wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 2C, putative (EC 3.1.3.16) (Q57UN2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tyrosine phosphatase
- SAP domain-containing protein
Sequence:
MYTSVRKPPLSTAKLSEKTDAAGKGNLNGVAESPTSRDGGIGSSMPYVARKPNSGDGQGRPGEVQRAGQVTYQTTNALFTGSTVPGKTKDVSTAKSSGGGDHLNNGDRPPLVGDNNEVSSPRTIKMNSSPPRRYFHRGAINCNSSENVAAVLGGSTLISGERVGSGSGYPRRVFSGPPSTRMLNQGGEEPAQKPQPPGSSRSKSGIRQLQFALNGNSSQRLLPVPPRQLCPSNPARRGGGAATVTPRCSDARRQKQDSTDPFDMTQVLNGVGTQLGLPSYCPGAESSQGSNRLRGSKPPSPSLLPLASLRSQQMPSTAGVPAPRSLSESQQLSINPSGVFGCATDCKNGLGYDFRVVASTGKSFNLPIKLTAGVGCVQGLRPTMEDEHFIRLQATTAVGQPVSLLGILDGHCGRRVAELAAKHVPDNFIAHPALGENNALAFVESIIQADRAIFHSIGKGSGGVGLSAGFGGSGGSTLIAAAVHGRMLYVACLGDARAVLYDGNTTIPMSEDHKPLNKKEHTRILQCGGFVQLGRVCGVLAVSRALGDYEFKFNGNRFISNRELMVSNVADVRQINLTDSSKFLLLACDGLWDAVQNEEATQFVRDFLSYTPDVGSSPEATKRAINNCCQKLAEFAVSRGSTDNVSVMLLFFHNVADVVASFDRASDATTSRATVTSPVSPRLFSASRGVNAGFTGMESRLAGISGGSSSGAFGGSSGAEGSSVRGAGRTKVDRGASWLTRSRSLW
Protein: Glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) (28 kDa milk glycoprotein PP3) (Lactophorin) (Proteose-peptone component 3) (PP3) (P81447)
Organism: Capra hircus (Goat)
Subcellular location: Membrane; Peripheral membrane protein.
Interaction partners:
- L-selectin
- Beta-casein
- Alpha-lactalbumin
- Kappa-casein
- Tyrosine-protein kinase
- Beta-lactoglobulin
Sequence:
MKFLCILLLASLAATSLAILNEPEDETHLEAQPTDASAQFIISNLQISTEDLSKEPSISREDLISKEPNVIRSPRQPQNQNPKLPLSILKEKQLRNATLGSEETTEHAPSDASTTEGKLMELGHKIMKNLENTVKEIIKYLKSLFPPASEVVKP
Protein: E3 ubiquitin-protein ligase RNF43 (EC 2.3.2.27) (RING finger protein 43) (RING-type E3 ubiquitin transferase RNF43) (Q5NCP0)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Along with RSPO2 and ZNRF3, constitutes a master switch that governs limb specification (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}. Note=May be secreted. {ECO:0000250}.
