAKLSLQQLMWKMRVNDCVWLRLAKGNHSVPAYEHCYREEILAKFLYWLMDSYVIELLKSFFYITETMFQKNMLFYYRKFIWGKLQNIGIRDHFAKVHLRALSSEEMEVIRQKKYFPIASRLRFIPKMNGLRPVVRLSRVVEGQKLSKESREKKIQRYNTQLKNLFSVLNYERTVNTSIIGSSVFGRDDIYRKWKEFVTKVFESGGEMPHFYFVKGDVSRAFDTIPHKKLVEVISQVLKPESQTVYGIRWYAVIMITPTGKARKLYKRHVSTFEDFIPDMKQFVSKLQERTSLRNAIVVEQCLTFNENSSTLFTFFLQMLHNNILEIGHRYYIQCSGIPQGSILSTLLCSLCYGDMENKLLCGIQKDGVLIRLIDDFLLVTPHLMQARTFLRTIAAGIPEYGFLINAKKTVVNFPVDDIPGCSKFKHLPDCRLISWCGLLLDVQTLEVYCDYSSYAFTSIRSSLSFNSSRIAGKNMKCKLTAVLKLKCHPLLLDLKINSLQTVLINIYKIFLLQAYRFHACVLQLPFNQKVRNNPDFFLRIISDTASCCYFILKAKNPGVSLGSKDASGMFPFEAAEWLCYHAFIVKLSNHKVIYKCLLKPLKVYKMHLFGKIPRDTMELLKTVTEPSLCQDFKTILD
Protein: MyoD family inhibitor (Myogenic repressor I-mf) (Q99750)
Organism: Homo sapiens (Human)
Function: Inhibits the transactivation activity of the Myod family of myogenic factors and represses myogenesis. Acts by associating with Myod family members and retaining them in the cytoplasm by masking their nuclear localization signals. Can also interfere with the DNA-binding activity of Myod family members. Plays an important role in trophoblast and chondrogenic differentiation. Regulates the transcriptional activity of TCF7L1/TCF3 by interacting directly with TCF7L1/TCF3 and preventing it from binding DNA. Binds to the axin complex, resulting in an increase in the level of free beta-catenin. Affects axin regulation of the WNT and JNK signaling pathways (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Myoblast determination protein 1
Sequence:
MYQVSGQRPSGCDAPYGAPSAAPGPAQTLSLLPGLEVVTGSTHPAEAAPEEGSLEEAATPMPQGNGPGIPQGLDSTDLDVPTEAVTCQPQGNPLGCTPLLPNDSGHPSELGGTRRAGNGALGGPKAHRKLQTHPSLASQGSKKSKSSSKSTTSQIPLQAQEDCCVHCILSCLFCEFLTLCNIVLDCATCGSCSSEDSCLCCCCCGSGECADCDLPCDLDCGILDACCESADCLEICMECCGLCFSS
Protein: Endonuclease V (EC 3.1.26.-) (Q8C9A2)
Organism: Mus musculus (Mouse)
Function: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Active against both single-stranded and double-stranded RNAs. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N8Q3}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N8Q3}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8N8Q3}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with PABPC1. {ECO:0000250|UniProtKB:Q8N8Q3}.
