wanglab/gogpt-training-data huggingface dataset:
Protein: Endoplasmic reticulum protein 44, isoform A (Endoplasmic reticulum protein 44, isoform B) (Endoplasmic reticulum protein 44, isoform D (EC 5.3.4.1)) (LD41494p) (Q95TL8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DnaJ homolog shv
Sequence:
MFGARIGIGKLGPCVALVAILQLLQYTQPADAAGAVPMTSDNIDMTLASNELVFLNFYAEWCRFSNILAPIFAEAADKIKEEFPEAGKVVLGKVDCDKETAIASRFHINKYPTLKIVRNGQLSKREYRGQRSAEAFLEFVKKQLEDPIQEFKSLKDLENLDSKKRLILGYFDRRDQPEYDIFRKVATNLKEDCQFHVGFGDAAQAMHPPGTPIIVFRPDVALSHENDETYTGSLQNFDELKIWVQEKCVPLVREITFENAEELTEEGLPFLILFHHPTDHNSIKDYKSIIERQLLDEKQNVNFLTADGKRFAHPLHHLGKSEDDLPLIAIDSFKHMYLFPHFSDMYSPGKLKQFLQDLYSGKLHREFHYGPDPSNDIEPDPHTGKGTSPPESKFKELGPSKHRYTLLEKDEL
Protein: Uncharacterized protein (E1JIS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- SCP domain-containing protein
- IP10051p
- GEO02601p1
- FI03584p
- Gliolectin
Sequence:
MSSISTIIGLCLLFFMLSNVDAYGQKCSPVFGNCNMHTDCCSGKCLTYGSRCGYPAHRLKETYLSASEFQSIKKQRAHSNNDEVKVIGLPSESEPSNVFFKIDSAAKCHNVGEPCSRGEECCNLRCHSYMHRCVT
Protein: ATP-dependent RNA helicase MSS116, mitochondrial (EC 3.6.4.13) (P15424)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- ATP-dependent RNA helicase SUV3, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- Intron-encoded DNA endonuclease aI5 beta
- Nucleolar protein 58
- Putative COX1/OXI3 intron 2 protein
- Cytochrome c oxidase subunit 1
- Eukaryotic translation initiation factor 4E
- Mitochondrial GTPase 1
- mRNA-binding protein PUF3
- rRNA methyltransferase 1, mitochondrial
Sequence:
MLTSILIKGRTPVLASRNLLAALSNCNHITWAVSRRLYNDGNRDQRNFGRNQRNNNSNRYRNSRFNSRPRTRSREDDDEVHFDKTTFSKLIHVPKEDNSKEVTLDSLLEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEAEVKKIHDMNYGLKKYACVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIMNKKECLFLDTVDKNEPEAHERIDQSVVISEKFANSIFAAVEHIKKQIKERDSNYKAIIFAPTVKFTSFLCSILKNEFKKDLPILEFHGKITQNKRTSLVKRFKKDESGILVCTDVGARGMDFPNVHEVLQIGVPSELANYIHRIGRTARSGKEGSSVLFICKDELPFVRELEDAKNIVIAKQEKYEPSEEIKSEVLEAVTEEPEDISDIVISLISSYRSCIKEYRFSERRILPEIASTYGVLLNDPQLKIPVSRRFLDKLGLSRSPIGKAMFEIRDYSSRDGNNKSYDYDDDSEISFRGNKNYNNRSQNRDYDDEPFRRSNNNRRSFSRSNDKNNYSSRNSNIY
Protein: Probable plastid-lipid-associated protein 1, chloroplastic (AtPap1) (Fibrillin-1a) (Plastoglobulin 35) (AtPGL35) (O81439)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in light/cold stress-related jasmonate (JA) biosynthesis. Contributes to the protection of photosystem II (PSII) against light stress.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}. Plastid, chloroplast thylakoid. Note=Located in the elaioplast, a tapetum-specific plastidial lipid organelle.
