wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein eL19 (60S ribosomal protein L19-B) (L23) (RP15L) (RP33) (YL14) (P0CX83)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eL19 may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA
Protein: Pv-fam-h protein (Q8IK17)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S15A, putative
Sequence:
MIKDHNNNEMSMNFYTYKKMINDNSTSYSSSKMEPESNRYIKGKNINIFPLLKFTVFTLLIWIVTFINNYGNYMNDGCRMTDLSTSRFLSEPLLEFDTVFDVFKDTFLKNMGCSDEETKNIRSTMKQYFDNIDMNALSKEMKENGNFFEQIGNNENTLERFMKKDISQLKCINVENAEEGEEIPKPYTVEEVDPNNPNKGEIGNMKFNSNFIRRSVITLKKIGTSPTFLITMTAILLKNDNFKTALLLMVALFLKGVNFALDLKAYNDKFHFIKFK
Protein: Gpr1p (A0A1D8PN42)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- Adenylate cyclase
- Ras2p
- Ras-like protein 1
- Polyubiquitin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Uncharacterized protein
- Uncharacterized protein
- Large ribosomal subunit protein eL40
- NEDD8 family protein
Sequence:
MPDLISIATSPTKAFTPAATPTTIPTTIATIAASVSAATATVTTIIKDSTDDSTTTASILSALFNDIILPTIFKRDYSTRDHKANQLGQFTDHQARVQRIVAISSSCGSIAAVLIAMYFLFAIDPKRIVFRHQLIFFLLFFDLLKACILLLYPTRILTHSSAYYNHNFCQVVGFFTATAIEGADIAIFAFAFHTYLLIFKPSFNTKVKNSNRVEGGLYKFRYYVYSLSFFVPLIVASLAFIHSDGYDSLVCWCYLPMRPVWLRLVLSWVPRYCIVVGIFVIYGLIYIRVISEFKTLGGVFKNAAGNGGAGNLHLASNSNPTFFSSLKYFFVSMKDQWFPNMSDDTIAPITSRHSHSHNASGTIASPHRNVIGEIDNDDGDDDSEELAEALEDESVDYQDIELNKQSSRNSYRHHNSDIQQANLENFRRRQRIIQKQMKSIFIYPFAYCLVWLFPFILQATQFNYEEDHHAVYWLNVLGALSQPLNGFVDTLVFFYRERPWRNTAMKNFEKENRQRVDNIIVNNLEQRKYSEGAESAQTVATASKRIAKNSLSASSGLVNINAYKPWRQFMNKYRFPFYQLPTDKNIAKFQDRYIKRKLRDSRKLDKLVQEVTRDRQDLTFPTNIAEKYGDGSGNGSGSGSGGHHGGSTISNTNDSSPMSMGAGINWTEPTNAHDFSNILNTGGNSNVSSWGTKDVPGFKPNFGKFTFGNRSSNLLSRKSSTVIGLHGTGRNVRQPSNDSFNDPVRSLGGRRNSSLVIGNNTTLNKPYEIVSSPTSSTFTPIDRVKSNEDIDELHTVDNDTDKADDNDDGELDLMEFLKKGPPM