Interaction partners:
- Protoporphyrinogen oxidase
- Ferrochelatase, mitochondrial
- Porphobilinogen deaminase
- Inosine triphosphate pyrophosphatase
Sequence:
MAHTAAERPPEETLSLWKGEQARLKARVVDRDTEAWQRDPSFSGLQKVGGVDVSFVKGDSVRACASLVVLSYPELKVVYEDSRMVGLKAPYVSGFLAFREVPFLVELVQRLQEKEPDLMPQVVLVDGNGVLHQRGFGVACHLGVLTELPCIGVAKKLLQVDGLENNALHKEKIVLLQAGGDTFPLIGSSGTVLGMALRSHDHSTKPLYVSVGHRISLEVAVRLTHHCCRFRIPEPIRQADIRSREYIRRTLGQLGVAPAQRKDRSQKEQRPNACPQGGPGALADQGRPPECDGRDSSSDRKAPEPGFQEQKDQQLEGTGHQEDSDLWPPSPAWVQSPP
Protein: cAMP-binding protein 1 (CABP-1) (P19198)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Glycogen phosphorylase 2
Sequence:
MYNPPPPSGSQGNNNYYRQPSSTPGVSNPNPQANQFLPPQPSNTTQTPGGYPPQQQQRPPTGAPQQPGGYPTPPPPGAPGGYPPQQQPAGQYGAPPQQQPAGQYGAPQPAGQYGAPQPAGQYGAPQPAGQYGAPPPPPGGAGISLVKNQQISLTKEDPTLRKLTIGLGWDVNTTPTAPFDLDAVVFMLNAQGRVRTSQDFIFYNNKVSRDNSVSHQGDNLTGQGEGDDEVVLVNLQAVSPDVTRLVFAVTIHLADERRQNFTMVPRAFIRVANQETGRNICRYDLSQEGGPNTALIAGEVYRDPSNPNNWSFVAVGKGMQGALPGLLQIFGCQ
Protein: Protein PSK SIMULATOR 3 (AtPSI3) (P0DO24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes plant growth, especially at the vegetative stage, probably via the regulation of phytosulfokine (PSK) signaling; PSK are peptide phytohormones acting as growth factors. Together with PSI2 and PSI3, required during vegetative growth and reproduction. May also have a function in carbohydrate metabolism.
Subcellular location: Nucleus {ECO:0000269|PubMed:25062973}.
Interaction partners:
Sequence:
MGSFCSKSLGINFGSEYSGSSVADDGREPDFGHSQPNGQTSLIVPGMRQLMVKDVKEQNQLKDVFSFREREAEDNFYDGIPTYTMAPSQKIRSAKSTQTAVSKVTEASKLLGKAGLGRAKDVLDTLGSSMTDLSSGGFTSGVATKGNELGILAFEVANTIVKSSNLIESLSKRNIEHLKGTILYSEGVQNLVSNDFDELLRLVAADKRQELQVFSGEVVRFGNRSKDFQWHNLQRYFDRISKELTPQRQLKEDAVLVVDQLMVLVQYTAELYQELQVLYRLEKDYEQKRREEENSANSSKGDGLAILKTELKAQRKVVKSLKKKSLWSRGFEEVMEKLVDIVHFLLLEIHNIFGGADDQPSKKGAAEYDKRLGPAGLALHYANIIVQIDTLVARASSITSNARDSLYQSLPPGIKLALRSKIKSFNVDKELSVTQIKDEMERTLHWLVPVAGNTTKAHHGFGWVGEWANTGTDFTSKPSGGDILRIETLYHASKEKTEIYILGQIIWLQHLVTKAKSDARGGPRLSSIKSPLDTTNQQLISEPLSVPIVTDEEQKMLQEASKRKRTPCVSKSQDFDSEYSRARKCDPLSKSSEYFRGVRRSKSAAVKRYSSGFPLLDFAIDKEKVLDVIDRVDVPRDYKALLKEGSLSF
Protein: Missing-in-metastasis, isoform N (A0A0B4KEK0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKELSAAHHAQQQQQQQNQQPQTPPTYVNMSELATMAALKQTNQQQKPSTPPLQQQSSIDSTSSQHSNDSTGSHQLLQQQQQHHQSQQNHHSATATRSHSISSTASSLHSHPSIDSTVACGSLVGQHNHSTSTNTNTTSPSSGSSTPQNHYSPLLTNSPTSTAAGTPSGSSLGPGSGLGFVYQVSSPTPPSSEVLKITEQAAAGQDQGPANSVADETDERSRASVLQKASMFEKAAAAAAVSPPAPMQIASGSPASGGGTRRSEAEQQEMDKSFEDSIQALNNLIGELDSFQREIDEGKVKPPSNIISGSTTSSNNNNTTTSSISSSDNNNLPATSNIEPCAISNQTNSSGCGTDISDTTSDELAGDDMDVRRRDRDRDRDLLGASDSELSRCYVSETSSLTGGLTAGGYENPTFAHFAANANREDAVSLASDSVCLGQPRHAYVDTCSDSGSAVVVIYDHQIPNTPDIEFVKQNSEIVVLRTKDPQPHALQLHEMRELQQLPANLAGSPDSSPDSAGGQAPPTATVAPAKQRLSSFRATSEQQLQLLGRGSPQRGKTPSEQAVQSRPQDQHFPQTQQQDIDGSSPPVELARRQLPPKPTSLSIFNGPVPTAGDRPVVPRKSDFKADLDAKIRRQKQKVKQQLQQQQQQQQQEQQETQQQQQAPQEQQHSPQSPQTRNCNVTNQQAANITASASAFATATASTDPYPNPNHRMPNQNQTATSNHTQCKTPTMALSPSSPRGHLPLSSSSLSSLPLPATTSSPSNARPSMLPASDRPPAHPYVCSNAPANPHHANSISNANAHLKPCITPRPASLSGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGPDPRICHESLMDQIKRGATLKRNQKINDRSAPKIH
