wanglab/gogpt-training-data huggingface dataset:
Protein: Grhpr protein (RCG54768, isoform CRA_a) (B0BN46)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Alanine--glyoxylate aminotransferase
- Glycerate kinase
- 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
- 2-Hydroxyacid oxidase 1
- Lactoylglutathione lyase
- 2-Hydroxyacid oxidase 2
- Putative hydroxypyruvate isomerase
- Glycerol-3-phosphate phosphatase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- D-amino-acid oxidase
Sequence:
MFAAAGLVKPARLMKVFVTGPLPAQGRAALAQATDCEVEQWNSDDPIPSKDLEQGVAGAYGLLCRLSDRVDKKLLDAAGANLRVISTLSVGVDHLALDEIKKRGIRVGYTPGVLTDATAELAVSLLLTTCRRLPEAIEEVKNGGWSSWSPLWMCGYGLSESTVGIVGLGRIGQAIARRLKPFGVQRFLYTGRQPRPQEAAEFQAEFVPIAQLAAESDFIVVSCSLTPATRGLCNKDFFQKMKNTAVFINISRGDVVNQEDLYQALASGQIAAAGLDVTTPEPLPPSHPLLTLKNCVILPHIGSATYKTRNTMSLLAANNLLAGLRGEPMPSELKL
Protein: FBD-associated F-box protein At2g26860 (Q84X02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDRISGLPDELLVEILHCLPTKEVVSTSILSKRWEFLWLWVPKLTFVMNHYESDLPIQDFITKNLRLLKPQVIESFHLQCFSSSFKPEDIKHWVVTTISRRVRELIINYCDLSWLDKPVVLLDLPNSLYTCTSLVTLKLIGHSIIVDVPRTVSLPCLKTLELDSVAYSNEESLRLLLSYCPVLEDLTIHRDMHDNVKTLVIIVPSLLRLNLPIDGAYSCDGYVIVTPALKYLKVPGLYREDFSYLLTHMPNVEEADLSVEQDVERLFESITSVKRLSLFVLLDIEDESMYHNGIYFNQLEHLNLHIYRDNWSKLLVRLLEDSPKLRVLKIVVDGEPSFDEEFEHVSWIYNDESSVPKCLLDSLEVFEFAGYTRRPEERDFVSFILKHACHLKSSSISRLSCYVLE
Protein: Prokineticin receptor 1 (PK-R1) (G-protein coupled receptor 73) (Q9JKL1)
Organism: Mus musculus (Mouse)
Function: Receptor for prokineticin 1. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase. May play a role during early pregnancy (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prokineticin-2
- Prokineticin-1
- Melanocortin-2 receptor accessory protein 2
- Endothelin-3
Sequence:
METTVGALGENTTDTFTDFFSALDGHEAQTGSLPFTFSYGDYDMPLDEEEDVTNSRTFFAAKIVIGMALVGIMLVCGIGNFIFITALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLRPRMKCQTAAGLIFLVWSVSILIAIPAAYFTTETVLVIVERQEKIFCGQIWPVDQQFYYRSYFLLVFGLEFVGPVVAMTLCYARVSRELWFKAVPGFQTEQIRRRLRCRRRTVLGLVCVLSAYVLCWAPFYGFTIVRDFFPSVFVKEKHYLTAFYVVECIAMSNSMINTLCFVTVRNNTSKYLKRILRLQWRASPSGSKASADLDLRTTGIPATEEVDCIRLK
Protein: LIMR family protein At5g01460 (Q9M028)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein OXIDATIVE STRESS 3 LIKE 4
- CASP-like protein 5A2
- Choline transporter-like protein
- Nuclear polyadenylated RNA-binding protein
- Protein RALF-like 31
- Protein OXIDATIVE STRESS 3 LIKE 3
- Ternary complex factor MIP1 leucine-zipper protein
- Putative RRM-containing protein family protein)
- AAA-ATPase At5g17760
- ADP-ribosylation factor-like protein 8c