Interaction partners:
- Probable starch synthase 4, chloroplastic/amyloplastic
- Probable plastid-lipid-associated protein 9, chloroplastic
- Probable plastid-lipid-associated protein 13, chloroplastic
- Plastid-lipid-associated protein 6, chloroplastic
- Probable plastid-lipid-associated protein 8, chloroplastic
- Probable plastid-lipid-associated protein 10, chloroplastic
- Phytyl ester synthase 1, chloroplastic
- RNA-binding
- Pentatricopeptide repeat-containing protein At1g20300
- Probable plastid-lipid-associated protein 12, chloroplastic
Sequence:
MATVPLFTQFPCKTLNPSSSNTKHQSKSPILLPINSINRRSEIGVSVHRPDFKIRATDIDDEWGQDGVERVFASSSTVSVADKAIESVEETERLKRSLADSLYGTDRGLSVSSDTRAEISELITQLESKNPTPAPNEALFLLNGKWILAYTSFVGLFPLLSRRIEPLVKVDEISQTIDSDSFTVQNSVRFAGPFSTTSFSTNAKFEIRSPKRVQIKFEQGVIGTPQLTDSIEIPESVEVLGQKIDLNPIKGLLTSVQDTASSVARTISNQPPLKFSLPSDNTQSWLLTTYLDKDLRISRGDGGSVYVLIKEGSSLLNP
Protein: Baseplate tube protein p140 (p140) (Minor tail protein p140) (Tail protein p140) (Q6QGE3)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Probable minor tail protein.
Subcellular location: Virion {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}. Note=Component of the tail (PubMed:24198424, PubMed:36961893). Located between the first TTP-pb6 trimer and the DTP-pb9 hexamer, and surrounded by the p132 collar protein dodecamer (PubMed:36961893). {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}.
Interaction partners:
Sequence:
MFYSLMRESKIVIEYDGRGYHFDALSNYDASTSFQEFKTLRRTIHNRTNYADSIINAQDPSSISLAINFSTTLIESNFFDWMGFTREGNSLFLPRNTPNIEPIMFNMYIINHNNSCIYFENCYVSTVDFSLDKSIPILNVGIESGKFSEVSTFRDGYTITQGEVLPYSAPAVYTNSSPLPALISASMSFQQQCSWREDRNIFDINKIYTNKRAYVNEMNASATLAFYYVKRLVGDKFLNLDPETRTPLIIKNKYVSITFPLARISKRLNFSDLYQVEYDVIPTADSDPVEINFFGERK
Protein: FERM domain-containing protein 4A (Q9P2Q2)
Organism: Homo sapiens (Human)
Function: Scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex (By similarity). Plays a redundant role with FRMD4B in epithelial polarization (By similarity). May regulate MAPT secretion by activating ARF6-signaling.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8BIE6}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8BIE6}. Note=Colocalized with CYTH1 at adherens junction and tight junction. Colocalized with PARD3 during the process of epithelial polarization. {ECO:0000250|UniProtKB:Q8BIE6}.
Interaction partners:
- Cytohesin-1
- Cytohesin-4
Sequence:
MAVQLVPDSALGLLMMTEGRRCQVHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSGPVVLYFCVRFYIESISYLKDNATIELFFLNAKSCIYKELIDVDSEVVFELASYILQEAKGDFSSNEVVRSDLKKLPALPTQALKEHPSLAYCEDRVIEHYKKLNGQTRGQAIVNYMSIVESLPTYGVHYYAVKDKQGIPWWLGLSYKGIFQYDYHDKVKPRKIFQWRQLENLYFREKKFSVEVHDPRRASVTRRTFGHSGIAVHTWYACPALIKSIWAMAISQHQFYLDRKQSKSKIHAARSLSEIAIDLTETGTLKTSKLANMGSKGKIISGSSGSLLSSGSQESDSSQSAKKDMLAALKSRQEALEETLRQRLEELKKLCLREAELTGKLPVEYPLDPGEEPPIVRRRIGTAFKLDEQKILPKGEEAELERLEREFAIQSQITEAARRLASDPNVSKKLKKQRKTSYLNALKKLQEIENAINENRIKSGKKPTQRASLIIDDGNIASEDSSLSDALVLEDEDSQVTSTISPLHSPHKGLPPRPPSHNRPPPPQSLEGLRQMHYHRNDYDKSPIKPKMWSESSLDEPYEKVKKRSSHSHSSSHKRFPSTGSCAEAGGGSNSLQNSPIRGLPHWNSQSSMPSTPDLRVRSPHYVHSTRSVDISPTRLHSLALHFRHRSSSLESQGKLLGSENDTGSPDFYTPRTRSSNGSDPMDDCSSCTSHSSSEHYYPAQMNANYSTLAEDSPSKARQRQRQRQRAAGALGSASSGSMPNLAARGGAGGAGGAGGGVYLHSQSQPSSQYRIKEYPLYIEGGATPVVVRSLESDQEGHYSVKAQFKTSNSYTAGGLFKESWRGGGGDEGDTGRLTPSRSQILRTPSLGREGAHDKGAGRAAVSDELRQWYQRSTASHKEHSRLSHTSSTSSDSGSQYSTSSQSTFVAHSRVTRMPQMCKATSAALPQSQRSSTPSSEIGATPPSSPHHILTWQTGEATENSPILDGSESPPHQSTDE
Protein: Tubulin--tyrosine ligase (TTL) (EC 6.3.2.25) (P38584)
Organism: Bos taurus (Bovine)
Function: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin.
