wanglab/gogpt-training-data huggingface dataset:
Protein: Inner kinetochore subunit CTF19 (CENP-P homolog) (Chromosome transmission fidelity protein 19) (Constitutive centromere-associated network protein CTF19) (Minichromosome maintenance protein 18) (Q02732)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:29046335}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:29046335}.
Interaction partners:
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit AME1
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit IML3
- Inner kinetochore subunit NKP2
- Inner kinetochore subunit MCM16
- Histone H3-like centromeric protein CSE4
Sequence:
MDFTSDTTNSHDTSNSHLSLEDAVGTHHAGEADVNIDGDEKQQLSLLDDDQVRALKLQEEKDALLTRRNTLLQEIQTYQNILMKENNSKTKNGDILQNDITQDFLNLISISSSNPNSAISDRKRVERINGLTNLQKELVTKYDTLPLLNMNLRLSYLRDHTYPHLQVSVQSRDRVHNDGIEVLVVNYKFCRNTMNPFEIQFKMFYKFEDSTLLKWEILRISTNVRLKAKQLLATRNFQKCLLSLYEFDKIKSKKTGIFQNLINLLKRKTRCYLMNNSDSLIVERVIREGRLTTIKLQINFIITMPGERGKPRNCFLPMSKISIALWKGGERFNQIDLDEICYGLIKEYGVKTGLKEICNVCLFPDMYAR
Protein: ATP-dependent RNA helicase eIF4A (EC 3.6.4.13) (Eukaryotic initiation factor 4A) (eIF-4A) (Stimulator factor I 37 kDa component) (Translation initiation factor 1/2) (p37) (P10081)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4F subunit p150
- Eukaryotic translation initiation factor 4B
- Eukaryotic initiation factor 4F subunit p130
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 2 subunit alpha
Sequence:
MSEGITDIEESQIQTNYDKVVYKFDDMELDENLLRGVFGYGFEEPSAIQQRAIMPIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQALMLAPTRELALQIQKVVMALAFHMDIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIKMFILDEADEMLSSGFKEQIYQIFTLLPPTTQVVLLSATMPNDVLEVTTKFMRNPVRILVKKDELTLEGIKQFYVNVEEEEYKYECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTIMKEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGAMRELEKFYSTQIEELPSDIATLLN
Protein: Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12] (P42575)
Organism: Homo sapiens (Human)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress.
Interaction partners:
- p53-induced death domain-containing protein 1
- Death domain-containing protein CRADD
- BH3-interacting domain death agonist
- 14-3-3 protein gamma
- GA-binding protein subunit beta-1
- Caspase-3
- Caspase-8
- Baculoviral IAP repeat-containing protein 2
- Apoptotic protease-activating factor 1
- Cytochrome c
Sequence:
MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT
Protein: Bub3 interacting GLEBS and zinc finger domain protein, isoform F (M9PBC6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitotic checkpoint protein BUB3
- FI21236p1
- Bub1-related kinase
- Bub1 kinase, isoform A
- Splicing factor 3B subunit 1
Sequence:
MGRKKKKASKPWCWYCNREFDDEKILVQHQKAKHFKCHICHKKLYTGPGLSIHCMQVHKETVDKVPNSLPNRSNIEVEIFGMDGIPAEDLRDHERQKNGGKSDSDDDEPVAKKKVEYAMSVPPPMMMPPNMMPPHMLGQYGMGMMQHMPPLPPYPVPMMPHMMPPRPLFPAAMATTSAAAAAAAAHHHHAAAMAQQKPTFPAYSNATISAPPTTNHAGGASSAPPSGPPDAQQHQQRPPAPPAASGTSAAAVTTKIMHPQEDLSLEELRARQPKIQARLAAALASLANPQSRKSPSNNGGPSTSIPTTPPPPSLAGISPTGSNSSSGMANSIVVSAAMSKAQENAALVAVAQAQAHAHAHAAQVQAQAQAQAVVQAQVQAAHVAHAVAAQQQAVQQQQAAQQQQQAAVQQQAAVQQQQQQQQAAVQQQQAAQQQVKQLEELNRAVMLQRFQAARQPGNPGAAAAAAAAAAVGMMPLPGHMQLMQPMLRPAMAIGPHGTLIGGNMLRAGGPGLHGMPAGLLPMQIGLPGMPGALPAGAMAMPGMGVMLQGHPNMLQMMQPRFRXCLPAAPGLLQAPAGQPPTHLQPQPHPQHVQPARSFSRTTAALQAQAPLLSLPLPLLFHE
Protein: Catecholate siderophore receptor Fiu (Ferric iron uptake protein) (TonB-dependent receptor Fiu) (P75780)
Organism: Escherichia coli (strain K12)
Function: Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492.