Sequence:
MGDFNLALVIVAIVVCVIVFISSIYLLVNYQHPDDANQAYFPKFVVVFGLSIAMISILMLPADVANRHACRHSIYNGACNLTLPMKDLWLAVYIVDAVLVFFIIPFAMFFYEGDQDKALGKRIKSALIWVVTTAVVCALVLGILYGVIGKVDFSVRHLSSATTTFPTSWQFSNNQPCIGNTARQCSAYTANAASEKTWSMRTTFPEYVVALATIVGSVLFTIFGGVGIACLPLGLITAFIRRPKAVITRSQYIKEATELGKKARDLKKAADALHQEERSGAKGRKWRKNVKAVEKELLQLEEDVNLLEEMYPQGEQAETAWAFTVLGYLAKFVLGILGLIVSVAWIAHIIIYLLVDPPLSPFLNEVFIKLDDVWGLLGTAAFAFFCFYLLLAVIAGAMMLGLKLVFITIHPMKWGATLMNSFLFNVGLILLCSISVIQFCATAFGYYAQATAAQEIFGHTLQSLRGIKYLYKYNVFQIGFVVLAGLTFLYYIAFGWRRKKPSGRFQLST
Protein: Cohesin subunit SA-3 (SCC3 homolog 3) (Stromal antigen 3) (Stromalin-3) (Q9UJ98)
Organism: Homo sapiens (Human)
Function: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:12034751}. Chromosome {ECO:0000269|PubMed:12034751}. Chromosome, centromere {ECO:0000269|PubMed:12034751}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. It however remains chromatin associated at the centromeres up to metaphase I. During anaphase I, it probably dissociates from centromeres, allowing chromosomes segregation. {ECO:0000269|PubMed:12034751}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Double-strand-break repair protein rad21 homolog
- Meiotic recombination protein REC8 homolog
- Double-strand-break repair protein rad21-like protein 1
- Structural maintenance of chromosomes protein 1B
- Structural maintenance of chromosomes protein 1A
- Shugoshin 2
- Cohesin subunit SA-1
- Cohesin subunit SA-2
- Synaptonemal complex protein 3
Sequence:
MSSPLQRAVGDTKRALSASSSSSASLPFDDRDSNHTSEGNGDSLLADEDTDFEDSLNRNVKKRAAKRPPKTTPVAKHPKKGSRVVHRHSRKQSEPPANDLFNAVKAAKSDMQSLVDEWLDSYKQDQDAGFLELVNFFIQSCGCKGIVTPEMFKKMSNSEIIQHLTEQFNEDSGDYPLIAPGPSWKKFQGSFCEFVRTLVCQCQYSLLYDGFPMDDLISLLTGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSVHQDNNQRQYEAERNKGPGQRAPERLESLLEKRKELQEHQEEIEGMMNALFRGVFVHRYRDVLPEIRAICIEEIGCWMQSYSTSFLTDSYLKYIGWTLHDKHREVRLKCVKALKGLYGNRDLTTRLELFTSRFKDRMVSMVMDREYDVAVEAVRLLILILKNMEGVLTDADCESVYPVVYASHRGLASAAGEFLYWKLFYPECEIRMMGGREQRQSPGAQRTFFQLLLSFFVESELHDHAAYLVDSLWDCAGARLKDWEGLTSLLLEKDQNLGDVQESTLIEILVSSARQASEGHPPVGRVTGRKGLTSKERKTQADDRVKLTEHLIPLLPQLLAKFSADAEKVTPLLQLLSCFDLHIYCTGRLEKHLELFLQQLQEVVVKHAEPAVLEAGAHALYLLCNPEFTFFSRADFARSQLVDLLTDRFQQELEELLQSSFLDEDEVYNLAATLKRLSAFYNTHDLTRWELYEPCCQLLQKAVDTGEVPHQVILPALTLVYFSILWTLTHISKSDASQKQLSSLRDRMVAFCELCQSCLSDVDTEIQEQAFVLLSDLLLIFSPQMIVGGRDFLRPLVFFPEATLQSELASFLMDHVFIQPGDLGSGDSQEDHLQIERLHQRRRLLAGFCKLLLYGVLEMDAASDVFKHYNKFYNDYGDIIKETLTRARQIDRSHCSRILLLSLKQLYTELLQEHGPQGLNELPAFIEMRDLARRFALSFGPQQLQNRDLVVMLHKEGIQFSLSELPPAGSSNQPPNLAFLELLSEFSPRLFHQDKQLLLSYLEKCLQHVSQAPGHPWGPVTTYCHSLSPVENTAETSPQVLPSSKRRRVEGPAKPNREDVSSSQEESLQLNSIPPTPTLTSTAVKSRQPLWGLKEMEEEDGSELDFAQGQPVAGTERSRFLGPQYFQTPHNPSGPGLGNQLMRLSLMEEDEEEELEIQDESNEERQDTDMQASSYSSTSERGLDLLDSTELDIEDF
