wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor SOX-4 (Q06945)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif. Required for IL17A-producing Vgamma2-positive gamma-delta T-cell maturation and development, via binding to regulator loci of RORC to modulate expression (By similarity). Involved in skeletal myoblast differentiation by promoting gene expression of CALD1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:16631117}.
Interaction partners:
- POU domain, class 5, transcription factor 1
- Histone-lysine N-methyltransferase EZH2
- Catenin beta-1
- Syntenin-1
- Lymphoid enhancer-binding factor 1
- SUMO-conjugating enzyme UBC9
- Trans-acting T-cell-specific transcription factor GATA-3
- Transcription factor 7-like 2
- Transcription factor 7-like 1
- Myc proto-oncogene protein
Sequence:
MVQQTNNAENTEALLAGESSDSGAGLELGIASSPTPGSTASTGGKADDPSWCKTPSGHIKRPMNAFMVWSQIERRKIMEQSPDMHNAEISKRLGKRWKLLKDSDKIPFIREAERLRLKHMADYPDYKYRPRKKVKSGNANSSSSAAASSKPGEKGDKVGGSGGGGHGGGGGGGSSNAGGGGGGASGGGANSKPAQKKSCGSKVAGGAGGGVSKPHAKLILAGGGGGGKAAAAAAASFAAEQAGAAALLPLGAAADHHSLYKARTPSASASASSAASASAALAAPGKHLAEKKVKRVYLFGGLGTSSSPVGGVGAGADPSDPLGLYEEEGAGCSPDAPSLSGRSSAASSPAAGRSPADHRGYASLRAASPAPSSAPSHASSSASSHSSSSSSSGSSSSDDEFEDDLLDLNPSSNFESMSLGSFSSSSALDRDLDFNFEPGSGSHFEFPDYCTPEVSEMISGDWLESSISNLVFTY
Protein: Basal body-orientation factor 1 (Coiled-coil domain-containing protein 176) (A0JMY4)
Organism: Xenopus laevis (African clawed frog)
Function: Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23900544}. Note=Localizes to a polar structure adjacent to the basal body.
Interaction partners:
Sequence:
MPKLKVKAGKGKKGKRKKAGKNEHRLDKESEVERARSNAALWEARLKVTEFSRVEYRDAARSLAQNNEDLTKQQYKLEKDMVEVIGFLKKQDLEKDELIEKLQQNLIAQKKSAQDEREKLVELYSKQIAHLEENYSQKTNEMQIIQSEFKLMREFRRQKVELEKELDEVKESLWRANQDHKETLARMERRFFEEKQRLEKEAEKKIMMLAEKAHSEAIIQLDEARKSVFKENVRLKEAFSYHLKEMKDIKKSKKMQEDAKLHLLQEKETNDLLVQEKVSQVSQKKVQIQELQQNVKALECALERMTMEMEKDAQGKEHQALLQEQAGNVELQKLQKVLHMKEREMNRIKKLARNILEERTEVESFFLEALWQVKQEIATSRNYYRQVAQSAYTSKMIQASLGKDQYPKIRTFHNKEHSTNDVSHDLSEAEKWTHIQAGKVDIGDLTWEQKEKVLRLLFAKMNGFQSRKSPGLKPSPPADVSSIKEKEINTSNLEEKPEESSSTFITQSIPELPAPSLVLPHIQTGRCQVTG
Protein: 5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg) (P54619)
Organism: Homo sapiens (Human)
Function: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-2
- Calcium/calmodulin-dependent protein kinase kinase 2
- Serine/threonine-protein kinase STK11
- Serine/threonine-protein kinase mTOR
- 5'-AMP-activated protein kinase subunit gamma-3
- Acetyl-CoA carboxylase 1
Sequence:
METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP
Protein: Nuatigenin 3-beta-glucosyltransferase (EC 2.4.1.192) (Glycosyltransferase 4A) (SaGT4A) (Q5H861)
Organism: Solanum aculeatissimum (Dutch eggplant) (Solanum khasianum)
Function: Glucosyltransferase involved in steroid saponin biosynthesis. Catalyzes the 3-O-glucosylation of steroidal sapogenins, such as diosgenin, nuatigenin and tigogenin. Can glucosylate steroidal alkaloids, such as solanidine, solasodine and tomatidine.