Interaction partners:
- R-spondin-1
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 5
- R-spondin-2
- R-spondin-4
- R-spondin-3
- Frizzled-5
- Frizzled-8
- Frizzled-1
- Frizzled-7
Sequence:
MSGGHQLQLAVLWPWLLMATLHAGFGHTGRVLAAAVESERSAEQKAVIRVIPLKMDPTGKLNLTLEGVFAGVAEVTPAEGKLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGANAVLFDITEDRSAAEQLQQPLGLTKPVVLIWGSDAAKLMEFVYKNRKAYVWIELKEPPAGANYDVWILLTVVGTVFVIILASVLRIRCRPHHSRPDPLQQRTARAISQLATRRYQAGCRRARAEWPDSGSSCSSTPVCAICLEEFSEGQELRVISCLHEFHRTCVDPWLYQHRTCPLCMFNIVEGDSFSQAPAASPSYQEPGRRLHLIRQHPGHAHYHLPSAYLLGPSRTSVARTPRPRPFLPSQEPSMGSRHQRLPRTSHLRAPEEQQHLAVSPHPYAQGWGLNRLRCTSQHPAACPVALRRARPHESSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVVNCTDVSLQGIHGSSSTFRSSLSSDFDPLVYCSPEGDLQGKGIQPSVTSRPRSLDSVVPRGETQVSSHIHYHRHRHHHYKRQFQWHGRKPGPETGIPQSMPAASHTQLEPSLPDQQLITPNPTASSMLPNPQRPRALTEPAPGLAEASSPSPSPKPNPSGLLNLQKSSLTVRHPHRKRRGGPSEPLPTSLPPDLTVHTACPVFPHYSPRLAYPWPPEVHPLMFRPPGPDRRLLHEVPGPCYSSSQPVWLYLNPCQPLGPCLPGEGHSKWTFDSPEGRRCPYSHCQVLPAQPGSEEELEELCEQAV
Protein: Uncharacterized protein (Q386C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAGTSLPSATTSRRYAAKVEKGENAWRREWSGFMSGVSLKDLRKGGGVSLPKSGDLGAMASAGSGEGCTYSYLFSSAADKKAERLAKKQEEAEKRKMRAQQSQCANDPLAHLSKHERTLEEAKQRGLKVDGMTRKEIRQFLNLTISKEQQEAEKRLQEEEFKPHKLMDEKLQWYQQGPHPIDIIAEKLVMRKAIKKGKQLGLRYNYLLPHPSWVARRERRRRETPLIGLGKRFIFDDEGNMLDNFGTCHEAPEAFPQTGEENETTQHGESGSHDQKSLLASTQQRQRASEPTTLCTSTLDAVAVLVDPREVSRSFVRAVVRNRDAAIAIKNANLTTSYINSSLIKGPSIGVEDAEKEEGEKRGAANSLLKRPRLNSTDGRKVVPHKRSKAASFEP
Protein: LD47649p (Q960J4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKQTFLEMKNMERFSERDALTIARRGFDDTMEPQMEWRPLLEVDNVPDHPNGNLSKQRQVQMDREATTLRALYFSPDMIPDSPAEAELEPHFAHDIPVIPMDDLTGNPDAVNDYSALAWPEPKKYAPSSGVGANISGSDMGFNDNMLTGLGAGPNLMQNPFDPFMGGMPAPTGMPPGPNMMPNQVPNGTPQIWQNQMGPVGGPPGVPPMMNGPGGPGMDMSNMNMNNMPPQNFMGNQFGSPVSPFGSGPPPGFNQYPPMMMNGPGPGPVMGPNGPVMGPNGPMMNGPPNGPMMNGPPNGMGPGLMMGGPRNNNNNNNRNKNNGGGIWRSGGNNFQENSGGNWRSAGSGPNRGGGGGNGNTGVCKQFMRGHCNMGKNCKYVHPQKKRL
Protein: Semaphorin-4F (Semaphorin-M) (Sema M) (Semaphorin-W) (Sema W) (O95754)
Organism: Homo sapiens (Human)
Function: Probable cell surface receptor that regulates oligodendroglial precursor cell migration (By similarity). Might also regulate differentiation of oligodendroglial precursor cells (By similarity). Has growth cone collapse activity against retinal ganglion-cell axons (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:Q9Z143}. Perikaryon {ECO:0000250|UniProtKB:Q9Z123}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z123}. Note=Colocalizes with DLG4 at synapses. {ECO:0000250|UniProtKB:Q9Z123}.