Protein: Ammonium transporter 2 member 4 (Ammonium transporter 2;4) (MtAMT2;4) (G7L1W7)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Involved in ammonium transport. May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9M6N7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nitrogen regulatory protein P-II
Sequence:
MELPSNLLPDEASPEWMNKGDNAWQLTAATMVGLQSIPGLVILYGSLVKKTWAINSAFMAFYAFASVLLCWVSWAYQMSFGEKMVFFLGKPNVALDEKFLLGKAFLGNFPNATMVFYQGVFAGLTLILIAGALLGRMNIRAWMLFVPLWVTFSYTVVAFSIWCPDGWLAKRGVIDFAGGYVIHLSAGVAGFTAAYWVGPRADKDRETFPAATNNMIMVLAGAGLLWMGWSGFNGGAPFVASTIASLAILNTHVCTAASITVWVMLDTFYFGKPTVFGAVQGMITGLVCITPAAGVVQGWAAILMGFISGSIPWYTMMVLHNKVNFLKKIDDPMAVFHTHAIAGALGGILTGFFAVPKLCRLFYMVPDWEKYIGLAYGLQNKGATQAGLKQMVIQIEAIVFVICYNVLMTSLICLIVRVIVPLRLNGDALQMGDKAIHGEDAFALHSEATKFVNIKRNQVYDTQDFSSIPESRSLGELQMV
Protein: Chorion transcription factor Cf2 (P20385)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional regulator; binds to the promoter region of Cp15. Also binds to its own promoter, thus having a probable autoregulatory role.
Subcellular location: Nucleus {ECO:0000269|PubMed:2120114}.
Interaction partners:
- Mitogen-activated protein kinase ERK-A
Sequence:
MIKSTTNPQEQRLPRPEDQSPAPPPPPPSSATTSTAAPATPTHQVATVIANMDTLKTAFLPNLSMDPNVHVSPHYCPMCHQQFERPQHVADHMQLCHGITLNAQGAIATLDGGHPQAQQHPKLSHPCFNCDEKFGNAVDLDEHHRLAHQTPAFLSRCLMCSIYGIHSATQQPNEYKCTQCGSICTTAMLAAGQQGFMEQQEAAVTPDDQLPAMAPRDMRLTPEEQHHQQQLQAEHHHQQQHQQQQQQQQQQQELLEQQQREMQEQAQQQQVHHHQQDQDLAGDQVALKVPPLTVKLNKNANGGAIVSHPQVIIKEEPLSLSDSGDVVNSVPVYAIQANPGVPAPASSGVLVGTQTVPADLAHKIRHKCPDCPKTFKTPGTLAMHRKIHTGEADATPKERPYTCSYCGKSFTQSNTLKQHTRIHTGEKPFRCGYCGRAFTVKDYLNKHLTTHTGEKPFHCGYCEKSFSVKDYLTKHIRTHTGEKPYTCPYCDKRFTQRSALTVHTTKLHPL
Protein: Probable serine/threonine-protein kinase DDB_G0279405 (EC 2.7.11.1) (Q54WW7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MGCIFTKPSPEQQKFDGEDYECENKKNLNLISYIRNLLFGNNSHQQLYNEIIPTTTSTTSTTTNSVYQNIGLDGYNNNNNNNNNNNNNNNIMNNYGYDDYGYSYEEDEDYYDEMPIPTIVAQPQPQPQPQPQPQPQPQQPIRIVSQNQQIPTTPPQQISQFNITGNKSPSSIGSRHRSKPKETLRAHKKRHKDGHKMVNEYVFVRKLGKGTFGKVKLAYHHDTHHLYAIKIFNKIRLKKQTMGIGRPNAFDDVLKEIAIMKKMNHINVVKLYEVINDPQEEYIYIVMEYIEGGSIMSANETSEDLARKYFRDIVFGLEYLHEQKVIHKDLKPENLLVNSEGVVKITDFGVSHIFDDDDVVRCSRGSPAFLAPELCRNESQPISGKGVDVWALGVSLYCLIFARTPFISKTNSLLDIYDQIVNHEPTYPREISNDLMDLFKRLLDKNPLTRIQIAEIKSHKWTTISGTWPMNELDHLILSVTDQEMIDAISTDHTIKPSDNTTTDEDDSDLSSSSGGESSGIIGSSNESKSMYNNVNSKQKIQNQNQNQNQNQNQNQNQNQNQNHNQNQNQNQNQNNNNNSLIEKSNISIPASSSSISNNDSCYENRNVYIKDEEMNMICNDSVIMDPIKELNKIDGLNYGCDFQIGKEYSDFQYNSGHFIYDLVDENESQISRESANDYYLPFKTNKYLNNKSIV
