wanglab/gogpt-training-data huggingface dataset:
Protein: Activin receptor type-1-like (EC 2.7.11.30) (Activin receptor-like kinase 1) (ALK-1) (Serine/threonine-protein kinase receptor R3) (SKR3) (TGF-B superfamily receptor type I) (TSR-I) (P37023)
Organism: Homo sapiens (Human)
Function: Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26176610}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Endoglin
- Bone morphogenetic protein 10
- Growth/differentiation factor 2
- Bone morphogenetic protein receptor type-2
- Activin receptor type-2A
- TGF-beta receptor type-2
- Transforming growth factor beta-3 proprotein
- Activin receptor type-1
- Transforming growth factor beta-1 proprotein
- Activin receptor type-2B
Sequence:
MTLGSPRKGLLMLLMALVTQGDPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQLALILGPVLALLALVALGVLGLWHVRRRQEKQRGLHSELGESSLILKASEQGDSMLGDLLDSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPHLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDFKSRNVLVKSNLQCCIADLGLAVMHSQGSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARRTIVNGIVEDYRPPFYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKISNSPEKPKVIQ
Protein: Exosome complex component RRP43 (Exosome component 8) (Ribosomal RNA-processing protein 43) (Q9D753)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96B26}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96B26}. Nucleus {ECO:0000250|UniProtKB:Q96B26}.
Interaction partners:
- Exosome complex exonuclease RRP44
- Exosome complex component RRP40
- Exosome complex component CSL4
- Exosome complex component RRP4
- Exosome complex component MTR3
- Exosome complex component 10
- Exosome complex component RRP45
- Exosome complex component RRP46
- Exosome complex exonuclease RRP42
- Exosome complex component RRP41
Sequence:
MAAGFKTVEPLEYYRRFLKENCRPDGRELGEFRATTVNIGSISTADGSALVKLGNTTVICGVKAEFAAPPVDAPDRGYVVPNVDLPPLCSSRFRTGPPGEEAQVTSQFIADVVDNSQVIKKEDLCISPGKLAWVLYCDLICLDYDGNILDACTFALLAALKNVQLPEVTINEETALAEVNLKKKSYLNVRTNPVATSFAVFDDTLLIVDPTGEEEHLSTGTLTVVTDEDGKLCCLHKPGGSGLTGAKLQDCMSRAVTRHKEVSKLLDEVIQSMRHK
Protein: Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain] (P04663)
Organism: Influenza A virus (strain A/Qu/7/1970 H3N2)
Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host apical cell membrane; Single-pass type I membrane protein. Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts.
Interaction partners:
Sequence:
QDLPGNDNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDGFQNETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTEVTQNGGSNACKRGPGSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGVHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGQSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQT
Protein: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (BPG-independent PGAM 1) (Phosphoglyceromutase 1) (EC 5.4.2.12) (PGAM-I 1) (O04499)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). Required for guard cell function (e.g. blue light-, abscisic acid- (ABA), and low CO(2)-regulated stomatal movements) and fertility (e.g. pollen grains production).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Bifunctional enolase 2/transcriptional activator