Interaction partners:
- Tubulin alpha-1B chain
- Small vasohibin-binding protein
- Tubulin beta-4A chain
- Stathmin
- Enhancer of mRNA-decapping protein 3
- Stathmin
- Stathmin
- Vasohibin 1
- Stathmin
- Vasohibin 2
Sequence:
MYTFVVRDENSSVYAEVSRLLLATGHWKRLRRDNPRFNLMLGERNRLPFGRLGHEPGLMQLVNYYRGADKLCRKASLVKLIKTSPELAESCTWFPESYVIYPTNLKTPVAPAQDGIHPPLHSSRTDEREFFLASYNRKKEEGEGNVWIAKSSAGAKGEGILISSDATELLDFIDNQGQVHVIQKYLERPLLLEPGHRKFDIRSWVLVDHQFNIYLYREGVLRTASEPYHMDNFQDKTCHLTNHCIQKEYSKNYGKYEEGNEMFFEAFNRYLTSALNITLESSILLQIKHIIRSCLMSVEPAISTKHLPYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDIAIASVFPPPDAEQQPPQPATFIKL
Protein: Beta-microseminoprotein A1 (msp-A1) (O97936)
Organism: Saguinus oedipus (Cotton-top tamarin)
Subcellular location: Secreted {ECO:0000250}. Note=Sperm surface. {ECO:0000250}.
Interaction partners:
Sequence:
MNVLLGGLVIFATFVTLCNGSCYLMPNKMVPGDSTKECTDLKGNKHPLNSRWKTENCDECDCLEKEISCCSLVAIPVGYDQDNCQKIFKQEDCKYIVVEKKDPNKTCEVTQWI
Protein: Deoxyribonuclease TATDN1 (U3KQS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRFKFIDIGINLTDPMFRGIYRGVQKHQDDLQDVIGRAVEIGVKKFMITGGNLQDSKDALHLAQTNGMFFSTVGCHPTRCGEFEKNNPDLYLKELLNLAENNKGKVVAIGECGLDFDRLQFCPKDTQLKYFEKQFELSEQTKLPMFLHCRNSHAEFLDIMKRNRDRCVGGVVHSFDGTKEAAAALIDLDLYIGFNGWYVLRLLWFLTFI
Protein: Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (P49350)
Organism: Artemisia annua (Sweet wormwood)
Function: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. Promotes anti-malarial and antimicrobial (toward Gram-positive bacteria B.subtilis and S.aureus) activities of plant crude extract probably by triggering artemisinin levels.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14230}. Nucleus {ECO:0000250|UniProtKB:O14230}.
Interaction partners:
- Solanesyl diphosphate synthase 1
- Diphosphomevalonate decarboxylase
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
- GHMP kinase family protein
- Protein farnesyltransferase subunit beta
- Uncharacterized protein
- Myrcene synthase protein
- Squalene synthase
Sequence:
MSSIDLKSKFLKVYDTLKSELINDPAFEFDDDSRQWIEKMLDYNVPGGKLNRGLSVVDSYQLLKGGELSDDEIFLSSALGWCIEWLQAYFLVLDDIMDESHTRRGQPCWFRLPKVGMIAANDGILLRNHVPRILKKHFRGKPYYVDLVDLFNEVEFQTASGQMIDLITTLVGEKDLSKYSLSIHRRIVQYKTAYYSFYLPVACALLMFGEDLDKHVEVKNVLVEMGTYFQVQDDYLDCFGAPEVIGKIGTDIEDFKCSWLVVKALELANEEQKKVLHENYGKKDPASVAKVKEVYHTLNLQAVFEDYEATSYKKLITSIENHPSKAVQAVLKSFLGKIYKRQK
Protein: Putative replication origin binding protein (D2 helicase) (Q6QGH9)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Displays bipolar ssDNA and dsDNA unwinding activities that require the same core catalytic residues for unwinding in either direction, the 3'-5' direction being more robust.
