wanglab/gogpt-training-data huggingface dataset:
Protein: Chromosomal passenger protein (Q586F4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Chromosomal passenger protein
- Kinesin motor domain-containing protein
- Kinesin-like protein
- Aurora kinase
Sequence:
MSNPWNAKLVEELLFRQYEKGEDVSMLLPPPPALSVDQYLKEYEQSTKVLFAYVRNGPANALTPQNINNPRMYGGTPTKGSSSMQRTGNQGGATCATTSSSSACGVDSKAQMQRHPRGLDGSQSAAPSLPLTAGDAAAGQGSMAPPEHIRKRIEWPATVPTNSALKSNSRSRVANLTTKRVAAQERVDPDLIFMQNPEELPLHTIFAKYPKAVESIAALRGGSGDWREDTFTEEEEILYKRELRYSHMGPSQCGFFRSNLIQR
Protein: Urotensin-2 receptor (Urotensin-2 receptor-like) (F1QSR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Urotensin-2 receptor 2.
- Urotensin II-related peptide.
- Kinesin-like protein
- Urotensin-related peptide 1.
- Centrosomal protein POC5
Sequence:
MDIPGSTSLFSSPSPSYTFPFFTNLSFPSSSPSLSPSPSVASTALFCFFLSLLSLLGILGNLYTLVLLLRRRRMSRRRHTAPMCCYSLSCLGSSSPSFSPSFSPSSSPTSSSSSSSLHLQVLSLALADLVYLSTAPFIVYDSLASDWAFGELGCRLLLSLDLLTMHASIFTLTAMSLDRYRAVADPLATTSTPSSGLLRVALAWGFAIALSLPMMITLHLEDGENHEGKLCVPAWDEQSSKAYLSILFCTSILGPGLAIGALYAALGRLYWVSQTQPAWAGGGNAYPPRAPRPKVLLLILGIVLTFWACFLPFWIWQLLPLYQPEVLRVVPVGTQVTINRILTGLTYGNSCVNPFFYTLLTGKRRRTSRKTISAAAPLCQKGSSEQ
Protein: B3 domain-containing protein REM1 (Protein REPRODUCTIVE MERISTEM 1) (AtREM1) (Q84J39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in flower development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326, ECO:0000269|PubMed:11842146}.
Interaction partners:
- Remorin
- Remorin family protein
- Uncharacterized protein At3g61260
- Remorin 1.4
- F12A21.28
- B3 domain-containing protein At3g06220
- Remorin family protein
- At2g02170/F5O4.6
- Remorin family protein
- AGAMOUS-like 98
Sequence:
MADPPHFSLFQQKFRTGDKPFLTLDADFLMNHTKVLLKSDASDKVWKVKLDGGRLSEGWEEFACDQKFRDGDVLVFKHHGDEVFHVAVVSPSVSGDIRNASSSQVITEDTYIDVDDVDDDDYGQDDEDDDDDDDEGEDNIENISEKTDKRQEADSSSDHSGFITARVTRYSLLHDRLDLSRNFTLLFGGHQKTCEIDVVDEQGRRWTMKLAKNISSGVFYIRLGWGNFCCANGLTQGDLCKFKLFQNEERPVLWLCPQESGNGRKEKRTFDEVSKGKEKKTPSPFLIVKYTPSRETTGQLSLPVSFTRNNSINKTGEVILLNQDGRKWSSYLQITGLGRGAGSEWFYLRRGWREMCEANGVGVNDSFKLELVWEGANPMFKFCSKIENHEYKGKGNQRTRKKRACETAPQPRNVKKTPRLGVEGPVYQVDEERGHTQVSNRTNTISGNLQRLLPPSCSVSDQVANVKQGIVDSLNTVRQCRTELETSEQNLQASLLAIDALGERIWGISKILSSNLV
Protein: Myosin heavy chain, embryonic smooth protein (F4I8Q1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g32630
- Probable xyloglucan galactosyltransferase GT15
- Putative acyl-activating enzyme 19
- GATA transcription factor 12
- aspartate-semialdehyde dehydrogenase
Sequence:
MEEATKVSSDVPQAKEVTKEDTVMEKEEEDTIFDGGFVKVEKEGINKKYDDDDDEKAEKQLKSLEDALQLHDVKHKELTEVKEAFDGLGLELENSRKKMIELEDRIRISALEAEKLEELQKQSASELEEKLKISDERYSKTDALLSQALSQNSVLEQKLKSLEELSEKVSELKSALIVAEEEGKKSSIQMQEYQEKVSKLESSLNQSSARNSELEEDLRIALQKGAEHEDIGNVSTKRSVELQGLFQTSQLKLEKAEEKLKDLEAIQVKNSSLEATLSVAMEKERDLSENLNAVMEKLKSSEERLEKQAREIDEATTRSIELEALHKHSELKVQKTMEDFSSRDTEAKSLTEKSKDLEEKIRVYEGKLAEACGQSLSLQEELDQSSAENELLADTNNQLKIKIQELEGYLDSEKETAIEKLNQKDTEAKDLITKLKSHENVIEEHKRQVLEASGVADTRKVEVEEALLKLNTLESTIEELEKENGDLAEVNIKLNQKLANQGSETDDFQAKLSVLEAEKYQQAKELQITIEDLTKQLTSERERLRSQISSLEEEKNQVNEIYQSTKNELVKLQAQLQVDKSKSDDMVSQIEKLSALVAEKSVLESKFEQVEIHLKEEVEKVAELTSKLQEHKHKASDRDVLEEKAIQLHKELQASHTAISEQKEALSHKHSELEATLKKSQEELDAKKSVIVHLESKLNELEQKVKLADAKSKETESTGKEEEVEVKSRDSDLSFSNPKQTKIKKNLDAASSSGHVMIQKAETWHLMTLKIALGVALVSVILGIIVGKNY
Protein: Actin cross-linking toxin VgrG1 (EC 6.3.2.-) (A0A0H3AIG7)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: Part of the type VI secretion system (T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (By similarity). Forms the spike at the tip of the elongating tube probably formed by hemolysin co-regulated protein/Hcp. Allows the delivery of the TseL antibacterial toxin to target cells where it exerts its toxicity (By similarity). Acts also directly as an actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin. Mediates the cross-link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding. The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners. Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9KS45}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:22898822}. Note=Secreted via the type VI secretion system. {ECO:0000250|UniProtKB:Q9KS45}.
Interaction partners:
Sequence:
MATLAYSIEVEGLEDETLVVRGFHGQESLSNSVFLGQACYGFRYEVQLASRVSNLTAEQMVDKRAELKLYRNSQLVQRVHGIVRAFSQGDIGHHHTFYQLTLVPALERLSLRHNSRIFQKQTVPEILSILLQEMGINDYAFALKRDGVQREFCVQYRESDIDFLHRLAAEEGLVYSFVHEAGKHTLYFSDASDSLSKLPEPIPYNALVGGAIDTPYIHGLTYRTQAEVSEVQLKDYSFKKPAYSFLQTVQGTELDYQQTRYQHFDAPGRYKDDVNGAAFSQIRLDYLRRHAHTATGQSNEPLLRAGYKFDLQEHLDPAMNRDWVVVSINHQGEQPQALQEDGGSGATTYSNQFSLIPGHLHWRAEPQPKPQVDGPMIATVVGPEGEEIFCDEHGRVKIHFPWDRYSNGNEQSSCWVRVSQGWAGSQYGFIAIPRIGHEVIVEFLNGDPDQPIITGRTYHATNTPPYTLPEHKTKTVLRTETHQGEGFNELSFEDQAGKEQIYLHAQKDFDGLIENDQFTQIKHNQHLTVEWESREAVTGEQVLSIEGSLHVKTGKVRVNEAGTEIHVKAGQKVVIEAGSEITVKAGGSFVKVDPAGVHLSGALVNLNSGGSAGSGSGFGGAMPALPGGLEPAVALAPPQTISYQALLQAEQANVPAVKVCPLAAQEATPAVNSITPPPPPPIAPPMAPPQPIMNPQPTANAQPNLGRSTKATPDFPTHFPKSSIGIENELAGLVVAMPANSAQKFGYVKSAQGDALFMLTKDMNQGSYQRPPSLQDGKNYQNWQTHTVELVSYPCEMDDKAAVETRKQAMLWLATHFTTHIDQSNHQPLAPIQSEDGRFVIEITNAKHVIAAGNGISAESQGQTITMTPSGQQATVGVAAKGFGTSATPELRLLESAPWYQKSLKSQFASLTSAENLDDKELAANVFAYLTSIYLKTAELAKKFGIYINEWDPMSEQITPNANGLTDPKVKNAWEILPRTKPSKIVEILSKSDAKAVMKHIKPQLQSRYSESLSKNVFQYFQDGGEVAGHGINNATVGDKHSPELAILFEFRTVPNELQSYLPKTESTTKSEVKLLDQFDPMKRKTVIQQVESLV
Protein: LD04521p (Monopolar spindle 1, isoform A (EC 2.7.11.1, EC 2.7.12.1)) (Q9VEH1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTPVPRRTKDMMALGLDSDSEDDFNTPYRPRQAAAGERKQQPVASFQVQTRGKENEPHPLPINMLPRRVSELTMMDSDSDEEDIKSNHNLNCAILNDSFVLSPSQELTNSNSNITTRRTPSAAPLKQSDSNLSFLGRFNDMGINCSSQGSPVANSEKQVAKKTAPTLQAAPSATERRPLQETETPLRNELPSTSKTKPDADFITPQVRTIGSTLAGKSRSAVSNDFRAQKVLFQTPMTVSRAAPVASDSISFSLCDTITESPDIPEPPKKAEPPKSQHPSKKSLDHVFRESDKDNVPDKVDNVEPKELVSIPAVAVPPEQPSHKTSNILKIKNHEYTIDKKLGCGGSSSVFLARRSDSGNEFALKVVDLQADPQVVQGYLNETKLLAKLQGNVCVVALYDYQLVREESKLYMVMEKGDCDLNKILQSYTTNLPLYSLMNILYQMLQAVNYIHQHGVIHSDLKPANFLMVSGRLKLIDFGIASNIAVDSTSIIKFSQAGTFNYISPEALTDTSTGNSPMRRADQPKIKISTKSDVWSLGCILYLLLYQKTPFGHIRNVYAKMSAITTPGTSIEYPAIPPYYPIMLVHMAKNCLQLNPKKRPSCTELLQYPFHMIIPLQNLQIPSRTANSN