- Enolase 1, chloroplastic
- Cytosolic enolase 3
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Cleavage stimulation factor subunit 50
Sequence:
MATSSAWKLDDHPKLPKGKTIAVIVLDGWGESAPDQYNCIHNAPTPAMDSLKHGAPDTWTLIKAHGTAVGLPSEDDMGNSEVGHNALGAGRIFAQGAKLCDQALASGKIFEGEGFKYVSESFETNTLHLVGLLSDGGVHSRLDQLQLLIKGSAERGAKRIRVHILTDGRDVLDGSSVGFVETLEADLVALRENGVDAQIASGGGRMYVTLDRYENDWEVVKRGWDAQVLGEAPHKFKNAVEAVKTLRKEPGANDQYLPPFVIVDESGKAVGPIVDGDAVVTFNFRADRMVMHAKALEYEDFDKFDRVRYPKIRYAGMLQYDGELKLPSRYLVSPPEIDRTSGEYLTHNGVSTFACSETVKFGHVTFFWNGNRSGYFNEKLEEYVEIPSDSGISFNVQPKMKALEIGEKARDAILSGKFDQVRVNIPNGDMVGHTGDIEATVVACEAADLAVKMIFDAIEQVKGIYVVTADHGNAEDMVKRDKSGKPALDKEGKLQILTSHTLKPVPIAIGGPGLAQGVRFRKDLETPGLANVAATVMNLHGFVAPSDYEPTLIEVVE
Protein: V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 2) (P62815)
Organism: Rattus norvegicus (Rat)
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P21281}. Melanosome {ECO:0000250|UniProtKB:P21281}. Cytoplasm {ECO:0000250|UniProtKB:P62814}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit
- V-type proton ATPase subunit E 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit F
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit G
Sequence:
MALRAMRGIVNGAAPELPVPTGGPMAGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFEKNFITQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH
Protein: Paired box protein Pax-9 (Q98866)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEPAFGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPNVVKHIRTYKQRDPGIFAWEIRDRLLADGVCDKFNLPSVSSISRILRNKIGNLSQQNQYESSKQASHPQPQPTIPYNHLYSYPTPIAAAGTKVPTPPGMPTLPGHMAMHRIWPSSHSVTDILGIRSITEQQNAEWIAHSEQLCHSSQHPSLPPSHPSVTLHGVQRHHVGLCDRPHMAAAQWQCSLSPQL
Protein: Elicitor peptide 2 (Q9LV88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Elicitor of plant defense.
Interaction partners:
- Elicitor peptide 3
- Leucine-rich repeat receptor-like protein kinase PEPR1
- Leucine-rich repeat receptor-like protein kinase PEPR2
- Elicitor peptide 5
- Elicitor peptide 7
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- NDR1/HIN1-like protein 10
- Elicitor peptide 6
- BRISC and BRCA1-A complex member 2
- LRR receptor-like serine/threonine-protein kinase EFR
Sequence:
MEKLDKRREEETYLWIPVQFLDQALIAVLKCIGLLCQPAKKTAPSPVTFNQPEEQEEDYGVALKDDDVVVLLRDNKAKSKKRDKEKPSSGRPGQTNSVPNAAIQVYKED
Protein: Flagellar protein FliL (Q9R7B5)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Subcellular location: Cell inner membrane {ECO:0000256|RuleBase:RU364125}. Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MTDASASLDTKPRRGRGLLRALVFLLLGAFLLAAGFGAGYFYFANPLSPAKDVLRLIERTPEADEPAADPDAPQKVPRPTPERESFVTSYYQFKEPLTTNLRASRRLLQAGIGLSTQYDQKVMDNVARNEVALRSDMLAIVGTFSEEELQDKAGRDRLAELRGAVNARLQQLEGFGGIEAVFFPSFILQ
Protein: Centromere protein J C-terminal domain-containing protein (Q386I1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Clathrin heavy chain
- Clathrin coat assembly protein, putative