Interaction partners:
- Plexin-B1
- Plexin-B2
- Plexin-B3
Sequence:
MPASAARPRPGPGQPTASPFPLLLLAVLSGPVSGRVPRSVPRTSLPISEADSCLTRFAVPHTYNYSVLLVDPASHTLYVGARDTIFALSLPFSGERPRRIDWMVPEAHRQNCRKKGKKEDECHNFVQILAIANASHLLTCGTFAFDPKCGVIDVSRFQQVERLESGRGKCPFEPAQRSAAVMAGGVLYAATVKNYLGTEPIITRAVGRAEDWIRTDTLPSWLNAPAFVAAVALSPAEWGDEDGDDEIYFFFTETSRAFDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPEHGRASSVLQDVAVLRPELGAGTPIFYGIFSSQWEGATISAVCAFRPQDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVTQVNTTNCGRLQSCSECILAQDPVCAWSFRLDECVAHAGEHRGLVQDIESADVSSLCPKEPGERPVVFEVPVATAAHVVLPCSPSSAWASCVWHQPSGVTALTPRRDGLEVVVTPGAMGAYACECQEGGAAHVVAAYSLVWGSQRDAPSRAHTVGAGLAGFFLGILAASLTLILIGRRQQRRRQRELLARDKVGLDLGAPPSGTTSYSQDPPSPSPEDERLPLALAKRGSGFGGFSPPFLLDPCPSPAHIRLTGAPLATCDETSI
Protein: Uncharacterized protein C2G2.14 (O43013)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Spindle pole body-associated protein sad1
- Lap-Emerin-Man domain protein 2
- Spindle pole body component alp14
- Outer kinetochore KNL1 complex subunit spc7
- Bouquet formation protein 4
- Meiotically up-regulated gene 61 protein
- Integral inner nuclear membrane protein ima1
- ADP,ATP carrier protein
- Uncharacterized protein C4D7.07c
- Karyogamy meiotic segregation protein 1
Sequence:
MSFNPAAGLLGKLKKLWNDTKNDYLEWERSQQGQISESVVKNHSPSKRKRRPSKEPSLSPKRRKNILNDQKKDEESIPNAGTQSQNFTHLSASKIRISDEDRIKPLVDLNQDHSFDMAYLTPASAPPPRFRFVPPKSDAKSHSAPRSLEGVTSLSDSHFNSLEANLKAISKDSNNKAHNNRYDESSLTNPEFSILVERLKSIEENLQSLQERISHCERSVSLSPSFAPPSNVKSPVQQHRSFVSSSARAKKNWGRQSNSPNSNKKTDHAYPGASMNTERGLIQNLEDSDDIHEESSDTLEEPLLINELNRTSFLNSNNNLKLNEAEENQNLLNLRSPKSSGKADNLTIKSSSNIDKVTSNDLYLDNNLQSHFKVTESQPTNLGRKEYSNSPFSIRARKDAATTSSSFESYHNTQTIQSPMKFTKATPLKDNESASVDESKVNVLSENQSLQADTATLEQLTPIPKARWNQLANKHPSLSNSAASPPVSSPGLRRSHIPVHEGLKHTRDGVAETKDALAKLREKMQERLKNHTS
Protein: Sugar ABC transporter, ATP-binding protein (A0A0H2ZMS4)
Organism: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Interaction partners:
Sequence:
MVELNLKNIYKKYPNSEHYSVEDFNLNIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGTASIDGVVVNDVAPKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDINKRVQEAAEILGLKEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATKNPAGTGTIGRVEQIGTPQEVYKNPVNKFVAGFIGSPAMNFINVKLVGSEIVSDGFRLKVPEGALKVLREKGYEGKELIFGIRPEDVNAEPAFLETFPDCVVKATISVSELLGSESHLYCQVGKDEFVAKVDARDYLQTGATVELGFDLNKAHFFDVETEKTIY
Protein: Glycine--tRNA ligase (EC 6.1.1.14) (Glycyl-tRNA synthetase) (GlyRS) (P9WFV6)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Function: Catalyzes the attachment of glycine to tRNA(Gly).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
Interaction partners:
Sequence:
MHHPVAPVIDTVVNLAKRRGFVYPSGEIYGGTKSAWDYGPLGVELKENIKRQWWRSVVTGRDDVVGIDSSIILPREVWVASGHVDVFHDPLVESLITHKRYRADHLIEAYEAKHGHPPPNGLADIRDPETGEPGQWTQPREFNMMLKTYLGPIETEEGLHYLRPETAQGIFVNFANVVTTARKKPPFGIGQIGKSFRNEITPGNFIFRTREFEQMEMEFFVEPATAKEWHQYWIDNRLQWYIDLGIRRENLRLWEHPKDKLSHYSDRTVDIEYKFGFMGNPWGELEGVANRTDFDLSTHARHSGVDLSFYDQINDVRYTPYVIEPAAGLTRSFMAFLIDAYTEDEAPNTKGGMDKRTVLRLDPRLAPVKAAVLPLSRHADLSPKARDLGAELRKCWNIDFDDAGAIGRRYRRQDEVGTPFCVTVDFDSLQDNAVTVRERDAMTQDRVAMSSVADYLAVRLKGS
Protein: LUC7 like 3 pre-mRNA splicing factor (H0YAR4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEVQRKYAQMKMELSRVRRHTKASSEGKDSVVLQNILRTTVRRFLEEY
Protein: DNA-directed RNA polymerase subunit beta (RNAP subunit beta) (EC 2.7.7.6) (RNA polymerase subunit beta) (Transcriptase subunit beta) (Q5F5R5)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