Protein: indole-3-glycerol-phosphate synthase (EC 4.1.1.48) (Q72EV0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Anthranilate synthase, glutamine amidotransferase component
- Tryptophan synthase beta chain
- Tryptophan synthase beta chain
- Tryptophan synthase alpha chain
- N-
- Anthranilate synthase, component I
- Anthranilate phosphoribosyltransferase
- Para-aminobenzoate/anthranilate synthase glutamine amidotransferase
- Para-aminobenzoate synthase, component I
- N-
Sequence:
MLERFRAAKRHEVDKLEQCARRGGLPAPFAGPRPAFGTALRGDGLAVIAEYKRASPSCGVIDTKLTPEEVATAYEAGGATAISVLTEEVHFRGELSYLGRMTAPGLPLLRKDFIMHPLQVTATAATPASALLLIVRLTPDAALLRDLREQAEAQGMDAVVEVFDTDDLDIARASGARIIQVNARDLDTLKVSMPACLGMGVLRDAAETWVAASGMSAPEHLAAAATAGYDAALVGTALMRGGDPGAALRALLGREAA
Protein: Calcium channel flower (3L5) (Q95T12)
Organism: Drosophila melanogaster (Fruit fly)
Function: A calcium channel that regulates synaptic endocytosis and hence couples exo- with endocytosis. Isoform A and isoform B are mainly required in the nervous system and necessary in photoreceptor cells.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:19737521, ECO:0000269|PubMed:33300871}; Multi-pass membrane protein {ECO:0000269|PubMed:19737521}. Presynaptic cell membrane {ECO:0000269|PubMed:28414717, ECO:0000269|PubMed:33300871}. Endosome {ECO:0000269|PubMed:33300871}. Note=Upon fusion of the synaptic vesicle (SV) with the presynaptic membrane, protein transfers from the SV to the periactive zones where endocytosis is known to occur (PubMed:19737521, PubMed:28414717, PubMed:33300871). Upon high K(+) stimulation, expression levels in NMJ boutons are higher in bulk endosomes than in synaptic vesicles, suggesting that it is recycled to bulk endosomes after it activates ADBE (PubMed:33300871). {ECO:0000269|PubMed:19737521, ECO:0000269|PubMed:28414717, ECO:0000269|PubMed:33300871}.; SUBCELLULAR LOCATION: [Isoform Ubi]: Cell membrane {ECO:0000269|PubMed:20627080, ECO:0000269|PubMed:25754635, ECO:0000269|PubMed:35301437}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:33300871}. Note=Localizes to the apico-lateral membranes in wing imaginal disks and salivary gland cells. {ECO:0000269|PubMed:20627080}.; SUBCELLULAR LOCATION: [Isoform Lose-A]: Cell membrane {ECO:0000269|PubMed:25754635, ECO:0000269|PubMed:35301437}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:33300871}.; SUBCELLULAR LOCATION: [Isoform Lose-B]: Cell membrane {ECO:0000269|PubMed:25754635, ECO:0000269|PubMed:35301437}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:33300871}.