Subcellular location: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}.
Interaction partners:
- PKHD-type hydroxylase YbiX
- Biopolymer transport protein ExbB
- Protein TonB
- Biopolymer transport protein ExbD
- Ferrienterobactin receptor
- Enterobactin synthase component F
- Colicin I receptor
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Isochorismate synthase EntC
- Enterobactin synthase component B
Sequence:
MENNRNFPARQFHSLTFFAGLCIGITPVAQALAAEGQTNADDTLVVEASTPSLYAPQQSADPKFSRPVADTTRTMTVISEQVIKDQGATNLTDALKNVPGVGAFFAGENGNSTTGDAIYMRGADTSNSIYIDGIRDIGSVSRDTFNTEQVEVIKGPSGTDYGRSAPTGSINMISKQPRNDSGIDASASIGSAWFRRGTLDVNQVIGDTTAVRLNVMGEKTHDAGRDKVKNERYGVAPSVAFGLGTANRLYLNYLHVTQHNTPDGGIPTIGLPGYSAPSAGTAALNHSGKVDTHNFYGTDSDYDDSTTDTATMRFEHDINDNTTIRNTTRWSRVKQDYLMTAIMGGASNITQPTSDVNSWTWSRTANTKDVSNKILTNQTNLTSTFYTGSIGHDVSTGVEFTRETQTNYGVNPVTLPAVNIYHPDSSIHPGGLTRNGANANGQTDTFAIYAFDTLQITRDFELNGGIRLDNYHTEYDSATACGGSGRGAITCPTGVAKGSPVTTVDTAKSGNLMNWKAGALYHLTENGNVYINYAVSQQPPGGNNFALAQSGSGNSANRTDFKPQKANTSEIGTKWQVLDKRLLLTAALFRTDIENEVEQNDDGTYSQYGKKRVEGYEISVAGNITPAWQVIGGYTQQKATIKNGKDVAQDGSSSLPYTPEHAFTLWSQYQATDDISVGAGARYIGSMHKGSDGAVGTPAFTEGYWVADAKLGYRVNRNLDFQLNVYNLFDTDYVASINKSGYRYHPGEPRTFLLTANMHF
Protein: Protein SOB FIVE-LIKE 1 (AtSOFL1) (Q67YG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin-mediated development. Together with SOFL2, triggers the endogenous content of specific bioactive cytokinins derived from the biosynthetic intermediates trans-zeatin riboside monophosphate (tZRMP) and N(6)-(Delta(2)-isopentenyl)adenosine monophosphate (iPRMP) such as N-glucosides trans-zeatin 7-glucoside (tZ7G), cis-zeatin 7-glucoside (cZ7G) and N(6)-(Delta(2)-isopentenyl)adenine 7-glucoside (iP7G).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29467189}. Nucleus {ECO:0000269|PubMed:29467189}.