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FKV7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MQTIQLIYLICALLGTALCAPYEAYPIPKQIPPVARTNQQFVFQISNDTYKSNVNDLVQISYQTYDLPKWLTFNTDSRTIQGLPPSDLFNGDNQVQYFKFILEGTDESDNSKLNNTYQLVVTNKPAITLSPNFNLLALLKNSGYTNGKNGLILTPNQIFNVTFDRSNFDSSDEIVAYYGRTDQYNAPLPNWVFFDPANLKFSGSAPVVNSQIAPQTAYDLTLIATDIDGYAGIEVPFELVIGAHTLTTSIQNTLVINVTETGNISYKVPLNYVYYDDAPITTNNLGSLNLVNNPAWIRLNNDTIEGTVPQDMIKSANGPIGNFSVVIYDINGDVIYLNFEVEATTKLFATSSLPNLNATRGEWFYYNFLPSQFTDFDNTNVSVKYEGDTDHDWLNFVSSNLTLMGRVPQNFQRLTIDLVAQKNSLSQQLPFTIIGMDKLTTNHTNITTSANATNSSTLYSSTRTSATHSKTSDVEVTSTSTESSSAVAPLSKASKKHSTKTAAIACGVAIPVAVIILVVLAFLFYRSKKKTEPKDEEKTPNISPPNPYNPANNPNKAATSLENPFEDDSDADSAKRRLDMLNALKLDDASTTDSDTSTMDEKRSNKSDIFYDTNNTNSRDLLLEHKDTNSTFFEPNIRSSSVYVDSIPAHKKSWRYTLASARSSHQPGNIRDSYSSLNTVSTAELMNTTISDEADIPKDPRKSTLGLRDSVFLDMGSKKKGNLTSSQGNSFSSQMLSESSGHSSQNIPHDTSMRTFERPILEEEASDKHTPGTVSSSSTDDFVPVKNGTSYEWVSKNSPNRKPSVKRFVDISNSSNINVSQAGNFEGHSPEHI
Protein: Tubulin beta-4A chain (Tubulin beta-4 chain) (Q3ZBU7)
Organism: Bos taurus (Bovine)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}.
Interaction partners:
- Doublecortin domain-containing protein
- Tubulin alpha-1B chain
- Tubulin alpha-4A chain
- Gap junction alpha-1 protein
- Tubulin alpha-1C chain
- Tubulin alpha-8 chain
- Tubulin alpha-3 chain
- Tubulin alpha-1D chain
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEGEFEEEAEEEVA
Protein: Heterogeneous nuclear ribonucleoprotein U (Q5RI18)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLVCVLGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY
Protein: Rifin (O96289)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYMNILLFALPLNILEHNERDHNNTTLHTSITRSLCEFELYEPANYDNDQEMKEVMQQFEVRTSQRFHEYDESLQSKRKQCKDQCDKEIQKIILKDKLEKHMAQQLSTLETRITTDDIPTCVCEKSMADKVEKGCLRCGCILGAAMPELGSVGGSLLYALNTWKPVALKAAIAAANKAGMAAGIKAGDAAGMNVVIVQLGKWGINEFCPEIFESILKINHYSKLKDFASAIVAEHDKICAITTSGENSMCLPFDIALGLSDAKGTPIGPPASQAIPKMMNQLVGKAKGTADFMANKVNSETYSKIITKQADLIEAGFNSCTTSIYASIIVILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: NTF2-related export protein 1 (Protein p15) (Q9UKK6)
Organism: Homo sapiens (Human)
Function: Stimulator of protein export for NES-containing proteins. Also plays a role in the nuclear export of U1 snRNA, tRNA, and mRNA. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5.