Interaction partners:
Sequence:
MDNGSNQLHVLFLPYFATGHIIPLVNAARLFVFHAGVKVTILTTHHNASLFRSTIDNDVEDGHSVISIHTLRFPSTEVGLPEGIENFSSASSPELAGKVFYAIYLLQKPMEDKIREIHPDCIFSDMYLPWTVNIALELKIPRLLFNQSSYMYNSILYNLRLYKPHKSKTITSTDSISVPGLPDKIEFKLSQLTDDLIKPEDEKNAFDELLDRTRESEDRSYGIVHDTFYELEPAYADYYQKVKKTKCWQIGPISHFSSKLFRRKELINAVDESNSCAIVEWLNEQEHKSVLYVSFGSVVRFPEAQLTEIAKALEASSIPFIWVVKKDQSAETTCLLEEEKLKNKGLIIRGWAPQLTILDHSAVGGFMTHCGWNSILEAIIAGVPLVTWPVFAEQFYNEKLVEVMGLGVKVGAEVHESNGGVEISSLVIESEKIKEAIEKLMDDSKESQKIREKVIGMSEMAKNAVEEGGSSWNNLTALIDDIKNFTSTTNV
Protein: Transcription factor TGAL1 (OsNIF4) (bZIP transcription factor 8) (OsbZIP08) (Q6IVC2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- Os01g0104800 protein
- Os04g0662100 protein
- Os12g0166500 protein
- U3 small nucleolar RNA-associated protein 18 homolog
- DEAD-box ATP-dependent RNA helicase 36
- Pre-mRNA-splicing factor SLU7
- Os03g0598200 protein
- Os05g0295100 protein
- BTB/POZ domain and ankyrin repeat-containing protein NPR3
Sequence:
MEGGRLGGAAASASAAAAADARGGMSGFAAPQHAIHTNLNNVQPTQVTDFGALAQSAGFRIEDLANLSTNGLFNLKSNAHTIINDPLQFENYVKSISPSNITTTATVTVVDPQTLVPQKGAQLNLVTIRTGNVENWGESTIADTSPRTDTSTDPDTDERNQMFEQGQLAAPTASDSSDRSKDKLDHKTLRRLAQNREAARKSRLRKKAYIQNLESSRLKLTQIEQELQRARQQGIFISTSSDQSHSASGNGALAFDMEYARWLEEHNKHINELRAAVNAHAGDNDLKSTVDSIMAHYNEIFKLKGVAAKADVFHVLSGMWKTPAERCFMWLGGFRSSELLKLLAGQLEPLTEQQLAGIANLQQSSQQAEDALSQGMEALQQSLAETLASGSLGPAGSSGNVANYMGQMAMAMGKLGTLENFLRQADNLRLQTLQQMQRILTTRQSARALLAISDYFSRLRALSSLWLARPRE
Protein: Glycosylphosphatidylinositol anchor attachment 1 (F7EVW7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLLSDPVRRRALARIVLRLNTPLCVLSYVAGIAWFLALAFPPLTQRTYMSENAMGSTMVEEQFVGGDRARNFARDFAAHRKKPGALPVAWLERAMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGPDTTNSQAVGLLLALAAHFRGQIYWAKDIIFLVTEHDLLGTEAWLEAYHDINVTGIQSSPLQGRAGAIQAAVALELSSDVVTSLDVTVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPQDWTSLEGPLQGLQTLLLMVLRQASGRPHGPHGLFLRYGVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFFYLLPALSRFVSIGLYMPATGFLLLVLGALELWMQLHEAGVNPEEAGKAPGPGSPPLATQSVSLASLMAPLLISQAMGLALYFLPVLGQHVAAQHFPVAEAEAVVLTLLAIYVAGLALPHNTHRVVSSQVPDRGWMALKLVALIYLALQLGCIALLNFSLGFLLAATMVPAAALTKPHGPRTLYAALLVVTSPAVTLFGSLFLWRELQEVPLSLAEGWQLFLTALAQGVLEHYTYGALLFPILALGLYPCWLLFWNVLFWK
Protein: TRPV3 protein (Transient receptor potential cation channel, subfamily V, member 3) (Q2M3L1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKAHPKEMVPLMGKRVAAPSGNPAVLPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTSPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKGRLKKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENNILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGADVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMGWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLGFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTADFNKIQDSSRNNSKTTLNAFEEVEEFPETSV
Protein: Protein SNA2 (P56508)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein. Lipid droplet. Note=Localized to punctate structures and lipid particles in the cytoplasm.