Interaction partners:
Sequence:
MFSILQGHAGFSRDLATGIWREIKAEDYTFAKRFSKEHPEGKPASMPFKFDVIEEHDPQSLAEMLPLMRRLTSDPHIVAVRGRCLAPKNNVRRKKGNFNVSNPSNIIAMDVDGILDTGGYDKFNLVGMARHIIKMLNSISEDMFPLDAGFIAHASSSAGLKPGIRMHLMLESNVKVTQGQLKFLFTSINDSSKQKFGFDIADLAYYSSVQLHYFADPLFSDGIVDPFKAESKPRLVYVKGSKVNLPNNLVDYETTRGEFKEEFYSLLDQIKGKKIASDKVEETISELEEADDGVYLRIIPKLYHRALEDGVDFAWLEREIKPALSEYIATKDNSRNIQDYFNNGRKQALKAFVNNSKREIPLNLKGVPLKKLEVDSPPEVPYLKINIVPPKGHITFVKASLGTGKTTAVTKWLDAGVLPGNFLAVTNTRALVSSNAKKFSAGQYDKSVDMLNFKRGAIDRMSTTIHSLHKFKSFIGQIDTIFIDECDAVMNDLLFAPVVKQRRECIQVLRDILMTAKTVILSDGDISAETIEAYGSLIDFDKPVAFYNHHRKMLSKAHAYEFPDESSIWVALQTSLEMGEKSILVSDCGPDELNEKGMALRRNTGALVKEIHSNSTSDVDIRRILDYTTNELIDQQIDCLLCSPSVTSGVDFNYFDNVFVITRTSNQAPNMRFQAIRRDRGAQNIYYFIDKSTSGFSAGSEQYNIDEGWLELAQQLYARRRELESRNYTSTLRYYLLDQGATIDIFSESWGTIEGAGKEYTEERIKAILHSTPDYCAPRHADAYEAKLLLVRYYHLESIKDVTVEHVEQYIKDKPNDRAAFFHKMHEMFWEDIKKCSNVTIKPFIEALKGKKKDFFLKTGQSANPKYARMYLGMMGIGKDMNTENIVDWYRTYCKIECMPIPFKFMTEEERAMAEEVMSELGATNEDA
Protein: Emopamil binding protein (A0A024QYX0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN
Protein: Meiotically up-regulated gene 110 protein (O43009)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Localizes to the barrier septum and cell tip.
Interaction partners:
- Uncharacterized protein UNK4.17
- Meiotically up-regulated gene 103 protein
- mRNA export factor crp79
- Meiotic PUF family protein 1
- Multicopy suppressor of sporulation protein msa1
Sequence:
MVESSDENDQASSFASTEDLKELRFVFWFSVLIPIFFIALIIIKRYHSCTYQKNRLLRSIFCCMSIDDEEELETDMYDLPIVEPSITLPKYSASLQENERLVGIEGEREGIDVVLNFSKAGEGGVNPYPSFDTPNARILQLRQLAKLKKHGPRISYHGIGIGRCNGNRVLPPYPEPALLPEAPNTREASNNTYLYGFSNNFINISRTLNLRYPSASASISDSLPPPYQVLSVPSVTSTHAFSNNANQT
Protein: Phenylalanine aminomutase (L-beta-phenylalanine forming) (EC 5.4.3.10) (Phenylalanine ammonia-lyase) (EC 4.3.1.24) (Q68G84)
Organism: Taxus chinensis (Chinese yew) (Taxus wallichiana var. chinensis)
Function: Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MGFAVESRSHVKDILGLINAFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNRLSELQESLIRCLLAGVFTKGCAPSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVIARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATAVASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQELSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLKQSCFDTILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSKFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGV
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 39 kDa subunit) (eIF-3 39 kDa subunit) (eIF3 p39) (P40217)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor eIF-1
Sequence:
MKAIKLTGHERPLTQVKYNKEGDLLFSCSKDSSASVWYSLNGERLGTLDGHTGTIWSIDVDCFTKYCVTGSADYSIKLWDVSNGQCVATWKSPVPVKRVEFSPCGNYFLAILDNVMKNPGSINIYEIERDSATHELTKVSEEPIHKIITHEGLDAATVAGWSTKGKYIIAGHKDGKISKYDVSNNYEYVDSIDLHEKSISDMQFSPDLTYFITSSRDTNSFLVDVSTLQVLKKYETDCPLNTAVITPLKEFIILGGGQEAKDVTTTSANEGKFEARFYHKIFEEEIGRVQGHFGPLNTVAISPQGTSYASGGEDGFIRLHHFEKSYFDFKYDVEKAAEAKEHMQEAN
Protein: CFA20 domain-containing protein (Q57VA3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEPLMARCASLLDILVPRSVECLSNAKVQNESCCAIQYDRILRVPVLIMKGDISNARVQIPRDGKSLPVVPLPCTLVALQAYIGSFDTFALEVSVSTKTSLRVKLIIGTHFNKTSLEDTGSSLILFRMPLIIPRNRWVQIVFHISGIVTHLLELPPIKFIDAISLSGTCKASRLMASNSEEVVVNATPSDMTLFAVPAYAPPIWQTVAASPPPNGTCSDNNKKISGRSPQKVAKDRLPVVVKSPLRRDDDTANEGENDSPKHNVVRTAATSASNGTPSPPYKQIGREVSAIESTSSANSFDVPPEGRAPSLPGDFTDARRVKQMPKQQVGQPAARCGSAAYIRLVSGANFPPRSSSNPTVKPRPLHLGAKEQSPSAVTTPPPPPVETYPGVCDLLFDASYGITGWGETACRASTAASASPPRAGSDVKCRSAPTAAVPTNRISGGAVSECKTNGLAEQVSPKAKRLKRVIEIRRRSFVPPTRRRKPCGGDGQNGEGNETGAAAGGTSRRSAVSVRRLYMRKRIRKLKEAQNSARRMQEMKRLPASELPIDPQDEALMMVGEETMNVTREPRCGYGFGYLGVLHESGGFEADENADTELKGALTLELSELSDGEENEE
Protein: 43 kDa receptor-associated protein of the synapse homolog (RAPsyn) (Q09485)
Organism: Caenorhabditis elegans
Function: Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction.
Interaction partners:
- Agrin
- RING-type E3 ubiquitin transferase
Sequence:
MGQRQAKQHMQAGVKLYHQRHYAQAINKWRQSLNRLNNAEDRFITLGYLAQALCDQGEYEGMLSYALSQMQLATDQNDSAMKCEAFLNLAKAYERLADFTKALQYGKASLEHPSMDPRTPGYAHLTIALAHLGMSQFQQCLESFESAMNVANETSDRLLELQICVGLGSLFTLLRDITKALIFLRNALAIVQSVTVDDVHAKYRCLILYHLSVALRMKGSLVDAKEACDEASQLAVEMGNRAIHARCMCSLADIYRELGESEAKETITKSWARYEDAYRVMRGANDKMGEVLVLSSMAKSASESRSHYTGQCECQAIQLNKKCIEIANQIGCKHVVLKCHLRLAELYSQLNDDDSEETARRAASRLTQEMQLFCNFCGQRYGLKDESLQALRCSHIFHEKCLHTYLLQRTDQTCPKCRCRAVLSDNISIRSSIASTIDVQSPSTSFAPPGGVATPLVSAAAELGDITPQATLTRRSQQDKILRGAEKDIDRVDRSLARLKSQQSAAANACSAVAVPSPEVPSTTASCASEPILTASTTSQSHTHSNANHKPPPPPRKPCCSQAALPPSSIVALPPAMPLAEDGPLVITHTPTVTDV
Protein: Protein phosphatase 1 regulatory subunit 3A (Protein phosphatase 1 glycogen-associated regulatory subunit) (Protein phosphatase type-1 glycogen targeting subunit) (RG1) (Q99MR9)
Organism: Mus musculus (Mouse)
Function: Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase.