Subcellular location: Nucleus. Nucleus speckle {ECO:0000305}. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
Interaction partners:
- Nuclear RNA export factor 2
- Nuclear RNA export factor 3
- Nuclear RNA export factor 1
- Nuclear RNA export factor 5
- Nuclear transport factor 2
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup98-Nup96
- THO complex subunit 4
- NTF2-related export protein 2
Sequence:
MASVDFKTYVDQACRAAEEFVNVYYTTMDKRRRLLSRLYMGTATLVWNGNAVSGQESLSEFFEMLPSSEFQISVVDCQPVHDEATPSQTTVLVVICGSVKFEGNKQRDFNQNFILTAQASPSNTVWKIASDCFRFQDWAS
Protein: Na(+)/dicarboxylate cotransporter 3 (NaDC-3) (rNaDC3) (Na(+)-coupled carboxylate transporter 3) (NaC3) (Sodium-dependent high-affinity dicarboxylate transporter 2) (SDCT2) (Solute carrier family 13 member 3) (Q9Z0Z5)
Organism: Rattus norvegicus (Rat)
Function: High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-6 carbon atoms, such as the citric acid cycle intermediates succinate and alpha-ketoglutarate (2-oxoglutarate), as well as other compounds including N-acetyl-L-aspartate. Transports the dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) for 1 divalent dicarboxylate, rendering the process electrogenic. Can transport citrate in a Na(+)-dependent manner, recognizing the divalent form of citrate rather than the trivalent form which is normally found in blood.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Solute carrier family 22 member 6
- Organic anion transporter 3
Sequence:
MAALAALAKKVWSARRLLVLLLVPLALLPILFALPPKEGRCLYVILLMAVYWCTEALPLSVTALLPIILFPFMGILPSSKVCPQYFLDTNFLFLSGLIMASAIEERNLHRRIALKVLMLVGVQPARLILGMMVTTSFLSMWLSNTASTAMMLPIASAILKSLFGQRDTRKDLPREGEDSTAAVRGNGLRTVPTEMQFLASSEGGHAEDVEAPLELPDDSKEEEHRRNIWKGFLISIPYSASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLLVGWLWISFLYGGMSWRGWRKKNSKLQDVAEDKAKAVIQEEFQNLGPIKFAEQAVFILFCLFAILLFSRDPKFIPGWASLFAPGFVSDAVTGVAIVTILFFFPSQKPSLKWWFDFKAPNSETEPLLSWKKAQETVPWNIILLLGGGFAMAKGCEESGLSAWIGGQLHPLEHVPPLLAVLLITVVIAFFTEFASNTATIIIFLPVLAELAIRLHVHPLYLMIPGTVSCSYAFMLPVSTPPNSIAFSTGHLLVKDMVRTGLLMNLMGVLLLSLAMNTWAQAIFQLGTFPDWANTHAANVTALPPALTNNTVQTL
Protein: Protein kes1 (O74178)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Phosphatidate cytidylyltransferase, mitochondrial
Sequence:
MSKTTSSDDSRDGEGDKRLRSTTKSTWLSFLKSIATFSGDLSSLTAPSFILSSTSLIEYSAYWAEHPELFISLPRGETPLERQLLVTKWFASTLKNQYAARNERYGSEKKPLNPILGELFTGKWNTDIGEDTELTSEQVSHHPPITAYHIYNKKAGVRLEGYNGHKSGFSGPQIHVKQIGHARLILEPHNEVYYITFPLVTLEGLWYGSPYIELGKKSYIISTSGYLTTIEYSGKGYFTGKKNTFKATIVNAKTKSEPIYRIEGSWTGMLKYCTFEDQKRSAWEDFLDCGNYKPVNISVAPIEEQGEYESRRVWKNFAVALDAGDYAAASQEKSKIEEGQRELRRQEEEHNEVWHRKYFEWKDKDEGFEEATKCLRQPVKEGFWYYLR