Interaction partners:
Sequence:
MSFAEKITGLLARPNQQDPIGPEQPWYLKYGSRLLGIVAAFFAILFGLWNVFSIITLSVSCLVAGILQMVAGFVVMLLEAPCCFVCFGQVNEIAEKVESKPLYFRAGLYIAMAIPPIILCFGLASLFGSGLIFGTGVVYGMMALGKKASAEDMRAAAQQTFGGNTPAQTNDRAGIVNNAQPFSFTGAVGTDSNV
Protein: Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 7.2.2.10) (Matrix-remodeling-associated protein 1) (Plasma membrane calcium ATPase isoform 4) (Plasma membrane calcium pump isoform 4) (P23634)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. By regulating sperm cell calcium homeostasis, may play a role in sperm motility (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:2137451}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calmodulin-1
- Nitric oxide synthase 1
- cGMP-dependent protein kinase 1
- Calmodulin-1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cGMP-dependent protein kinase 2
- Phospholamban
- Alpha-1-syntrophin
Sequence:
MTNPSDRVLPANSMAESREGDFGCTVMELRKLMELRSRDALTQINVHYGGVQNLCSRLKTSPVEGLSGNPADLEKRRQVFGHNVIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPAGEENELCGQVATTPEDENEAQAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQCRIEQEQKFSIIRNGQLIQLPVAEIVVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIILTLLGVNEDDEGEKKKKGKKQGVPENRNKAKTQDGVALEIQPLNSQEGIDNEEKDKKAVKVPKKEKSVLQGKLTRLAVQIGKAGLLMSALTVFILILYFVIDNFVINRRPWLPECTPIYIQYFVKFFIIGITVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYIGGIHYRQIPSPDVFLPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALLGFVTDLKQDYQAVRNEVPEEKLYKVYTFNSVRKSMSTVIRNPNGGFRMYSKGASEIILRKCNRILDRKGEAVPFKNKDRDDMVRTVIEPMACDGLRTICIAYRDFDDTEPSWDNENEILTELTCIAVVGIEDPVRPEVPDAIAKCKQAGITVRMVTGDNINTARAIATKCGILTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGEHRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTESLLKRRPYGRNKPLISRTMMKNILGHAFYQLIVIFILVFAGEKFFDIDSGRKAPLHSPPSQHYTIVFNTFVLMQLFNEINSRKIHGEKNVFSGIYRNIIFCSVVLGTFICQIFIVEFGGKPFSCTSLSLSQWLWCLFIGIGELLWGQFISAIPTRSLKFLKEAGHGTTKEEITKDAEGLDEIDHAEMELRRGQILWFRGLNRIQTQIDVINTFQTGASFKGVLRRQNMGQHLDVKLVPSSSYIKVVKAFHSSLHESIQKPYNQKSIHSFMTHPEFAIEEELPRTPLLDEEEEENPDKASKFGTRVLLLDGEVTPYANTNNNAVDCNQVQLPQSDSSLQSLETSV