Interaction partners:
- Protein SNA3
- Plasma membrane proteolipid 3
- Membrane protein TMS1
Sequence:
MHARDWFLVFIAIFIPPLAVWLKRGFFTKDLLINFLLFLLGFFPGLIHALYVISCHPYEENEARYSHLSSSDDNYGSLA
Protein: Secretory 16, isoform J (X2JEY9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MLHNNAPWLPPHQQQQQQAPQQHPTPQQQHAMPQQQQTLPAQQQQQQVYASQMFQQHQPNYWPEDQHQQQQQPQSLNYNNYFPGQQQQHPMQQQQLPPQQQLPPQQQQPTQQQHTIQQQLYYPTQQQPQVPAPAEPALDSFDNNNSGGGGGGGRSDGWGDWGDWNDNSNNNNSNGTDGLLEPTGQLLEDSFNVQSSQGSWQAFATSNNVNNNGELPPPANPQSTSLQQQPLNQQSIPLLHQQPQSPPELGQEPELDAIVPPQAFQNQPPTAAPPPTSLTSFSAQMTAVGSPIYAVGASSAHSAGVGASPAPPTGVVAPPAHLAGIGAPPAHLAGVGASPAPSALVGASPAPIIGVGAPPVGAPPVGAPPADATTIAPPAALPPSIVPSSGSNPFKRSTGLNKRVNIMADPAAGAPSPPAPAAAIAPVAPVAPIPPPADQLFGMPAEAHGEGFNLIAAPPVEASLGTPLSAPIPAPIPVPNASLYASPAVPQAFAHLEPDNQEVLSAPNDERAQYLQTSHLSEQLGEGEADQDAGLLPPPGLSRLVLGQPELDSQQQRQVTGATEQPPLNVAQAAALHMQERRADGEDTSDGEQQVRNIQTPPRRVVTGVETNAPSLREQREVVLDGENLEDREAIPPPTLAELPTTSVHHNILPDEAEQLHHNNPPQAMTPLNAQQPHQQQSTLQQQHQQHSTTQQEKKRAAVGRRTTASLDLESDESDEFLQSERERDRERERRDLMEERHSRGRSHSHYPYEGETEDSVRGAAHHETKSLRETHHKRNHDSARSRRHQDPKVERERERDRERDRTWRRRSNKYHSGGEDPDRSYDHSRRYNNSNYEGESDNPEYNHMGDAELDGSGGRSSKTSRHRRSAAEEDFDDYERERNRSRRSTKPQSSAEKSRSSGGRRNYENSGRSARADDGRRRYQDQRNPGAQYPVSATGYVPYGMYEQMSRNPQVYADMYAKFYGQMINSMNAAVSAAASKGGVPAGAGVIPGLMPSAVPVSAAQLVAATSGGSVSGSSEAAMLRERERYTHAYITQANEFHRHQYKELIYQQQQQQQQQQQQQQQREDHLNSSFSVAEDNASFYGSHGGGSIYNQYQSYPLSSARSLSNLNGDGRNSRCGPYYAGSECGLDIRAAADAAPSTYGGVAGTAGPVTNTAVARPPRRRTPLQFSRPHLVASYAMSLLLKVKPKYAGRGRLRNDVEVAPPRIRDGTSSLLRMYPGPLQGRKLHKDKIISFCKEQIRLGPTKGCTALYATQKKPQGSVTKYRASHALMWHLLILLLRQNGYIADTDVGDLLLENQQEYPYDPSEFEAENEPDADAEQDAAAPADKTVDSDLDSESAAGVTPAEPLAAGAATSSINGADAANAATPLSEQAATDKFRSYVLRGNVEEALQWATDNGLWTHAFFLALYEDRYALTDVAQKFLNRAIKANDPLQTLYQMKSCHTPACVSQLRDEQWGDWRSHLSILVTNKSRQPEYDRSSVVALGDTLFQRGDIYAAHFCYLVAQEEFGRYDSSATELTTLTANVPRLILLGSSHYKHFNEFASNEAIIMTEIYEYARSLFDPKFSIAHFQHYKFLLATRILDYGQHFRCTNYLEQIARHIELKPESYDSNFIQRVCGLAERLRYHDPILINRVSFASPPNATSKDSAAAEEKAWLRQLRSLAYVPQQEQLQQLQQNQQVQQEQNDIDQQFAEVNKQFRELNMQYESNSNMENTLQPQLPPVDQQPPQQQQQVLSESYQQPTQQYYEPPPQAPTESDPYGQGQPSYYDPNAGQLHYDPNAAQHQYDQQQPQPQPTPSYGQIEPGTEAYQPGQATADPAAVPSGYGYDYWSGTQQPPYGDEPNENQAALKDEEEEDEEQDEQQILQYAKQQILQQTKQQQLQQEQHTRSNGAASINNRFKSNALKQERSSGSLRKRQEASRTATIAAAAAAIAQITPATVAAAATPPAASAKAFNLNDLQQQTRPAISMPKSKSYGDEDDGGSGGVADPGQKTKPVGSSEAAGKQQASGKQANSGSDLGAPGNKNAGWFGGLWNKLSLKPKNQMILPDDKNPAIVWDKERKCWTNTEGNGDEAESFKPPPKMSDLGMALGGPPAAPIGNAGLGMGLMPVANNAPGSHQSAPLMDQQTPSQPQTYGSPIDYTAAPAPELIPTVPSPAPLSVPSSAPAALAAPNPAAVPGGPQPKLQSNMFKMQRNRTLKNSYVDVFNPSGAPMSAAPENVLAPMMAPAAVPQGGYFVPQQ
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWW9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein URE2
- Ammonium transporter
- Importin subunit alpha
Sequence:
MEGFQDDLDGMGVLNSFLKDGSGESKSGAEKSSTTKPQAENVVPFVNDNYDSMLEALPDELNLDFTSLLSPFPAPGQGNDDDITVNVNPYIGQSNNDFYKIDEVPEEDLQQGSEIINSTTQLQPITINNSKQQNYNQINVDSSNQQNGEIAQFWDFNVDTLNITPSNSSGSATISAPNSYNSEIPLGVTTGFNNNNNNHLFAHGVLGGGSSIGNSNIINNTSLTYSNQQNSFPGSSLHSKPTTATTVTYTNTPPIKENQSIIANSSLKASQFTGKRPISVVGSNNSYSENPYILSAANTSNSVRKNSLPRQLSSTSLNNYRKSVSSSERPPDPDAVHCDNCKTYKTPLWRRSPEGKVLCNACGLFQKLHGTMRPLSLKTDVIRKRNSKKRTKIQMNPQQTQSQQRQHIQYQTQQNSMQKLLSNHSSPTDTFSSGKSRRKLSSTRLNQDMTTIRYSREGGSLTKQGFTTTPTYNSRSPNYSNSAAASNTRKSKSRRSSTSSVNSNSSRSSSRSNVPILPKISGHSSSGNSPMNIQSTTPGGGPQTSNSVGNFLAMGAYSNSLTSSPRNASIYGTNAPSRNLSSSASKYGVSMPGRKLSRNASYSSSFINTNPQQTQDIGNFNDDQSIQGNGTGVNSQNIRRINSNYDSPQPNFDLFRLDSNKDSPENIPDVLRSDSRLSQKSQVSHTSLLSQQIQNQQRMRGEKSISQENLQFKQTPTMQGQTERNIPSRTTSSASYSESVFQQRGMQPNNSNSQFFENQHQANSNTDQRQFLEGMSYDLHNGDNTIKTVILGQEQNFANPEANGNEAKKSALEQDLDWLKFGI
