wanglab/gogpt-training-data huggingface dataset:
Protein: Opsin-5 (E6P6L8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MENETSISSGYIPHYLLRGDPFASKLSKEADIVAAFYILVIGILSATGNGYVMYMTFKRKTKLKPPEIMTLNLAIFDFGISVSGKPFFIVSSFSHRWLFGWQGCRYYGWAGFFFGCGSLITMTVVSFDRYLKICHLRYGTWLKRHHAFLSVVFIWAYAAFWATMPVVGWGNYAPEPFGTSCTLDWWLTQASVSGQSFVMCMLFFCLIFPTVIIVFSYVMIIFKVKSSAKEVSHFDTRNKNNHSLEMKLTKVAMLICAGFLIAWIPYAVVSVMSAFGEPDSVPIPVSVVPTLLAKSSAMYNPIIYQVIDCKKKCVKSCCFQAWRKKKPSKTSRFYTISGSIKQRPADEASIEI
Protein: Leucine zipper protein 1 (Filamin mechanobinding actin cross-linking protein) (Fimbacin) (Leucine zipper motif-containing protein) (Q8R4U7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q86V48}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q86V48}. Midbody {ECO:0000250|UniProtKB:Q86V48}. Chromosome, centromere {ECO:0000250|UniProtKB:Q86V48}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q86V48}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q86V48}. Nucleus {ECO:0000250|UniProtKB:Q9ESV1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ESV1}. Perikaryon {ECO:0000250|UniProtKB:Q9ESV1}. Cell junction, tight junction {ECO:0000269|PubMed:33346378}. Note=Localizes to the proximal end of basal bodies (By similarity). During mitosis, localizes at the inner centromere in metaphase, at the central spindle in anaphase, and at the midbody in telophase (By similarity). Central spindle localization requires KIF20A while centromere localization requires the kinase activity of the chromosomal passenger complex (By similarity). {ECO:0000250|UniProtKB:Q86V48}.
Interaction partners:
Sequence:
MAELTNYKDAASNRHLRFKLQSLSRRLDELEEATKNLQRAEDELLDLQDKVIQAEGSDSSTLAEIEVLRQRVLKIEGKDEEIKRAEDLCHTMKEKLEEEENLTRELKSEIERLQKRMVDLEKLEEALSRSKNECSQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLVSELEKLKSLTLSFVNERKYLNEKEKENEKIIKELTQKLEQNKKMNRDHMRNASTFLERNDLRIEDGISSTLSSKESKRKGSLDYLKQVENETRDKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMRAKNNDLQDNYLTELNRNRSLASQLEEIKLQVRKQKELGNGDIEGEDAFLLGRGRHERTKLKGHGSEASVSKHTSRELSPQHKRERLRNREFALSNEHYSLSSKQASSPVFTNKRAAKASNMGMGTDSGTQETKRTEDRFAPGSSHSEGKRGREQPSVLSRYPPAAQEHTKVWKGAPKPGTESGLKGKVEKTTRTFSDSTHVSVPNDIVGKGDKTSDLSSEAHCGKRGQVPGHASQGTQAVESSCSKAIGALSSSQKASSEGLSKGKKTANGLAADANFSNSKAPILSKYPYSSRSQENILQGFSLPNKEGVDQPVAVVMEDSSQHEALRCRVIKSSGREKPDSDDDLDIESFVTAKLVNTTITPEPEPKPQPNSREKVKSRGGTRTALFENDKNAAIENDSVKPTRPSSNAIEFPDANCAGVKNQRPFSPREALRSRAIIKPVIIDKDVKKIMGGSGTEVVLEKQKSTSKSVTSKVTSSITIYPSDSSGPRAVPSEAPRERHTSTSNIQVGPPELTAISNHVSSPLELSIHKHDITLQLTEAERVGDGSPKNRAEMVVSRSSILIKPSESVEKNSHVPPAETIRWKSHSASSDSRHITVRNAWKSKRDLKCSEDPPTGIGRNMEATNAYTQRPCTDFLELEQPRSQPSEQGARRVGNSGDAPELSPRRTQSSLTASEVLTRRDRMGGAITAASCNHSSSMEEGEDSTFVTSRRIHNPLEHSELPGKQGLPEPEPVWTEERLHPAKPYAEED
Protein: Translation initiation factor eIF2B subunit beta (eIF2B GDP-GTP exchange factor subunit beta) (Q62818)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UT76}.