Protein: Coronin-7 (G5EDS2)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAWRFAASKFKNTTPKVPKKEETIFDVPVGNLSCTNDGIHASADFLAFHIEGEGGKLGVLPITAKGRRTRNDIGIIAAHGEQVADFGFLTFADELLATCSRDEPVKIWKLSRDHSPKLATEIDVGGGNVIAECLRAHSTADNILAVGSHGSTYITDISTGKTAVELSGVTDKVQSMDWSEDGKLLAVSGDKGRQIVVYDPRASMEPIQTLEGHGGMGREARVLFAGNRLISTGFTTKRIQEVRAYDTGKWGAPVHTQEFVSTTGVLIPHYDADTRLVFLSGKGTNKLFMLEMQDRQPYLSHVFELTLPEQTLGATIGAKRRVHVMDGEVDTYYQLTKSSIVPTPCIVPRRSYRDFHSDLFPETRGAEPGCTAGEWLNGTNAVPQKVSMAPSQSSSSPPPPEPVPTPKVAQTPAPVPVPTPAAAPRPMSNNNSSSNNVPSVQEQHSVPKKEEVRELDYRPYEKENGVHTPNAETNSTQGNSSPISTISPEPVTIVKPASTPATDSVSTPSVVGPAFGKKVPEQPPVNFRKPIGASNRVPLSQRVRPKSCVVGQITSKFRHVDGQQGTKSGAVFSNLRNVNTRLPPESNGVCCSNKFAAVPLAGLGVIGIYDVNEPGKLPDGVMDGIFNKTLVTDLHWNPFDDEQLAVGTDCGQINLWRLTTNDGPRNEMEPEKIIKIGGEKITSLRWHPLASDLLAVALSNSTIELWDVANAKLYSRFVNHTGGILGIAWSADGRRIASVGKDATLFVHEPASREQRVYERKTVVESTRAARVLFACDDRIVIVVGMTKSSQRQVQMYDAQTVDLRHIYTQVIDSATQPLVPHYDYDSNVLFLSGKGDRFVNMFEVIYDSPYLLPLAPFMSPVGSQGIAFHQKLKCNVMAVEFQVCWRLSDKNLEKITFRVPRIKKDVFQDDLFPDSLVTWEPVTTGTKWMLGEQAAPVFRSLKPDGVFSSIPRAITASVRHSEMPSSSSTTNSAAQTPSTSVTHSTTEKHHHHQHHQHQEPTSVPTPSSRNMQSCGVESTQQPDRKQVAAAWSTKIDVDTRLEQDQMEGVDEAEWDK
Protein: Zinc finger protein, putative (O97273)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGTFINNTGNFRNKTLNSTNKTLNINYKVHSISPNSSLFCPVCNIPFTYKIRINPCYHIICKTCYKLSLQDQKCLMCNNDINDIENIFIKDQIYICPHNDCKKGFINEKSYQYHIYFKHKFLKEKNEINRKGSNNSNINHDIYNNNINDTINYTIPDQKNNNLGNFNNNMKNGGMNDSLSLHTSQWPNELIKNSLDSNINANMNNLNNINNVNNVSNINNINNINNVNNINNINNINNVNNVNTNDKCNVPNNNNINPFDIKAKKLQEGNEPLFTNITTTNKFMNTNKMSTSNILTNNNNITSNNNYKFLNNVPGTDTWTNSVFSIKSNFEKDVNTNKGEQNVTDVQNNKNNQQDDELDNLEDFM
Protein: Alcohol dehydrogenase, iron-containing (EC 1.1.1.1) (A0A0H2USH2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MAIFYVPAVNLIGKGVVNEVGPYIKELGYKKALLVTDKYIEGSDILPKTLKPLDTEGIEYVIFSDVEPNPTCKNVTDGVAALQEHGCDFIISLGGGSPQDAASCISIMATNGGKPQDYEGLHKSAKKGLPVVAINTTAGTSAEITINYVITDEERKVKMVMVDKNSLALISVNDPELMLSKPKGLTAATGMDALTHAVEALVTPGAYDVTKKLSIGAIELIKEYLPRAVENGHDIEAREGMVNAIFLGGMSFNNAGLGYVHSMAHQLGAVYNLPHGVCCAMLLPVIERENAKRVPEAFRNVAKALGLHVEGKSDQECADYAIAEIEKLSETVGIPKKLTELGIEEKDFDFEYLSKNALIDACAPGNPFMPTLEETIAFYKELF
Protein: Phosphatidylinositol transfer protein alpha isoform (PI-TP-alpha) (PtdIns transfer protein alpha) (PtdInsTP alpha) (Q00169)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. Shows a preference for PI and PC containing shorter saturated or monosaturated acyl chains at the sn-1 and sn-2 positions. Preference order for PC is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 and for PI is C16:1 > C16:0 > C18:1 > C18:0 > C20:4 > C20:3.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53810}. Nucleus {ECO:0000250|UniProtKB:P53810}.
