wanglab/gogpt-training-data huggingface dataset:
Protein: Aspartate--tRNA ligase, mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (O94242)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, cytoplasmic
- CTP synthase
- Alanine--tRNA ligase
- Putative glutamine amidotransferase-like protein C13C5.04
- Glutamate--tRNA ligase, mitochondrial
- GMP synthase
- Probable arginine--tRNA ligase, cytoplasmic
- Probable transcriptional regulatory protein C8D2.12c
- Large ribosomal subunit protein bL32m
Sequence:
MVLSRLPACLLPLVGTKVSIQGWLVATSRQVSKSISFHQLRDTHGTILQLLSTDKIILQQKREPLVSSTDFSQQKSTSVMRTLSSIPPESVVQVTGKLQRRPEHDRRPGNEFELHVEDVKLLNVAKNLQLFPGDEKPGMRIQLANRHIQLRAPKYNSYLRQRSRLAYQVHSFFNDREFCEVETPLLFKSTPEGAREFVVPSRLNPGKFYALPQSPQQYKQILMASGIGNYYQIARCFRDEDLRFDRQPEFTQIDLEMSFVDKPHEIMEVVEDLLVRLVSFAKGITLAKPFQHITYQHAIDKYGSDKPDIRFELPLKNITSLLPKQDPLISTEILVYNDLSHSLSNAESRKLCEAVGENVVVTSIREHSQLQTWVKKLPQLRQLPIVAEELNQKLQIGINSIVFMTNRPKYLVSGTTPLGKLRLLLHELLVKKKALPELDKDLLKFVWVVDFPLFSPTEEKNQSITSTHHPFTAPHWDDVHLLEKKPLSVRGLHYDIVVNGIELGGGSIRIHNPDIQRFVLKDVLKLPENRYATFEHLIRVLSSGCPPHGGIALGFDRLAALLTNAPGIREVIAFPKTSSGADLLIGSPSAIPEEMLKDYNVAITRQTQNRN
Protein: Ricin B-like lectin (Clitocybe nebularis lectin) (CNL) (B2ZRS9)
Organism: Clitocybe nebularis (Clouded agaric) (Lepista nebularis)
Function: Lectin specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). Specific also for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Agglutinates human blood group A, AB, B and O erythrocytes with a strong preference for group A. Agglutinates bovine erythrocytes with a very low specificity. Binds carbohydrates bivalently, which is required for its biological activity. Exhibits insecticidal activity against the fruit fly D.melanogaster, mosquito A.aegypti, and amoebozoa A.castellanii. Has anti-nutritional activity against Colorado potato beetle L.decemlineata, and against worm C.elegans. Has antiproliferative activity against human leukemic T-cells. Has an immunostimulatory effect on human antigen-presenting dendritic cells, which are subsequently able to induce efficient T-cell immune responses.
Interaction partners:
Sequence:
MSITPGTYNITNVAYTNRLIDLTGSNPAENTLIIGHHLNKTPSGYGNQQWTLVQLPHTTIYTMQAVNPQSYVRVRDDNLVDGAALVGSQQPTPVSIESAGNSGQFRIKIPNLGLALTLPSDANSTPIVLGEVDETSTNQLWAFESVSAV
Protein: Glutamate transporter homolog (Glt(Ph)) (Sodium-aspartate symporter Glt(Ph)) (Sodium-dependent aspartate transporter) (O59010)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake. Has only very low glutamate transport activity. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport. Na(+) binding enhances the affinity for aspartate. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport. In contrast to mammalian homologs, transport does not depend on pH or K(+) ions.
Subcellular location: Cell membrane {ECO:0000305|PubMed:15483603, ECO:0000305|PubMed:17230192, ECO:0000305|PubMed:17435767, ECO:0000305|PubMed:19380583, ECO:0000305|PubMed:28137870, ECO:0000305|Ref.11}; Multi-pass membrane protein {ECO:0000269|PubMed:15483603, ECO:0000269|PubMed:17230192, ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:22343718, ECO:0000269|PubMed:23563139, ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870, ECO:0000269|Ref.11}.
