wanglab/gogpt-training-data huggingface dataset:
Protein: Polyribonucleotide 5'-hydroxyl-kinase Clp1 (EC 2.7.1.78) (Polyadenylation factor Clp1) (Polynucleotide kinase Clp1) (Pre-mRNA cleavage complex II protein Clp1) (Q92989)
Organism: Homo sapiens (Human)
Function: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double-stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a key role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Its role in tRNA splicing and maturation is required for cerebellar development. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by DICER1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03035, ECO:0000269|PubMed:11060040, ECO:0000269|PubMed:24766810}.
Interaction partners:
- Pre-mRNA cleavage complex 2 protein Pcf11
- tRNA-splicing endonuclease subunit Sen2
- tRNA-splicing endonuclease subunit Sen15
- Cleavage stimulation factor subunit 2
- tRNA-splicing endonuclease subunit Sen54
- tRNA-splicing endonuclease subunit Sen34
- General transcription factor 3C polypeptide 3
- Cleavage and polyadenylation specificity factor subunit 6
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MGEEANDDKKPTTKFELERETELRFEVEASQSVQLELLTGMAEIFGTELTRNKKFTFDAGAKVAVFTWHGCSVQLSGRTEVAYVSKDTPMLLYLNTHTALEQMRRQAEKEEERGPRVMVVGPTDVGKSTVCRLLLNYAVRLGRRPTYVELDVGQGSVSIPGTMGALYIERPADVEEGFSIQAPLVYHFGSTTPGTNIKLYNKITSRLADVFNQRCEVNRRASVSGCVINTCGWVKGSGYQALVHAASAFEVDVVVVLDQERLYNELKRDLPHFVRTVLLPKSGGVVERSKDFRRECRDERIREYFYGFRGCFYPHAFNVKFSDVKIYKVGAPTIPDSCLPLGMSQEDNQLKLVPVTPGRDMVHHLLSVSTAEGTEENLSETSVAGFIVVTSVDLEHQVFTVLSPAPRPLPKNFLLIMDIRFMDLK
Protein: Uncharacterized protein C26H5.07c (O13989)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}.
Interaction partners:
Sequence:
MAILKSALVGFICFLHFFIVNASDNKSLLTEDIMASQVCNGMFAKKGKTSEITLKIDSYTSDFGGAIRLLIFNWKDVNAIGMEDDDGEKHYICNYEDIEAGVCKDDDYGLYLINQTAPHDSIYSAAVDAESMVSPLKYPVEQSGLYCVFTAPLEGSSEAYKITVTWENYFGNLDATDYPHLFLNPILLAINCLIGIWWSFIMFRYRHDLLQVQKYISGVVALSIVCTMVSTGYFYFANSKGYTTGSKVFAFFLSLAQSARQSYFGFLLLIVSLGYSIVVPSLGSLLRKCQILAGLQFVSSCFFLSSLFISPSNKESLVILFAAPVFLITLFAMFLWIVLALNNTIRDLRIRKQTVKAQMYTRLWIVICFGIVAYASIVAANAILIGIYGQMNYYLKYWKLLWFLNYGYTDILVLILMLTILYLWRPTENNRRFAMSEQVAQDVDEFEMTSSLSNDSLHLHHERPTSPANPHIIHGSADEHQALFAVDDESDDDASTLATSKQKPA
Protein: Enhancer of polycomb-like protein (A0A0B4KET9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361124}.