Protein: Protoheme IX farnesyltransferase 1 (EC 2.5.1.141) (Heme B farnesyltransferase 1) (Heme O synthase 1) (O31652)
Organism: Bacillus subtilis (strain 168)
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Heme A synthase
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Quinol oxidase subunit 3
- Quinol oxidase subunit 1
- Quinol oxidase subunit 2
- Quinol oxidase subunit 4
- Cytochrome c oxidase subunit 4B
- Protoheme IX farnesyltransferase 2
Sequence:
MENTRDSAAISETKYIKASNRVTIYDFIKLAKPGIIISNSIAAFGGFWIAFASAEKTLTGLAFLMTMVTAMLGTAFVMASGTVYNNYFDRHMDAKMARTRSRASVTGKMPPAMILTYGSVLGIAGLAMLYSLNPLTAFLGLAAFIFYAIIYTVWVKRTSVWSTFVGSFPGAAPPLMGYCAVTGDFSMTAVLLYTIMFLWQPPHFWAIGIRRKEEYRAAGVPLLPVVKGNHVTKIKMMQYIAVLVPVTLLFPFSLGTGHISPFYFLAALVLGGIWIKKSIKGFKTDDDVKWAKDMFVYSLIYFCLLFFIMMIDSFMMFLIR
Protein: Proline dehydrogenase (EC 1.5.5.2) (A0A1D8PNH4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Multifunctional fusion protein
- Pyrroline-5-carboxylate reductase
- Arginase
- Citrate synthase
- Put3p
- NAD-specific glutamate dehydrogenase
- Ornithine cyclodeaminase
- Ornithine aminotransferase
Sequence:
MSIRLYSKQSLNTFKKATFIPLTTTATAITTTQFRYFHDTPNKQNVTVNNMMPRVTKPTPTNTFTTSPQLPSTEYLKAFNNKELISFFMIGLATLNKPILQLCIKLFPYVPMSIIKALVYRIYCGGETIDQVKKTGLRLHERGINNMMISLTIEACDGNDNVDPKYIVEETAKSIETILVPHTVAMIEQATDDINDIPPGYVALKPTGFAKDAANVLKNYNTTMIKEFDELVDKAIIVCQKIYDSNKELSQKYPERVSPFVVGVIDAEKHELQEGVYELQRRLYQKFNKLNQPISIVGTLQMYLSDSANLLTKEENLANENNYRLGLKLVRGAYIHSEKNRDIVIHKTKQDTDNNYNSGISYCIDSILNQNQNQNGSTIGHLVVASHNAESMRLASDKVYNPMNESNKNKTNVVLGQLLGMADNVTYDLITNNKIGNVIKYVPWGPPLETKEYLLRRLEENGDAVKNDNGWPLVKASFKMLTKRLFGSG
Protein: Large ribosomal subunit protein uL22m (39S ribosomal protein L22, mitochondrial) (L22mt) (MRP-L22) (Q3SZX5)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069, ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:16510155}.
Interaction partners:
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS9m
Sequence:
MAAVILERLGALWVQNLRGKLALGILPQSHIHTSASLEISRKWEKKNKIVYPPQLPGEPRRPAEIYHCRRQIKYSKDKMWYLAKLIRGMSIDQALAQLEFSDKKGAQIIKEVLLEAQDMAVRDHNVEFRSNLYIAESTSGRGQYLKRIRYHGRGRFGIMEKVFCHYFVKLVEGPPPPPEAPKTAVTHAKEYIQELRNRTIIHAL
Protein: Metal-nicotianamine transporter YSL2 (Protein YELLOW STRIPE LIKE 2) (AtYSL2) (Q6R3K9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the lateral transport of nicotianamine-chelated metals in the vasculature.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15255869}; Multi-pass membrane protein {ECO:0000269|PubMed:15255869}. Note=Found almost exclusively on the lateral plasma membranes.