Interaction partners:
- Protein SUPPRESSOR OF PHYTOCHROME B 5
- Protein SOB FIVE-LIKE 4
- Protein SOB FIVE-LIKE 3
- Protein SOB FIVE-LIKE 5
- Uncharacterized protein
Sequence:
MESPRNHGGSEEEEYSSCESGWTMYIEDAFHGNDQSSVVVDDDDDDTQVKEADDGYENDDGDTSDDGGDEESDDSMASDASSGPSNQLPKHINKHAARKNGSKQVYLQKRQHTEKTISNEGEKSDLKARTRTSAASRVQSRGKVSKTK
Protein: WIZ zinc finger (A0A669KBG4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTAQCRVTKAESKAAAGPRAGGARERAPAGAPPPSPPSPGPAAPPAPPPPPPPPPPPPPPPPPPPPPRDGPKAEPEPGPGPASAPAPGLGSEENAMVAMDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLKAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
Protein: UTP-monosaccharide-1-phosphate uridylyltransferase (EC 2.7.7.64) (Q4QE75)
Organism: Leishmania major
Interaction partners:
- Galactokinase-like protein
- UTP--glucose-1-phosphate uridylyltransferase
- UDP-glucose 4-epimerase
- phosphoglucomutase
- Phosphomannomutase-like protein
- Glucosamine 6-phosphate N-acetyltransferase
Sequence:
MTNPSNSNLQALREELCTPGLDQGHLFEGWPETVDECNERQIALLTDLYMFSNMYPGGVAQYIRNGHELLARESEEVDFAALEMPPLIFEAPSLHRRTAERTALENAGTAMLCKTVFVLVAGGLGERLGYSSIKVSLPVETATNTTYLAYYLRWAQRVGGKEVPFVIMTSDDTHDRTLQLLRELQLEVPNLHVLKQGQVFCFADSAAHLALDETGKLLRKPHGHGDVHSLIYNATVKRDVVPDSGDGTATAQPLVNDWLAAGYESIVFIQDTNAGATITIPISLALSAEHSLDMNFTCIPRVPKEPIGLLCRTKKNSGDPWLVANVEYNVFAEVSRALNKDGGDEVSDPTGFSPFPGSVNTLVFKLSSYVDRLRESHGIVPEFINPKYSDETRRSFKKPARIESLMQDIALLFSEDDYRVGGTVFERFSYQPVKNSLEEAAGLVAQGNGAYCAATGEAAFYELQRRRLKAIGLPLFYSSQPEVTVAKDAFGVRLFPIIVLDTMCASSGSLDDLARVFPTPEKVHIDQHSTLIVEGRVIIESLELYGALTIRGPTDSMALPHVVRNAVVRNAGWSVHAILSLCAGRDSRLSEVDRIRGFVLKKTAMAVMDCNTKGESEAGAPSGAADPAKL
Protein: Seminal plasma protein A3 (BSP-A3) (P04557)
Organism: Bos taurus (Bovine)
Function: The BSP-A proteins from seminal plasma exhibit both simulatory and inhibitory actions on the release of pituitary gonadotropins. The exact function of these proteins is not known.
Subcellular location: Secreted.
Interaction partners:
- Spermadhesin-1
Sequence:
MALRLGLFLIWAGVSMFLQLDPVNGDEQLSEDNVILPKEKKDPASGAETKDNKCVFPFIYGNKKYFDCTLHGSLFLWCSLDADYTGRWKYCTKNDYAKCVFPFIYEGKSYDTCIIIGSTFMNYWCSLSSNYDEDGVWKYC
Protein: Non-structural polyprotein pORF1 [Includes: Methyltransferase (EC 2.1.1.-) (EC 2.7.7.-); Putative protease (EC 3.4.22.-) (Putative papain-like cysteine protease) (PCP); NTPase/helicase (EC 3.6.4.-); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48)] (Q81862)
Organism: Hepatitis E virus genotype 1 (isolate Human/China/HeBei/1987) (HEV)
Function: Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP (Probable). GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure (Probable).
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:29112323}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:35283856}.
