wanglab/gogpt-training-data huggingface dataset:
Protein: Galectin-9B (Gal-9B) (Galectin-9-like protein A) (Q3B8N2)
Organism: Homo sapiens (Human)
Function: Binds galactosides.
Interaction partners:
- Hepatitis A virus cellular receptor 2
- Lymphocyte activation gene 3 protein
- C-type lectin domain family 7 member A
- Cytotoxic T-lymphocyte protein 4
- T-cell immunoreceptor with Ig and ITIM domains
- Programmed cell death protein 1
- CD44 antigen
- Programmed cell death 1 ligand 1
- Tumor necrosis factor receptor superfamily member 9
- Lymphokine-activated killer T-cell-originated protein kinase
Sequence:
MAFSGSQAPYLSPAVPFSGTIQGGLQDGFQITVNGAVLSSSGTRFAVDFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQKGRWGPEERKMHMPFQKGMPFDLCFLVQSSDFKVMVNGSLFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRTVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPSVRPANPAPITQTVIHTVQSASGQMFSQTPAIPPMMYPHPAYPMPFITTIPGGLYPSKSIILSGTVLPSAQRFHINLCSGSHIAFHMNPRFDENAVVRNTQINNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHVFEYYHRLRNLPTINKLEVGGDIQLTHVQT
Protein: Ubiquitin-like-conjugating enzyme ATG3 (EC 2.3.2.-) (Autophagy-related protein 3) (APG3-like) (hApg3) (Protein PC3-96) (Q9NT62)
Organism: Homo sapiens (Human)
Function: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11825910}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Autophagy protein 5
- Ubiquitin-like protein ATG12
- Autophagy-related protein 16-1
- Ubiquitin-like modifier-activating enzyme ATG7
- Gamma-aminobutyric acid receptor-associated protein
- GABA type A receptor associated protein like 1
- Microtubule-associated protein 1 light chain 3 beta
- Microtubule-associated protein 1 light chain 3 alpha
- CASP8 and FADD-like apoptosis regulator
Sequence:
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM
Protein: Translation initiation factor eIF2B subunit beta (eIF2B GDP-GTP exchange factor subunit beta) (O76863)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2 subunit 3
- Eukaryotic translation initiation factor 2 subunit 2
- non-specific serine/threonine protein kinase
- Eukaryotic translation elongation factor, selenocysteine-specific
- Rabaptin-5-associated exchange factor for Rab5
Sequence:
MKEQPLKEITQLIHAIKVGLVEGSYNITNKTLDIFKYIIMSKSWQNADALMQIVRDQCKILQAALPQETVTSNIARRILKLTREEFDLLHAKVQHFADDSQASLSLHKLVTQTSESNVSVDYSVPQHGLREALLDHLQEVETELETSSENICVQAEEHIHSSEIILTLGHSRSVENFLKRAIKKRQFLTIIVAECAPACRGHNLAASLANEKNVEIVVIPDAAIFAMMSRVNKVIIGTHSVLANGGLRAACGAYTVALAAKHYSVPVIVLAPMYKLSPLHLCEQDAFNMVGCAEDVIPYDSIPAREAKVYSPMFDYVPPELVTLFISNTGGHAPSYVYRLLTELYHPEDLEI