Interaction partners:
Sequence:
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMPIVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQQFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSAETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLTLQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYSFTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGAIMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGELEKGVIA
Protein: LD16921p (Tonalli, isoform D) (Q7JR52)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNQQAGSSRAPATGGQISPPGATTVGVEQQQHLQQQHQQQYYNQQQQQQQQQYQQQHQRDNFLAYQQQQQQQQQQQQQLQRSGGGGGNFMLGNDLVGGDSLRSLNNTFGPNSEFTSLGGANSSASSSLSGLSSSSSQGYTGMVAASQQHQQQQPHHHQQQQQQQQQQHMGSMDAMGGYSQMGGGMHPGPNSGMMGNMNGQYMNGGSGQGGYNGAQGMGMGYGGGGSMGPQRHHQMTPMNQMQNMSMGPGVGGSGGMGGGMNPLQQQAAQQQMGGMNPMAKMQGMANGGYPQQAPPSLTQQQQQQQQRRMAPYPHPQMHMAQKRAAAGVGGAGGMYPGNPMQQQQAQMYGNQQMHPGSGGGVPLPMQAGGAGNGYGRSGPMGVGNGGYGRMSAGNGMGPTGGPVMGPMGPGGMTAGGMGPGPGCMSQQRFMPQGSGGGMPGVGYGGVGGAASHQGQFYPGSGQSAGMQQAGGMCPAGPGAVATTGNPYQNQGFQQNYQHSPVPGNPTPPLTPACSVPYVSPNPDIKPPMDNSEEMRLTFPVRDGIILAPFRLLHNLSVSNHVFHLKQNVYNTLMCRNDLELQLKCFHQDDRQMNTNWPHTVTVSANATPLNIERSEKNSTALRPLYLKAVCQPGRNTLQLTASSCCCSHLFVLQLVHRPSVRQVLQTLHKRNLLPLEHSVQKIKRNLSQPEANAGPDATPQQQQQQGGGQQCAKISLKCPITKSRIRLPARGHECKHVQCFDLEAYLMINSERGSWRCPECSKSAITDTLEIDQYIWAILNTLGNSDVDEVIIDSSANWRALQHNGGMPNAPPPSNVPSNPSGGSGSNSGNGSVNPTLPVIKQELCDDIAKVMSPGSTQLPTWDSAQAMSPYNMHDMNSIASGNMMGNGGNTNQHGNRSSYDGFSGNHSDGSGGLPGGDGGVNSLDQLNAMEKSLSDQMPHTPHTPGAASHPMTPGGPPSVSSSHNEPISGGTPNANGSGSATNGSGNNNSSTGHNSPQTPGTPSRMGGGMGGSGSADSQQQQQEQLLNSLMSSQTQLKFSESDLSAELQSFDAAAAAINDTAHDLNLLQDVDPMEILSYLDPQPDLNTPPSSGSSNNNASDDLLATLFD
Protein: Mannose-1-phosphate guanylyltransferase regulatory subunit alpha (GDP-mannose pyrophosphorylase A) (GTP-mannose-1-phosphate guanylyltransferase alpha) (Q5XIC1)
Organism: Rattus norvegicus (Rat)
Function: May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Phosphomannomutase
- Phosphomannomutase
- GDP-mannose 4,6 dehydratase
- Dolichol-phosphate mannosyltransferase subunit 1
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- dTDP-D-glucose 4,6-dehydratase
- Phosphoacetylglucosamine mutase
Sequence:
MLKAVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQPDEALTQFLEAAQQEFNLPVRYLQEFTPLGTGGGLYHFRDQILAGAPEAFFVLNADVCSDFPLSAMLDAHRLQRHPFLLLGTTANRTQSLNYGCIVENPQTHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEESPGSWPGAGTIRLEQDVFSALAGQGQIYVHLTDGIWSQIKSAGSALYASRLYLGRYQITHPERLARHTAGGPRIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPNDPNPNDPRARMDSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKELSRSFTNQIIL
Protein: VPS39 subunit of HOPS complex (A0A8I5ZMY7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MVLTVFRFFITVPADVASPESGSCNRFEVTLEKSNKNFSKKIQQIHVVSQFKILVSLLENNIYVHDLLTFQQITTVSKAKGASLFTCDLQHTETGEEVLRMCVAVRKKLQLYFWKDREFHELQGDFSVPDVPKSMAWCENSICVGFKRDYYLIRVDAKGSIKELFPTGKQLEPLVAPLADGKVAVGQDDLTVVLNEEGICTQKCALNWTDIPVAMEHQPPYIVAVLPRYVEIRTLEPRLLVQSIELQRPRFITSGGSNIIYVASNHFVWRLIPVPMATQIQQLLQDKQFELALQLAEMKDDSDSEKQQQIHHIKNLYAFNLFCQKRFDESMQVFAKLGTDPTHVMGLYPDLLPTDYRKQLQYPNPLPTLSGAELEKAHLALIDYLTQKRSQLVKKLNDSDHQSSTSPLMEGTPTIKSKQKLLQIIDTTLLKCYLHTNVALVAPLLRLENNHCHIEESEHVLKKAHKYSELIILYEKKGLHEKALQVLVDQSKKANSPLKGHERTVQYLQHLGTENLHLIFSYSIWVLRDFPEDGLKIFTEDLPEVESLPRDRVLNFLIENFKALAIPYLEHIIHVWEETGTRFHNCLIQLYCEKVQNLMKDYLLSLPTGKSPVPAGEEAGELGESRQKLLTFLEISSSYDPGRLICDFPFDGLLEERALLLGRMGKHEQALFIYVHVLKDTKMAKEYCHKHYDQNKEGNKDVYLSLLRMYLSPPSIHCLGPIKLELLEPQANLQAALQVLELHYSKLDTTKAINLLPANTQINDIRIFLEKVLEENAQKKRFNQVLKNLLHAEFLRVQEERILHQQVKCIITEEKVCMVCKKKIGNSAFARYPNGVVVHYFCSKEVNSADT
Protein: Transcription factor TGAL9 (bZIP transcription factor 17) (OsbZIP17) (Q0E342)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional regulator involved in defense response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
Sequence:
MGDRPWQQQLQPHDQQAASCSVTAGMMMQASATSSSIHGNNIIRKDPGGGYDMAELDHIFLYLNSQDQASAAIQEQPQTLNIFPSQPMHAGEPSPKGSSSMAAINSAPSNNALAIAAGSSKRPPAAAAAGGQPSRLNNPADQPSASGKDGKAAVVKKEGGGGGGKHHGGASSAAASEHEGPKTPDAKTLRRLAQNREAARKSRLRKKAYIQNLETSRIRLSQLEQELVQRSRTQGAILGGGAFSAGIGGQSPEAAWFDGEYARWVESHERMMAHMRAAVEEQPQHGGVAAAAAEAQLRQLVDAAVAHHGVLVELKAAVASADVFHLVSGTWLPAAERCFLWIGGFRPSELIKVST
Protein: Envelope glycoprotein N (Q77CE4)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}. Host membrane {ECO:0000255|HAMAP-Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04037}. Note=When coexpressed with gM, localizes in the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04037}.
Interaction partners:
Sequence:
MPRSPLIVAVVAAALFAIVRGRDPLLDAMRREGAMDFWSAGCYARGVPLSEPPQALVVFYVALTAVMVAVALYAYGLCFRLMGASGPNKKESRGRG
Protein: Phenoloxidase 8 (EC 1.10.3.-) (EC 1.14.18.-) (Prophenoloxidase 8) (Q8MZM3)
Organism: Anopheles gambiae (African malaria mosquito)
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (Probable). Catalyzes the oxidation of o-diphenols such as dopamine. Also oxidizes monophenols such as tyramine.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8I6K1}.