Interaction partners:
- Oligopeptide transporter 3
- Nicotianamine synthase 1
- Copper transporter 2
- Zinc transporter 2
- Probable nicotianamine synthase 4
- Oligopeptide transporter 4
- Ferric reduction oxidase 5
- Ferric reduction oxidase 4
- Oligopeptide transporter 8
- Protein DETOXIFICATION 43
Sequence:
MENERVEREQSQFQEDEFIDSRKPPPWRKQITVRAIVASLLIGIVYSVICLKLNLTTGLVPNLNISSALLAFVFLKSWTKVLQKAGIATTPFTRQENTIAQTCAVACYSISLAGGFASYLLGLNRRTYEETGVNTEGNNPRGIKEPGVGWMTSFLFVTSFIGLVVLVPLRKVMIIDYKLTYPSGTATAVLINGFHTSKGDKTAKKQIRGFIKSFGLSFFWAFFGWFYSGGEKCGFSQFPTFGLQALDKTFYFDFSMTYVGAGMICSHLVNLSLLFGAILSWGIMWPLIARLKGEWFPATLKDNSMQGLNGYKVFICIALILGDGLYNFVKILFFTGRSFHSRLSKTNSISTLVEVPEDSTKESDNLKRENEVFVRESIPLWMACVGYLFFSLVSIIAIPLMFPQLKWYFVLVAYLLAPSLSFCNAYGAGLTDMNMAYNYGKAALFVMAALAGKNDGVVAGMVACGLIKSIVSVSADLMHDFKTGHLTQTSPRSMLVAQAIGTAIGCVVAPLTFFLFYKAFDVGNQNGEYKAPYAMIYRNMAIIGVQGPSALPKHCLELCYGFFAFAVAANLARDLLPDKPGKWIPLPMAMAVPFLVGGSFAIDMCIGSLVVYVWKKVNRKKADVMVPAVASGLICGDGLWILPSSLLALAKVRPPICMNFTAAH
Protein: UDP-glycosyltransferase 73C25 (EC 2.4.1.-) (A0A2R4LMF9)
Organism: Barbarea vulgaris (Yellow rocket) (Erysimum barbarea)
Function: Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc to the C-28 carboxylic group of oleanolate 3-O-beta-D-glucoside to form oleanolate 3,28-O-beta-D-diglucoside.
Interaction partners:
Sequence:
MASITNHKSDPLHFVLFPFMAQGHMIPMVDIARLLAQRGLTITIVTTPHNASRFKNVLNRAIESGLPINILHVKLPYQEVGLPEGLENIDCFDSMEHMIPFFKGVNMVEESVQKLFEEMSPRPSCIISDFCLPYTSKVAKKFNIPKILFHGMCCLCLLCMHVLRKNPKILENLKSDKEHFVVPYFPDKIELTRPQVPMDTYVPGELKEFMEDLVEADKTSYGVIVNTFQELEPAYVKDYKETRSGKAWSVGPVALCNKARIDKAERGNKSDIDQDECLKWLDSKEERSVLYVCLGSICNLPLAQLKELGLGLEESTRPFIWVIRGWDKNKQLVEWFSESGFEERIKDRGLLIKGWSPQMLILSHQSVGGFLTHCGWNSTLEGITAGLPLLTWPLFADQFCNEKLVVQVLNSGVRAGVEQPMKWGEEEKIGVLVDKEGVKKAVEELMGESDEANERRRRAKELGELAHKAVEEGGSSHSNITFLLQDIMQLAQSNN
Protein: Mitogen-activated protein kinase kinase kinase 3 (X1WGZ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNERQALHSIMKDLVALQMTRRQPTTTYDTAKTKPVIPASSSNRLEDVRIKFEFCGERRILMFGRPVQFEEVQQKVKTFFGQQLDLHYMNNELSIPLRDQDDLDKAIDLLDRSSNMKSIKIMLLTQEQSNASSSSHHTVCKQVRIKTSQSTGDVSTAYQSSEPRGRHHSTSSQNTGRSSPPPGYVPERQQRIARQGSYTSINSEGEFIPETSDQCVLDPWSSAENSVSGSCQSLDSNSDSPSLRKSRTHRIKSYPDNRQDCSDRENHVYDKIVGKGGTYPRRYHVSMHHKDHSEGRRTFPRIRRPQGNLFTLVPSRRSLNGSEESLGSWQLENTQSRLRPQDRAVPHKSPTAPVTWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVHFDPASPETSKEVSALECEIQLLKNLHHERIVQYYGCLRDHNEKTLTIFMEYMPGGSVKDQLKAYGALTENVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSSTGVRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPSHISEHTRDFLRCIFVEAKYRPSAEELLRHPFSQILC