Interaction partners:
Sequence:
MSKLSFRARHLDPSKQMPIYLAEELPDLPEYSAINRAVPQMPSGMEKEEESEHHLQRAICTGLIIPTPEVLQTDQPFYDAYYPPDYKMPRQMIHMQPLGLDTEVPDYDMDSADEDWLSQQQRLELTELKFEQMMDRLEKSSGQTVVTLNEAKSLLNQDDETSISVYDYWLNKRLKMQHPLILTVKTESRPGASSNNPYLAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLQRATTILEMVRRREETKRDHLKMTVNIFEKRVEMRDFNGAVYSELNSQYKNTRPAYNPLYTNQYSQGAAAVGTAGAILAALPTGLLPGGAGAAGNANVFGSASQYLNSSNLTMDAISGSGNGNSSRKEKRPYKKRKHKLPRDKQQHQQQQTQQHQQQQYLPASGGAGVSPAHHLPHHLHHLSRQQSASPAANDSIADSEEEDYFGAGAQNGNKLGSESEEETPFAFRRRSSCVYLPTRQRDGRYPWDSADEDMAPSGACSDAKYRYTLTSLNYPRPRCIGFARRRLGRGGRILLDRATTNFDDFWSQLDYTVMESVTVNKCRDKIKQRDPDQLCKPSSPPTVVDLVPAGKPVDGEHPVPELIKEEPSSDTEKPVAATESGRESKERELEEKFENDVDDEFVASDDENVSRLGIYSSAVTLPQSCADLRQKRRRLRRKKQQLRELNAAKRLKRSSEAVATAEDVQLEDEDTKPDLRPLPRAYLQRLALILGQKLKVEEDDNTEVSENVAPELLEMNDPEQLQPPRANHQQHHRSNHNNNNNTVLNNNNSSSSNVMNKDVSISEKINVIKQEAEELVGGKCEDQPVASTSAAAAAARAAEAAAAAEAASSTTTLAAPNPGPSLEEVAKTIKREMIDADDSNEPLSSIRTAAVMLSTQTSVSELMDDEAEDDVNLAQLSSIIRHTAVKKELEAQQHQQQVQHEQMQAARKMEEDEAAPCLNQLPDVIRLRNIRNSQVHARPKDLFVQAPVDEEFNADYMGGLSPTSSQRLDICNELLSEIRRDWLHFRPKTPTDELSDSQDCEVGKTCDSHAVDWTQDTPISVELNRLGKREAEESDSSSYFLSSGFKYRDLESDAQLLQTVQAQDYARGSSKSPNCSGSGSGSALEFNLSGGDSLNDINNLLGCDDEDDNHEHMLDNILQECAMDDPKALNQATNFWNGILDGEAAVDEVEMADQLLDCIDEKKSKVGAADTSKRAGRNRKARLIQAPVGSSAFTVCPTAETLKERELFFSQAPPVEVPPKEKTPAEVELPEVVVKETANLPVKVEAVEKPQSEVLPVAPQPQQLQPQAITLPTTQLINIPAQISTQKQHQQPQVTQLLNQFANAGPQIIARTEYGGGAAVGDIVTITPHTGSSPLPTLTAQQQLQHQLAQAQLRNVTVQQRQATPQNPNQNQNPQQQLLFQMQRDPSRSLTPLQAAGAGATGNHLIYTTSCGEIVTAGAAASASQKVTYAIQKAGVSSGGATTASIGPNTVITLSNVKVQNDDISSGGSGNSGSSVNIINTASGQQLAVHSIAGMQQQGQQQVQQVTTSTPLLVATPTRNNVQQQQQQLVQQQPIVWRQVSGTNTAVATTAVLSTTVDSSPKAVTNQILWTSRATQKRQLNGPENTDINKLLLNRKLPRKQQIQQQHQQIQLTKQQLQQLVQHEELDDLVATSTGNSGDQMETGDGLQQQQQQQQQQQQLQKLSKVIKMSQFPLLVSDVSLQQQQSVSGQAQQQQLKPNSAAAIAANHNYSLHPASTAIITAQATPQQANKIFLTSSNSGGGGSAGNFTIATASELQAAAAGQKLHYKELPNSNLKLNFVSSAGTGEQTQQVGATTVLLNKSQQQQQQQQHQKLKTLATTGNSQTGQGDKRVLYTSLLNVKPLQKNNSGQMQMQLGPGGLQQVLRGRLNNSAIITRTLPLGTTVNSTGGAVGPTTTTIRQLVTTNANNVSSQDGNLLSAKEVGKALTVEQVIASANNGGVVLPTSNNNNNNNGSGAGGNGGPLNSGVNATGAGGGGSTGAGVGGAGVTSTINRXDADGSGSNS
Protein: Putative NrdI-like protein (Q97T03)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKTISLVYISLSGNTESFVTRLKDYLLSQYKGIEVQKIHIKDLVKEGKNFYEMDHPYVAFLPTYLEGGNGVDNGDVEILTTPVGDFIAYGNNASKCFGVVGSGNRNFNNQYCLTAKQYSQRFGFPVLADFEMRGMLEDIKHVAAIIADLYELEKEN
Protein: Single-stranded DNA-binding protein (A4D1U3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00004436}.