Interaction partners:
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2, subunit 2
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- Beta-catenin-like protein 1
- eIF-2-alpha kinase GCN2
Sequence:
MPGAAAKGSELSERIESFVETLKRGGGRRTSEDMARETLGLLRRLITDHHWNNAGDLMDLIRREGRRMTAAHPPETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLSEDFSFHYAPLKSNIIEAINELLVELEGTTENIAAQALEHIHSNEVIMTIGFSRTVEAFLREAAQKRKFHVIAAECAPFCQGHEMAVNLSEAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGSLRAVAGTHTLALAAKHHSTPLIVCAPMFKLSPQFPSEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPDLITLFISNIGGNAPSYVYRLMSELYHPDDHVL
Protein: Thioredoxin domain-containing protein 16 (Q9P2K2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000269|PubMed:25122923}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:21359175, ECO:0000269|PubMed:25122923}.
Interaction partners:
- FAD-dependent oxidoreductase domain-containing protein 2
Sequence:
MFSGFNVFRVGISFVIMCIFYMPTVNSLPELSPQKYFSTLQPGKASLAYFCQADSPRTSVFLEELNEAVRPLQDYGISVAKVNCVKEEISRYCGKEKDLMKAYLFKGNILLREFPTDTLFDVNAIVAHVLFALLFSEVKYITNLEDLQNIENALKGKANIIFSYVRAIGIPEHRAVMEAAFVYGTTYQFVLTTEIALLESIGSEDVEYAHLYFFHCKLVLDLTQQCRRTLMEQPLTTLNIHLFIKTMKAPLLTEVAEDPQQVSTVHLQLGLPLVFIVSQQATYEADRRTAEWVAWRLLGKAGVLLLLRDSLEVNIPQDANVVFKRAEEGVPVEFLVLHDVDLIISHVENNMHIEEIQEDEDNDMEGPDIDVQDDEVAETVFRDRKRKLPLELTVELTEETFNATVMASDSIVLFYAGWQAVSMAFLQSYIDVAVKLKGTSTMLLTRINCADWSDVCTKQNVTEFPIIKMYKKGENPVSYAGMLGTEDLLKFIQLNRISYPVNITSIQEAEEYLSGELYKDLILYSSVSVLGLFSPTMKTAKEDFSEAGNYLKGYVITGIYSEEDVLLLSTKYAASLPALLLARHTEGKIESIPLASTHAQDIVQIITDALLEMFPEITVENLPSYFRLQKPLLILFSDGTVNPQYKKAILTLVKQKYLDSFTPCWLNLKNTPVGRGILRAYFDPLPPLPLLVLVNLHSGGQVFAFPSDQAIIEENLVLWLKKLEAGLENHITILPAQEWKPPLPAYDFLSMIDAATSQRGTRKVPKCMKETDVQENDKEQHEDKSAVRKEPIETLRIKHWNRSNWFKEAEKSFRRDKELGCSKVN
Protein: LD37466p (Q8SWW0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYQINTNGSQCLSFDISSSSQAMAFGDQSGHINMIAAVQTPQPQFNLYSRSTEFADVVPQLPMVSITDTNFPLSSVMLPHLTTGTQWFSDWPEELLRYRYHRPKTIDPEVLSNMKMQGPIGYSPNPRTARRNQIPYVIEQGGVCSPNGNGTAAATKAENGVKIIPRRYRKVELKYTKLGTQDFDFDQHNQTCFAGLEATLPNSYCNAMLQILYFTDALRVKLLEHSCIKEFCLSCELGFLFNMLDKSTASSPCQASNFLRSFRTVPEASALGLILTDRSSNVNLISLIQNWNRFILHQMHYEIFDSSKNASTYSGSVQTSTNAENAGSSETSGSSDLYDSISDENSKEDDRERSKINAETDISKIFGTKQICINRCIKCQEEKIKESILLACNLSYPNHIKDSDQYFNFGTILKRSLSSEKSIQAFCERCKKFSPTNQSVKVTSLPQILSINCGLNNEKDITFLKRQLNRCSEKTTVDAAASLSTSKPCRYGANCSRSDCHFMHPDRKSPSHTSQPNAVNNSPNGRQKSWFPLTFTMGINDQGEVQVQTQSDASSGKSEQEEETEKPPTKGLDNNRMYALHAVVCQVDDGTQKNLVSLINVQRPYHTMKLAESADDPQSQWYIFNDFSISPVSPQESVWFTLDWKVPCILFYRHVEDDSESASTTSSTVTESEETIPSESSSGSPTNLSNPFLEEIVSPMLGNLSADATLQPLQSDEMPQSGDLVAMDAEFVTLNPEENEIRPDGKTATIKPCHMSVARISCIRGQGPAEGVPFMDDYISTQEKVVDYLTQFSGIKPGDLDANFSKKRLTALKYSYQKLKYLVDVGVIFVGHGLKNDFRVINIYVPSEQIIDTVHLFHMPHHRMVSLRFLAWHFLGTKIQSETHDSIEDARTTLQLYKHYLKLQEEKKFANALKNLYERGKQLQWKVPED
Protein: Malate dehydrogenase, mitochondrial (EC 1.1.1.37) (P04636)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:24098488}.