- Polyubiquitin, putative
Sequence:
MAEVKLPRPGRSPSSGKVTVTTSSKRQAKSAPFKFLRKDEGRLSYSCTPESPVSVCGNVSHGNSMTNRELAAMDRNSSRSLREAIANDMRKGKANDPFGGFEVAVPKRGPPPGASPREERGMSLEGSQLHDNVSVSSPPAAVQHTSSRLAVGDANHSESIGDKSVSTKRLESRTSDESERTVEPQPQQHQQLQLQQHQLQQQQQMQLQQQLQQQQQLQLQQQQQQLQLQQQQQQQIQLQQQQHQLLPNHSHQMQLQTQLPQQHPPQGYQQQLLNHGQQWQHSQVQAQPQPTRQRVSPMNTNTFSRNIEESELGDWCPSPVQQRRWRNGESDNGHTRRSIATRYGDPGELDGEYVSGGRSLRNYFRPPLPEYHQPREEEELVGQLEEELRVTKEERSRYYQLRMQLERERQRFEEYRSGVEQDMEDERVRLDAARASEQRQAKKDVKVVEERYKSTLELLRTERDSNTKLTQENEMLRQQLEVTTARLRESQKLQKAETNRLRREIESLTRRNEELLELAREQQLTALERGETLTPPLLLHSGPNIRHKASANSSSAPRSGEDVYELHGSSLPTRSYSSEQNRYLDIVERERRLAEEEEHERKRLEAEDRRRAEMEERRRRIEAEEARRAKEEEERRRRIEEEDRRRAHEEEERRKRVEAEDRRRAEEAKRKSAEAEERRRAEEEEKRKRAEAENRKRVEEDKVRRADAEVAPRRKVDAKKVVREERSQAIDEGATSKKLEARQQRRSSGHPVLTPRAQSSKTANSAVATARAASQACTYATRKGRRAPTASELTADNEPVPDEDFPNDTVVSQTSLGENPNKREVLYRSGKREIHYTNGTRKIILPSSHVMLYFANGDIKRTFPSGKSTYWYAVAQTTHTQYADGAQVFQFHSTGQVERHLPDGKKEILYPDGIYKVVHPDGRDETIFPDES
Protein: Protein kinase, putative (EC 2.7.1.-) (Q382D0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTKEDHGEEMVTHTPQVLNVRTTGESVSANPLRGVGLKDCGVFSPTSSTFCDTSRLMGNTGRSVENSTVTFVTGAPGKEEADRRHCRVGTIAAVALLMLTGVFTLSFTSLLSAHYIGSSVVIGTTGLIEKEAVRSVVKIMRSTVLQLPDFAHIVNAKYIRNQTSLYTVNRFPRDPRALLYSLMSLLSTFKDTIAYFKFVHEGGSYAFAVNYDVGDGGNNSVVLGAYNNDSSRASFVVYDAIRLKRLHEDSNRNWDISHDLSRTLSPFGAVARQWHESGSNKRWIPSEIEHTGEYFNYVIPFHVGGALGACIVGLSTDRLLLESRPLVEALRSHGRAMLFDDSRDIVILNSWGQPQSWDENPSDGELVFKHLTLEGINDSIVVDLVREMEKHRDPTTDRLSDSVELTFPNSGSHVDGRLGRITDESGLDVTLAVVTMRSDFLEGVVRTRNVTIVSISVIILLSAVFSLVSTYYLVKPLMLLVSALKSASNLEIPDNADIFLGRSRIVEVRKIQGHYAKLRRQLAVLLKFIPEAILARVESKSEAGGHIRANGSATETPGESSTAFVRIMGASISVTWNAGDQQRDVALNCGIFKEKPNVFNRRHCTVIAIQVYHPDVWKSSTKYHAALIEVATEHSGCVEALDPDRALISFGAHAALPMHCRRCCQFAFDLFAKLPLDHRDSVTMLVDTNEFLVGTCGAFSRNARVLFGADHLFQLSHAVRDGPCRIAATSGGASHMQGFLAFPVDCVLLPCSTLPIVLFELRPGESSSEVSLSISKQFRLGFAAMRQGRYGEAMAHYLPMVKMDMQAKRLMRLCRQRCRRNDTVPYVRVLDNHYCVNSSDCKPEEQDESDIKDRVPETIDSPRRPDGEGSESDSSDQGSESLFKMYAPSSSSSLDGSGCAEGANAADVVPLFLTDSNRNVWTRSLKKISEGAFSTIFLGVAEDGAQVAIKCIPRLRRDVVAESLEKEMEVASKLHHPNIVRYVSCSITPSHLSIIMEYVPGGSLHSVIKNFGCVSPYVARRFTVDILQGLNYLHNLGIVHCDVKPHNVLLGTDGVCKLSDFGSTISEASVMARTLADGVMLRGTALYMAPEVAAGGRCTPQSDIFSFGISLLEMLLGRPPWQWSSTAPAGSDATRLRSLFNRDLLFVQSLALGHLEPVIPASVDHEAAAFVRACCHMNPSMRPSASSLLSYAFLL
Protein: Uncharacterized protein (Q57WR4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MPEQLGAEAPQHVVPEGDQSAGSEAGNVTRGTKNHDDSDPFVSLRHMEDRKQLETQARAVVTALLAEKGEVYVQGLLQAEIQRVKKKESEAAAIKKKISAATKLAGELKGDIRRETEAKAEEEHMCKNLQAEMKRRSTLTEEATRRMESRRLTLKKDVETSVRDVREKYDDRKRQAMELVEENKRLTDEVAKMRKEFDEARATYADTCKERETYVESLIRSYREVTREVETLEAKIALVRRERQASEQRKASLEKQLESYNSQFGSLSEGQSVEDAERMAKEQREEAEARIAQLESEKKEASEIRLRLDKETATWRAALAAHKRELPRLEKAKLAAEKRCRQAQERARQQLKEDATTTKDQEDGGM
Protein: Serine/threonine-protein kinase 17A (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 1) (rDRAK1) (Q9GM70)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Acts as a positive regulator of apoptosis. May also act as a regulator of cellular reactive oxygen species.