Interaction partners:
Sequence:
MEAHQFIKAPGITTAIEQAALAAANSALANAVVVRPFLSHQQIEILINLMQPRQLVFRPEVFWNHPIQRVIHNELELYCRARSGRCLEIGAHPRSINDNPNVVHRCFLRPAGRDVQRWYTAPTRGPAANCRRSALRGLPAADRTYCFDGFSGCNFPAETGVALYSLHDMSPSDVAEAMFRHGMTRLYAALHLPPEVLLPPGTYRTASYLLIHDGRRVVVTYEGDTSAGYNHDVSNLRSWIRTTKVTGDHPLVIERVRAIGCHFVLLLTAAPEPSPTPYVPYPRSTEVYVRSIFGPGGTPSLFPTSCSTKSTFHAVPAHIWDRLMLFGATLDDQAFCCSRLMTYLRGISYKVTVGTLVANEGWNASEVALTAVITAAYLTICHQRYLRTQAISKGMRRLEREHAQKFITRLYSWLFEKSGRDYIPGRQLEFYAQCRRWLSAGFHLDPRVLVFDESAPCHCRTAIRKAVSKFCCFMKWLGQECTCFLQPAEGAVGDQGHDNEAYEGSDVDPAESAISDISGSYVVPGTALQPLYQALDLPAEIVARAGRLTATVKVSQVDGRIDCETLLGNKTFRTSFVDGAVLETNGPERHNLSFDASQSTMAAGPFSLTYAASAAGLEVRYVAAGLDHRAVFAPGVSPRSAPGEVTAFCSALYRFNREAQRLSLTGNFWFHPEGLLGPFAPFSPGHVWESANPFCGESTLYTRTWSEVDAVSSPAQPDLGFISEPSIPSRAATLTPAAPLPPPAPDPSPTPSAPARGEPAPGATARAPAITHQAARHRRLLFTYPDGSKVFAGSLFESTCTWLVNASNVDHRPGGGLCHAFYQRYPASFDAASFVMRDGAAAYTLTPRPIIHAVAPDYRLEHNPKMLEAAYRETCSRLGTAAYPLLGTGIYQVPIGPSFDAWERNHRPGDELYLPELAARWFEANRPTCPTLTITEDVARTANLAIELDSATDVGRACAGCRVTPGVVQYQFTAGVPGSGKSRSITQADVDVVVVPTRELRNAWRRRGFAAFTPHTAARVTQGRRVVIDEAPSLPPHLLLLHMQRAATVHLLGDPNQIPAIDFEHAGLVPAIRPDLAPTSWWHVTHRCPADVCELIRGAYPMIQTTSRVLRSLFWGEPAVGQKLVFTQAAKAANPGSVTVHEAQGATYTETTIIATADARGLIQSSRAHAIVALTRHTEKCVIIDAPGLLREVGISDAIVNNFFLAGGEIGHQRPSVIPRGNPDANVDTLAAFPPSCQISAFHQLAEELGHRPAPVAAVLPPCPELEQGLLYLPQELTTCDSVVTFELTDIVHCRMAAPSQRKAVLSTLVGHYGRRTKLYNASHSDVRDSLARFIPAIGHVQVTTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKAILALLPQGVFYGDAFDDTVFSAAVAAARASMVFENDFSEFDSTQNNFSLGLECAIMVECGMPQWLIRLYHLIRSAWILQAPKESLRGFWKKHSGEPGTLLWNTVWNMAVITHCYDFRDLQVAAFKGDDSIVLCSEYRQSPGAAVLIAGCGLKLKVDFRPIGLYAGVVVAPGLGALPDVVRFAGRLTEKNWGPGPERAKQLRLAVSDFLRKLTNVAQMCVDVVSRVYGVSPGLVHNLIGMLQAVADGKAHFTESVKPVLDLTNSILCRVE
Protein: Prostate androgen-regulated mucin-like protein 1 homolog (PARM-1) (Castration-induced prostatic apoptosis-related protein 1) (CIPAR-1) (Prostatic androgen-repressed message 1 protein) (Q6P9X9)
Organism: Rattus norvegicus (Rat)
Function: May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MVCKALITLCIFAAGLRVQGSPTPTLLPVSLTTKSTAPMATWTTSAQHTAMATTPVASATHNASVLRTTAASLTSQLPTHPREEAVTSPPLKREVNSTDSSPTGFSSNSSGIHLAPTPEEHSLGSPETSVPATGSQSPTLLFSQGPTSASTSPATSPSEPLSASVTSNHSSTVNNIQPTGAPMAPASPTEEHSSSHTPTSHVTEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGAAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS
Protein: Mitogen-activated protein kinase hog1 (MAP kinase hog1) (EC 2.7.11.24) (Q9P419)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- mitogen-activated protein kinase kinase
- protein-tyrosine-phosphatase
- High osmolarity signaling protein sho1
- Basic leucine zipper
- Type 2C protein phosphatase
- Cytoplasmic response regulator
- Transcription factor
- Protein arginine N-methyltransferase
- Histidine-containing phosphotransfer protein
- Two-component system protein B
Sequence:
MAEFVRAQIFGTTFEITSRYTDLQPVGMGAFGLVCSARDQLTAQPVAVKKIMKPFSTPVLSKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVTELLGTDLHRLISSRPLEKQFIQYFLYQIMRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDAKVDVWSAACIFAEMLLGAPLFPGKDHVNQFSIITELLGTPPDDVIQTICSENTLRFVKSLPKREPQDLAKLPKFLALVHPDKKPEEDEDYKNTINLLKAMLVYNPKDRISAEAALAAPYLAPYHDETDEPVAEEKFDWSFNDADLPVDTWKIMMYSEILDFHNIDQGGDINPALVEGAGLNQQGFQ