Interaction partners:
Sequence:
MFRRPVLQVLRQFVRHESETTTSLVLERSLNRVHLLGRVGQDPVLRQVEGKNPVTIFSLATNEMWRSGDSEVYQLGDVSQKTTWHRISVFRPGLRDVAYQYVKKGSRIYLEGKIDYGEYMDKNNVRRQATTIIADNIIFLSDQTKEKE
Protein: GH01039p (Q961X5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAAPFLPEILTMTSRICLSSTHAWQGENGPPLASSAQAVACQFFRCVLHQLAPNGIFLQVFQTQMKMKIRHHHFRSIAKALQDFQDLNSTSPIYMVCESLTSKKSLPIEQLPVIFRNMAEYLNLQCVPTEAGVGLAVWSQAMQAMESLLRQVIVIMPSLTNAEYMLDIMAATLRLNCVPKTLLDPYSKIMAYCVQHTNLEYQTLYELCTLNIRSFSKDRDKNLLCRQMIFEFVQALKFKSNIPDHNLLTIIGFVLLDAGGTLPPGAAPGLPDAAPMMTTNSADCLRQYINDVIDFLADFHTLSKIKNFKNGQTSSGLGEDTLGGVLKGAVAQYLALEMSRGNSRDNKAVSRYLPWLNNAPSSLQQGPKEFTECVGHMRLLSWLLLGSLTHMALMQRRQETHSIPTPLPQQNSQGTGPAASVHYQHQGVTYSQPVPQEASCHIADHIQVIFAGFAEQSKTSVLHMSSLFHAFTLCQLWTVYLEQMAHNTNSNAEGSTLGVLFEFWAKVTPCILQLVSHAKPTVNKDQPQTPLDFQTQSANSKLSEMVNLHFLSLLEALKDTNSTVLGKLLPMWSPVLSSQTQLSDTLHVRLQNVRDYAPDYEEQQTYKSEALLKWLQRLQFKMGQIELQASTATQFYSI
Protein: Putative nickel-responsive regulator (B5Z8Y5)
Organism: Helicobacter pylori (strain G27)
Function: Transcriptional regulator.
Interaction partners:
Sequence:
MDTPNKDDSIIRFSVSLQQNLLDELDNRIIKNGYSSRSELVRDMIREKLVEDNWAEDNPNDESKIAVLVVIYDHHQRELNQRMIDIQHASGTHVLCTTHIHMDEHNCLETIILQGNSFEIQRLQLEIGGLRGVKFAKLTKASSFEHNE
Protein: Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein) (D0ZSY8)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Function: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (periplasmic or acid stress or heat shock) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E (Probable). In this organism acid stress response does not require DegS degradation.
Subcellular location: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MQKEKLSALMDGETLDSELLKALTHDPEMQKTWESYHLIRDSMRGDTPDVLHFDISARVMAAIENEPVRQVSPLIPEAQPAPQQWQKMPFWKKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEAAPVGSQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ
Protein: Pro-neuregulin-1, membrane-bound isoform (Pro-NRG1) [Cleaved into: Neuregulin-1 (Acetylcholine receptor-inducing activity) (ARIA) (Glial growth factor) (Heregulin) (HRG) (Neu differentiation factor) (Sensory and motor neuron-derived factor)] (Q6DR98)
Organism: Mus musculus (Mouse)
Function: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. Perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Binds to ERBB4 and ERBB3. Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling (By similarity). Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1, and ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons (By similarity).
Subcellular location: [Pro-neuregulin-1, membrane-bound isoform]: Cell membrane {ECO:0000250|UniProtKB:Q02297}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q02297}. Note=Does not seem to be active. {ECO:0000250|UniProtKB:Q02297}.; SUBCELLULAR LOCATION: [Neuregulin-1]: Secreted {ECO:0000250|UniProtKB:Q02297}.