Interaction partners:
- Citrate synthase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Fumarate hydratase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Aspartate aminotransferase, cytoplasmic
- Pyruvate carboxylase, mitochondrial
- ATP-citrate synthase
- Malic enzyme
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Malic enzyme
Sequence:
MLSALARPVGAALRRSFSTSAQNNAKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGVAADLSHIETRANVKGYLGPEQLPDCLKGCDVVVIPAGVPRKPGMTRDDLFNTNATIVATLTAACAQHCPEAMICIISNPVNSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANTFVAELKGLDPARVNVPVIGGHAGKTIIPLISQCTPKVDFPQDQLATLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVDAMNGKEGVIECSFVQSKETECTYFSTPLLLGKKGLEKNLGIGKITPFEEKMIAEAIPELKASIKKGEDFVKNMK
Protein: Kinesin-like protein KIN-14N (AtKIN14d) (Kinesin-like protein KatC) (P46875)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-like protein KIN-10A
- WPP domain-containing protein 3
- L-type lectin-domain containing receptor kinase VIII.2
- Kinesin-like protein KIN-8A
- Kinesin-like protein KIN-7D, mitochondrial
- Kinesin-like protein KIN-7C, mitochondrial
- Kinesin-like protein KIN-8B
- Microtubule-associated protein RP/EB family member 1B
- Kinesin-like protein KIN-UB
- Kinesin-like protein KIN-UA
Sequence:
MVGAMANNGRIRSAFPVTNGSKDLTPNSAPASTTGSEYGPVEFTREDVETLLNERIKYKSKFNYKERCENMMDYIKRLRLCIRWFQELELDYAFEQEKLKNALELNEKHCVDMEVSLKNKEEELNMIIEELRKNFESVQVQLAREQTEKLAANDSLGKEKEARLSVEKAQAGLTEELGKAQGDLQTANQRIQSVNDMYKLLQEYNSSLQLYNSKLQGDLDEAHETIKRGEKERTAIIENIGNLKGQFSALQEQLAASKASQEDIMKQKGELVNEIASLKVELQQVKDDRDRHLVEVKTLQTEATKYNDFKDAITELETTCSSQSTQIRQLQDRLVNSERRLQVSDLSTFEKMNEYEDQKQSIIDLKSRVEEAELKLVEGEKLRKKLHNTILELKGNIRVFCRVRPLLPGENNGDEGKTISYPTSLEALGRGIDLMQNAQKHAFTFDKVFAPTASQEDVFTEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPGNVEEKGLIPRCLEQIFETRQSLRSQGWKYELQVSMLEIYNETIRDLLSTNKEAVRTDSGVSPQKHAIKHDASGNTHVAELTILDVKSSREVSFLLDHAARNRSVGKTQMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSKSGSTGDRLKETQAINKSLSSLGDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDAKTLMFVNIAPESSSTGESLCSLRFAARVNACEIGTPRRQTNIKPLENRLSLG
Protein: Steroid transmembrane transporter SLC22A24 (Organic anion transporter 5) (rOat5) (Solute carrier family 22 member 24) (Q76M99)
Organism: Rattus norvegicus (Rat)
Function: Renal transmembrane organic anion/dicarboxylate exchanger that participates in the reabsorption of conjugated steroids, as well as bile acids, driven by an outward gradient of dicarboxylates such as glutarate or succinate. Transports estrone 3-sulfate and estradiol-17-glucuronide (17beta-estradiol 17-O-(beta-D-glucuronate)), but not androstanediol glucuronide (5alpha-androstane-3alpha,17beta-diol 3-O-(beta-D-glucuronate)), nor taurocholate. Prefers sulfate conjugates of steroids rather than glucuronide conjugates.