Protein: Oxidoreductase, DadA family protein (A0A0H2UQX6)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKKVAIIGAGIVGATAAYYLSRESDLEVTVFDHEQGQATKAAAGIISPWFSKRRNKAWYKMARLGADFYVDLLADLEKSGQEIDFYQRSGVFLLKKDESNLEELYQLALQRREESPLIGQLAILNQASANELFPGLQGFDRLLYASGGARVDGQLLVTRLLEVSHVKLVKEKVTLTPLASGYQIGEEEFEQVILATGAWLGDMLEPLGYEVDVRPQKGQLRDYQLAQDMEDYPVVMPEGEWDLIPFAGGKLSLGATHENDMGFDLTVDETLLQQMEEATLTHYLILAEATSKSERVGIRAYTSDFSPFFGQVPDLTGVYAASGLGSSGLTTGPIIGYHLAQLIQDKELTLDPLNYPIENYVKRVKSE
Protein: Phosphoglycerate mutase (EC 5.4.2.11) (EC 5.4.2.4) (Q9VAN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Enolase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Pyruvate kinase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Phosphoglycerate kinase
- Phosphoglycerate mutase
Sequence:
MGGKYKIVMVRHGESEWNQKNQFCGWYDANLSEKGQEEALAAGKAVKDAGLEFDVAHTSVLTRAQVTLASILKASGHKEIPIQKTWRLNERHYGGLTGLNKAETAAKYGEAQVQIWRRSFDTPPPPMEPGHPYYENIVKDPRYAEGPKPEEFPQFESLKLTIERTLPYWNDVIIPQMKEGKRILIAAHGNSLRGIVKHLDNLSEDAIMALNLPTGIPFVYELDENFKPVVSMQFLGDEETVKKAIEAVAAQGKAK
Protein: CID domain-containing protein (Q9XVN9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVVLTSDVVYSRLQDVKNPTQEAIETMSMWIMHYKDNASIDLIVDGWLNCFKTAGTDNKRIALFYVMNDVVQKAKMKHADTLIPAFQPAVLTAVGIGRKQDKVKAVMKRCIQIFKSRNVFSPASTTAMENLLDEGYEAEDQALEVDSDDLVKKITNFISARNVVADMMKCVNEGNFDYKEMCKHGMRDREEGGHILHEVHEAIDTMVQVRHSMEDQKKKMMALSETLELAKRVFLHQKREVLVVEEAYVNFRDGIKAVHTELLDMEAKKVYPGLLSPRNEDDRQTYGRSNNRSLSQQWGDNRNQIDMEMDEDERPQAPMMKPSLQALVGIASQPSLQSRIMQLGLKKIANGDEEMFQPTTTTTADTPLPSTFQPPPSKPAVINASKFSMPPPAITSAPLSDPRIRSDGEGPSQYAIALKQHGLPPPTGQQPVQNRMNAPPPAQPSPYQAIPQKPVEQTVYQGQFGGARDPRLANSVTPQSVAVAQQPPITGYQAQYEQIRDPRILQQAAPQQGYQATFEVQKPQLVSPQIQNNGYQARFEQSQLSPSIPQHQPVGQYHQQKNTYCQPPPQHHQYQQQSQQSHGYSSDYHSGDRRDDRGRDNYQNSRYDDRRGSSAPYNNQRGDRWRGSGSHHNDRNRNSGRDSWRGGNHRSGGGYHRY
Protein: Prkag2 protein (Q4QRB9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
RRMSFSGIFRSSSKESSPNSNPSTSPGGIRFFSRSRKTSSVSSSPSTPTQVTKQHPFPLESYKQEPERLESRIYASSSPPDTGQRFCLAFQSPVRLPLASPTHHAPLRTAALAAAPGPAEAGMLEKLEFQEEEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCSKLETLETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Protein: Uronyl 2-sulfotransferase (EC 2.8.2.-) (Chondroitin sulfate 2-O-sulfotransferase) (CS-2OST) (Q9Y2C2)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
Sequence:
MKKKQQHPGGGADPWPHGAPMGGAPPGLGSWKRRVPLLPFLRFSLRDYGFCMATLLVFCLGSLLYQLSGGPPRFLLDLRQYLGNSTYLDDHGPPPSKVLPFPSQVVYNRVGKCGSRTVVLLLRILSEKHGFNLVTSDIHNKTRLTKNEQMELIKNISTAEQPYLFTRHVHFLNFSRFGGDQPVYINIIRDPVNRFLSNYFFRRFGDWRGEQNHMIRTPSMRQEERYLDINECILENYPECSNPRLFYIIPYFCGQHPRCREPGEWALERAKLNVNENFLLVGILEELEDVLLLLERFLPHYFKGVLSIYKDPEHRKLGNMTVTVKKTVPSPEAVQILYQRMRYEYEFYHYVKEQFHLLKRKFGLKSHVSKPPLRPHFFIPTPLETEEPIDDEEQDDEKWLEDIYKR
Protein: Membrane-associated phosphatidylinositol transfer protein 3 (Phosphatidylinositol transfer protein, membrane-associated 3) (PITPnm 3) (Pyk2 N-terminal domain-interacting receptor 1) (NIR-1) (Q9BZ71)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro) (By similarity). Binds calcium ions.
Subcellular location: Endomembrane system {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- C-C motif chemokine 18
- Phosphatidylinositol transfer protein alpha isoform
- Phosphatidylinositol transfer protein beta isoform
- Cytoplasmic phosphatidylinositol transfer protein 1
- Protein-tyrosine kinase 2-beta
- Retinal guanylyl cyclase 1
- Retina and anterior neural fold homeobox protein 2
- Protein unc-119 homolog A
- Aryl-hydrocarbon-interacting protein-like 1
- Regulating synaptic membrane exocytosis protein 1
Sequence:
MAKAGRAGGPPPGGGAPWHLRNVLSDSVESSDDEFFDAREEMAEGKNAILIGMSQWNSNDLVEQIETMGKLDEHQGEGTAPCTSSILQEKQRELYRVSLRRQRFPAQGSIEIHEDSEEGCPQRSCKTHVLLLVLHGGNILDTGAGDPSCKAADIHTFSSVLEKVTRAHFPAALGHILIKFVPCPAICSEAFSLVSHLNPYSHDEGCLSSSQDHVPLAALPLLAISSPQYQDAVATVIERANQVYREFLKSSDGIGFSGQVCLIGDCVGGLLAFDAICYSAGPSGDSPASSSRKGSISSTQDTPVAVEEDCSLASSKRLSKSNIDISSGLEDEEPKRPLPRKQSDSSTYDCEAITQHHAFLSSIHSSVLKDESETPAAGGPQLPEVSLGRFDFDVSDFFLFGSPLGLVLAMRRTVLPGLDGFQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRFPLGDGQSLLLADALHTHSPLFLEGSSRDSPPLLDAPASPPQASRFQRPGRRMSEGSSHSESSESSDSMAPVGASRITAKWWGSKRIDYALYCPDVLTAFPTVALPHLFHASYWESTDVVAFILRQVMRYESVNIKESARLDPAALSPANPREKWLRKRTQVKLRNVTANHRANDVIAAEDGPQVLVGRFMYGPLDMVALTGEKVDILVMAEPSSGRWVHLDTEITNSSGRITYNVPRPRRLGVGVYPVKMVVRGDQTCAMSYLTVLPRGMECVVFSIDGSFAASVSIMGSDPKVRPGAVDVVRHWQDLGYMILYITGRPDMQKQRVVSWLSQHNFPQGMIFFSDGLVHDPLRQKAIFLRNLMQECFIKISAAYGSTKDISVYSVLGLPASQIFIVGRPTKKYQTQCQFLSEGYAAHLAALEASHRSRPKKNNSRMILRKGSFGLHAQPEFLRKRNHLRRTMSVQQPDPPAANPKPERAQSQPESDKDHERPLPALSWARGPPKFESVP
Protein: Protein CYCLOPS (LjCYCLOPS) (Protein IPD3 homolog) (A9XMT3)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: Involved in symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis, by binding, as a complex comprising CCaMK, CYCLOPS, and DELLA, to RAM1 promoter cis element thus promoting its expression. Acts downstream of CCAMK. Binds to the promoter of ERN1 and strongly transactivates ERN1, a transcriptional regulator required for nodulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:19074278}.