Protein: SD21394p (Q8MT12)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDVCREIQKWVLNKGVGQSTMHKAARQGLIDVVVYCLDRMNMNPDQKDNAGYTPLHEACTQGWLEIARILLQYGANHSEAAQSGIRPLHGAIENDHEEVVRLLLSYGADPLLATYSGQTPLMLASSKLMRGILRAHLSDAQSAAADIKPMRFNGPWEIFDAKEYGYDIFSNVPNTACDMSRALRRERKEAKQQRMSSNSDRTSNLNGLLPGKKEEQKPEDLDQERVTTTIKQNGETSATKTGSATTTTATTMVKLEPGTDEDSNNNKNNEELNANVENNLVTSVVNVKNEVKKEVEAEAETEAETETNAKANTNSSTRLDEDQTDIETMDSELNGDIFEFEEADVPLPPLYLLKDEGSDKWVLLNDLCNLLKVKSKDTLLNKLCPNNSNALASSQKHLLREFKIDDFLEKATCLQLLCAGEKLNMFSSSKVVLIKYNDSVRNLLGVKTILMKF
Protein: Transcription cofactor vestigial-like protein 4 (Vgl-4) (Q80V24)
Organism: Mus musculus (Mouse)
Function: May act as a specific coactivator for the mammalian TEFs.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional enhancer factor TEF-3
- Transcriptional enhancer factor TEF-1
- Interferon regulatory factor 2-binding protein 2
- Transcriptional coactivator YAP1
- Transcriptional enhancer factor TEF-4
- Transcriptional enhancer factor TEF-5
- WW domain-containing transcription regulator protein 1
- Transcription cofactor vestigial-like protein 1
- Protein salvador homolog 1
Sequence:
MLFMKMDLLNYQYLDKMNNNIGVLCYEGEASLRGEPRMQTLPVASALSSHRTGPPPISPSKRKFSMEPGDKDLDCENDHVSKMSRIFSPHLNKTVNGDCRRDPRERSRSPIERAAAPAVSLHGGHLYASLPSLMEQPLALTKNSSDTGRSAVERQQNRPSVITCASAGARNCNLSHCPIAHSGCSAPGSASYRRPPSATATCDPVVEEHFRRSLGKNYKEPEPAPNSVSITGSVDDHFAKALGDTWLQIKAAKDSASSSPESASRRGQPASPTAHMVSHSHSPSVVS
Protein: UPF0489 protein C5orf22 (Q49AR2)
Organism: Homo sapiens (Human)
Interaction partners:
- WW domain-binding protein 11
Sequence:
MSDSAGGRAGLRRYPKLPVWVVEDHQEVLPFIYRAIGSKHLPASNVSFLHFDSHPDLLIPVNMPADTVFDKETLFGELSIENWIMPAVYAGHFSHVIWFHPTWAQQIREGRHHFLVGKDTSTTTIRVTSTDHYFLSDGLYVPEDQLENQKPLQLDVIMVKPYKLCNNQEENDAVSSAKKPKLALEDSENTASTNCDSSSEGLEKDTATQRSDQTCLEPSCSCSSENQECQTAASTGEILEILKKGKAFVLDIDLDFFSVKNPFKEMFTQEEYKILQELYQFKKPGTNLTEEDLVDIVDTRIHQLEDLEATFADLCDGDDEETVQRWASNPGMESLVPLVQSLKKRMEVPDYEMVHQAGLTCDYSELPHHISTEQEIECLIQSVHYLLKNLPNPTLVTIARSSLDDYCPSDQVDTIQEKVLNMLRALYGNLDLQVYAAESPPS
Protein: Dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase (EC 3.1.2.31) (Esterase lovG) (Lovastatin biosynthesis cluster protein G) (Q0C8M2)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Esterase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
Sequence:
MRYQASPALAKAPRALLCIHGAGCSPAIFRVQLSKLRAALREDFEFVYVTAPFPSSAGPGILPVFADLGPYYSWFESSSGNNNNGPSVGERLAAVHDPIRRTIVDWQTQHPHIPIVGAIGFSEGALVTTLLLWQQQMGRLPWLPRMSVAMLICPWYQDEASQYMRNEVMENHDDDHDSKDTEWQEELVIRIPTLHLQGRDDFALAGSKMLVARHFSPREAQVLEFAGQHQFPNRPRDVLEVINRFRKLCVTVQTLE
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9PWM7)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MSSGDNSGVAKEIEKLYAAVPQLHNIFYIKSKIGEGTFSSVYFAIGRLRSGEDAKFALKHLIPTSHPTRIAAELQCLSVAGGEDNVMGVKYCFRNKDHVVIVMPYLEHECFADILHSLSFEETKEYMFNLLKALRHIHSFGIVHRDVKPSNFLFNRSLKKFALVDFGLAQGTSDTKIDLLKVLQPKKQDGLVGSSTQRSVFGERNFNVHSAVTIDNTTLKAAKPSKTIDVTTRKLATRKTVSTKSTSSAVPKKAASTCQTSLTCDCYAKDQVCNICLARTRQVAPRAGTPGFRAPEVLTKCPHQTTAIDMWSAGIIFLSLLSGRYHFFNAADDMNALAQIMTIRGSKETIQASKCFGKSVLCSKELPSKDLRTLCEGLRSAIVLPNGNQHDIQKQRAALQMRIMENQDGWFLPESPDITPDSPAVVRSSCVSTPDNMEQSNHNGWDRVPNEAYHLLDRLLDMNPATRITAEEALIHPLFKNMR