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Retinoblastoma-like protein 2
- Glycogen [starch] synthase, muscle
- Glycogen [starch] synthase, liver
- Protein phosphatase 1 regulatory subunit 3C
- Protein phosphatase 1 regulatory subunit 3B
- Protein phosphatase 1 regulatory subunit 3E
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 3F
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Sequence:
MEPAEEPGQISKDNFLEVPNLSDSVCEDEEVKATFKPGFSPQPSRRGSGSSEDMYLDTPTSASRRVSFADSLGFSLVSVKEFDCWELPSVSTDFDLSGDVFHTDEYVLSPLFDLPSSKEKLMEQLQVQKAVLESAEHLPGSSMKGIIRVLNISFEKLVYVRMSLDDWQTHYDILAEYVPNSCDGETDQFSFKISLVPPYQKEGGKVEFCIRYETSAGTFWSNNNGTNYILVCQKKRKEPEPVKPLEEAPSRQIKGCLKVKSRSKEEPLLAPEENKFETLKFTESYIPTIICSHEDKDDLGANHPNVDDINKKHDEHNGKELDLMINQRLITSQDEKNTFATDTVNFTNKAEGSEKKQAYHEINTDLFMGPLSPSLSAESSLKRDFYHSRSSSPGNEYGHPHSEEIISDMGEKGPSLGDTSSDELMQLELCSKEDLDDNANPANGSGRVCSSFDQRMACGLKNNEAGIKKTGIQDYKYSHGDSTKLEESNASSRDDYAKVDNKKEKQTCLGVNENPSKNFQSVFQTQEGHMGYPKISTEGDKANNQDLTSLLSKDITANTWAVTVDPCPSTNAKRSWREVGSGSNLEPGTSDLSSPRNFSPLTDDHLFQADRENSDSSNPENQNMNTRHRKKWNVLETQSETSETESDIAKHTKEQAEYKDMWEKTDNSRNLKATPTEHLFTCRETECYGLSSLADHGITEKAQAVTAYIIKTTLESTPESASARGKAIIAKLPQETAGNDRPIEVKETAFDPHEGRKDDSHYSLCHGDTAGVIHDNDFERESHLDICNLRVDEMKKEKTTSTCFPQKTYDKEKHGIGSVTSIDEPSQVITGNQKATSKLDLHLGVLPTDRAIFQANADLELLQELSRRTDFNAVPSAFNSDTASASRDSSQVYRHCSKKSVPSYGEEKAVTNTTLQSIPTKSEYNWHPESEVLGHAMSKPEDVFKSSEIMKSGSGGERGGGPILQQKEGSLENSQGPMFFTNEPLENLDEASSENEGLMHSGQSQCYLGDKGLVSSASATVSTQELEAQGRESLLSISTNSKIPYFLLFLIFLATVYYYDLMIGLAFYLFSLYWLYWEGGRQRESVKKK
Protein: Contig An11c0340, genomic contig (A5ABP0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MADFIAFHTYYSRHNFLSPSTMLPRPTSHKRSNSSENNSLSPDKTVTKARSTNDLSGTATAKPTPGVRSSSVGNFQETSFSTLKDPRLASHSEDSETPESTQSHHPDLSNEVAALSVKLVQAINNQTTLDDNLVATRQELEQAQAKIRVLELENEKYKRDIDQEVLIKKSDVDYEMLRLQAALAEEKAQRALVEKEKKGIEQELETLTAALFEEANKMVAAAKLEREAVEKKNEQLRSQVKDTEALLASHQEQLAELKSVLQGPNIAKEDSETRTIISTAPSSPTMPRHPLHISKNSDIPDIPEEIPTLEELTPGPSTSFPHLIKPVCRTDIQAYEDFRELFTTSRASKPASRATSGSYTGLNVMSLASGFGSASSSPAKSQTHSPNGSVSSPQPVTSHIPLKETRFYKRVLSEDIEPTLRLDAAPGISWLTRRSVLSGICDGTLLVEPMPPSAKKYEFPCSMCGERRNGPTNERTHRFRTSDSETAQRYPLCVLCLERVRSSCEFTGYLRLILDGHVRIGDTEEEKDAWDETIRLRERMFWSRIGGGIIPLFAHANGFQGNIPTSTENVEAPVADGRDDCQRSIISTVPEDITIETKNLGEIDEHNHDEGSVADDPFVSAPSESESTASSAAVSPTDASAPVVKTDLVDDMHEQPDVQVVVPEPTHDEADSVKLPTQVEETPINHDTTKHGDN
Protein: Forkhead box protein fkh-3 (A0A078BQN7)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Binds to DNA sequence motif 5'-CTGTTTCA-3'. Regulates expression of a class of small RNAs, known as 21U-RNAs, perhaps acting redundantly with fkh-4 and fkh-5.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:12568714}.