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31553721}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAFQDLITQIGCLGRFQILHLIFVLICFILVVPHTVLENFTAAIPSHRCWVPILDNNTMSDNNSRILSQDDLLRISIPMDSNLRPEKCRRYIQPQWDLLHLNGTFSTVTEPDTEPCVDGWVYDQSTFLSTTVTQWDLVCGSQTLNSVAKFIYMTGIFIGHLMGGHLSDKFGRKFIVTCGLLTLAVTETSVAFAPTFLIYCSLRFLTGISSSCIRTNSALLILEWTSPKFQAMVMALIFSAGGIGQVLLGVLAFGIRNWQHLQLAMSVPVFFLLIPTRWLSESARWLIITNKPQEGLKELIKVAHINGIKNSRDVLTLEVVKTTMKDELEAAETKPSPLVLFRTPNLRKRICLLSFVRCVSLISTVGLLINLQYLSNKVFLLQCLYGVVCTPANLLGNFSMNYMGRRTTQIIFMSVMGISILSITFLTQEMQIPRLVLASLGGAISSASLTSTAVLSNELVPTVIRATALGVIGIFGSAGAALSPLLMILMTYSASLPWIIYGVLPILSSLVVLLLPETRNQPLPDSIQDVENKRKSSREVKKDAVAKVTPF
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Autocrine motility factor) (AMF) (Neuroleukin) (NLK) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (P06745)
Organism: Mus musculus (Mouse)
Function: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis. Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (By similarity). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons. It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P06744}. Secreted {ECO:0000250|UniProtKB:P06744}.
Interaction partners:
- Triosephosphate isomerase
- GDH/6PGL endoplasmic bifunctional protein
- ATP-dependent 6-phosphofructokinase, liver type
- Phosphoglucomutase-1
- ATP-dependent 6-phosphofructokinase, muscle type
- Transaldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent 6-phosphofructokinase, platelet type
- Mannose-6-phosphate isomerase
- Fructose-bisphosphate aldolase A
Sequence:
MAALTRNPQFQKLLEWHRANSANLKLRELFEADPERFNNFSLNLNTNHGHILVDYSKNLVNKEVMQMLVELAKSRGVEAARDNMFSGSKINYTENRAVLHVALRNRSNTPIKVDGKDVMPEVNRVLDKMKSFCQRVRSGDWKGYTGKSITDIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLASLSPETSLFIIASKTFTTQETITNAETAKEWFLEAAKDPSAVAKHFVALSTNTAKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGAHWMDQHFLKTPLEKNAPVLLALLGIWYINCYGCETHALLPYDQYMHRFAAYFQQGDMESNGKYITKSGARVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKLPEEARKELQAAGKSPEDLEKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFVQGIMWDINSFDQWGVELGKQLAKKIEPELEGSSAVTSHDSSTNGLISFIKQQRDTKLE
Protein: E3 ubiquitin-protein ligase RNF149 (EC 2.3.2.27) (DNA polymerase-transactivated protein 2) (RING finger protein 149) (RING-type E3 ubiquitin transferase RNF149) (Q8NC42)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAWRRREASVGARGVLALALLALALCVPGARGRALEWFSAVVNIEYVDPQTNLTVWSVSESGRFGDSSPKEGAHGLVGVPWAPGGDLEGCAPDTRFFVPEPGGRGAAPWVALVARGGCTFKDKVLVAARRNASAVVLYNEERYGNITLPMSHAGTGNIVVIMISYPKGREILELVQKGIPVTMTIGVGTRHVQEFISGQSVVFVAIAFITMMIISLAWLIFYYIQRFLYTGSQIGSQSHRKETKKVIGQLLLHTVKHGEKGIDVDAENCAVCIENFKVKDIIRILPCKHIFHRICIDPWLLDHRTCPMCKLDVIKALGYWGEPGDVQEMPAPESPPGRDPAANLSLALPDDDGSDDSSPPSASPAESEPQCDPSFKGDAGENTALLEAGRSDSRHGGPIS