Protein: Transcription factor SOX-11 (P0C1G9)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that acts as a transcriptional activator (By similarity). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7M6Y2, ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- POU domain, class 3, transcription factor 3
Sequence:
MVQQAESSEAESNLPRDALDTEEGEFMACSPVALDESDPDWCKTASGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLKDSEKIPFIREAERLRLKHMADYPDYKYRPRKKPKTDPAAKPSAGQSPDKSAAGAKAAKGPGKKCAKLKAPAGKAGAGKAAQPGDCGAGKAAKCVFLDDDDEEDDEDDELQLRPKPDADDDDDEPAHSHLLPPPAQQQPPQLLRRYSVAKVPASPTLSSAAESPEGASLYDEVRAGGRLYYSFKNITKQQPPPAPPALSPASSRCVSTSSSSGSSSGSGAEDADDLMFDLSLNFSQGAHSACEQPLGAGAAGNLSLSLVDKDLDSFSEGSLGSHFEFPDYCTPELSEMIAGDWLEANFSDLVFTY
Protein: Exocyst complex component 84B (F4K7F5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAAKTARSKATPTKENGVRVEEGLSLFKSDKFDADAYVQSKCSINEKEIVIVEWILGSSRFYTLEKMMSNVTILIACMVVLVIFWKKIQFGYGIGYKGCLVCVVTFCDGDIKQLCSYLLDLKRASAEEMRRSVYANYPAFIRTSKEISDLEGELSSIRNLLSTQATLIHGLADGVNIDDDKVSDESLANGLLNFEDNGLSDLEKWATEFPDHLDALLAERRVDEALAAFDEGEILVSQANEKHTLSSSVLSSLQFAIAERKQKLADQLAKAACQPSTRGGELRSAIAALKRLGDGPRAHTVLLDAHFQRYQYNMQSLRPSSTSYGGAYTAALSQLVFSAISQASSDSLGIFGKEPAYSSELVTWATKQTEAFSLLVKRHALASSAAAGGLRAAAECAQIALGHCSLLEARGLSLCPVLLKHFKPIVEQALEANLKRIEENTAAMAAADDWVLTSPPAGSRHASTAFQNKLTSSAHRFNLMVQDFFEDVGPLLSMQLGSKALEGLFRVFNSYVDVLVRALPGSIEEEDPNFESSCNKIVQMAETEANQLALLANASLLADELLPRAAMKLSLDQTGQRTDDLRRPLDRQNRNPEQREWKRRLLSTVDKLKDAFCRQHALDLIFTEEGDSHLSADMYVNIDENGEDVDFFPSLIFQELFAKLNRMASLAADMFVGRERFAISLLMRLTETVILWLSGDQSFWDDIEEGPRPLGPLGLRQLYLDMKFVICFASQGRYLSRNLHRGTNEIISKALAAFTATGIDPYSELPEDDWFNDICVDAMERLSGKTKGNNGDVHSPTASVSAQSVSSARSHGSY
Protein: Ameloblastin (Q9NP70)
Organism: Homo sapiens (Human)
Function: Involved in the mineralization and structural organization of enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Enamelin
- Tuftelin
- Amelotin
- Amelogenin, X isoform
- Matrix metalloproteinase-20
- Dentin sialophosphoprotein
- Extracellular serine/threonine protein kinase FAM20C
- Kallikrein-4
- Pseudokinase FAM20A
- Integrin-binding sialoprotein
Sequence:
MSASKIPLFKMKDLILILCLLEMSFAVPFFPQQSGTPGMASLSLETMRQLGSLQRLNTLSQYSRYGFGKSFNSLWMHGLLPPHSSLPWMRPREHETQQYEYSLPVHPPPLPSQPSLKPQQPGLKPFLQSAAATTNQATALKEALQPPIHLGHLPLQEGELPLVQQQVAPSDKPPKPELPGVDFADPQGPSLPGMDFPDPQGPSLPGLDFADPQGSTIFQIARLISHGPMPQNKQSPLYPGMLYVPFGANQLNAPARLGIMSSEEVAGGREDPMAYGAMFPGFGGMRPGFEGMPHNPAMGGDFTLEFDSPVAATKGPENEEGGAQGSPMPEANPDNLENPAFLTELEPAPHAGLLALPKDDIPGLPRSPSGKMKGLPSVTPAAADPLMTPELADVYRTYDADMTTSVDFQEEATMDTTMAPNSLQTSMPGNKAQEPEMMHDAWHFQEP
Protein: Protein phosphatase 1A, magnesium dependent, alpha isoform (Protein phosphatase 1bb (EC 3.1.3.16)) (Protein phosphatase, Mg2+/Mn2+-dependent, 1Bb) (Q5U386)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 7.