Interaction partners:
Sequence:
MSERKEGRGKGKGKKKDRGSRGKPAPAEGDPSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRRNKPQNVKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNDLTTGMSASTERPYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLIKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKHLGIEFMEAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRQKLHDRLRQSLRSERNNMVNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREVETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESIISESHSVIMMSSVENSRHSSPAGGPRGRLHGLGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSVAVSPFVEEERPLLLVTPPRLREKKYDHHPQQLNSFHHNPAHQSTSLPPSPLRIVEDEEYETTQEYEPIQEPIKKVTNSRRAKRTKPNGHIANRLEMDSNPSSVSSNSESETEDERVGEDTPFLGIQNPLAASLEVAPAFRLAESRTNPAGRFSTQEELQARLSSVIANQDPIAV
Protein: Proto-oncogene c-Rel (V-rel avian reticuloendotheliosis viral oncogene homolog) (V-rel reticuloendotheliosis viral oncogene homolog) (Q6DGE6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- V-rel avian reticuloendotheliosis viral oncogene homolog B.
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B inhibitor alpha
- N-lysine methyltransferase setd6
- Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon.
- Myeloid differentiation primary response protein MyD88
- Inhibitor of nuclear factor kappa B kinase subunit beta.
- NF-kappa-B inhibitor beta
Sequence:
MDVQSLSMHRDPHLMGEPCVQIFEQPKQRGMRFRYKCEGRSAGSIPGERSSDNNRTYPSIQILNVTGKGKVRVTLVTKSEPYKPHPHDLVGKDCKDGYYEAEFGPERRAIAFQNLGIQCVRRREVKDAIMQRVTRGINPFNVPREQLLQTEEYDLNVVRLCFQIYLQDESGMYSTMLPPIVSNPIYDNRAPNTAELRICRVNKNSGSVKGGDEIFLLCDKVQKDDIEVRFFTQTWEAKGSFSQADVHRQVAIVFKTPAYCDTSITAPVTVRMQLRRPTDQEVSEPMEFRYLPDDKDPYGCREKKRKIDMQMKSSFPSFSQEAMSFMNRTKAVSSTNLMNQRIKTEPPNFYRPPNQGVARQNQPVYYNKGLRSCPMMPHPSETTTQGALSQWTSQVTNTSVPNNVVSLQQVNPSPNMPSAGENGNSLPLLTSMDLEILQPNGPTGNQPRQDLLNQQVQQSQQPPQRQGQEGAWYNYSSQQPQNTQNGASGASGSLATGYQFTSGLEDDILQSLMGNHQPGIQLKQEPQGLSNMAPLVNSDCVQSFTALLNCNNGSTPEHMRQIDPNGANQRVSQIQYPSGNMGQESHLEHYTWHFPE
Protein: Solute carrier family 12 member 3 (Na-Cl symporter) (Thiazide-sensitive sodium-chloride cotransporter) (P59158)
Organism: Mus musculus (Mouse)
Function: Electroneutral sodium and chloride ion cotransporter. In kidney distal convoluted tubules, key mediator of sodium and chloride reabsorption (By similarity). Receptor for the pro-inflammatory cytokine IL18. Contributes to IL18-induced cytokine production, including IFNG, IL6, IL18 and CCL2. May act either independently of IL18R1, or in a complex with IL18R1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26099046, ECO:0000269|PubMed:36370249}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:29993276}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 1
- Serine/threonine-protein kinase WNK4
- Claudin-16
- Barttin
- Serine/threonine-protein kinase WNK1