Interaction partners:
Sequence:
MATLTQKFHGLLQHPLEPLFLPKNDGTLFYDLPERFLTSRYSPIGQNLANRFGPNSPASSQVSNDTGVPPTVVTIKDLDELPDLTFATWIKRRDSFSLFNPEHRKAAGKLTKLFLDQPNADRLVDVAAYARDRLNAPLFQYALSVALLHRPDTKSVSVPSLLHLFPDQFIDPAAQVRMMEEGSIVLDENRMPIPIPMNYTATDAEPEQRMAFFREDIGVNLHHWHWHLVYPASGPPDVVRKDRRGELFYYMHQQLLARYQIDRYAQGLGRIEPLANLREPVREAYYPKLLRTSNNRTFCPRYPGMTISDVARSADRLEVRIADIESWLPRVLEAIDAGFAVSDDGVRVPLDETRGIDVLGNILERSAISINRNLYGDVHNMGHVLLAFIHDPRGTYLESSGVMGGVATAMRDPIFYRWHKFIDNIFLRNKARLAPYTMAELSNSNVTLEALETQLDRAGGAVNSFVTFWQRSQVDLRAGIDFSAAGSAFVSFTHLQCAPFVYRLRINSTARSNRQDTVRIFLLPRQNEQGRPLSFEDRRLLAIELDSFRVNLRPGMNNIVRQSSNSSVTIPFERTFGNVEQANAGNAQSRFCGCGWPAHMLLPKGNANGVEFDLFAMVSRFEDDNANVNYDENAGCDDSYAFCGLRDRVYPSRRAMGFPFDRRASNGVRSVADFVAPYKNMRLATVTLRFMNTIIDRPTN
Protein: Beta-catenin protein (Catenin beta-1) (Q63ZT4)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- Uncharacterized protein.
- Lymphoid enhancer-binding factor 1
- Blastomere cadherin
- Cadherin
- Uncharacterized protein
- Cadherin-1
- Lymphoid enhancer-binding factor 1
- Glycogen synthase kinase-3 beta
- Axin-2 isoform X1
- Axin-2 isoform X1
Sequence:
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEDEDVDTNQVLYEWEQGFSQSFTQDQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDIHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMPWNEAADLGLDIGAQGEPLGYRQDDSSYRSFHAAGYGQDAMGMDSMMDHDMGGHHPGADYPVDGLPDLSHAQDLMDGLPPGDSNQLAWFDTDL
Protein: Group IIF secretory phospholipase A2 (GIIF sPLA2) (sPLA2-IIF) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2F) (Q9BZM2)
Organism: Homo sapiens (Human)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids (phospholipase A2 activity), the catalytic efficiency decreasing in the following order: phosphatidylglycerols > phosphatidylethanolamines > phosphatidylcholines > phosphatidylserines. May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases (By similarity).