Subcellular location: Nucleus {ECO:0000269|PubMed:11279167}.
Interaction partners:
- Ig-like domain-containing protein
- Titin
- Chromosome 7 open reading frame 25
Sequence:
MIPLEKPGSGGSPSAAASGSGPGGLLTEIRTAIRTEPFQDCYSLSPGRELGRGKFAVVRKCIQKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQDNPWVINLHEVYETSSEMILVLEYAAGGEISDQCVADRDEAFNEKDVQRLMRQILEGVHFLHTHDVVHLDLKPQNILLTSESPLGDIKIVDFGLSRIVKNSEELREIMGTPEYVAPEILSYDPISMATDMWSIGVLTYVMLTGISPFLGDNKQETFLNISQMNLSYSEEEFDTVSESAVDFIKKLLVKKPEDRATAEECLKHPWLTQSSIQDPVLRVKEALEEANALQKGDSVPEISSATEKPGTEESIVTEELIVVTSYTLGQCRQSEKEKMEQKAISKRFKFEEPLLQEIPGEFIY
Protein: Kekkon 6, isoform B (A0A0B4KHL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform E
- Uncharacterized protein, isoform F
- Male sterile
- Glycoprotein 3-alpha-L-fucosyltransferase A
Sequence:
MHRSMDRRRSRTPRTLPVCWILLCLVAWTVADDWSLSCASNCTCKWTNGKKSAICSSLQLTTIPNTLSTELQVLVLNDNHIPYLNREEFSTLGLLNLQRIYLKKSEVQYIHKESFRNLKILVEIDLSDNKLEMLDKDTFMGNDRLRILYLNGNPLKRLAAYQFPILPHLRTLDMHDCLISYIDPMSLANLNLLEFLNLKNNLLESLSEYVFQHMANLKTLSLEENPWQCNCKLRKFRGWYVNSRLSSVSLVCKGPPAQKDRTWDSVDDELFGCPPRVEIFNNEEVQNIDIGSNTTFSCLVYGDPLPEVAWELNGKILDNDNVLFESESIASDKLWSNLTVFNVTSLDAGTYACTGSNSIGSMTQNISIYLSEIVQHVLEKTPETFWYFGLIMGIFGTVFLLISISFVVCLCKRTTRQHRHANKAGVKSSVSFNDQEKKLLDSSVTTTTNDRGDSYGIDNQPTSIGMNKGDSAGMGFNQIEIHAVESHRHGSMLVQQQPQQQQVAGGGGMRQQLMQVKDSTCGMMSVPTSMAGHAHSHPAQISEEFPLNVGVFPPPPEFCSNIVPNPAFGGNIFIRVSVTQDMLDGADLNMYPDLLNIPKRMQDVQESGAGAVAVPEGQFATLPRHTARRGILKKDTSLQQQQQQHQQQHQHQQQQQQQQIQQQQHQQLQQQHQPSGLYTHDEIVTYNLEASGYDPHQSGYHSNAMELPPPPPPPAVTAVVQCHHPSPNNCASCINNAPPPPSACQSPPVEVTPMRPLDSSAYPKYDNMGRRITASGGLGGSNLSLHDEERYENETLFGQAESQTKGMPEQSQDLHQPQEVTQGQDKGGGPGEFVSLXYYGTQV
Protein: Glutaredoxin-1 (Q9NLB2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- Glutathione peroxidase
- Glutathione reductase
- Glutathione reductase.