- Protein phosphatase 1B
- Myoneurin
Sequence:
MGAFLDKPKTEKHNAHGAGNGLNFGLSSMQGWRVEMEDAHTAVVGLPHGLDDWSFFAVYDGHAGSRVANYCSKHLLEHIITSSEDFRSGPDSVEGVKIGIRSGFLKIDEYMRNFSDLRNGMDRSGSTAVGVLVSPEHLYFINCGDSRAVLSRAGQVRFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVFEVPRVSDEDEFVVLACDGIWDVMSNEELCDFVRSRLEVWDDLEKVCNSVVDTCLHKGSRDNMSVVLVCFPNAPKVSEEAVKKEAELDKFLEARVEELMEKSGEEGIPDLSHIMHNLHPETIPNLPPGGGLPSKRSVIEAVYNRLNPHREEDGSGGDLDDPW
Protein: Serpentine Receptor, class D (Delta) (Q9XWA0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Serpentine Receptor, class T
- Serpentine receptor class r-10
- Seven TM Receptor
- Serpentine receptor class r-10
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Serpentine Receptor, class AB
Sequence:
MYFGTYQIIHAILSIFGVGINIFLLFLALTKSPKIMRPCSALITNKSLTDIMSSVANFFVMQRILTDGSSVTIIPTGPCTMIGPTACYAGHMFMGSFLEHNLIWLIACYLFRYYILYVCDPSIKSIIFAAFLVYTPSFVHMAMWIKLFDAEQMEIKMNETELFANELEFPEMQLTGRIVYWSSIVVYVQLVFTALLVVIAYTWIRNVLINFLISMGVSLSKDVKIINRQLVKILTFQVCIPIWIFLGVFFFLAMYTQSTRPDTLQYAITISFMLAPVVSPFAYIFFVPHYWNFCIGKKYVAPANSSICGTSATCGSVEKKSVA
Protein: Phosphatidylinositol 4-kinase (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (PI4K-alpha) (P54677)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol 4-kinase
- Probable phosphatidylinositol phosphate kinase DDB_G0267588
- 1-phosphatidylinositol-5-phosphate 4-kinase
- PIPK domain-containing protein
- Inositol 5-phosphatase 4
- Phosphatidylinositol-3-phosphatase SAC1
- SAC domain-containing protein
- Phosphatidylinositol 3-kinase VPS34-like
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
Sequence:
MNKISDTIIITSTSNEDEVDNNNNNNNLKEIDRSPRVNNNNNNILTNVNNNKNNTITSSGGSDSSSSSSNNNNNKIKKSKKHKEKEHMDSIVKLYSGKFDSWMVICHLFKYRDNPGIVDFLCNKMYNLEDKDIDFYITQLCILLINQPHDQKASFSSLARFILDRCASSFRFAIKAYWIFQAFEEDGEKNLFSIEGSVYLHSPSTSPKDVPMYSNDQIVPIDLDKIYNQSQYDDDDFDLSDDDGGFEIIKKNDHHYENDHHIENDPKKDINSNNNNNNNINNNNSNNDDNNNNEILPNENSDNSINDENNQYGNSNNNNNISGENDNIKIDINSQNKSDSNIETLNSTLCEETKTSPIKDDMENNNNNNNNNNNNNNNNNNNNNINNNNINNNNINNNNNINYGHINGSLSTLDGIGQPYISQPNDPIENITQILKRNRIIYKKVEEKKELATRLREFCEMSVITCSRPLITRPRTSSLPSPLISYNSGKIGGNYHKILSPSSVDSTSLISEDDKIIEKEEEDNVVEDDDDDEVNSEDFIPTATTTATTTTTTIPNHLSKTTSGVGINSNSSTPININSAGAGAGGGGEINHIGYDDISYLDKCKTPPAESKLSDHDFEFELSKSHRCDYLNDILSFIQKLAHISKILLPIPIDLRQAKLKHEISLLNINLPLGLYVPLWQSSNHHCVVRIPPEEVKILNSRERVPFLLVLEVIESEHEALSSNIFEVVSSYLQYTTGNSALKKDDIKRKYYSEKFKKSFLNSSINSTISNSSDSCTTETTTTSPVATSPTLPINIPHSKLINDGSNSISKSLPVTPTQSTVLNNLISTSTAISPPSQQQQLPSPSNTTTTTTTTTTNTNNTTTTTTTTTTTLSTSPTNEKILNENKQNSSPFGESWQEKIERYKKISPFGDYPNWRLYSVIVKTGDDCRQEQMAVQLISKFDEIWKETRLPLYLRPYSILVTSSGGGIIETIPDTMSLHNLKKSTPGFTTLLNYFKSTYGDPSGLRFRTAQSNFIESMAAYSIVTYILQIKDRHNGNILIDKEGHIVHIDFGFILSNSPGNISFESAPFKLTQELVDVMGGIQSGQFQYFKVLCVRGLIEARKQVDKIISLIEIMMSGPKMSCFVGGKEVIEQLKARFFLDVNERECSTLVENLISYSIDHFKTRYYDKYQSWLNGIYQ
Protein: Ectonucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) (NTPDase 8) (NTPDase8) (EC 3.6.1.5) (Q5MY95)
Organism: Homo sapiens (Human)
Function: Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleoside triphosphate diphosphohydrolase 6
- Nucleoside diphosphate phosphatase ENTPD5
- Soluble calcium-activated nucleotidase 1
- Adenosine kinase
- Ectonucleoside triphosphate diphosphohydrolase 4
- CTP synthase 2
- CTP synthase 1
- Cancer-related nucleoside-triphosphatase
Sequence:
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQWLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPTFLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGLGTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVYTHSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLSLPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFHFLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFSEETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALVAVVGAALVQLFWLQD
Protein: Protein virilizer homolog (Protein EMBRYO DEFECTIVE 2016) (F4J8G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs. Associates with MTA, MTB, FIP37 and HAKAI to form the m6A writer complex which is essential for adenosine methylation at specific mRNA sequences. N6-methyladenosine (m6A) plays a role in mRNA stability, processing, translation efficiency and editing.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:28503769}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28503769}.
Interaction partners:
- FKBP12-interacting protein of 37 kDa
- E3 ubiquitin-protein ligase HAKAI homolog
- N6-adenosine-methyltransferase non-catalytic subunit MTB
- N
- THO complex subunit 2
- YTH domain-containing protein ECT4
- YTH domain-containing protein ECT3
- DExH-box ATP-dependent RNA helicase DExH7, chloroplastic
- At4g36090
- RNA demethylase ALKBH9B
Sequence:
MVRSEPCVLFAQTFVHPQLDEYVDEVIFAEPVIITACEFLEQNASSSSQAVSLVGATSPPSFALEVFVRCEGESKFKRLCNPFLYTPSAPYPLEVEAVVTNHLVVRGSYRSLSLIVYGNIVKDLGQYNIILEGRSVTDIVSSTEGNLEDLPLVLHSVNRTIEECLSSLDIVSLPLAAVDLPVEVKRLLQLLLKIFDKLATNDVVNKFVDTVVSGVSSYVTDNVDFFLKNKNCSAVTSSLDSGLFHDIVDRVKEDILDLNEIQESDVALGLFSFLESETYLATSQQLVVMLSPYIQFERDSLCTVLPKLSKGKATLLGLSLAFLLCSGREGCLQFVNSGGMDQLVYLFGHDGQNSTTITLLLLGVVEQATRHSVGCEGFLGWWPREDGSIPSGKSEGYCLLLKLLMQKPCHEIASLAIYILRRLRIYEVISRYEFAVLSALEGLSNSHGAATHNLNMLSDAKSQLQKLQNLMKSLGSVEDPSPSAYAERSLVSDHSEGWLSYKATSKLTSSWTCPFYSSGIDSHILALLKERGFLPLSAALLSMPELHSKVGDIMDVFTDIAMFIGNIILSFMFSRTGLSFLLHHPELTATIIQSLKGSVDLNKEECVPLHYASILISKGFTCSLLEIGINLEMHLRVVSAVDRLLKSIQQTEEFLWILWELRDVSRSDCGREALLTLGVFPEALAVLIEALHSAKDMEPAVENSGISPLNLAICHSAAEIFEVIVSDSTASCLHAWIEHAPVLHKALHTLSPGGSNRKDAPSRLLKWIDAGVVYHKHGVGGLLRYAAVLASGGDAQLSSSSILALDLTPAENGAGESTNVSEMNVLDNLGKVIFEKSFEGVNLSDSSISQLTTALRILALISDNSTVAAALYDEGAVTVVYAILVNCSFMFERSSNIYDYLVDDDHGCSSISDFLSERNREQSLVDLLIPSLVLLISVLQRLQGTKEQYRNTKLMKALLRLHREVSPKLAACAADLSSHYPDSALGFGAVCHLIVSALVCWPVYGWIPGLFHTLLSGVQTSSVPALGPKETCSFLCILSDILPEEGVWFWKSGMPLLSGLRKLAVGTLMGPQKEKQINWYLEPGPLEKLINHLTPNLDKIAKIIQHHAVSALVVIQDMLRVFIVRIACQRVEHASILLRPIFSSIRDGILDQSSTRDTEAYMVYRYLNFLASLLEHPHAKGLLLEEGIVQLLVEVLERCYDATYPSENRVLEYGIVSASSVIQWCIPAFRSISLLCDSQVPLLCFQKKELLASLSAKDCALIFPFVLKFCQVLPVGNELLSCLGAFKDLSSCGEGQDGLVSLLFHLFSGTEESVSERWCDTNSLSLDQLDMKKNPPFLSCWIKLLNSINSKDGLSSLAMKAVNVLSVGSIRLCLDGKSLDSKKVAALKSLFGLPSEFSGTDTFREENIGLIEQMVTLLSSMTSGSDSSATAEMKPYLHEASQSLLSLLKDGNIDDIISCKGVFVSPGNLDMDDLVSRNIEDDLYQRGLEDKFWWECPETLPERLPQSSLPAKRKLPTLESSSRRAKGENSSVDIPTQNSIQRGMGSVSLPPAPTRRDAFRQRKPNTSRPPSMHVDDYVARERSVDTAGNSNAITISRAGSSSGRPPSIHVDEFMARQRERGQNPSTIVVGEAVVQVKNPTPARDTEKVAGKPKQFKADPDDDLQGIDIVFDGEECEGPDDKLPFLQPDENLMQPAPVMVEQNSPHSIVEETESDANGSSQFSHMGTPVASNVDENAQSEFSSRISVSRPEMSLIREPSISSDRKFVEQADEAKKMAPLKSAGISESGFIPAYHMPGSSGQNSIDPRVGPQGFYSKSGQQHTGHIHGGFSGRGVYEQKVMPNQPPLPLVPPPSVSPVIPHSSDSLSNQSSPFISHGTQSSGGPTRLMPPLPSAIPQYSSNPYASLPPRTSTVQSFGYNHAGVGTTEQQQSGPTIDHQSGNLSVTGMTSYPPPNLMPSHNFSRPSSLPVPFYGNPSHQGGDKPQTMLLVPSIPQSLNTQSIPQLPSMQLSQLQRPMQPPQHVRPPIQISQPSEQGVSMQNPFQIPMHQMQLMQQTQVQPYYHPPQQQEISQVQQQQQHHAVQGQQGAGTSQQQESGMSLHDYFKSPEAIQALLSDRDKLCQLLEQHPKLMQMLQEKLGQL
Protein: Rhamnosyltransferase WbbL (EC 2.4.1.-) (P36667)
Organism: Escherichia coli (strain K12)
Function: Rhamnosyltransferase involved in lipopolysaccharide biosynthesis.