Subcellular location: [Isoform 1]: Secreted {ECO:0000250|UniProtKB:Q9QZT4}. Cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QZT4}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Cytochrome P450 2E1
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Phospholipase A and acyltransferase 3
- Phospholipase B1, membrane-associated
- Lysophosphatidylcholine acyltransferase 1
- Platelet-activating factor acetylhydrolase
Sequence:
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEVDWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLCLMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Protein: 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 (EC 2.4.1.152) (Fucosyltransferase 9) (Fucosyltransferase IX) (Fuc-TIX) (FucT-IX) (Galactoside 3-L-fucosyltransferase) (O88819)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth. Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (By similarity). Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (By similarity). May also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y231}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane {ECO:0000269|PubMed:12626397}.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Galactoside 2-alpha-L-fucosyltransferase Sec1
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
Sequence:
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWVFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDFNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
Protein: GH01987p (Q8IH76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SPATVLPSSQFPSSTQHPGGAGAGDYEPDEEVGLELPPPMKPIQEPHLIANGPPAFAKDAKESSGNMASPGKMDGNPLSEIEEIVKTTTEQHESNSRVDGGGGVENASTNGHGRSHDNNDESHTAVSDKAAALKKRQCVFAELMSTEEAYVQDLHEIVNGYMTEINNTNSDIPMPEDLKGGKMKLVFNNIKDIYEWHRDFFLRALRNCQKSPADLGPLIKRSATKFALYYTYCSNKPLSEYIASPIFK
Protein: Down syndrome cell adhesion molecule 1, isoform BL (A0A0B4K6Z3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVHQFYQTRVIDEFVLRGNSATLKCLVPSFVADFIDVEGWIDEEGVEILRPLPDDSVDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPISGAAPRVALIQKTNIEYVRLGEIVSIMCPAQGFPVPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPHISPFEFGDEPANFGDSVTVQCTISKGDLPVDITWLFNDYAINEYHGVTSSKIGKKVNVLTIDSVNGNNAGNYTCRARNKAQMVEYTAALIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Exocyst complex component 3 (Exocyst complex component Sec6) (O60645)
Organism: Homo sapiens (Human)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O54921}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54921}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54921}. Midbody {ECO:0000269|PubMed:18756269}. Golgi apparatus {ECO:0000305|PubMed:18756269}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62825}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). During mitosis, early recruitment to the midbody requires RALA, but not RALB, and EXOC2. In late stages of cytokinesis, localization to the midbody is RALB-dependent (PubMed:18756269). {ECO:0000250|UniProtKB:O54921, ECO:0000269|PubMed:18756269}.
Interaction partners:
- Exocyst complex component 4
- Exocyst complex component 1
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 6
- Exocyst complex component 8
- Exocyst complex component 5
- Exocyst complex component 6B
- Synaptosomal-associated protein 25
- Rho-related GTP-binding protein RhoQ
Sequence:
MKETDREAVATAVQRVAGMLQRPDQLDKVEQYRRREARKKASVEARLKAAIQSQLDGVRTGLSQLHNALNDVKDIQQSLADVSKDWRQSINTIESLKDVKDAVVQHSQLAAAVENLKNIFSVPEIVRETQDLIEQGALLQAHRKLMDLECSRDGLMYEQYRMDSGNTRDMTLIHGYFGSTQGLSDELAKQLWMVLQRSLVTVRRDPTLLVSVVRIIEREEKIDRRILDRKKQTGFVPPGRPKNWKEKMFTILERTVTTRIEGTQADTRESDKMWLVRHLEIIRKYVLDDLIVAKNLMVQCFPPHYEIFKNLLNMYHQALSTRMQDLASEDLEANEIVSLLTWVLNTYTSTEMMRNVELAPEVDVGTLEPLLSPHVVSELLDTYMSTLTSNIIAWLRKALETDKKDWVKETEPEADQDGYYQTTLPAIVFQMFEQNLQVAAQISEDLKTKVLVLCLQQMNSFLSRYKDEAQLYKEEHLRNRQHPHCYVQYMIAIINNCQTFKESIVSLKRKYLKNEVEEGVSPSQPSMDGILDAIAKEGCSGLLEEVFLDLEQHLNELMTKKWLLGSNAVDIICVTVEDYFNDFAKIKKPYKKRMTAEAHRRVVVEYLRAVMQKRISFRSPEERKEGAEKMVREAEQLRFLFRKLASGFGEDVDGYCDTIVAVAEVIKLTDPSLLYLEVSTLVSKYPDIRDDHIGALLAVRGDASRDMKQTIMETLEQGPAQASPSYVPLFKDIVVPSLNVAKLLK