Interaction partners:
- Membrane-associated phosphatidylinositol transfer protein 3
- 14-3-3 protein epsilon
- Platelet-activating factor acetylhydrolase IB subunit beta
- Scavenger receptor class F member 1
- Class A basic helix-loop-helix protein 9
- Trafficking regulator of GLUT4 1
- Adapter molecule crk
- Mitochondrial import inner membrane translocase subunit Tim22
- Signal transducer and activator of transcription 4
- Netrin-1
Sequence:
MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD
Protein: Uncharacterized protein (Q388M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MATIAELQQAIRDEKEKHEQAMEELRSQRESLASVVAEQQQYTQDIIMRVSELRGRKSQQMLAGNAAPNFAEIDTGCKAVDDILYSIEEGLETSTGKSSVVLGKILAAAVQAVVPGGDKKPSTLSSSSSATRTTDVVVISRNEIRGTHEWVKKHCKKCTACGELNGRPRPWEPPKKTDKGKSIKGNASAPNLRCIPGKNFRSLSLCFRREPCSGTVLELMRISAVVNVQGQSGEQITNPREVAAKITALVVEWVRKEMENAREAAKKAPWCEDGEDGQKFAVAVEMLLHNIDTRVEVFVIPPKNGGNVGGSNHVPMKINVFVVSPLFLSTLQPFVELWGNERDREYMLQGLIKPAIKRIAKLFGVDGVVDHGITVGLKAVDALVRMTKGKHFFEPTSPVKSKSGRPSASQPEQLIGFMHSVILAMSLLGTRIELECAVPDLGDLKDLEDAKRSAFNIAKAFLQRLLPPRQDVAVSLTDPAAADAVLWLRRMPTRMLEVLNNAFSSNSRLPSSLRTGVIDHLASPRLKINYALKNFSEIVIDIFRPYAPNSGMMTVEEKHKGEKARIGACAPVVDIPRDIVRASAEAAAWAKDMQQELLKREAAGVNTKEGEDAVNVVLERTKGDEIMANFLKEMQDLRLEVVELLEFGCDVCLPFGVAMQNGTTQPSEIIYARVEGVRNA
Protein: Uncharacterized GPI-anchored protein At4g28100 (Q9SUC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- SAC3 family protein C
- Dynamin-related protein 4C
- Calmodulin-like protein 5
- Putative RING-H2 finger protein ATL12
- xyloglucan O-acetyltransferase 2
- Aspartyl protease AED3
- Phospholipase D zeta 1
Sequence:
MKKSLTLLILLLCSLLFSTVLSNLLVEPVQPNTVPAFPVETQAQSCRLDLSNELFGGVNEACGRNLDRSRCCPVLAAWLFAAHARSALQLPAPAPTPESSDPDEPMKPDDSQKCVNTLQSALLTKQIKIPQPNSSCDAILCFCGIRLHQISSLSCPAAFNVSSGFKNATPTAAVKNLEKECRNSSYSGCTRCLGALQKLKVRGGNKKTTTERGTKMMSKDCQLMGLTWLLARNKTAYIPTVSAVLRAIMYSPHPPHLNKCSPDQENMPLAVDSLQFQKSFSSSSHLFGVLPFLPLVLCIFLFLL
Protein: Antifungal lectin AMML (P85004)
Organism: Astragalus mongholicus (Milk vetch) (Astragalus membranaceus var. mongholicus)
Function: Lectin that binds strongly to galactose, lactose, D-raffinose, L-rhamnose and cellobiose, and less strongly to D-glucose, D-xylose and L-arabinose. Does not bind D-galacturonic acid, D-fructose, D-mannose, D-ribose, L-sorbose, maltose and sucrose. Has hemagglutinating activity towards human type O and rabbit erythrocytes. Has strong antifungal activity against B.cinera with an IC(50) value of 1.2 uM, and weaker antifungal activity against D.turcia, F.oxysporum and Colletorichum sp. Lacks antifungal activity against F.oxysporum and M.arachidicola.
Interaction partners:
Sequence:
ESGINLQGDATLANN
Protein: Coatomer subunit delta (Q7K7G0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}; Cytoplasmic side {ECO:0000256|RuleBase:RU364018, ECO:0000256|RuleBase:RU366052}.