- STE20/SPS1-related proline-alanine-rich protein kinase
- Chloride channel protein ClC-Kb
- Sodium-dependent phosphate transport protein 2A
- Uromodulin
- G protein-activated inward rectifier potassium channel 1
Sequence:
MAELPVTELPGDALCSGRFTISTLMGGDEPPPAACDSSQPSHLTHGSTLYMRTFGYNTIDVVPAYEHYANSALPGEPRKVRPTLADLHSFLKQEGSHLHALAFDGRQGRELTDGLVEDETGTNSEKSPGEPVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWLIILLSVMVTSITGLSISAISTNGKVKSGGTYFLISRSLGPELGGSIGLIFAFANAVGVAMHTVGFAETVRDLLQEYGTPIVDPINDIRIIGVVTVTVLLAISLAGMEWESKAQVLFFLVIMVSFANYLVGTLIPASEDKASKGFYSYHGDIFVQNLVPDWRGIDGSFFGMFSIFFPSATGILAGANISGDLKDPAVAIPKGTLMAIFWTTISYLAISATIGSCVVRDASGDVNDTMTPGPGPCEGLACGYGWNFTECSQQRSCRYGLINYYQTMSMVSAFAPLITAGIFGATLSSALACLVSAAKVFQCLCEDQLYPLIGFFGKGYGKNREPVRGYLLAYAIAVAFIIIAELNTIAPIISNFFLCSYALINFSCFHASITNSPGWRPSFRYYSKWAALFGAVISVVIMFLLTWWAALIAIGVVLFLLLYVIYKKPEVNWGSSVQAGSYNLALSYSVGLNEVEDHIKNYRPQCLVLTGPPNFRPALVDFVSTFTQNLSLMICGHVLIGPGKQRVPELRLIASGHTKWLNKRKIKAFYSDVIAEDLRSGVQILMQASGLGRMKPNILVVGFKRNWQSAHPATVEDYIGVLHDAFDFNYGVCVMRMREGLNVSEALQTHTTPEALIQEEQASTIFQSEQGKKTIDIYWLFDDGGLTLLIPYLLHRKKRWGKCKIRVFVGGQINRMDEERKAIISLLSKFRLGFHEVHVLPDINQKPQAEHTKRFEDMIAPFRLNDGFKDEATVTEMRRDCPWKISDEEINKNRIKSLRQVRLSEILLDYSRDAALIILTLPIGRKGKCPSSLYMAWLETLSQDLRPPVLLIRGNQENVLTFYCQ
Protein: Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase) (Q05728)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic
- AICARFT/IMPCHase bienzyme family protein
- Amidophosphoribosyltransferase 3, chloroplastic
- Amidophosphoribosyltransferase 2, chloroplastic
- Amidophosphoribosyltransferase 1, chloroplastic
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- phosphoribosylaminoimidazole carboxylase
Sequence:
MEARILQSSSSCYSSLYAVNRSRFSSVSSPKPFSVSFAQTTRTRTRVLSMSKKDGRTDKDDDTDSLNYKDSGVDIDAGAELVKRIAKMAPGIGGFGGLFPLGDSYLVAGTDGVGTKLKLAFETGIHDTIGIDLVAMSVNDIITSGAKPLFFLDYFATSRLDVDLAEKVIKGIVEGCRQSECALLGGETAEMPDFYAEGEYDLSGFAVGIVKKTSVINGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLARSNLSLKDALPGGSSTLGDALMAPTVIYVKQVLDMIEKGGVKGLAHITGGGFTDNIPRVFPDGLGAVIHTDAWELPPLFKWIQQTGRIEDSEMRRTFNLGIGMVMVVSPEAASRILEEVKNGDYVAYRVGEVVNGEGVSYQ
Protein: Uncharacterized protein RSN1 (Rescuer of SRO7 at high Nacl protein 1) (Q03516)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as an osmosensitive calcium-permeable cation channel.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YMR007W
Sequence:
MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV
Protein: Bi-functional coumaroyl CoA and feruloyl CoA ortho-hydroxylase F6H2-1-8 (IbF6H2-1-8) (EC 1.14.11.61) (EC 1.14.11.62) (2-oxoglutarate-dependent dioxygenase F6H2-1-8) (2OGD F6H2-1-8) (G9M9M5)
Organism: Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Function: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA, but has no activity with caffeoyl-CoA.