Protein: Histone deacetylase (EC 3.5.1.98) (A0A8I5XW09)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MNSPNESVEVKPVLPAAMPSSMGGGGGGSPSPVELRGALAGPMDPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLLGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGTGPGVSSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGSTLTGKFMSTSSIPGCLLGVALEGDTSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQMQLGKILTKTGELSRQPTTHPEETEEELTEQQEALLGEGALTMPREGSTESESTQEDLEEEEDEEEDEEDCIQVKDEDGESGPDEGADLEESSAGYKKLFADAQQLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGSMKSPTDHPTVVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSINAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTGEKEEAETVSAMALLSMGAEQAQAAATQEHSPRPAEEPMEQEPAL
Protein: Small integral membrane protein 2 (Q9BVW6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEAGERIDASQLPHRVLETRGHAISILFGFWTSFICDTYIVLAWISKIKGSPDVSASSDEPYARIQQSRRQCHAEEDQSQVPEAG
Protein: Uncharacterized protein (Q583Y5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKVSSFIVQLRPGFFRLMIHAKPGARSTALAAQPQALDEALEVRLAAPPVDGKANTELVEFMQTLLEQQLATLRITQKQHLRKSGCEDGEDEVYTYEHYAKKKKSKNNKRMNEDSKSGEAKVEYPDDKVRVSLVSGLTSRNKVLEVTFPGTEEDLLAVLKSADFS
Protein: Zn(II)2Cys6 transcription factor (Eurofung) (C8V955)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- ATP citrate synthase
- ATP citrate synthase
- Multifunctional tryptophan biosynthesis protein
- dihydrolipoyllysine-residue succinyltransferase
- L-lactate dehydrogenase
- malate dehydrogenase
- Malate dehydrogenase
- malate dehydrogenase
Sequence:
MGQPETDDTQLPVSHQSHQPLKTKRFTRSQVACDWCHFNHARCDQTFPCSRCLNKGTRCEFTRGRRKRGRLPKVGTPGTARIEGINSSHTVSSASEGRGASVTQSLQTPEDPRPAPAHVLNHQDQMHAHDVVILSPGMEYLSSGSIVWPMQEAEKSPSAVGSLSPTRGAVSPCAGTAALTAGGSSAPLDYTNFAGLADLDAFILANLAAEPPIATLEPYSSLQYPVLQPLIPFIRAELTPELACGLLELYFTSAFSTHMHPVCHSIPCYVLRKASFLSRTNYRPSSPALLASMLWVASSDDHALASPLTTPYCRKKISRLLGSLTLDLMRSSTHTPFDKNGHAAAGGTAGSPASPDAFRDFALYLPTVSGGVQGFGYSVGSLDDVITCIHVASVLSLNDQNAFDLRWWQAAFTLARELQLNREIEPGPSIDSQGACFPHSPAASTPKPLDCVCRRSYGSTVLITEEQREERRRVWWLLYMMDRHLALCHNRPLMLLDSESKGLLLPLDEEAWWAGEIHSNSPDFNGPQCVMSGTGSLRRVFSDSTCHDPSLFGFFLPLMTILGQLLDINQARNHPMLGLGVLGEKTWETRLHEVLGRLDQYEASLYGFVARCGDRKSPSLADDDTAHCLHVQTRFWLAKTVKAYASYYIDLLHILQNGKWDPRSLAADHTLWASSLNLASAVPQALRAAESVRQVLHFDPNLSFMPTFFSAQLLQGGFYFLVLLEQLQDQAGEPFLSACETMLRAAESCTVTLNNGYLKGFCLVMRSTVAQARGRPITQYEVRQRWSAIAALHAWSG
Protein: Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (Q38BZ6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Pyruvate kinase
- pyruvate dehydrogenase
- 6-phosphogluconolactonase
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase, putative
Sequence:
MDGDLSQLGFLQEVDRFFDVLREKTLRDRPDNIPEYVMQNCRKVADTLRKDSCDIIPDAAAPELKERALTIVVLGASGDLARNKTFPALFQLFCNGLIPRTINIVGYARTKMPDVEQWKKESLAKHFPRTKDRCPHIEAFLKTITYISGSYDGAEDFFRLNDVITKFEESFPGKQKGGNRLFYLALPPSVFMHACTGIRTHVMQKPGLGWVRIIIEKPFGHDTESSNELSRQLEPLFEESQIFRIDHYLGKEMVQNIVVTRFANRVFSALWNNNNIACVRITFKESIGTEGRGGYFDKAGIIRDVVQNHLTQILSLLAMEKPRSLSPEDIRDEKVIVLRHVNPVTPADCVLGQYTRSEDGSIPGYLEDPTVPRGSKCATFVVLRLFINNDRWDGVPFIIEAGKAVERRYLGIRIQFKDEIRPFGVAAQRNELIIRAQPSEAMYLRLTAKTPGVLSDTHQTELDLSYEHRYNITLPDAYESLIHEALLGRSTNFVRKDELDAAWRIYTPLLEAIERGETTTYPYSAGSKGPAEAQKFVDDTGFKPLTGDIYQQRKLHHL
Protein: Neurotrophin-4 (NT-4) (P24727)
Organism: Xenopus laevis (African clawed frog)
Function: NT-4 could play a role in oogenesis and/or early embryogenesis. NT-4 interacts with the low affinity NGF receptor and elicits neurite outgrowth from explanted dorsal root ganglia with no and lower activity in sympathetic and nodose ganglia, respectively.
Interaction partners:
Sequence:
MILRLYAMVISYCCAICAAPFQSRTTDLDYGPDKTSEASDRQSVPNNFSHVLQNGFFPDLSSTYSSMAGKDWNLYSPRVTLSSEEPSGPPLLFLSEETVVHPEPANKTSRLKRASGSDSVSLSRRGELSVCDSVNVWVTDKRTAVDDRGKIVTVMSEIQTLTGPLKQYFFETKCNPSGSTTRGCRGVDKKQWISECKAKQSYVRALTIDANKLVGWRWIRIDTACVCTLLSRTGRT
Protein: VhaAC45-related protein, isoform B (Q0KHY8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Probable V-type proton ATPase subunit d 2
- ATPase H
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit E
- V-type proton ATPase subunit H
- V-type proton ATPase subunit G
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit B
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MQLILVATLLCLIIGSCSASISGPFIFWGHSRVSSQQTQALVESSSRELPLTQLFTEAKAIVVFVRNTTNRLEGTRYPKFQNLVKSGAWTYLPQRSLAAEPFGLNANIEVVSLSGHGEEDDSEILLAYNEAVNTYGRGEVLGILGSREEEAHFLAKREAAPGGEEEEKAKAAEGSEETEASFIYVAEGNKAVLSLNGPLELRVTNDTLKLEEHIKQITFDDQRAKGYGRLSITFMHSGEKCTLRFKFSLIRGSWTLRNVEVEYRELKSVLVARGDEYTLPSAPLGFSYRCSAESVNFLNPARNETIQSLLLSDFQVQPWLNGRPEYGEVYDCIGFVSAPILAGLFVVTLLLGILGLGISAMLSMHTPNRFESSRSKQSRAAMFIQITYVAFKPLALFTLAIEFFLIHLLFVLIVLYVYVLWYY
Protein: Signal recognition particle 19 kDa protein (A0A087WYR0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MACAAARSPADQDRFICIYPAYLNNKKTIAEGRRIPISKKNKMYSREWNRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK
Protein: Protein phosphotransferase ChpT (EC 2.7.99.-) (Histidine phosphotransferase) (Q2YQA5)
Organism: Brucella abortus (strain 2308)
Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. ChpT efficiently and specifically shuttles phosphoryl groups from the CckA kinase to the receiver domains of both CtrA and CpdR. Does not bind ATP. Overexpression of chpT results in a defect in cell morphology, DNA content, and intracellular survival in human macrophages.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:26124143}.