Protein: Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.-) (A0A4Y1WAR4)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MTKIGINGFGRIGRNVFRAALNNSEVEVVAINDLTDAKTLAHLLKYDTVHGTLNAEVSANENSIVVNGKEIKVIAERDPAQLPWSDYGVEVVVESTGRFTKKSDAEKHLGGSVKKVIISAPASDEDITVVMGVNHEQYDAANHNVVSNASCTTNCLAPFAKVLNEKFGVKRGMMTTIHSYTNDQQILDLPHKDLRRARAAAENMIPTSTGAAKAVALVLPELKGKLNGGAVRVPTANVSLVDLVVELDKEVTVEEVNAAFKAAAEGELKGILGYSEEPLVSIDYNGCTASSTIDALSTMVMEGNMVKVLSWYDNETGYSNRVVDLAAYMTSKGL
Protein: Protein APCDD1 (Adenomatosis polyposis coli down-regulated 1 protein homolog) (cAPCDD1) (Protein primglo1) (Q5R2I8)
Organism: Gallus gallus (Chicken)
Function: Negative regulator of the Wnt signaling pathway. Inhibits Wnt signaling in a cell-autonomous manner and functions upstream of beta-catenin.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MFVPYGSLMRYLFPALLLHGLGEGSALLHPDSRSHPRSLEKSAWRAFKESQCHHMLKHLHNGARITVQMPPNIEGHWVSTGCEVRAGPEFITRSYRFYHNNTFKAYQFYYGGNRCTNPIYTLVIRGKIRLRQASWIIRGGTEADYQLRNIQIISHNEAVAKKLSELVNNTCPGFIPEDSPWEQDVSYDLLREENGCECTKALNFAMHELQLIRVEKQYLHHNLDHLVEELFLGDIHTDATQRRYYRPSSYQPPLQNAKNHDRTCIACRIIYRSDEHHPPILPPKADLTIGLHGEWVSQRCEVRPEVLFLTRHFIFHDNNNTWEGHYYHYSDPICKHPTFTIYAKGRYSRGVHSAKVMGGTEFVFKVNHMKVTPMDVSTASLLNVFNGNECGAQGSWQVGVQQDVTHTNGCIALGIRLPHTEYEIFKMEQDARGRYLLYNGQRPSDGSSPDRPEKRATSYQMPLIQCASSVPRSEESPEENKIRLYSSRAPAKHPSASALALVLFICTVSYWDILS
Protein: Guanylate-binding protein 2 (EC 3.6.5.-) (GTP-binding protein 2) (GBP-2) (HuGBP-2) (Guanine nucleotide-binding protein 2) (Interferon-induced guanylate-binding protein 2) (P32456)
Organism: Homo sapiens (Human)
Function: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP. Exhibits antiviral activity against influenza virus. Promotes oxidative killing and delivers antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity). Confers protection to the protozoan pathogen Toxoplasma gondii (By similarity).
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9Z0E6}; Lipid-anchor {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:31091448}; Lipid-anchor {ECO:0000269|PubMed:21151871}. Cytoplasm {ECO:0000269|PubMed:21151871}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Note=GBP2-GBP5 dimers localize to the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
Interaction partners:
- Guanylate-binding protein 1
- Guanylate-binding protein 5
- Guanylate-binding protein 3
- Signal transducer and activator of transcription 1-alpha/beta
- Guanylate-binding protein 4
- Interferon regulatory factor 1
- Interferon regulatory factor 9
- Interferon-induced protein with tetratricopeptide repeats 2
- Signal transducer and activator of transcription 2
- Interferon-induced helicase C domain-containing protein 1
Sequence:
MAPEINLPGPMSLIDNTKGQLVVNPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKKNGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDIEKGDNENDSWIFALAILLSSTFVYNSMGTINQQAMDQLHYVTELTDRIKANSSPGNNSVDDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRKGTDKKSKSFNDPRLCIRKFFPKRKCFVFDWPAPKKYLAHLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTLSGGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFMKNSFKDVDQMFQRKLGAQLEARRDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFTQKLQELKNKYYQVPRKGIQAKEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEEMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFENESKRLQKDIWDIQMRSKSLEPICNIL