Protein: Sodium/potassium-transporting ATPase subunit alpha (A0A075QE41)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
YKLAATSEDDGNKKNKKEVKKAKEKKDMDDLKKEVDLDDHKLTLDELHRKYGTDLARGLSSARAKEILLRDGPNTLTPPPTTPEWVKFCRQLFGGFSMLLWIGAMLCFLAYGIQAASEDEPANDNLYLGVVLSVVVIVTGCFSYYQEAKSSKIMDSFKNLVPQQALVVRDGEKKNINAEEVVVGDLVEVKGGDRIPADLRIVSASGCKVDNSSLTGESEPQTRTPDFSNDNPLETRNIAFFSTNCVEGTARGIVINTGDHTVMGRIATLATSLEGGKTPIAKEIEHFIHIITGVAVFLGVSFFVLSLILGYGWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGTCFDKSSATWASLARVAGLCNRAVFLAEQNNVPILKRDVAGDASESALLKCIELCCGSVKDMREKYSKIAEIPFNSTNKYQLSIHKNIMAGESKHLLVMKGAPERILDRCSTILIQGKEQSLDDELKEAFQNAYEELGGLGERVLGFCHFQLPDDQFAEGFNFDCEEVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLKIPVSEVNPRDAKACVV
Protein: Lariat debranching enzyme (AtDBR1) (EC 3.1.4.-) (Q94K01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis. Plays en essential role during embryogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Protein HASTY 1
- Zinc finger CCCH domain-containing protein 64
- Eukaryotic aspartyl protease family protein
- Nucleolar complex-associated protein 2
Sequence:
MKIAIEGCMHGDLDNVYKTIQHYEQIHNTKVDLLLCCGDFQAVRNEKDMDSLNVPRKYREMKSFWKYYSGQEVAPIPTIFIGGNHEASNYLWELYYGGWAATNIYFLGFAGVVKFGNVRIGGLSGIYNERHYRSGHFERPPYNESTIRSVYHVRDYDVQKLMQLEEPLDIFLSHDWPVGITDYGDSESLMRQKPYFRQEIEEKTLGSKPAALLLEKLKPQYWFSAHLHCKFAAAVQHGNDGSVTKFLALDKCLPGKKFLQIIEIESEPGPFEVLYDEEWLAITRKFNSIFPLTRRYTNVSTAGTIQESREWVRKKLEERQFKPFEFARTVPAYNPSQRVFDSIPEIPQNPQTLSLLELLGLPYLLDSSPVTGERTDIPASLAPSDLPTYDSEEIPIDDIDEIEEMEEAKADDHTRDDA
Protein: Glial cell line-derived neurotrophic factor (hGDNF) (Astrocyte-derived trophic factor) (ATF) (P39905)
Organism: Homo sapiens (Human)
Function: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake.
Subcellular location: Secreted {ECO:0000269|PubMed:21994944, ECO:0000269|PubMed:9811930}.