Interaction partners:
Sequence:
MMPSTTLSTVLSDINEFVVKQGHGVKGLSELGLQTLPNQYVHPPEERLSSMDVVSDDSIPVIDVSNWEDPKVAKLICNAAEKRGFFQIVNHGIPLEMLEKAKAATYRFFREPAQEKKKYSKENCPTSHVRYSTSFLPQIEKALEWKDHLSMFYVSDQEAAQYWPPSCRDDALEYLKSCELVSRKLLEALMQGLNVNQIDDSKESLLMGSRRININYYPKCPNPDLTVGVGRHSDISTLTLLLQDDIGGLYVRKLEHEAWSHVPPVKGALVINIGDALQIMSNGRYKSIEHRVMANESNDRISVPVFVNPKPNDIVGPLPEVLASGEKPVYKPVLYSDYAKHFYRKAHNGKDTIAFARIE
Protein: Geranylgeranyl pyrophosphate synthase 4 (GGPP synthase 4) (GGPS4) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 4) (EC 2.5.1.10) (Dimethylallyltranstransferase 4) (EC 2.5.1.1) (Farnesyl diphosphate synthase 4) (Farnesyltranstransferase 4) (Geranylgeranyl diphosphate synthase 4) (EC 2.5.1.29) (Geranyltranstransferase 4) (Q9SLG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the trans-addition of the three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl diphosphate.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Dehydrodolichyl diphosphate synthase 8
- Phytoene synthase 1, chloroplastic
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Isopentenyl phosphate kinase
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
- Dehydrodolichyl diphosphate synthase 2
Sequence:
MEAQNIFLYLLIVFLSLHFVFTTLKGRLSPANTRRLIRLLHIPIKSPVAAAIFARKDTREFLDSSIKLVNEEDDFGFSFDFKPYMISKAETINRALDEAIPLIEPLNIHKAMRYAILAGGKRVRPILCLAACELVGGEERLAIQAACAVEMIHTMSLIKDDLPCMDNDDLRRGKPTTHKVFGESVAILSGGALLALAFEHLTEADVSSKKMVRAVKELAKSIGTKGLVAGQAKDLSSEGLEQNDVGLEDLEYIHVHKTGSLLEASAVIGAVIGGGTEKEIEKVRNFARCIGLLFQVVDDILDETKSSEELGKTAGKDKVAGKLTYPKVIGVEKSKEFVEKLKRDAREHLQGFDSDKVKPLIALTNFIANRNH
Protein: Rifin (Q8IK32)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYSNILLFFFPLNILVTSYHVYNKNKIYITPHHTTTTTLRMLSEYGVHTSIYKNDENMKSLKENFDRQTSQRFEEYEQRMIRKRKKYKEQCDKDIQKIIEKDKMDKSLAEKVETGCLKYGCGLGGVAGSVGLFGGFGIYGWKTAALAASKNAAVAEATAKGVAKAIDLVKSTFDVQNIAGQPLETVLNVINYTDVSNIYHLIYSQYKTTCISTSSTPVTGGPETFCISIWNKSLSGLGSNVVFVEETKVIEATVKTIVSSAEKVAGEALEKATEGVIKTSTATIESTYASCQIAIIASVVALLIIALVMIIIYLVLRYRRKKKMNKKAHYTKLLNQKIYSFKILNPFLCCMNSRCLNT
Protein: Calcium/calmodulin-dependent protein kinase II association-domain domain-containing protein (E7EM33)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTCFEPEALGNLIEGIEFHRFYFDGNRKNQVHTTMLNPNVHIIGEDAACVAYVKLTQFLDRNGEAHTRQSQESRVWSKKQGRWVCVHVHRSTQPSTNTTVSEF
Protein: GH16255p (Jelly Belly) (Jelly belly, isoform B) (Q95NU8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- receptor protein-tyrosine kinase
Sequence:
MFCSLAQTLFCVLLIQGGLYALHLSGNGNGNGNGNGNGEKSLGEAKAVQVPSHPVGPSTGVAAAWQTAPSQQQQHQQHPGGSPPGGGSSPHGHRSAAAAAFDATTVRLNKEIADMAQLERERLMLLARAKQTAEQPPAGSNHRGHPFIAGRIQMQPSEELEVGDYPALLQQAARGYIFGNVQKQPPTPVTLEQDYEQLRDLENRPVKYYGRVVQPAEREEQVEALYEPLHSFGDFDDFSELEQEPQEPHLGEDELLRELDAYQYHGLEDETLPENPYRTLEQLELGAPDSLQQLFEQEQEQRDAPFKAMHTGKIHNPGNYNIRVQQKWARKRNGQGIAHNPEAEKQLQRQIFAQHFKPQRNGKLSLSANSEATASKHLKPSTRSGSKDNEKPHSELGSSASSAVSSATSSSGKQAAGDGLPKQQQVEQQSQQDKKDPSHKRSGSGSAGSMGSPGGGYSAQPPISHSIASQLMLRTARGQRQYDVPQIECPTAMDGMERFACPIPDRQGRYRCIDDHVLCDGFIDCPDGEDEDRRSCMFYKTTKAHLDVLADALLRWARGR
Protein: MutL homolog 3 (A0A1Y7VJX4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VTLGRMVYINRMTGLSTFVAPTDDLHTACTKDLTTVAVDVLLGNDAVDAAAAAVSEPLQSLFSEWSNPVFARYPEVAVDVSSGQAESLAVKIHNVLYPYRFTKEMIHSVKVLQQVDNKFIACLMSTRMDEDGRTGGNLLVLVDQHAAHERIRLEQLITDSYEKQDPQSAGRKKLLSSTIIPPLAITVSEEQRRLLRN
Protein: Cystatin-F (Cystatin-7) (Cystatin-like metastasis-associated protein) (CMAP) (Leukocystatin) (O89098)
Organism: Mus musculus (Mouse)
Function: Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein NKG7
- Transmembrane protein 119
- P2Y purinoceptor 12
- Triggering receptor expressed on myeloid cells 2
Sequence:
MWLAILLALCCLTSDTHGARPPDFCSKDLISSVKPGFPKTIETNNPGVLKAARHSVEKFNNCTNDIFLFKESHVSKALVQVVKGLKYMLEVKIGRTTCRKTMHHQLDNCDFQTNPALKRTLYCYSEVWVIPWLHSFEVPVLLCQ
Protein: Cold shock domain-containing protein 3 (AtCSP3) (Q94C69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Promotes freezing tolerance.