Protein: Obelus (EC 5.6.2.4) (Q9VF56)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- EG:95B7.9 protein
- CD2 antigen cytoplasmic tail-binding protein 2 homolog
- Uncharacterized protein, isoform B
- Thioredoxin-like protein
- Probable small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-processing factor 6
- Probable small nuclear ribonucleoprotein G
- Splicing factor 3B subunit 3
Sequence:
MWEPPRLSASLRAKTELEARSRRLNVLRQARTTSAASTTTNSQNKEEQTIARLLAQMPTEKQPAAKVQLQKLRNLVQECMGYEEQPQVVEHAALFLFWLLLDQRVLLVATTQRLHGMFGQTFDRKKTQIHDCVQAIGDLLEDHERSALKRWRQTHHKVPGVGPLWGAHIHVKCTPSEWMDISLLTDLAPDALLKNRTVNKFSMKHTTKAAPVASTSSEAAKLSPELQTLLEISAKLDDEHLIIRVGDILGSQRSSEVLQNELMEILGFDYFELVEKLLMERDKIARQLDQFATRSRRVMEVKQKRMEAAASGGAAERRPTVASAVVVQSAQEKQLSKMQRREEKKLQRIMRSIKDEEAEDDPNCAVAVSVQQLRMQHQRKLLEAAQREPLLLSTKAAKAEYKQSSYNQPIHYPYVFDSQLLAKQHAGFIGGSRITLPDNAQRIDNKQWEEVKIPASEPPPLSVGNKRVQIEELDDVGRLAFANCKELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQGVINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRLVESSQSMIRIVGLSATLPNYIDVAHFLRVNPMKGLFYFDSRFRPVPLDTNFVGIKSVKQLQQIADMDQCCYQKCVEMVQEGHQIMVFVHARNATVRTANVIRELAQQNNTSALFLPKDSAAHGLATRSIQRSRNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTDIYDAKHGSFVDLGILDVLQIFGRAGRPQFDKSGVGTIITSYDKLNHYLSLLTNQFPIESNFVNCLADNLNAEIGLGTITNVDEAIEWLSYTYLFVRMRINPHVYGIEYSELEKDPTLEARRRALIMSAAMSLDKARMMRFNQRTMDMNITDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELKNAYCKIKPYGGSENVHGKVNILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTINAETIDKLERRGLSVYRLRDMEHRELKEWLRSNTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRVHGKTCQSFWLWIEDPESNYIYHSELFQVTRKLVMSGQSQQLVMTIPLKEPLPPQYYIRVSSDNWLGSTTCIPLSFQHLVLPEHHPPLTELLPLRPLPVSCLKNVVYESLYKFTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQRSSLGLKVVELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISSHTGRAIRIVGLSTALANAQDLANWLGINKMGLYNFKPSVRPVPLQVHINGFPGKHYCPRMATMNRPTFQAIRTYSPCEPTIVFVSSRRQTRLTALDLITFVAGESNPKQFLHIPEDEIELILQNIREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGKVKKYVDMPITDVLQMMGRAGRPQFDNEGVAVVLVHDEKKNFYKKFLYDPFPVESSLLGVLPEHINAEIVAGTVQSKQAALDYLTWTYFFRRLLRNPSYYQLQDIEPENVNNFMSNLVERVVYELSAAACLVERDGCLIPTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFRPPSSSWDSSYTKTFLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEFLTLPGVNEDNLDAFLNIPHDDYDYLTLPVLKELCKQEYEVLAKPLRDAFEEHEIEKMYKVIQDLPEIAIQIFVEGRHMENEYAKRPLSLSDDTRGEWMSLHANEDYVLIVNLQRLNVSGQRRGGGQSYTVHCPKYPKPKNEAWFLTLGSQANDELLAMKRVSIRGQRCTNRISFQATPRLGRLQLTLYLMSDCLMGFDQQYDLQFEIIDAKEV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q95SL7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKNQSSKDLILTEIRVLKDFNHKNLVNFLDAYLLEPEDQLWVVMEYMDGGPLTDVVTETVMKERQIACVCRETLYAISFLHAKGIIHRDIKSDNVLLGMDGSVKVTDFGFCANIEGDEKRQTWWERRTGWRPKWSRARSTARRWTSGLSASWPSR
Protein: Acetylcholine receptor subunit beta-type lev-1 (Levamisole-resistant protein 1) (Q27218)
Organism: Caenorhabditis elegans
Function: Non-alpha subunit of nicotinic acetylcholine receptor (nAChR). Involved in nAChR sensitivity to nicotine.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with unc-29 and unc-38 at nerve cord synapses. {ECO:0000269|PubMed:15990870}.