Protein: ATP synthase small subunit 6-B, mitochondrial (AtMtATP6) (MtATP6) (ATP synthase 6 kDa subunit, mitochondrial) (P0DO45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (Probable). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). Part of the complex F(0) domain (Probable). Confers tolerance to several abiotic stresses (e.g. salt, mannitol, drought, oxidative and cold stresses), probably by providing additional energy needed for cell homeostasis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P0DO44}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRLFDPWPVFFKREWKRCWPFLTGFAVTGVLITKLTAGLTEEDAKNSKFVQQHRR
Protein: Kexin kexB-Aspergillus niger (EC 3.4.21.61) (Kexin precursor kexB-Aspergillus niger) (A2Q9N6)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MRLTGGVAAALGLCAAASASLHPHRSYETHDYFALHLDESTSPADVAQRLGARHEGPVGELPSHHTFSIPRENSDDVHALLDQLRDRRRLRRRSGDDAAVLPSLVGRDEGLGGILWSEKLAPQRKLHKRVPPTGYAARSPVNTQNDPQALAAQKRIASELGIADPIFGEQWHLYNTVQLGHDLNVTGIWLEGVTGQGVTTAIVDDGLDMYSNDLRPNYFAAGSYDYNDKVPEPRPRLSDDRHGTRCAGEIGAAKNDVCGVGVAYDSRIAGIRILSAPIDDTDEAAAINYAYQENDIYSCSWGPYDDGATMEAPGTLIKRAMVNGIQNGRGGKGSVFVFAAGNGAIHDDNCNFDGYTNSIYSITVGAIDREGNHPPYSESCSAQLVVAYSSGASDAIHTTDVGTDKCSTTHGGTSAAGPLAAGTVALALSVRPELTWRDVQYLMIEAAVPVHEDDGSWQDTKNGKKFSHDWGYGKVDTYTLVKRAETWDLVKPQAWLHSPWQRVEHEIPQGEQGLASSYEVTEDMLKGANLERLEHVTVTMNVNHTRRGDLSVELRSPDGRVSHLSTPRRPDNQEVGYVDWTFMSVAHWGESGIGKWTVIVKDTNVNEHTGQFIDWRLNLWGEAIDGAEQPLHPMPTEHDDDHSYEEGNVATTSISAVPTKTELPDKPTGGVDRPVNVKPTTSAMPTGSLTEPIDDEELQKTPSTEASSTPSPSPTTASDSILPSFFPTFGASKRTQVWIYAAIGSIIVFCIGLGVYFHVQRRKRIRDDSRDDYDFEMIEDEDELQAMNGRSNRSRRRGGELYNAFAGESDEEPLFSDEDDEPYRDRGISGEQEREGADGEHSRR
Protein: CG14514 (Q2XY62)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
RLQLSRMPLDTWSKREQLILASAVSCSGDQNWITVSRTLKTICGNGSSNRPADWFSQKNCAMQYGNLLESVEATKRKKRSSESSAGVSSPATVETPTELLLRRLTEERQAEIKAQMRQDQETYRRIQREIESLQSDAVTEQELQDMWLEIEKEQEARRIEEMKLENRMREREQRKKDLASNWRNSSLAVKRSNQAADTTSVDMDVEDINTSGNGKQQTGPSPLLTSLLKSPTGNAPATPTPGGAAPAAGGTGSVARATAPTITSLLTSGPSSAVANQPVITMKSPTDAAFMSRPITGPPASEALASTTPTLERSPSQAAPTLSMLLEKNKAAAKVNEGGSLVKPEGSGNQEQGVDEDTSSAAGTADSDEADPNEAQLLEVFKNIDQIIDDIDIDMASVIDDEILKNVDDVVASPSNDKAEVIDFEDKLDALKREQSKSSPASDKPKSVELVIGSSDDSNDNIPLAAVASQESKDRGQSGGESTRGTEDAESEPLTSEVAVEEIGETITIISTSSEDTAGSPPTKMEEDGATDSLPKKEDAAEDKSEQESSSQGQNKAGGSTDEPELIDHQATREAQSKSGKDTAGKPVTMQEKTTTQSAPVPVDLHDTDEESSSLTDSSKHDDHPRSAKAKPPALKLALDDSKSELELSGTPQPPSAPARTPLLRKLPHRDRSESPMVDDDATTASDHSTARSTRRRCSSTPVIDSIPNSPASSEHTDDRRETRAASKKLFLSIYAMLLDSKHAAPFKRPFHDEHAQRHADLCLRPMDFPTIKRNIDSGFIRSLSELHRDVLLMAHNVLVAYKPHTTQHKTARLFVQDCQAIKEFSQLPDVQAGITATPVSNTGSLRADKSSGSKARSGSR