- Thioredoxin reductase
- Thioredoxin-like protein
- Thioredoxin reductase.
- Dihydrolipoyl dehydrogenase, apicoplast
- Dihydrolipoyl dehydrogenase
- Ribonucleoside-diphosphate reductase small chain, putative
Sequence:
MAGTSEAVKKWVNKIIEENIIAVFAKTECPYCIKAISILKGYNLNSHMHVENIEKNPDMANIQAYLKELTGKSSVPRIFINKDVVGGCDDLVKENDEGKLKERLQKLGLVN
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) [Cleaved into: Ghrelin; Obestatin-23; Obestatin-13] (Q9QYH7)
Organism: Rattus norvegicus (Rat)
Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
Subcellular location: Secreted.
Interaction partners:
- Growth hormone secretagogue receptor type 1
- Leptin
- Insulin-2
- Membrane-bound ghrelin O-acyltransferase MBOAT4
- Pro-neuropeptide Y
- Pro-glucagon
- Agouti-related protein
- Peptide YY
- Somatotropin
- Insulin-1
Sequence:
MVSSATICSLLLLSMLWMDMAMAGSSFLSPEHQKAQQRKESKKPPAKLQPRALEGWLHPEDRGQAEEAEEELEIRFNAPFDVGIKLSGAQYQQHGRALGKFLQDILWEEVKEAPANK
Protein: Auxin-responsive protein IAA18 (Indoleacetic acid-induced protein 18) (O24408)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 7
- Auxin response factor 5
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 18
- Auxin response factor 1
- Auxin response factor 8
- Auxin-responsive protein IAA10
- Auxin transporter protein 1
- Auxin response factor 6
- Auxin response factor 9
Sequence:
MEGYSRNGEISPKLLDLMIPQERRNWFHDEKNSVFKTEEKKLELKLGPPGEEDDDESMIRHMKKEPKDKSILSLAGKYFSPSSTKTTSHKRTAPGPVVGWPPVRSFRKNLASGSSSKLGNDSTTSNGVTLKNQKCDAAAKTTEPKRQGGMFVKINMYGVPIGRKVDLSAHNSYEQLSFTVDKLFRGLLAAQRDFPSSIEDEKPITGLLDGNGEYTLTYEDNEGDKMLVGDVPWQMFVSSVKRLRVIKTSEISSALTYGNGKQEKMRR
Protein: RFX transcription factor (Q9U1K2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTRLAPQRQFILSTRSAIVDATSPPEDSAEEQQQLTVEVESATNGVITNSTTSPPPHAEQFEFCTEDGVVVSATLEDVMTQVKLFPLLQNCQLLQKKLVDEDDDSTGVGATDADQLEVISVILPMDAEDSTSDAHLHGHVVNSSSDTMGTITTTEPNGTTVTHSIPIHSMADLAAIKDGVDLAQQVANGQVTVVQTTEDDDGTPFITVTVSGQEQNYQVQYVDSELYHSNSSQTQMTYPFCPVGDYQGNGQTAYYSTTGQYGTTSSAGGSSNGAHSTTLPYLVPVEEGILLNGSAHSLSQSQSQSHGRDSPHSLTEVAYIQEAQSTPQTPTSTTTTHSASGGSLGTGGGGASPDSDQSALSSSNKIASATIKWLSRNYETADGVSLPRSTLYNHYMHHCSEHKLEPVNAASFGKLIRSVFSGLRTRRLGTRGNSKYHYYGIRIKPGSLLNSQAMDDKQMLAAGYGPSSDGTGGPGSGPMVSVTSSTAGQLTGSNGLGGGHGQRHSNGTKKHTFKPETYEACIQYIGDGTSALPSFPPIELNHSFNSELTLEDVDTFRGLYREHCESFLDAVLNLEFNTVEFLLRDFWRASDNNNLDECEEEKYLSKTKLYLLCHCAEVQKFVREVDYQFYQNTVDVIIPDVLRSIPNALTQAIRNFAKNLEIWLCESMLGVPEQLAQIKNSAVSAFCQTLRRYTSLNHLAQAARAVLQNGAQISQMLSDLNRVDFHNVQEQAAWVSQCAPAVVQRLESDFKAALQQQSSLEQWASWLQLVVESAMEEYNGKPTYARAARQFLLKWSFYSSMIIRDLTLRSASSFGSFHLIRLLFDEYMFYLVEHKIAEAQDKTAIAVICERMKKDMDFEFECQFAYITSDTEHQTTPSSASSGGDVGNEAKRLKQE