Protein: Mre11 protein (Q8WPP1)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MGSRVTVLHIIMAERASTQSHALPASTQADPSLAASTFKFLVTSDNHLGYQERDSRRGDDSFTTFEECLRAARVEHEVDAILLAGDFFHDNKPSLGCLARTSSLLRSYVLGDKPISFTLLSDPKRNFPTHPVPLANFQDPNINVALPIFMIHGNHDDPVGGTSSIDILSTAGLVNYFGHTSSLDDIVVEPVLLKKGDTYIALYGLGNVRDDRLHRCFRMKKLHFVQPKTEPGKDWFKILLFHQNRGVRSGGNMKCGIYETMLAGHGMDLVIWGNEHEQQMEPSPSEGFDIIQPGSTILTSLSEHECNPKKYGVLEVRGGSYRVTGFPLRSIRPVVRRTVELWRDNPGCRTLDAVEDFLRSVVEQMIEEAEEQVSRIPDDVLKFHPNIKFPIMRLAVDFTDPDSTTFPQPNINRFGQQYMDIVVNPSELLRPIKPKQVPRVASSASATGGEAPVVPVPRLNTSDIRTKVAEVFNANARDACSLLSESEVSAAVYAFAEKGERDAIDERICELLSKCQKSVWVSMRRGESESILKPESIYEEVVRHKKEANKRYEELSRAAEEALQRSTQGNELTERLRADTELAASMDSGNFSRVGGELADGAALGLLSATAPRRAGGSGATNNGEGANDALSQVGFTFPDFSNSLSPPDASGGAAARGKRSRDELNVFDVATERDTNEVNSHPNVSTVKGGGKAVKSETSAPKPARGRKPKRPVDGGVNGLPLFPSLELTREPVPDENFLLPPVVGGGVKGASTSSSGMPDNY
Protein: Uncharacterized protein YML108W (Q03759)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- 5-oxoprolinase
- Uncharacterized membrane protein YLR326W
Sequence:
MSKSNTYRMLVLLEDDTKINKEDEKFLKGKPGKMHEFVDELILPFNVDELDELNTWFDKFDAEICIPNEGHIKYEISSDGLIVLMLDKEIEEVVEKVKKFVEENN
Protein: RNA polymerase III subunit G (D6RIT0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYM
Protein: Cullin-2 (CUL-2) (Q17390)
Organism: Caenorhabditis elegans
Function: Core component of multiple cullin-RING-based CBC (Cul2-ElonginB-ElonginC) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the CBC complex depends on the variable substrate recognition component (By similarity). May function in ubiquitin-mediated degradation of CKIs to target cki-1 for degradation. CBC(zif-1) may ensure germline precursor cell asymmetry by targeting germline proteins for destruction if expressed in non-germline cells. As part of the CBC(fem-1) complex directs ubiquitination of tra-1. As part of the CBC(lrr-1) complex, required for the ubiquitination and dissasembly of the CMG helicase complex from chromatin at the end of DNA replication. Positive cell-cycle regulator that is required at two distinct points in the cell cycle; the G1-to-S-phase transition and mitosis. Also required for proper cytoskeletal movement and mitotic chromosome condensation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10587644}. Nucleus {ECO:0000269|PubMed:10587644}. Note=Nuclear in oocytes.