Protein: Cathepsin L-like proteinase (EC 3.4.22.-) (Q24940)
Organism: Fasciola hepatica (Liver fluke)
Function: Thiol protease. Probably involved in interaction with host tissues. Displays a similar activity to that of papain. Has high activity on Z-Phe-Arg-NHMec, but no activity on Z-Arg-NHMec.
Subcellular location: Secreted {ECO:0000269|PubMed:8192668}.
Interaction partners:
Sequence:
MRLFILAVLTVGVLGSNDDLWHQWKRMYNKEYNGADDQHRRNIWEKNVKHIQEHNLRHDLGLVTYTLGLNQFTDMTFEEFKAKYLTEMSRASDILSHGVPYEANNRAVPDKIDWRESGYVTEVKDQGNCGSCWAFSTTGTMEGQYMKNERTSISFSEQQLVDCSGPWGNNGCSGGLMENAYQYLKQFGLETESSYPYTAVEGQCRYNKQLGVAKVTGYYTVHSGSEVELKNLVGARRPAAVAVDVESDFMMYRSGIYQSQTCSPLRVNHAVLAVGYGTQGGTDYWIVKNSWGTYWGERGYIRMARNRGNMCGIASLASLPMVARFP
Protein: Histone H3K27 methylase (O41094)
Organism: Paramecium bursaria Chlorella virus 1 (PBCV-1)
Interaction partners:
Sequence:
MFNDRVIVKKSPLGGYGVFARKSFEKGELVEECLCIVRHNDDWGTALEDYLFSRKNMSAMALGFGAIFNHSKDPNARHELTAGLKRMRIFTIKPIAIGEEITISYGDDYWLSRPRLTQN
Protein: Ankyrin 1 (D3Z9Z0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Neurofascin
- Neural cell adhesion molecule L1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- CD44 antigen
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Titin
- TIAM Rac1 associated GEF 1
- Ankyrin 2
- Transient receptor potential cation channel subfamily V member 1
Sequence:
GSCTPRPSGADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTEKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTSMVKLLLENDASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVQLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGKKSFSWVSGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKPMKYEDAQHILCHLNVTMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMKMAVIREHLGLSWAVENLYTALRNIDRSEIVNMLEGSGRQSRNLKPDRRHGDREYSLSPSQVNGYSSLQDELLSPASLHYALPSPLCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSSGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQQRVHARITDSPSVRQVLDRSQARTVDWYKQGSAASYPQEAAQSSWQEEVTQGPQSFQRRITTIQGPEPGTLQEYEQVVVSTREHVQRGPPESDSPKAGKDPSLWASESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: Proline dehydrogenase (EC 1.5.5.2) (Q57U33)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Multifunctional fusion protein
- Pyrroline-5-carboxylate reductase
- Citrate synthase
- Acetyl-coenzyme A synthetase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MFRLLCRRSAANVKMQDASLRTMTKVDFSDPSIFRQKSLWWLLRALFVLRICKFEFISNNSVALMKRAEAIFGPFLTYNTLVKGTVYGHFCAGESDREVKNTVKSLENLGIGSVLDYAAEAEAEGFAPSPGIAEAPNLSMASLVNNTSVTYLPHKQAFDENMKLYVMCVLHAALHKPEGGVGLAAVKVTGMCDPQLLARVSAILHSVHRDWIEYFTEEQPPPVEECNVVMGTKTEHKRYITRDQVRKGLTKLASSQKYTEDEINAVLQVLDPNNEGKTNYYKFKTVVSEAVLALDPTPVQKIIIDKLPKLTTEERELWRHLHWRLSVIVRTAKDLRVRVLFDAEQTFYQLAIDNIVLQFQRQFNKKEAIVYNTYQCYLTYTEDRVFNDLTRAELEGWVWGGKIVRGAYMRQERETAEKYHYKSPIWPTYEETNACYKAVAERILREIARLPETRFEALFGTHNQKSLEEITEAVLQLPPVKGYVAFAQLYGMSDNLTIPLKRAGFPVFKYVPYGPVKETVHYLGRRAMENASILSNGGSREVRLMRKELRRRVFWM