Interaction partners:
- Forkhead box protein fkh-4
- Fork-head domain-containing protein
- Fork-head domain-containing protein
- Forkhead transcription factor fkh-9
Sequence:
MQSNDENIYFPANQYVNAGQYSPLQQSFSQNSQYDLFDGFAEFGFLEQVPTTNMHSFSQSTQMEQNCLPNVNNSTRKRKAPGQNEQATVKRRQIGIEKWRLPSRSVVQPSADISDLRRPPISYVALCALACRNAPDMKITPAGVYAFILHHWRYYRYANENWKNSVRHQLSSKEHFDEETFQPDPSNQTVRRKFYIVKNPNMIRQNLISDADFDFFRKDSRGIEFYQKMFAGQIGLPRSLFYQIIGNEIPFLAGPENSSMFYQLLGMGKVVGYLETRYFREHYRSEHAATEPKYEEDYANFTEKIPSNAENLMSYGAATERNFQKFDFTDEEIELFHLNISSYHSVQKTCKECNLPNWCTPSVGDVETYVFGRQVPMPVNTPVILQQFETVAEQEGIRNNPLEEQKTTKDPRDISVLEALA
Protein: Exocyst complex component EXO84C (AtExo80c) (Q9SY60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall (By similarity).
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5B
- Exocyst complex component SEC3A
- Exocyst complex component SEC5A
- Exocyst complex component SEC3B
- Exocyst complex component SEC15A
- Exocyst complex component SEC15B
- Exocyst complex component SEC10a
- Exocyst subunit Exo70 family protein
Sequence:
MESSEEDDEYPFIESITPQSKIDSVHQSLTEKGIRKLCCELMDLKDAVENMCGDMRTKYLAFLRISEEAVEMEHELVELRKHISSQGILVQDLMAGVCREMDDWNRLPGDVHDAEVEEDPLPNEVTDPKSEFLEKIDLLLAEHKVDEALEAMDAEERSSPDLKGSVEMSSYKSAFMERKAVLEDQLLRIAKQPSICVAELKHALIGLIRLGKGPSAHQLLLKFYATSLRRRIEAFLPSCLTCPNTFPATLSKLVFSNISVATKESAAMFGDDDNPAYSNKVVQWAEREVEYLVRLVKENASPSETASALRAASICLQDCLNYCKVLEPQGLFLSKLFLVLFRPYVEEVLELNFRRARRVIFDLNETDEGLESPSDFVTILSEFAIASDTMMTDCSIRFMQIVQDILEQLTHLVVLHFGESVLTRILQLYDKYIDFLIKALPGHSDEDGLPELQDNTVLARAETDSEQLALLGAAFTILDELLPRSLVKVWKLQIENGGGEGENSAALNSSAAPELKEWKRHMVQAFDKLRNYFCLQFVLSFIYSREGLTRLDALIYLTETPDDLHLPSLPFQALFSKLQQLAIIAGDVLLGKEKLQKILLARLTETVIIWLSNEQEFWSAFEDESNPLQPSGLQQLILDMNFTVEIARFAGYPFKVVQNHASVVINRAINIFSERGINPQSSLPKTEWFTEAAKSAINRLLMGSEDASEPEEYECEEEEEDDHHIVLPEMDDDSDSEDTSSLSTVDSFESFASASMADLESPSFTDSES
Protein: Cytochrome c551 peroxidase (CCP) (Cytochrome c peroxidase) (EC 1.11.1.5) (P14532)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Cbb3-type cytochrome c oxidase subunit
- Azurin
- Nitrite reductase
- GDP-polyphosphate phosphotransferase
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- cytochrome-c oxidase
- alcohol dehydrogenase
- Oxygen-independent coproporphyrinogen III oxidase
- Arginine/ornithine antiporter
- UspA domain-containing protein
Sequence:
MQSSQLLPLGSLLLSFATPLAQADALHDQASALFKPIPEQVTELRGQPISEQQRELGKKLFFDPRLSRSHVLSCNTCHNVGTGGADNVPTSVGHGWQKGPRNSPTVFNAVFNAAQFWDGRAKDLGEQAKGPIQNSVEMHSTPQLVEQTLGSIPEYVDAFRKAFPKAGKPVSFDNMALAIEAYEATLVTPDSPFDLYLKGDDKALDAQQKKGLKAFMDSGCSACHNGINLGGQAYFPFGLVKKPDASVLPSGDKGRFAVTKTQSDEYVFRAAPLRNVALTAPYFHSGQVWELKDAVAIMGNAQLGKQLAPDDVENIVAFLHSLSGKQPRVEYPLLPASTETTPRPAE