Interaction partners:
Sequence:
MEGRGFSGLYRNSSEELFLKTVMESPIGMPVPSMEMLGFKNVSQGFRADSEELFKRWLTNGEGYNSSSIGFSSRLSKRISTELVNGSNQLQVGVASDGRNNDKPFIQNNLLANDVSGDFNFPIRDPVDRELQPSNLFLAKAWFLSDQRMTRSRSSELRRRYSEMQNGLATQGIESICMDPQHGAEATKQEVANFNGYNYLSMCELPSQKGSFMSPSNSCSSNFNTPQFGDMDKVSSCVSMLKGTLQRRRLSSQLEKEAAEDDLNGIFYPQEPLFQTGFDQGQENWSNQTPVNVQVDSIGEVKDHGVLQTLEGSTNPVVDGFANQINQIYVGTASGEPSQSESSNAAPVISSGLDTCEGPINSNQTLCESSWKQVGVSKSSENTQNRVKGFREQIMDNLKDDKKRKSLERYGSITSAVSDDKGDTTKKRRVERSRKMAEAKERNSTPSVPSDMQAVLKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEELADEKERLLEEIERILSETEKM
Protein: Cingulin-like protein 1 (Junction-associated coiled-coil protein) (Paracingulin) (Q0VF96)
Organism: Homo sapiens (Human)
Function: May be involved in anchoring the apical junctional complex, especially tight junctions, to actin-based cytoskeletons.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q6AW69}. Note=Localizes to the apical junction complex composed of tight and adherens junctions (PubMed:22891260). In the liver and kidney, it is also found along non-junctional actin filament bundles in addition to the apical junction (By similarity). {ECO:0000250|UniProtKB:Q6AW69, ECO:0000269|PubMed:22891260}.
Interaction partners:
- Rho guanine nucleotide exchange factor 2
- Tight junction protein 1
- Tropomodulin-3
- Rho guanine nucleotide exchange factor 18
- Rho guanine nucleotide exchange factor 18
- Rac GTPase-activating protein 1
- Pleckstrin homology domain-containing family A member 7
- Aromatase
- Tropomodulin-2
- Occludin
Sequence:
MELYFGEYQHVQQEYGVHLRLASDDTQKSRSSQNSKAGSYGVSIRVQGIDGHPYIVLNNTERCLAGTSFSENGPPFPPPVINNLPLHSSNGSVPKENSEELQLPENPYAQPSPIRNLKQPLLHEGKNGVLDRKDGSVKPSHLLNFQRHPELLQPYDPEKNELNLQNHQPSESNWLKTLTEEGINNKKPWTCFPKPSNSQPTSPSLEDPAKSGVTAIRLCSSVVIEDPKKQTSVCVNVQSCTKERVGEEALFTSGRPLTAHSPHAHPETKKTRPDVLPFRRQDSAGPVLDGARSRRSSSSSTTPTSANSLYRFLLDDQECAIHADNVNRHENRRYIPFLPGTGRDIDTGSIPGVDQLIEKFDQKPGLQRRGRSGKRNRINTDDRKRSRSVDSAFPFGLQGNSEYLIEFSRNLGKSSEHLLRPSQVCPQRPLSQERRGKQSVGRTFAKLQGAAHGASCAHSRPPQPNIDGKVLETEGSQESTVIRAPSLGAQSKKEEEVKTATATLMLQNRATATSPDSGAKKISVKTFPSASNTQATPDLLKGQQELTQQTNEETAKQILYNYLKEGSTDNDDATKRKVNLVFEKIQTLKSRAAGSAQGNNQACNSTSEVKDLLEQKSKLTIEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNEKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELERRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVHARKEEKEAVSARRALENELEAAQGNLSQTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEMRLMEEELRDYQRAQDEALTKRQLLEQTLKDLEYELEAKSHLKDDRSRLVKQMEDKVSQLEMELEEERNNSDLLSERISRSREQMEQLRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRANLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLRLKKLPSKVLDDMDDDDDLSTDGGSLYEAPVSYTFSKDSTVASQI
Protein: Alpha-2B adrenergic receptor (Alpha-2 adrenergic receptor subtype C2) (Alpha-2B adrenoreceptor) (Alpha-2B adrenoceptor) (Alpha-2BAR) (P18089)
Organism: Homo sapiens (Human)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine > p-tyramine = phenylephrine > serotonin > p-synephrine / p-octopamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > spiperone > prazosin > alprenolol > propanolol > pindolol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23105096, ECO:0000269|PubMed:26811329, ECO:0000269|PubMed:27901063}; Multi-pass membrane protein {ECO:0000269|PubMed:23105096}. Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the cell membrane. {ECO:0000269|PubMed:23105096, ECO:0000269|PubMed:26811329, ECO:0000269|PubMed:27901063}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-12
- Protein transport protein Sec24C
Sequence:
MDHQDPYSVQATAAIAAAITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFRRTWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALEYNSKRTPRRIKCIILTVWLIAAVISLPPLIYKGDQGPQPRGRPQCKLNQEAWYILASSIGSFFAPCLIMILVYLRIYLIAKRSNRRGPRAKGGPGQGESKQPRPDHGGALASAKLPALASVASAREVNGHSKSTGEKEEGETPEDTGTRALPPSWAALPNSGQGQKEGVCGASPEDEAEEEEEEEEEEEECEPQAVPVSPASACSPPLQQPQGSRVLATLRGQVLLGRGVGAIGGQWWRRRAQLTREKRFTFVLAVVIGVFVLCWFPFFFSYSLGAICPKHCKVPHGLFQFFFWIGYCNSSLNPVIYTIFNQDFRRAFRRILCRPWTQTAW
Protein: Pannexin-2 (P60571)
Organism: Rattus norvegicus (Rat)
Function: Structural component of the gap junctions and the hemichannels.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6IMP4}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IMP4}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6IMP4}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Note=Localizes to Golgi apparatus and endoplasmic reticulum in multipotential neural stem and progenitor cells and to plasma membrane in terminally differentiated neurons. {ECO:0000250|UniProtKB:Q6IMP4}.