Interaction partners:
Sequence:
MVLIAAAVCTKNGKVILSRQFVEMTKARIEGLLAAFPKLMTAGKQHTYVETDSVRYVYQPMEKLYMLLITTKASNILEDLETLRLFSKVIPEYSHSLDEKEIVENAFNLIFAFDEIVALGYRESVNLAQIKTFVEMDSHEEKVYQAVRQTQERDARQKMREKAKELQRQRMEASKRGGPSLGGIGSRSGGFSADGIGSSGVSSSSGASSANTGITSIDVDTKSKAAAKPASRNALKLGGKSKDVDSFVDQLKNEGEKIANLAPAAPAGGSSAAASASAAAKAAIASDIHKESVHLKIEDKLVVRLGRDGGVQQFENSGLLTLRITDEAYGRILLKLSPNHTQGLQLQTHPNVDKELFKSRTTIGLKNLGKPFPLNTDVGVLKWRFVSQDESAVPLTINCWPSDNGEGGCDVNIEYELEAQQLELQDVAIVIPLPMNVQPSVAEYDGTYNYDSRKHVLQWHIPIIDAANKSGSMEFSCSASIPGDFFPLQVSFVSKTPYAGVVAQDVVQVDSEAAVKYSSESILFVEKYEIV
Protein: Alpha-1,3-mannosyltransferase MNT2 (EC 2.4.1.-) (P53059)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase involved in adding the 4th and 5th mannose residues of O-linked glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Glycolipid 2-alpha-mannosyltransferase
Sequence:
MRRKNRLFILVVLLGIVLVVYYSQLNSLDLVEPVQSSSSGNGGCWSYYEGLTPGWLNDFYDVNQITPNPAKDVIELVTRIKIFFNCLQQVDGHNIQRLRDIEKKLFPYINFEKLETDESAFWHTTTRWNGEVYHASMLEFDPKNHQFLRSKPINFDTGLSFWENWLHTVTQSGSKGIVISASDVQLNETIRLLKVLRFIKNDYPIQIVHNADLSQDSMKSIIKYARSLDTAEYPAQELWFLNVHSLLNPKYSKKFTTYSNKWLALTFSSFEIPILMDSDTVPFVSIEKFYELEEFQKTGVLFFKDRVISDDLFESSELKILREIVYGCIGLDLEDESKIHEQVEDPVVAQVLENMFIKKYKHHLESGLVILHKGKHLFSMLTSIALQFSPIAEYFHGDKDFFWLGELLSNNRFTFHPVDASNIGQLGNVVSKESTGEFYQICSVQLSHTDRDGSLLWLNGGLNICKKTSWEYDYEHRQRLNDMFQNADELREYYASPVKLEGIIIPDTSISGWINSGECFLFNYCTLFKEGEFGKLIKFKEDEKLRLSQIVDIWNKDI
Protein: Calumenin (H0Y875)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Melanosome {ECO:0000256|ARBA:ARBA00004223}. Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
XIATKEEFTAFLHPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF
Protein: Cytoplasmic envelopment protein 2 (Tegument protein BGLF2) (P0CK55)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating. Activates the AP-1 pathway and enhances EBV reactivation and virus release. Inhibits type I IFN-induced TYK2, STAT1 and STAT3 phosphorylation, thereby impairing type I IFN signaling and counteracting the ability of IFN-alpha to suppress the reactivation of EBV. Recruits SHP1 phosphatase to dephosphorylate STAT1. Mediates STAT2 ubiquitination and proteasomal degradation. Also suppresses type II and type III IFN signaling. Contributes to G1/S arrest in the host cell. Acts as an miRNA regulator that interferes with the function of RISC in miRNA-mediated mRNA silencing. As a result, SUMOylation is increased. When encapsulated in the exosomes released by EBV-infected host cells, may facilitate the infection in recipient cells.
Subcellular location: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04039}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04039}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04039}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04039}. Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. Associates with the capsid before the final envelopment. Recruited to the TGN via the interaction with BBLF1. Also found in the exosomes released by the host cell. {ECO:0000255|HAMAP-Rule:MF_04039}.
Interaction partners:
Sequence:
MASAANSSREQLRKFLNKECLWVLSDASTPQMKVYTATTAVSAVYVPQIAGPPKTYMNVTLIVLKPKKKPTYVTVYINGTLATVARPEVLFTKAVQGPHSLTLMYFGVFSDAVGEAVPVEIRGNPVVTCTDLTTAHVFTTSTAVKTVEELQDITPSEIIPLGRGGAWYAEGALYMFFVNMDMLMCCPNMPTFPSLTHFINLLTRCDNGECVTCYGAGAHVNILRGWTEDDSPGTSGTCPCLLPCTALNNDYVPITGHRALLGLMFKPEDAPFVVGLRFNPPKMHPDMSRVLQGVLANGKEVPCTAQPWTLLRFSDLYSRAMLYNCQVLKRQVLHSY