- DNA-directed RNA polymerase subunit alpha
- Multifunctional fusion protein
- DNA-directed RNA polymerase subunit beta'
- Large ribosomal subunit protein uL6
- DNA-directed RNA polymerase subunit omega
- Large ribosomal subunit protein uL11
- Transcription termination/antitermination protein NusA
- RNA polymerase sigma factor RpoD
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL10
Sequence:
MNYSFTEKKRIRKSFAKRENVLEVPFLLATQIDSYAKFLQLENAFDKRTDDGLQAAFNSIFPIVSHNGYARLEFVYYTLGEPLFDIPECQLRGITYAAPLRARIRLVILDKEASKPTVKEVRENEVYMGEIPLMTPSGSFVINGTERVIVSQLHRSPGVFFEHDKGKTHSSGKLLFSARIIPYRGSWLDFEFDPKDLLYFRIDRRRKMPVTILLKALGYNNEQILDIFYDKETFYLSSNGVQTDLVAGRLKGETAKVDILDKEGNVLVAKGKRITAKNIRDITNAGLTRLDVEQESLLGKALAADLIDSETGEVLASANDEITEELLAKFDINGVKEITTLYINELDQGAYISNTLRTDETAGRQAARVAIYRMMRPGEPPTEEAVEQLFNRLFFSEDSYDLSRVGRMKFNTRTYEQKLSEAQQNSWYGRLLNETFAGAADKGGYVLSVEDIVASIATLVELRNGHGEVDDIDHLGNRRVRSVGELTENQFRSGLARVERAVKERLNQAESENLMPHDLINAKPVSAAIKEFFGSSQLSQFMDQTNPLSEVTHKRRVSALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYARTNDYGFLETPYRRVIDGKVTEEIDYLSAIEEGRYVIAQANADLDSDGNLIGDLVTCREKGETIMATPDRVQYMDVATGQVVSVAASLIPFLEHDDANRALMGANMQRQAVPCLRPEKPMVGTGIERSVAVDSATAIVARRGGVVEYVDANRVVIRVHDDEATAGEVGVDIYNLVKFTRSNQSTNINQRPAVKAGDVLQRGDLVADGASTDLGELALGQNMTIAFMPWNGYNYEDSILISEKVAADDRYTSIHIEELNVVARDTKLGAEDITRDIPNLSERMQNRLDESGIVYIGAEVEAGDVLVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRMPTGMSGTVIDVQVFTREGIQRDKRAQSIIDSELKRYRLDLNDQLRIFDNDAFDRIERMIVGQKANGGPMKLTKGSEITTEYLAGLPSRHDWFDIRLTDEDLAKQLELIKLSLQQKREEADELYEIKKKKLTQGDELQPGVQKMVKVFIAIKRRLQAGDKMAGRHGNKGVVSRILPVEDMPYMADGRPVDIVLNPLGVPSRMNIGQILEVHLGWAAKGIGERIDRMLKERRKAGELREFLNKLYNGSGKKEDLDSLTDEEIIELASNLRKGASFASPVFDGAKESEIREMLNLAYPSEDPEVEKLGFNDSKTQITLYDGRSGEAFDRKVTVGVMHYLKLHHLVDEKMHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYENIVKGEHKIDAGMPESFNVLVKEIRSLGLDIDLERY
Protein: Response regulator (Q9X181)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Interaction partners:
Sequence:
MKRILVVDDEPNIRELLKEELQEEGYEIDTAENGEEALKKFFSGNYDLVILDIEMPGISGLEVAGEIRKKKKDAKIILLTAYSHYRSDLSSWAADEYVVKSFNFDELKEKVKKLLS
Protein: Probable peptide/nitrate transporter At3g43790 (Protein ZINC INDUCED FACILITATOR-LIKE 2) (Q3EAQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Zinc transporter ZTP29
- At5g23760
- SPX domain-containing membrane protein At1g63010
- Vacuolar iron transporter homolog 2
- Zinc transporter 4, chloroplastic
Sequence:
MADDESRTILLEKNEDCPGCIIDRTKQQQRGVPYLHLSFIWLVSLCTALPISSLFPYIYFMIRDFHIAKQEEDIGFYAGFVGSSFMIGRALTSIFWGKLADRYGRKPIILIGTFSVIIFNTLFGLSTSFWLAISVRFLLGCFNCLLGVIRAYASEVVSEEYNALSLSVVSTSRGIGLILGPAIGGYLAQPAEKYPNIFSQSSVFGRFPYFLPSLVISVYATAVLIACWWLPETLHTRCRIAQGRLNPTELNDDESRGGGLDEQKIINKPSLLRNRPLMAIIIVYCVFSLQEIAYNEIFSLWAVSDRSYGGLSFSSQDVGEVLAISGLGLLVFQLLVYPPLEKSVGLLAVIRLSAVLLIPLLSCYPYIALLSGVTLHLVINCASIIKNALSISLVTGLFIMLNKAVPQNQRGAANGISMTAMSVFKSFGPAGGGVLFSWAQKRQDATFLPGQIFAPCDEMVFLVLNLVQLVGLILTFIPYISQIQ
Protein: Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase (PRPn C-P lyase) (EC 4.7.1.1) (P16688)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose 1,2-cyclic phosphate 5-phosphate (PRcP).
Interaction partners:
- Putative phosphonates utilization ATP-binding protein PhnK
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Probable transcriptional regulator PhnF
- Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
- Phosphonates-binding periplasmic protein
Sequence:
MANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTGGIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDATVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYGVMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPALQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYLDEVVLDDAGNRMFVCSDTDYCRQQSEAKNQ
Protein: RNA polymerase-binding protein RbpA (A0QZ11)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Binds to RNA polymerase (RNAP), probably stimulating transcriptions from principal, but not alternative sigma factor promoters (By similarity). Partially restores transcription in the presence of rifampicin (Rif) in vitro; overexpression leads to an increase in the Rif tolerance in vivo, with smaller colonies. Seems to act by removing Rif from its binding site and preventing its further binding. No longer stimulates transcription in Rif-resistant RNA polymerase (with mutations in rpoB).
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta
- RNA polymerase-binding transcription factor CarD
- RNA polymerase sigma factor SigA
- DNA-directed RNA polymerase subunit beta'
- RNA polymerase sigma factor
- DNA-directed RNA polymerase subunit alpha
- Transcriptional regulator WhiB7
- Protein pafC
- Transcriptional regulator, MerR family protein
Sequence:
MADRVLRGSRLGAVSYETDRNHDLAPRQVARYRTDNGEEFDVPFADDAEIPGTWLCRNGLEGTLIEGDVPEPKKVKPPRTHWDMLLERRSVEELEELLKERLDLIKAKRRGTGS
Protein: Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA (EC 1.2.99.6) (P77165)
Organism: Escherichia coli (strain K12)
Function: Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage.
Subcellular location: Periplasm {ECO:0000305|PubMed:19368556}.
Interaction partners:
- Putative xanthine dehydrogenase FAD-binding subunit XdhB
- Aldehyde oxidoreductase molybdenum-binding subunit PaoC
- Aldehyde oxidoreductase FAD-binding subunit PaoB
- Putative xanthine dehydrogenase molybdenum-binding subunit XdhA
- Molybdenum cofactor insertion chaperone PaoD
- Probable hypoxanthine oxidase XdhD
- Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC
- Adenine deaminase
- Guanine deaminase
- Xanthine-guanine phosphoribosyltransferase
Sequence:
MSNQGEYPEDNRVGKHEPHDLSLTRRDLIKVSAATAATAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEIQDGIPSHVTVDLVSAPETTADEIRERMSGNICRCGAYANILAAIEDAAGEIKS
Protein: Fructose-bisphosphate aldolase (EC 4.1.2.13) (Q7KQL9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (Probable). Stimulates actin polymerisation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P14223}. Membrane {ECO:0000250|UniProtKB:P14223}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14223}; Cytoplasmic side {ECO:0000250|UniProtKB:P14223}. Host cell membrane {ECO:0000250|UniProtKB:Q27744}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14223}; Cytoplasmic side {ECO:0000250|UniProtKB:P14223}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Probable ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- transketolase
- Enolase
- Phosphoglycerate mutase
- Phosphoglycerate kinase
- Phosphotransferase
Sequence:
MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY
Protein: E3 ubiquitin-protein ligase listerin (EC 2.3.2.27) (Listerin E3 ubiquitin protein ligase 1) (RING-type E3 ubiquitin transferase listerin) (Q9VW09)
Organism: Drosophila melanogaster (Fruit fly)
Function: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to TER94/VCP recruitment for extraction and degradation of the incomplete translation product (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O94822}.