Protein: 1-aminocyclopropane-1-carboxylate synthase-like protein 1 (ACC synthase-like protein 1) (Q96QU6)
Organism: Homo sapiens (Human)
Function: Does not catalyze the synthesis of 1-aminocyclopropane-1-carboxylate but is capable of catalyzing the deamination of L-vinylglycine.
Interaction partners:
- Exostosin-2
- Folliculin
Sequence:
MFTLPQKDFRAPTTCLGPTCMQDLGSSHGEDLEGECSRKLDQKLPELRGVGDPAMISSDTSYLSSRGRMIKWFWDSAEEGYRTYHMDEYDEDKNPSGIINLGTSENKLCFDLLSWRLSQRDMQRVEPSLLQYADWRGHLFLREEVAKFLSFYCKSPVPLRPENVVVLNGGASLFSALATVLCEAGEAFLIPTPYYGAITQHVCLYGNIRLAYVYLDSEVTGLDTRPFQLTVEKLEMALREAHSEGVKVKGLILISPQNPLGDVYSPEELQEYLVFAKRHRLHVIVDEVYMLSVFEKSVGYRSVLSLERLPDPQRTHVMWATSKDFGMSGLRFGTLYTENQDVATAVASLCRYHGLSGLVQYQMAQLLRDRDWINQVYLPENHARLKAAHTYVSEELRALGIPFLSRGAGFFIWVDLRKYLPKGTFEEEMLLWRRFLDNKVLLSFGKAFECKEPGWFRFVFSDQVHRLCLGMQRVQQVLAGKSQVAEDPRPSQSQEPSDQRR
Protein: Protein OPG173 (Q80HU0)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Plays a role in the inhibition of host protein synthesis. Specifically, inhibits the initiation of cap-dependent and cap-independent translation. In turn, affects the outcome of infection by decreasing recruitment of inflammatory leukocytes and reducing the memory CD8+ T-cell response.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:26334635}. Note=Localizes in cytoplasmic structures that differ from virus factories. {ECO:0000269|PubMed:26334635}.
Interaction partners:
Sequence:
MLLEMDKIKITVDSKIGNVVTISYNLEKITIDVTPKKKKEKDVLLAQSVAVEEAKDVKVEEKNIIDIEDDDDMDVESA
Protein: Pcdhgb1 protein (Q4KMS2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MENQVLLHFLVPLFCGALSQPIHYSIPEELAKGSLVGSLAKDLGLSIQELPARKLRVAEDYFSVSAELLLETPLDREHQSSHHLILTAMDGGDPPLSSTTQVWIKVTDANDNAPVFSQDTYKVSLRENIPPGTLVLQVTASDQDESIHGEITYAFLNAPASTNLVFNLNPNTGAITTNGTLDFEEKNRYTLGVEAKDGGVHTAHCNVQIEILDDNDNAPEVTFMSFSNQVPEDSVLGTVIALIKVRDKDSGQNGLVACHIQEELPFKLQPTSKNYYKLVIDKALNREQTPEYNVTITATDSGKPSLSSKTCVTVHITDINDNAPVFHQASYLVHVAENNPPGASIAQVSASDPDLGSNGLISYSIIASDLEPRALSSFVSVNQDSGVVFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRVLVGDRNDNAPRVLYPTLEPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDDPLPSDPQSELQFYLVVALALISVLFLLAVILAIALRLRHSSRSAAWGCFQPGLSLKSQPVVPPNYNEGTLPYSYNLCVASHSTTMAGFNFHHVAPEVAPPQDLLCDDPSVVVCGNNEDPQVSDDSAFQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Vimentin-type intermediate filament-associated coiled-coil protein (Q2NL98)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}. Note=Colocalizes with vimentin-type intermediate filaments. {ECO:0000250}.