Interaction partners:
- Pannexin-1
Sequence:
MHHLLEQSADMATALLAGEKLRELILPGSQDDKAGALAALLLQLKLELPFDRVVTIGTVLVPILLVTLVFTKNFAEEPIYCYTPHNFTRDQALYARGYCWTELRDALPGVDASLWPSLFEHKFLPYALLAFAAIMYVPALGWEFLASTRLTSELNFLLQEIDNCYHRAAEGRAPKIEKQIQSKGPGITEREKREIIENAEKEKSPEQNLFEKYLERRGRSNFLAKLYLARHVLILLLSVVPISYLCTYYATQKQNEFTCALGASPDGPVGSAGPTVRVSCKLPSVQLQRIIAGVDIVLLCFMNLIILVNLIHLFIFRKSNFIFDKLHKVGIKTRRQWRRSQFCDINILAMFCNENRDHIKSLNRLDFITNESDLMYDNVVRQLLAALAQSNHDTTPTVRDSGIQTVDPSINPAEPEGSAEPPVVKRPRKKMKWIPTSNPLPQPFKEQLAIMRVENSKTEKPKPVRRKTATDTLIAPLLDAGARAAHHYKGSGGDTGPSSAPPAASEKKHTRHFSLDVHPYILGSKKAKTEAVPPALPASRSQEGGFLSQTEECGLGLAAAPTKDAPLPEKEIPYPTESALPSGGPFHVCSPPTASAAASLSPSSLGKADPLTILSRNATHPLLHISTLYEAREEEEGGPCAPSDMGDLLSIPPPQQILIATFEEPRTVVSTVEF
Protein: Zinc finger CCCH domain-containing protein 41 (AtC3H41) (Q9LVX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Zinc finger C3H1 domain protein
- Uncharacterized protein At1g21580
- Polyadenylate-binding protein 1
- At5g59460)
- polynucleotide adenylyltransferase
- Nucleotidyltransferase family protein
- DExH-box ATP-dependent RNA helicase DExH9
Sequence:
MELSVSSPKQSVLSPPDCMSDPEEEHEISEEEDDDRNHKHRRKEETRSQSLEQDSSDQAFSRPYRKNYRHYENGNSFSEHEKRSFGTGSGQRVQFDNQRMRSNPMFSRDSGPGRGRGNYGSWAQRDSRFNPVDLSSHMVQVGSMGQGMFGGRGLAGVSAAQSAPWPPFGMIPGVPNGGLDGFHHLQGSLRPPLNAPLNMGIPRQRCRDFEERGFCLRGDMCPMEHGMNRIVVDDVQSLSQFNLPVSVPGAPHLAASSKQVPAQFGGASFMNPKGAHGRTNEGGMAVDGLGYGDAYPSAGGTDFYDPDQPLWNNSTGETSGAISTLNSHGVDENVAPLDDSNQDAAENGCGIRDSRSTSQSVWGRMKGSNSQANSKEKADAVLNSSAVPEDQLKEVSVNSSRHGKQNHVGESVAKVVDSSNISNDMMNNTRKPTQKAMRTLFVNYVPHESNRRDLILAHFQKFGKVIDIHIPVNSERAFVQFSKREEAESALRAPDAVMGNRFIKLWWANRDSIPDNGLSTGSGASMKGRSMTASGAQNQFPIAAASKSNHVSSIAKVPTFQTGGAPSSSEQPKPVVVTTSGPKVTPLQQKKADTLERLKETLRKKQEMLEQKRNEYRKKLATLEKQGTVVKREEADEPDAKRVKLDTASDSGAAIASPKTESSTDKKVPILKPLSTAKLSTETPSPDSKNFKQRPYSFTTSLNAPMVNRYKLDNRTTTIKVVPPLPTGLADVAVVKEHFSSYGEVSKVELEDNASIDSGKDHETQNESRAACVTFVKRSAAEKAFANAKCWQEHTLQLVWVTRQSNRESNNNNNNSNSLSVSRDNLSSKNKCASVSNDPKPAVEVKTSSTEEPENTNVSGDNDSTLDKQETKESDNDNNKSNHESIEGASEVIATAGTDEEQSEQIHQ
Protein: Cinnamoyl-CoA reductase-like protein (Dihydroflavonol 4-reductase-like) (NAD(P)-binding Rossmann-fold superfamily protein) (Putative cinnamoyl-CoA reductase) (Q9FGH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Non-phototropic hypocotyl-like protein
- At1g73390
- Probable xyloglucan glycosyltransferase 8
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein eS12z
- SAGA-associated factor 29 homolog B
- Small ribosomal subunit protein eS10y
- Small ribosomal subunit protein eS7z
Sequence:
MLTDEREVVCVTGASGCIGSWLVHQLLLRGYSVHATVKNLQDEKETKHLEGLEGAATRLHLFEMDLLQYDTVSAAINGCSGVFHLASPCIVDEVQDPQKQLLDPAVKGTINVLTAAKEASVKRVVVTSSISAITPSPNWPADKIKNEECWAAEDYCRQNGLWYPLSKTLAEKAAWEFAEEKGLDVVVVNPGTVMGPVIPPSLNASMHMLLRLLQGCTETYENFFMGSVHFKDVALAHILVYEDPYSKGRHLCVEAISHYGDFVAKVAELYPNYNVPKLPRETQPGLLRDKNASKKLIDLGLKFISMEEIIKEGVESLKSKGFIS