Interaction partners:
- GDNF family receptor alpha-2
- GDNF family receptor alpha-1
- Proto-oncogene tyrosine-protein kinase receptor Ret
- GDNF family receptor alpha-3
- BDNF/NT-3 growth factors receptor
- High affinity nerve growth factor receptor
- GDNF family receptor alpha-4
- Transcription factor Jun
- NT-3 growth factor receptor
- Neurotrophic factor BDNF precursor form
Sequence:
MKLWDVVAVCLVLLHTASAFPLPAGKRPPEAPAEDRSLGRRRAPFALSSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCRPIAFDDDLSFLDDNLVYHILRKHSAKRCGCI
Protein: Sodium/potassium exporting P-type ATPase 5 (EC 7.2.2.3) (Q12691)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of sodium or lithium ions to allow salt tolerance.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MSEGTVKENNNEEFNAYHTLTTEEAAEFIGTSLTEGLTQDESLRRLKAVGENTLGDDTKIDYKAMVLHQVCNAMIMVLVISMAISFAVRDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEALGAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYSHNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGDPTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDSTVKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSLSNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVKKFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEVDDLPVLPLVIARCSPQTKVRMIEALHRRKKFCAMTGDGVNDSPSLKMANVGIAMGINGSDVSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDENGKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPNDSEVGIFTWEVIIDTFAYGIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWEVVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHKPIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNSENDLERSSKHDPFEAYSTSTTLQSEINISVKH
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (A0A0B4J206)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGKPGCRTCCKIKFYLLFSYFQVQASHFEGLITTIVGYILLAITLIICHGLATLVKFHRSRRLLGVCYIVVKVSLLVVVEIGVFPLICGWWLDICSLEMFDATLKDRELSFQSAPGTTMFLHWLVGMVYVFYFASFILLLREVLRPGVLWFLRNLNDPDFNPVQEMIHLPIYRHLRRFILSVIVFGSIVLLMLWLPIRIIKSVLPNFLPYNVMLYSDAPVSELSLELLLLQVVLPALLEQGHTRQWLKGLVRAWTVTAGYLLDLHSYLLGDQEENENSANQQVNNNQHARNNNAIPVVGEGLHAAHQAILQQGGPVGFQPYRRPLNFPLRIFLLIVFMCITLLIASLICLTLPVFAGRWLMSFWTGTAKIHELYTAACGLYVCWLTIRAVTVMVAWMPQGRRVIFQKVKEWSLMIMKTLIVAVLLAGVVPLLLGLLFELVIVAPLRVPLDQTPLFYPWQDWALGVLHAKIIAAITLMGPQWWLKTVIEQVYANGIRNIDLHYIVRKLAAPVISVLLLSLCVPYVIASGVVPLLGVTAEMQNLVHRRIYPFLLMVVVLMAILSFQVRQFKRLYEHIKNDKYLVGQRLVNYERKSGKQGSSPPPPQSSQE
Protein: Beta-hexosaminidase subunit alpha (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit alpha) (N-acetyl-beta-glucosaminidase subunit alpha) (A0A0S2Z3W3)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
Protein: Receptor-type guanylate cyclase gcy-4 (EC 4.6.1.2) (Q23681)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward Br(1-) and I(1-) salt ions in ASE right (ASER) sensory neuron.