Interaction partners:
- Cell cycle response regulator CtrA
- Response regulator receiver protein CpdR
- histidine kinase
- histidine kinase
- Cell-division control histidine kinase PdhS
- Polar-differentiation response regulator DivK
- histidine kinase
- DUF1134 domain-containing protein
- Membrane protein, putative
- DUF1153 domain-containing protein
Sequence:
MSLPVTLSALDLGALLCSRICHDIISPVGAINNGLELLEEGGADEDAMALIKSSARNASARLQFARIAFGAAGSAGVQIDTGDAQNVATEYFRNEKPEFTWEGARVLLPKNKVKLLLNMLLIGNGAIPRGGSLAVRLEGSDTDPRFVITVKGRMLRVPPKFLELHSGAAPEEPIDAHSVQPYYTLLLAEEAGMKISIHATAEDIVFSAE
Protein: Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta) (P79384)
Organism: Sus scrofa (Pig)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate. Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:13752080}.
Interaction partners:
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Methylcrotonyl-CoA carboxylase subunit 1
- Methylmalonyl-CoA epimerase.
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-coenzyme A oxidase
- Pyruvate carboxylase
- Uncharacterized protein
- Ethylmalonyl-CoA decarboxylase
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MAAAVRVTAARARLRVVVRSLHAGVRSLCTQPVSVNERIENKRQAALLGGGQRRIDSQHKRGKLTARERISLLLDPGSFIESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMTVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVSASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGARTHTTMSGVAHRAFDNDVDALCNLREFFNYLPLSNQDPAPIRECHDPSDRLVPELDTVVPLESTRAYDMVDIIYSIVDERDFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
Protein: Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta-glucanase) (Beta-1,3-endoglucanase) (allergen Hev b 2) [Cleaved into: Glucan endo-1,3-beta-glucosidase minor form 3; Glucan endo-1,3-beta-glucosidase minor form 2; Glucan endo-1,3-beta-glucosidase minor form 1; Glucan endo-1,3-beta-glucosidase major form] (P52407)
Organism: Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Function: Possesses beta-1,3-endoglucanase activity in vitro. Is thought to be an important plant defense-related product against fungal pathogens (Probable).
Subcellular location: Vacuole {ECO:0000305}.
Interaction partners:
Sequence:
MAISSSTSGTSSSFPSRTTVMLLLFFFAASVGITDAQVGVCYGMQGNNLPPVSEVIALYKKSNITRMRIYDPNRAVLEALRGSNIELILGVPNSDLQSLTNPSNAKSWVQKNVRGFWSSVLFRYIAVGNEISPVNRGTAWLAQFVLPAMRNIHDAIRSAGLQDQIKVSTAIDLTLVGNSYPPSAGAFRDDVRSYLDPIIGFLSSIRSPLLANIYPYFTYAYNPRDISLPYALFTSPSVVVWDGQRGYKNLFDATLDALYSALERASGGSLEVVVSESGWPSAGAFAATFDNGRTYLSNLIQHVKGGTPKRPNRAIETYLFAMFDENKKQPEVEKHFGLFFPNKWQKYNLNFSAEKNWDISTEHNATILFLKSDM
Protein: ADIPOR-like receptor IZH1 (Implicated in zinc homeostasis protein 1) (Q03419)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Zinc-responsive transcriptional regulator ZAP1
- Uncharacterized protein YDR274C
Sequence:
MSITTTRRRNQDSVCCKATRASIKVEAVSGQTVFEKQKLLHNFDELPEWQKDNDKILTGYVRETLSWKKCLYSLFYWNNETVNIYTHLVPAIVYFVFAITLTNYFLIPVFPSTSWSDYTVINIFLMGAFSCLMCSSCFHCMKQHSEKQSNFWSKLDYLGIISLISCSMIPIIYFGYFDHISYFSLFTIVTLVLATFCTVCVLHDKFNTSTFRPFRAMFFILFGFSGLLPLTTGFFKFGIQGVLNRIKVSFVFWEALFYISGAVIYGFRIPETLAPGKFDFFGSSHQIFHIMVVLGSVCHLKAIIDSYKLMHSHIHP