Interaction partners:
- RNA polymerase II transcription factor SIII p18 subunit
- RING-box protein 1
- Elongin-C
- Elongin-C
- Leucine-Rich Repeat protein
- RING-box protein 2
- Ubiquitin-like protein NEDD8
- von Hippel-Lindau tumor suppressor homolog
- Sex-determining protein fem-1
- Early embryogenesis protein zyg-11
Sequence:
MASSTKVSLRRPPRPQVMYSLKPKVVEFDKVWVQLRPSIIDIINLRPITNVQWHHKFSDVYDICVSIPTPLSERLYNEVKACIQEHVRQKRQDIVDVDPDLLLQEYHKMWRVFHEGAIFIHRLFGYLNKQFVKQKRCTDLDNFAQYAAFLQIPDVKEIGCLALEIWKEDLVKTILPQLVKLLLIAIDNDRKGNFPHIANEVSGVINSFVKMEETDFDVVPAEGARYKARESTTAFYQESFEKPLLTDTEQYYSALAQKMLTDLSCSEYMEQVIVLLEQEEMRAKKYLHESSVEKVITLCQKVMIKAHKDKLHAVCHDLITNEENKDLRNMYRLLKPIQAGLSVMVKEFEEYVKKKGLEAVSRLTGENVPQQFVENVLRVYNKFNDMKTAVFMDDGEFSSGLDKALQGVVNSKEPGQSVPKASERLARYTDGLLKKSTKGLSETDLEAKLDSAIVIFRYIEDKDIFQKFYSKMLANRLIASTSISMDAEELMINKLKQACGYEFTSKLSRMFTDIGLSQELSNNFDKHIADIKTVQPDVKFVPTQTMILQAGSWPLNAPQLSTNSNNQTAQDVANFHLPRILQPVIQEFEKFYTGKHNGRKLTWLFNMSQGDVRLTYLDKQYVAQMYVYQMAALLCFERRDAILVKDIGEEIGVSGDYLLKTIRTILDVTLLTCDDQNLTADSLVRLNMSMTSKRMKFRLQAPQVNKAVEKEQEAVANTVSQDRKYYMECAIVRIMKTRKVLKHNALVTEIMDQTKGRFSPDVPFIKKSIEDLIEKMYIQRTDQNDEYQYLA
Protein: Allatotropin (AT) (P21786)
Organism: Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Function: Neuropeptide stimulator of juvenile hormone synthesis. Cardioregulatory neurohormone that increases heart beat rate in the adult but not in the larva. Inhibits active ion transport in the midgut of feeding fourth instar and day 2 fifth instar larva, but not in the midgut of pharate or wandering fifth instar larva.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNLTMQLAVIVAVCLCLAEGAPDVRLTRTKQQRPTRGFKNVEMMTARGFGKRDRPHPRAERDVDHQAPSARPNRGTPTFKSPTVGIARDFGKRASQYGNEEEIRVTRGTFKPNSNILIARGYGKRTQLPQIDGVYGLDNFWEMLETSPEREVQEVDEKTLESIPLDWFVNEMLNNPDFARSVVRKFIDLNQDGMLSSEELLRNF
Protein: Cytochrome c oxidase subunit 12, mitochondrial (Cytochrome c oxidase polypeptide VIb) (Q01519)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:30598554}; Intermembrane side {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}. Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1 machinery.
Interaction partners:
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Respiratory supercomplex factor 1, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome c oxidase subunit 2
Sequence:
MADQENSPLHTVGFDARFPQQNQTKHCWQSYVDYHKCVNMKGEDFAPCKVFWKTYNALCPLDWIEKWDDQREKGIFAGDINSD
Protein: Nitrogen regulatory PII-like protein (D8ITX3)
Organism: Herbaspirillum seropedicae (strain SmR1)
Interaction partners:
- Ammonium transporter
- Ammonium transporter transmembrane protein
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Sensory histidine kinase/phosphatase NtrB)
- Glutamine synthetase
- Membrane protein
- Acetylglutamate kinase
- Nitrogenase iron protein
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- Amino-acid acetyltransferase
Sequence:
MKLITAIIKPFKLDEVREALSAIGVQGITVTEVKGFGRQKGHTELYRGAEYVVDFLPKTKIEAAVDDAIVERALEAIETAARTGKIGDGKIFVQDLLDVIRIRTGETGKDAL