Protein: Pectate lyase A (EC 4.2.2.2) (Pectin lyase) (EC 4.2.2.10) (D3JTC1)
Organism: Paenibacillus amylolyticus
Function: Catalyzes the depolymerization of both polygalacturonate and pectins with low (20-34%) and high (90%) levels of methyl esterification, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Does not show xylanase and cellulase activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKKMLTLLLSAGLVASIFGVMPAAAAPTVVNSTIVVPKGTTYDGQGKTFVANPSTLGDGSQAENQKPVFRLEAGATLKNVIIGAPAADGVHCYGNCNISNVVWQDVGEDALTLKSSGTVNITGGAAYKAYDKVFQINAAGTINIKNFRADDIGKLVRQNGGTTFTVNMTLDNSNISNVKDAIMRTDSSSSQGRITNTRYSKVPTLFKGFASGKTSQSGNTQY
Protein: F-box protein At3g57580 (Q6ICX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDRGKMNVSLPTDLIREIFARLPSKSVARFRTLSKQWASILRSTDFTKLFLSRSSNRPRLLFAVERYKCNEWQFFSSPQSQNRYEKSAHLEFHSKFSGDVSHYICSYASGLLYFPAVHIVDTETIVICNPITGMYTGLPVIMKDRRSRGFLVFDPVDKRFKAFDTHFILTLGSGELKWREKNIPCPLYERCSSNQGICINGVLYYLAKTVLVETVFGLTFLIVRFDVSSEEFKFIDAARFNDRLKDPTRLSLVNYMGKLGVTDCNCVDAGGRRTVELCLWVLEDVEKLEWVKYVYTLPENEVLASCEFSVAGVTATGDIVLCMKYTCKPYYVFYFNPEKKTLQTVEIQGFGAKLEEVENRGEVFAYVDYVEDLSLNDAKQLKSSISHVKSLCPCCQKLVQPENIGEVV
Protein: Structural maintenance of chromosomes protein (Q9V3A7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
- Chromosome associated protein G, isoform F
- Condensin complex subunit 2
- Condensin-2 complex subunit
- Structural maintenance of chromosomes protein
- Condensin complex subunit 1
- Chromosome associated protein H2, isoform E
- DNA topoisomerase 2
- Structural maintenance of chromosomes protein 5
- Nipped-B protein
- DNA replication licensing factor Mcm7
Sequence:
MQKARPSKGTPKAAGGARQSGQFRVPQLTAQQQLRAQQQQEEEDAAVDALDDALIFDDEEGGTRIGDIYIPPPVPPHCSMESTGPRLIISKIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNLRSCSVAVHFKQIVDKGDGTCEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPKGQTENETGMLEYLEDIVGTQRYIRPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMRMKMEGKIPGILGRLGDLGGIDAKYDIAISTACGRLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEHHRREANSRINTPENVPRLYDLVKVEDDRVRTAFYFALRNTLVCDDLEQGTRIAYGRERYRVVTLRGEMIEMTGTMSGGGSRPIRGKMGTQVRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQLAPLKLNEIPGETEPQAPLKELNEEELEAETLEALQYKQTMLEEDLKTKKPNLSCIKEFNEKRLVYLDRVRVLEDITSKRNEMRDKYEEVRKRRYKEFMDGFSIITRKLKEMYQMITLGGDAELELVDSMDPFTEGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGIYKVSDCTDSITMLNYPPTLPTQSPVVANSQYVGGTIEGDNTIAAENQDDTPTKKSQSPPSEQIVRLISELGRDTTFAPPLESTVRDTILAQNLKQAATEVAAQPSDATGRVTTDVSLASPPSSPAILNV