Interaction partners:
Sequence:
MSAPPALQIREANAHLAAVHRRAAELEARLDAAERTVHAQAERLALHDQQLRAALDELGRAKDREIATLQEQLMTSEATVHSLQATVHQRDELIRQLQPRAELLQDICRRRPPLAGLLDALAEAERLGPLPASDPGHPPPGGPGPPLDNSTGEEADRDHLQPAVFGTTV
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A5I9F0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Receptor protein-tyrosine kinase
Sequence:
MDVAAAALPAFVALWLLSPWPLLGSVQGQFSAGGCTFDDGPGACDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGEKARLQLPTMKENDTHCIDFSYLLYSQKGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWPNEYQVIFEAEVSGGRSGYIAIDDIQVLSYPCDKSPHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSNFAQLIVREPPRPIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRVLLTRPGEGGTGLPGPPLITRTKCAEPMRTPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGRKESEETIIQTDEDVPGPVPVKSLQGTSFENKIFLNWKEPLEPNGIITQYEVSYSSIRSFDPAVPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQFFIRASTVKGFGPATAINVTTNISAPSLPDYEGVDASLNETATTITVLLRPAQAKGAPISAYQIVVEQLHPHRTKREAGTMECYRVPVTYQNSLSGGAPYYFAAELPPGNLPEPAPFTVGDNRTYKGFWNPPLAPRKGYNIYFQAMSSVEKETKTQCVRIATKAAATEEPEVIPDPAKQTDRVVKIAGISAGVLVFILLLLVVIVIVKKSKLAKKRKDAMGNTRQEMTHMVNAMDRSYADQSTLHAEDPLSLTFMDQHNFSPRYENHSATAESSRLLDVPRYLCEGTESPYQTGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLESS
Protein: Down syndrome cell adhesion molecule 1, isoform AL (Q0E9K6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVNQFYEAEIMTEYVIRGNAAVLKCSIPSFVADFVRVESWIDDEGNVLSFSDNYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSVAPKVDMHDKMDFTIRSSNRSLNLFCKAQGFPMPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFDFGDEPTNVEDSVSVTCLISSGDLPIDIEWFFNDYGISSYSGVTVVKGGKRSSVLGIDNVQARHAGKYSCRAKNRAAAVNYTFDLVVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Tuberoinfundibular peptide of 39 residues (TIP39) (Parathyroid hormone 2) (Q8QGA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role as a potent and selective agonist of pth2r resulting in adenyl cyclase activation and intracellular calcium level elevation.
Subcellular location: Secreted {ECO:0000305|PubMed:15297442}.
Interaction partners:
- Parathyroid hormone 2 receptor
- Parathyroid hormone 1 receptor b
- Parathyroid hormone 2 receptor
- Parathyroid hormone/parathyroid hormone-related peptide receptor
- Parathyroid hormone
- Parathyroid hormone 1a.
- Parathyroid hormone-like hormone
- Parathyroid hormone-like hormone b
Sequence:
MALSLPPRPALLFLVLMSVTLMASAFPQPQLRPLQSNLPAIGQEDSKGEQWEVVYPSISLRDWSIQMLTAPDFGAAKTGREQLVADDWLPLSQSQMEEELVKGWTGDWPSRVGHQQKRNIVVADDAAFREKSKLLTAMERQKWLNSYMQKLLVVNSK