Interaction partners:
- Ribosome quality control complex subunit NEMF homolog
- BcDNA.GH11023
- FI01658p
- E3 ubiquitin-protein ligase UBR1
- AT08232p
- Uncharacterized protein
- Uncharacterized protein, isoform D
- Protein HBS1
- RING-type E3 ubiquitin transferase
- Large ribosomal subunit protein uL5
Sequence:
MGGKTKQAPRTKNNAKPSSSSRTAELLGSSTPIFVGFSAQTDGGGLVPFAPGFASAEQMPDSFDAAISPQTQIILRKLSKKDPMTKKKALQELHELIEQSDVEVLKNILPLWPKYYLNLASDPEHTVREQTQTVLQLLMAKCKKAMAPYLKLLVPVWLGSRFDTYAPAASIASQSFRDTFAGNANRSREVCMHCQVEILEYATRNLTFHTAATLSIGKSLTPEDAEQKYQRVIISSLKLLSFFMGQTAQTEELSQVKEGFGTLVAHQKFWSFAKHKVPAIKAAWFECIYHILQSVALLDVITPQKTQLTNLCFQFIDDADPVVAPHIWGCVLLLQSNYVDWFVPLNIRKTLLPKLSSLLQNGFNRNAQAICPNLLPFLSKVTQASLQDLDIYDFYQRFFDDMKLAVTKKFDPPLSKSDCIVIHNAYFECLRFLMQQINNNKQREQKEEEFSFSLLDNNVLEPIAWLLKSDSTHVKIFFQHSSALVAFWDRQINNRLDNGDLYAKLLNKFWIRIFELVTQDLSAEEVNEQLLGHVLLLVQDLHMANPSLESPSVKFVEGPNEKIEKSEPTTPVKKAQEAAAFIQKELKQLVIKLVRICLDKANKGSGSGTSSSRYIEQIRTLTKMFNDAAFYKSLTDDGDLASALNKFVSLLGQLSCQACESVVEIVFEILPLLETGKRFEYIENTLMKLPQHGVQNLLLHRLLSYPLCAEAAVRQMLSGPETCEMIARIAEEVVVDNDREKLNLLHKCFFQTDTGDILINAKTVDKILLSMCGPLEQPVVDDAVEVCGSFIAQIMPVICSNNNSSLHVRQHIFLKLFKFSLEHRPEDYLSEDTLWEITTCWQDGLSSKDIEIDDDMLKCCAGIVEELANSAELKADTLDGMAEAMAKFVICSTENIEDEYKRLERIDETLTALLETPLKTTDKVQQFENHCVLLEALHGSVTAGVPFENACLSRNEILPLLQRSTLNFSTIYKLVYQFPPPQDTNDPEDELTEDYCDPNADVLKKWNEPLIAELLQCIRVAGTAECWLEMSVLQSSTEELVLILSEKVQSFMGNSSDLVAIVKERLQQAAVQQSSVIDCRLLSYLRFCPQYAAFEESASILLHEDLSENLVTQGALKTYVIALQFLLPKLSQKAITLSSAIMGTEPPEIWVKAAVFHALLLNNFEGDVNEQTDRNIIVSAVQFMTSIGERQASQKDLLHYNVEIQRQPYESVINTVEFIKLLTEVLKRFPYELSIKNWDAIRIGLSSWVLSVSKSIAQYQDPKTSLFIVAVYELFAALIDFIRSEKQKSSTELLKNMIDEWDSLFAKEVNLVLFKSYYLLTHEVSVDPGFQACYEALLEQITPVIERLDYSFVYSFCKSNSNITLDHLCNFLFKQLYSVQHSVRLSAVHSLRQLTPHFVADDIELNEKQSESLDASTTICKWHFLNRFEDYLTRYDALITKYLEEFTFKLSELDDLEPIDRHNALSYLFLWDCIINACAKSPVALRAVYTNWLNDNKYEENFLHFLFRAMPVDILKNHGAKVHSNGVYKELTWSQQKDRHLPLERYACHLYTEVLRKLPAVVRRWWNATQSRQKNFIDNLTTNYVSSLICSEELKAIANRKEKHENMQVTVHSSTREVLAVYAIDEARMELVITLAPNYPLGAVKVECGKQIGGRASSRNVGMQLTIFLTHQNGTIYDGLTMWKNNLDKKFEGVEECYVCYTVIHQETCQLPKLTCKTCKKKFHGPCLYKWFTTSSKSTCPICRNVF