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRQLNYYIFISTILTYNLTHGQGPRPVIRVGITAALKTENGSIGWAYTGGAVPLALQYLKSHGYMLNFDFEFHVEYTECDLANTVRAGLNFMKTNNYDVIIGPPCAPALKMMGTLSTIYKKPVLGWGFVSESEISDMNRFPFVASVLPSTKTLGVVTSKLLEIYGWDRVALLYFKNELDYCSSVVNDVEKSLYNESKSVQIVMKAEIDGSNSESTSATLQVVKTRARVILFCAHAGGEKRFYLIQAGLLGMNSSEYVHVMLSMRSVGFGVQTSVGKKPLTLSGLPPIWESFTVNPDGMEDLAKSVAAKMIVIDTSSEVRDKTFLQYMTKNIVYAIREPPLSCKVPECLITNATGMGAYARHLFDVFYMYGMAVSSLNSTDPNVYGNLSLLIPKFTTAFEGMTGEVKLNEDLARKPLYQVYGLNSEYDQISLIDISLINDTVNVVFNYADGNTEVWHFWGGTRPPDTPVCGFLGKSCPLPIFEQYRALVIVAIAVTILILLAIIICMSSKIRNRRVEQSRLHSEWQIHAIKLRLPMHRRASKSSQESETESASETENFTSKSGDTMTSEFKETYTIQYLENDLVLTTAHQVQELSQAEMMKFVKLRKLDHENLNKFIGLSIDGSRFVSVWKMCSRGSLQDIISKGSFSMDYFFMFCMIRDIAEGLHYIHKSFLRHHGNLRSATCLVNDSWQVKLADFGLQFLQDEEEKPFKKNMLWAAPEVIRGSLSIEQMDSSADIYSFAIVASEILTKREAWDLSRRKEGYEEIKYAVKKGGQFVLRPDLHIDIEVNQTLLALVKDCWCENPEERPSAENVCKVLFDMTPNTEDNLMDHVFSMLEEYTSSLEVEVGERTKELTLEKKKSDILLGRMLPKQVAERLKAGQAVEPESFDLVTVFFSDLVKFTDLASKCSPFQVVNLLNDVFSNFDSIIEKHDVYKVESIGDGFLCVSGLPNRNGMEHIRQIVGMSLCFMEFCRNFRIPHLPRERVELRVGINSGPCVAGVVGLSMPRYCLFGDTVNTASRMESNGKPSMIHMSEAAHSLLVNNYPYQFETNSRGEVIIKGKGVMETYWLLGKMSLSNQSTPPITKVNHKPRKIASFTDSELTNYSFRSVSPYVENLSDNDDEEIRRVLRREMMRVEV
Protein: Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) [Includes: Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC); Phosphoribosylaminoimidazole succinocarboxamide synthetase (EC 6.3.2.6) (SAICAR synthetase)] (P51583)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Adenylosuccinate lyase
- Amidophosphoribosyltransferase
- Bifunctional purine biosynthesis protein ATIC
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Adenylosuccinate synthetase isozyme 2
- GMP synthase
- Phosphoribosylformylglycinamidine synthase.
- Galectin-4
- Uridine monophosphate synthetase, isoform CRA_a.
Sequence:
MATAEVLNIGRKLYEGKTKEVYELLDSPGRVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTKKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYRFYPPKVEMFFKDDANNDPQWSEEQLIAAKFCFAGLVIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVADRVELLLKSNSQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPITADWGAQDVWSSLRLPSGIGCSTILSPEGSAQFAAQIFGLNNHLVWAKLRASKLNTWISLKQADKKIRECNL
Protein: FAS1 domain-containing protein CAGL0M08734g (Q6FJ69)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Vacuole {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Chromatin modification-related protein EAF3
- Chromatin modification-related protein
Sequence:
MVALKYVLVPVALVAAKNIVEMITFRDENGKLHRRLAPEEYRGGVLDGEESRLLQKRDLEMHPPVDLGVYFSNRPIHRTIDVPDIYLDSQISVLTELDIFASYSRNDEKSYDMFRDPESDLIVIAPTNAAITALAKKPWQFPMDIDTMEQAGSSERDIDNAIHNNIVNFVRSHVVAYQKDTKTSKDGTVLLQSKQYSMQHSNGKGGDVLLKREGEKYCVASVVDEVFHDVQNIYSTKNGVILVIDATLSRPGA
Protein: BCL2 associated agonist of cell death b isoform 2 (BCL2-associated agonist of cell death b) (Bad) (Q9I9N2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAHMFNISDDSETETMEDSEDSSLDKHKSGSAQKKQHLTVPDRLKGEQLGRQRNLSMNEEDLLETGVAEDPHMLGDPFRPRSRSAPPALWAAKKYGQQLRRMSDEFDKGMKRVKSAGTARQMSQSPSWLAFLWSHKESDAESRPAE
Protein: Large ribosomal subunit protein eL20 (60S ribosomal protein L18a) (Q02543)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein P2
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL27
Sequence:
MKASGTLREYKVVGRCLPTPKCHTPPLYRMRIFAPNHVVAKSRFWYFVSQLKKMKKSSGEIVYCGQVFEKSPLRVKNFGIWLRYDSRSGTHNMYREYRDLTTAGAVTQCYRDMGARHRARAHSIQIMKVEEIAASKCRRPAVKQFHDSKIKFPLPHRVLRRQHKPRFTTKRPNTFF