Subcellular location: Nucleus {ECO:0000269|PubMed:19556243}. Cytoplasm {ECO:0000269|PubMed:19556243}.
Interaction partners:
- Protein decapping 5
- DEAD-box ATP-dependent RNA helicase 7
- Heterogeneous nuclear ribonucleoprotein 1
- Large ribosomal subunit protein uL24z
- Small polypeptide DEVIL 16
Sequence:
MAMEDQSAARSIGKVSWFSDGKGYGFITPDDGGEELFVHQSSIVSDGFRSLTLGESVEYEIALGSDGKTKAIEVTAPGGGSLNKKENSSRGSGGNCFNCGEVGHMAKDCDGGSGGKSFGGGGGRRSGGEGECYMCGDVGHFARDCRQSGGGNSGGGGGGGRPCYSCGEVGHLAKDCRGGSGGNRYGGGGGRGSGGDGCYMCGGVGHFARDCRQNGGGNVGGGGSTCYTCGGVGHIAKVCTSKIPSGGGGGGRACYECGGTGHLARDCDRRGSGSSGGGGGSNKCFICGKEGHFARECTSVA
Protein: 1,2-dihydroxynaphthalene dioxygenase (1,2-DHN dioxygenase) (DHNDO) (EC 1.13.11.56) (P74836)
Organism: Sphingobium xenophagum
Function: Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the meta-cleavage of 1,2-dihydroxynaphthalene (1,2-DHN) to yield 2-hydroxychromene-2-carboxylic acid. Can also cleave 1,2,5-trihydroxynaphthalene (1,2,5-THN), 1,2,6-trihydroxynaphthalene (1,2,6-THN), 1,2,7-trihydroxynaphthalene (1,2,7-THN), 2,3-dihydroxybiphenyl, 3,4-dihydroxybiphenyl, catechol, 3-methylcatechol and 4-methylcatechol.
Interaction partners:
Sequence:
MSSVSELGYLGMSVTDLDAWRAYAAEVAGMEVVDEGESDRIYLRMDLWHHRIALIKGDTDDLAYMGWRLGDPTEFESMVEKLTNAGIAVTVASDAEARERRVLGLAKLTDPGGNPTEIFYGPQVDAHKPFHPGRPMFGKFVTGSEGIGHCILRQDDVEAAAAFYRLLGLRGSVEYQLHLPNGMVAMPYFMHCNERQHSVAFGLGPMEKRINHLMFEYTELDDLGLAHDIVRERQIDVALQLGKHANDLALTFYCANPSGWLWEFGWGARKAPAQQEFYTRDIFGHGNEAQGYGMDVPL
Protein: PBP1-interacting protein LSM12 (Q38E83)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Involved in post-transcriptional regulation of gene expression.
Interaction partners:
Sequence:
MPVCNNDSQLIGLGVSVTLADDTTVNGTVYTYNSSEGLLVLFQGFSGSNPNVKIIRTPFIKEVTALRDNEEKLPPQLEAKARLPSMQAARDRSLFKHASSQLRNAKDKRNQLLQTDDQKTPIAALDTLIKLERIYPDIHWDKDAGVIRFNQDVVVKGKPDWTSPAVVIAEGAGDISRSLMERVQKTLSKK