Protein: Kinesin-related protein 1 (Kinesin family member 1) (Kinesin-3) (Q9NGQ2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. Transports cytoplasmic vesicles and particularly phosphatidylinositol 4,5-bisphosphate-containing liposomes along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12015984}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12015984}; Peripheral membrane protein {ECO:0000269|PubMed:12015984}; Cytoplasmic side {ECO:0000269|PubMed:12015984}.
Interaction partners:
- ADP-ribosylation factor-like protein 8
- Lis-interacting protein
- Kinesin-related protein 12
- Kinesin-related protein 8
- Kinesin-related protein 3
- Kinesin-related protein 7
Sequence:
MNVQVAVRVRPFNSREKERNAELIVQMNNKSTILTRPSALRANPLAAPTADDEKSFSFDYSYWSYDSNDPHFASQSTVYNDLGKEVLKNAWDGFNCSIFAYGQTGSGKSYSMMGYGEEKGIIPLICEELFQRIQSTPSNSNEQTIYKTTVSYMEIYNEKVKDLLNPNNNKTGGLKVRNNPSTGPYVEDLSKLAVKSFSEIDMLMDEGSKARTVASTNMNATSSRSHAVFTIVFTQSKIDKTRGTAIDRVSKISLVDLAGSERANSTGATGVRLKEGANINKSLSTLGKVISALAENSTSKKAVFVPYRDSVLTYLLKETLGGNSKTIMIAAISPADINYEESLSTLRYADSAKKIKTVAVVNEDAQSKLIRELQGEVERLRAMMDQGGQYHANDSKLMNSDYDETVSTLNEKIEQYEKLMAELNKSWEEKLSEAEAIREDRMAALKDMGVAIKVVSSIPHLINLNEDPLMSESLIYYVKEGKTRIGRSDSEIPQDIILNGLNIHKEHCIFENINGKVIISPSNNFMNNNNNKENSSSTTPTSSKSPSKPKSEKEKENNNDDDDGEKKLDRSYIYVNGVEINKPTILTTGNRVILGNNHIFRFNNPEEAIKIARERNQTTGGIVSSTKSPVDQIMDYDFALNELASIQGTLAMSKHINDKQEYKKQMRALYDQIRLQLENDCDPEVKEQREKLALLAFRRWRSKVHRSKLLNKISFIILSLNEANAISSTLNKKINLSLKLYSVFPEPDQISDNIEPEIDWRKTQILIKATDSSTGESTLVTDQDFVDRIYLMRELYQNDGRLDTELPEDPFQFTFTKDSLIGVSHVYLKNTLYLVESNRPVPILDENGNQKGYLNLLVSSSSTDITESERGLYLENPSNNKSLLLGKNLEITIGFEGFSEFIDENKFSDVFIKFNFPNQNGTIVDTFLTEPQPISAFIDQKRIVITSLTESLINLLQTQYVSFEIRGHKKSKQQPKLTSSSSSASTTSSSSKNQPMLENFEFLATLNILESEKNTGTDDQYKPVHILEDPDVYNTHLPSVTFRLKKDKTNRQILFKVIKNESNSIIKECKSARISDIKIFGKRDNPLLSSSATPNTPNTPNNSRIAGIQNTPGTPMTPYSNQTNNQQSSSSQPPLPQQQGTPYNPQSNNPNVISNAPPTPNSNLLKDLSLAANVQTSSSSSSSSLNVLLNNQQQQQQSQQSQQQQQQQSQQSSETSSTTNSITNSASNSSLSLLVNNQTTNSNNSGGNIFEIPVLSCTDDSVLLLWKTNDPSFIFNQKTRKGDKILFKLTFDLLIQGFPDVVSISKDIAIKILSSESMPSATMPDGTSSSSMSNLLDKFKTHFKGESILSEPSIHAGSVFSINLTKSRQQEHQNRIGEMIDAHQENILKLGYAMKMEKLRQELDLREKLTNLKEKTIDSTNTDDVNAANGVAESSNSSTIDVEEIVKKMLLMNSTHQQQQQNFSSPSSTSPTLVNGESSPKSGRSSNTTSSSSGGGGGGGRKRSSTIVEVKVKEVPSSALLKEDETSGYLKKKSAFKEEWKPRWFVFKKPYLYYSHNQKDTHKLKKIDLTNSSVAITQDEVPFGFAIIQLRRVWLLQANSVEDRDKWVQTLDPLRKVTELKDEELRTAKQQIEKSSSQLDQIKSQLQTGQQIVLAKQKEIEELTNTISQLQLEKEINTQQFDGLRDEIQNRDEELEQYKSQQSQKINQLSGQVNKLENVTQEKELTIGSLSSTLNNTNQIIELINEQSKSYKNVAEMEIESLRDETTQLRETSQLLANRLKECRSSIQSAESLLSERDLEITQLKALLTQQEESSGITSLNLKNLQSDQTMKQGQIDILSKTVQQSTATIQNISSQLDSTTKASDSKDEQITSINSAYKDESDRLKDQTTQLNSLTTNLRQQMRSLEQTHLQQKETSASDQKTLLLLLHDMEQGLTRASQTITDQSAQVTVLKKQLEDSKKSNEQLPTVEKQLSLMKDRLIQSENQLIDRECENTILSDKLKLWEEEIKIKDSKLSLLENNVKEVRAEYANGMAFSREFSQHHTDSGSISGKFNRRSKQISAEEQMETLRESSIAHQSHNAFLNSQIQRLETEMRTQEKVYSDTIQRIKKDLQQRNQQNIAFMKHQVGDEIVKKMEDVTASMEILKKKYFVSLVVAAKLQNAMMGNICNVDAYELYEQSVVEHILDQDQWPNWIAQTISTQNKHL
Protein: Interferon, alpha-inducible protein 27 (D3ZIG6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MALSGTGTLVASIASKVASSVAVVKAGGAVSSTILASSQGLNLLAQTALGSGASALGSALGALKAGTVLSSLPASALAVCPIGDITPLPTAMTVAAVPPVLSAVGFTGSGIAASSLAAKLMSVSAIANGGGVPAGGLVATLQSAGAAGLSMTSKVLVGSTGSAVVASVMGVCKHLYSFL
Protein: Alanine--glyoxylate aminotransferase 2-like (EC 4.2.3.-) (Q9VU95)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Hydroxylysine kinase
- Ethanolamine kinase
- RE24176p
- Arginase
- RE20371p
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MPFAHEQLNLVASEQLSKTETIKLRNQHIGQACQLFYRSDPLKIVRGQGQYMFDEEGTRYLDCINNVAHVGHCHPEVVRAGALQMATISTNNRFLHDELVQCARTLTSKMPEPLSVCFFVNSGSEANDLALRLARNFTKRQDVITLDHAYHGHLQSVMEVSPYKFNQPGGEAKPDYVHVAPCPDVYGGKFTDKMYPDADMGALYAQPIEEICQKQLAKGQGVAAFIAESLQSCGGQILPPAGYFQAVYDAVRSAGGVCIADEVQVGFGRVGSHYWAFETQNVIPDIVCVAKPMGNGHPVGAVVTTPEIAQAFHATGVAYFNTYGGNPVSCAIANAVMRVIEEEGLQQKALVLGDYLLEECNRLKQEFECIGDVRGAGLFVGIELVQDRKERIPDKKAAHWVVNRMKQLHRVLVSSDGPNDNVIKLKPPMCFNRENADEFLLGFRECLTAVMQERLASATSAAMAATSGVIATATETLANKTKLFERQDRLIKSV