Interaction partners:
- Acetylcholine receptor subunit alpha-type unc-38
- AcetylCholine Receptor
- Acetylcholine receptor subunit alpha-type unc-63
- Acetylcholine receptor subunit beta-type unc-29
- Protein unc-50
- Resistance to inhibitors of cholinesterase protein 3
- START domain-containing protein
- CUB domain-containing protein
- Cell-death-related nuclease 7
- AcetylCholine Receptor
Sequence:
MMLGGGGGCGAGGTWLGFLVFLAVSLRNHSTCEDIDAEDRLMVDLFRGYNSLVQPVRNRSELPMIVKIGMQLVLLINVDEKEQVMHTNVWLTMKWDDFQLKWDPRDYANITQIRVAPEKVWLPDIVLFNNADGNYEVSFMCNVLILSTGTVLWVPPAIYKSSCIIDVEFFPFDDQLCSLTFGSWTYNRDEIKLDFLTSDRVDFSEYSTSSIWDMMDGPAVLTSDRSRIEFQIRIRRKTLFYTVVLILPTVLMAFLNVTVFYLPTASGEKMGLTMNVLLSIVVFLLLVSKILPPTSSSIPLVAKYLLLTFVLNIITIMVTTIICNIYFRSPITHRLPPWVRKVFLDILPLLMCMQRPHRKNVIQRSHRRLLETGPSVEENPMRSGEHHPLCRHTHNQDSCRRVRIQSDELDDELSPEAQRAIDAIEFITENRRDEEITKQFRDDWKFIASVVDRFLLYGFFGATVGGTIGIIFTAPSVFETFDENATLVKLKQLYDMGLANDTVLGIF
Protein: Delta(12) fatty acid desaturase FAD2 (CoFad2) (EC 1.14.19.-) (Q9AT72)
Organism: Calendula officinalis (Pot marigold)
Function: Catalyzes the desaturation of oleic acid to linoleic acid. Introduces a double bond at position 12 of 16:1(9Z) and 18:1(9Z).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGAGGRMQDPTNGGNKTEPEPIQRVPHEKPPFTVGDIKKAIPPHCFNRSVIRSFSYVFYDLTIASILYYIANNYISTLPSPLAYVAWPVYWAVQGCVLTGVWVIAHECGHHAFSDHQWLDDTVGLVLHSFLLVPYFSWKYSHRRHHSNTGSIEHDEVFVPKLKSGVRSTARYLNNPPGRILTLLVTLTLGWPLYLTFNVSGRYYDRFACHFDPNSPIYSKRERAQIFISDAGILAVVFVLFRLAMTKGLTWVLTMYGGPLLVVNGFLVLITFLQHTHPSLPHYDSTEWDWLRGALTTIDRDYGILNKVFHNITDTHVAHHLFSTMPHYHAMEATKVIKPILGDYYQFDGTSIFKAMYRETKECIYVDKDEEVKDGVYWYRNKI
Protein: Pentatricopeptide repeat-containing protein At5g19020, mitochondrial (P0C8Q8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Phosphoglycerate mutase family protein
Sequence:
MIKLIRFFRSRRCWVISLQARCFSAPSRTHFDFSGESSDTERALVSALGSCASSNDVTCGRQIHCRVLKSGLDSNGYICNSVLNMYAKCRLLADAESVFRDHAKLDSASFNIMVDGYVRSRRLWDALKLFDVMPERSCVSYTTLIKGYAQNNQWSEAMELFREMRNLGIMLNEVTLATVISACSHLGGIWDCRMLQSLAIKLKLEGRVFVSTNLLHMYCLCLCLKDARKLFDEMPERNLVTWNVMLNGYSKAGLIEQAEELFDQITEKDIVSWGTMIDGCLRKNQLDEALVYYTEMLRCGMKPSEVMMVDLLSASARSVGSSKGLQLHGTIVKRGFDCYDFLQATIIHFYAVSNDIKLALQQFEASVKDHIASRNALIAGFVKNGMVEQAREVFDQTHDKDIFSWNAMISGYAQSLSPQLALHLFREMISSSQVKPDAITMVSVFSAISSLGSLEEGKRAHDYLNFSTIPPNDNLTAAIIDMYAKCGSIETALNIFHQTKNISSSTISPWNAIICGSATHGHAKLALDLYSDLQSLPIKPNSITFVGVLSACCHAGLVELGKTYFESMKSDHGIEPDIKHYGCMVDLLGKAGRLEEAKEMIKKMPVKADVMIWGMLLSASRTHGNVEIAELAATELAAIDPSHGGCKVMLSNVYADAGRWEDVALVREEMRTRDVEWSRAFSGVV
Protein: Meiotic recombination protein rdh54 (EC 3.6.4.12) (ATP-dependent helicase rdh54) (Meiotically up-regulated gene 34 protein) (RAD54 protein homolog 2) (Q09772)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts with rhp54 to repair meiotic double strand breaks via homologous recombination. Involved in meiotic DNA recombination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA repair protein rhp51
- DNA repair protein rhp54
- DNA repair protein rhp55
- DNA repair and recombination protein rad22
- Meiotic recombination protein dmc1
- ATP-dependent DNA helicase srs2
- DNA repair protein rhp57
- Crossover junction endonuclease mus81
- Exodeoxyribonuclease 1
Sequence:
MKRRATFQCPLIESTIKHQSTNYTKTETATTSHEVSENANEHKGKSNIDINKIAYYNVVWRKITMKKHKTWEGDGFLVREDSNLTLYNSDFTRLGSCHSRVPQIKEGELLRISGKEISIEKEISAESYEAGTHIDDSLRDVHMPEMKRKFKPPLRPNTMYQTISALPKPRHDPTVLGALVMSRPKTWDPRTHVDVVIDPFLSKHLYSHQREGVSFLYDCLLGMEGKCGYSAILADEMGLGKTLQTITVVWTLLKQSYYANRSSTINNAMVVAPVTLLKNWENEFYNWLGHERIHVYIARCAEDFQEFTSNKTYSIIITGYETVCTYLRNYGCGIDIDLLICDEAHRLKSMSSQTWITLNKLKTRKRLLLTGTPLQNDLSEYFSMVNFIIPGSLGTPNSFKAQYERPILRSRSMNASSRDISLGAARLQRLFEFTSNFTLRRKANILAKHLPPRTDIVLFIKPTHQQENVYGHVLDGFKSSVDQKGYYLKILTRLSKICNSTILLRNEKENFLSTELQDKHVFEQENMLLSSSKLQILAALLKSFQRGCQKAVIVSQYKETLELIELFLSILHVRFCKLLGSTPFSERDLIVHNFNTSSFKEFSVLLLSSKAGGCGLNLTGSTRLIIYEPSWNPAQDLQALSRIYRSGQKRPVCIYTFLSSGMLDERIFIRQNTKQGLSSSFIDSDASQKKNFFTGEDIKTLFSYSKTETCLTYELAFDSDEIDSLTKKKDPLTKIDHTIDSPNTKEKDKEISSWKKASEYMDTNLGKKCPENAFQGWTWQFPNDLSIMNGVEDYIPLEPLPINCLMHKKFE