Interaction partners:
Sequence:
MVYIIIVSHGHEDYIKKLLENLNADDEHYKIIVRDNKDSLLLKQICQHYAGLDYISGGVYGFGHNNNIAVAYVKEKYRPADDDYILFLNPDIIMKHDDLLTYIKYVESKRYAFSTLCLFRDEAKSLHDYSVRKFPVLSDFIVSFMLGINKTKIPKESIYSDTVVDWCAGSFMLVRFSDFVRVNGFDQGYFMYCEDIDLCLRLSLAGVRLHYVPAFHAIHYAHHDNRSFFSKAFRWHLKSTFRYLARKRILSNRNFDRISSVFHP
Protein: Defense against restriction protein A (DarA) (O21970)
Organism: Escherichia phage P1 (Bacteriophage P1)
Function: Internal capsid protein that is probably ejected along with the viral DNA and prevents degradation of viral DNA by the host type I restriction-modification antiviral defense system. Plays a role in directing proper capsid assembly.
Subcellular location: Virion {ECO:0000269|PubMed:28509398, ECO:0000269|PubMed:3029955}. Note=Internal capsid protein. A proteolytically cleaved 60 kDa form is incorporated into the virion. {ECO:0000269|PubMed:3029954}.
Interaction partners:
Sequence:
MEQFNINKGMTIKPGLDVLPPPVTDDEYRALMAGEDRYLMTESNTLEEIEATFFYDTPIHWCATDLLEAISSTRLQLHRTMQAFVRALNQKLNGTGISAGSDKTGDVAQSGARAIGGAEIGRARNVNGLPVLPAIIPLSDGQTISILFHSPTAENRITNSDTLVAFQFLLNKKDVTHTVAPMSGRDMTLAQVTMKLANLAEKNSAKFQRAQKKKKALVDEITQLQADSDQKEDAMSDLADQVAAVEGQKADLEQKINAVASEADSLYEENERLQGEIDRLNRTGGRDTIAPAGMTGGHSRALTDRLASIKNRMHMDGEATLSNGASMKQFIGDGEGYIQLTDPDGSVYMIKAKSIQGVDMADAIGKLFKAYKAGNVSEYLVQPEEHKPENVEPESAEDTGSSSPEPEVSVGAYRYALQMRPAAPGAIPEGNKAILPRPDEGDPYYEYARYGIATYDTPLSDQQMSEYDLKLLPREDSFDFLAKTLTNGPFGKYAQKALELATNSPDEFRVMLKTQFQKTFPNIAFPGGAGTEKMVQSMINALQAEVGEITQPEPAPAQPDETVSEADAEANKAIEYLNNVMDMQSTDMAEIRNARGNVREAIAALQTAGRFEENEELVNGAARHLADLLVAIQKAGVAA
Protein: Ankyrin repeat domain-containing protein 55 (Q3KP44)
Organism: Homo sapiens (Human)
Interaction partners:
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 70A
- Intraflagellar transport protein 70B
Sequence:
MMRQATMDFSTPSVFDQQRGDSSEEVDLTMVYQAASNGDVNALTAVIREDPSILECCDSEGCTPLMHAVSGRQADTVKLLLKMGANINMQDAYGRTSLCLATYLGWLEGCVSLLRNGAKHNIPDKNGRLPLHAATAEPDMRLLTVLLQQSNISEINHQDNEGMTPLHWAAFHNQPQHTQMLLKKGADPTLVDKDFKTALHWAVQSGNRILCSIILSHHQGPSIINYDDESGKTCVHIAAAAGFSDIIHELARVPECNLQALDVDDRTPLHWAAAAGKAECVQSLLELGMDSNLRDINESTPLAYALYCGHTACVKLLSQESRTEPTRPPPSQSSRPQKKERRFNVLNQIFCKNKKEEQRAHQKDPSRDRYREEDTSEVNDIITTFDSIVGTNCQEQPGDQVAMVEFKKKTSDNSKYLLPEKKPLARKGLPPIRTQSLPPITLGNNFLTASHRATSHAGLSSAPHHMAQRSQKSRSEQDLLNNRTGCQMLLDNPWKSDSNQVFSYKVWTVSSSDKLLDRLLSVRPGHQEVSVPPHLRHLHNPSSGQNFQHLSPNRHKIRDLPFTRNNLAPLPDQKFLSGEPLRTNRVLPAIPSQRRHSTAAEESEHSANPTSDEN