wanglab/gogpt-training-data huggingface dataset:
Protein: Low-density lipoprotein receptor (LDL receptor) (Q28832)
Organism: Sus scrofa (Pig)
Function: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P01130}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000250|UniProtKB:P01130}.
Interaction partners:
- E3 ubiquitin-protein ligase MYLIP
- Proprotein convertase subtilisin/kexin type 9
- DAB adaptor protein 2.
- Low density lipoprotein receptor adapter protein 1
- E3 ubiquitin-protein ligase SH3RF2
- Apolipoprotein E
Sequence:
FQCQDGKCISYKWICDGNTECKDGSDESLETCMSVTCKIGDFSCGGRVNRCIPESWRCDGQQDCENGSDEEGCSPKTCSQDEFRCQDGKCIAPKFVCDSDRDCLDGSDEASCPTPTCGPASFQCNSSTCIPELWACDGDPDCEDGSDEWPQHCRSHSSSLPERSNNPCSALEFHCHSGECIHSSWRCDGDTDCKDKSDEENCDVATCRPDEFQCSDGTCIHGSRQCDREYDCKDMSDEQGCVNATLCEGPNKFKCQSGECISLDKVCNSVRDCRDWSDEPLKECGTNECLDNKGGCSHICNDLKIGYECLCPEGFQLVDKHRCEDIDECQDPDACSQICVNLEGSYKCQCEEGFQLEPLTKACKAIGTIAYLFFTNRHEVRKMTLDRSEYTSLIPNLKNVVALDTEVASNRIYWSDLSQRKIYSTQIDRAPSFSSYDTIIGEDLQAPDGLAVDWIHSNIYWTDSILGTVSVADTKGVKRKTLFQEKGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDVYSLVTEDIQWPNGITLDLSGGRLYWVDSKLHSISSIDVNGGNRKTVLEDKTKLAHPFSLAIFEDKVFWTDIINEAIFSANRLTGSDIHLMAENLLSPEDIVLFHNLTQPRGVNWCERTALQNGGCQYLCLPAPQINPRSPKFTCACPDGMLLAKDMRSCLTETEPAGTTQGPSMVNSTAVGPKHTASSELTTAESVTMSQHALGDVAGRGVTEKPQSVGALYIVLPIALLILLFFGTFLLWKNWRLKSINSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLED
Protein: Interferon gamma receptor 1 (Q5TFC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALLFLLPLVMQGVSRAEMGTADLGPSSVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKGSLWIPVVAALLLFLVLSLVFICFYIKKINPLKEKSIILPKSLISVVRSATLETKPESKYVSLITSYQPFSLEKEVVCEEPLSPATVPGMHTEDNPGKVEHTEELSSITEVVTTEENIPDVVPGSHLTPIERESSSPLSSNQSEPGSIALNSYHSRNCSESDHSRNGFDTDSSCLESHSSLSDSEFPPNNKGEIKTEGQELITVIKAPTSFGYDKPHVLVDLLVDDSGKESLIGYRPTEDSKEFS
Protein: A-kinase anchoring protein 5 (F1SA75)
Organism: Sus scrofa (Pig)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
Sequence:
METTVSEIQVESKDEKRSAEVSPQDERQEEKASMLCFKRRKKATKARKPKAGSDAPEAARKFPPEAGASDQPQPPGGAWVSVKRLITCRKRSDSSKQQKPCKAKVQPESKDADLSKKKAKSRLKIPCIKFSKGGKRSNHSKIIEDSDCSIKVQEEAESLDIKTPVQLDDQATKTKSTLDIREDVSQKDGDEVCESNVNKSITSPGEKVISVELELGTGHSAIPTGTLILEKDIETTEEKPSIHPQQGSPLETSDIEHPLPVVSDVPPLPAVPDQQIVEEARSSILESGPDWKDHESREIVAEESKPKDTELSQESDFQENEITAEKPKPEESKRMEPIAIIITDTEISEFDVKKAKNVPKQFLISIESEQVGVFANDSGFEGRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNTINNLVQ
Protein: Heterogeneous nuclear ribonucleoprotein D-like (hnRNP D-like) (hnRNP DL) (AU-rich element RNA-binding factor) (JKT41-binding protein) (Protein laAUF1) (O14979)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence.
Subcellular location: Nucleus {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}. Cytoplasm {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}. Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner. {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}.
Interaction partners:
- Polypyrimidine tract-binding protein 1
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein U
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein H3
- Heterogeneous nuclear ribonucleoprotein A1
- RNA-binding protein FUS
- Heterogeneous nuclear ribonucleoproteins A2/B1
Sequence:
MEVPPRLSHVPPPLFPSAPATLASRSLSHWRPRPPRQLAPLLPSLAPSSARQGARRAQRHVTAQQPSRLAGGAAIKGGRRRRPDLFRRHFKSSSIQRSAAAAAATRTARQHPPADSSVTMEDMNEYSNIEEFAEGSKINASKNQQDDGKMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVKKLLESRYHQIGSGKCEIKVAQPKEVYRQQQQQQKGGRGAAAGGRGGTRGRGRGQGQNWNQGFNNYYDQGYGNYNSAYGGDQNYSGYGGYDYTGYNYGNYGYGQGYADYSGQQSTYGKASRGGGNHQNNYQPY
Protein: Glutathione-binding protein GsiB (P75797)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex GsiABCD involved in glutathione import. Binds glutathione.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Glutathione transport system permease protein GsiC
- Glutathione transport system permease protein GsiD
- Glutathione import ATP-binding protein GsiA
- Isoaspartyl peptidase
- Sulfate/thiosulfate import ATP-binding protein CysA
- Dipeptide transport system permease protein DppC
- Probable D,D-dipeptide transport system permease protein DdpB
- Probable D,D-dipeptide transport system permease protein DdpC
- Putrescine export system permease protein SapC
- Putrescine export system permease protein SapB
Sequence:
MARAVHRSGLVALGIATALMASCAFAAKDVVVAVGSNFTTLDPYDANDTLSQAVAKSFYQGLFGLDKEMKLKNVLAESYTVSDDGITYTVKLREGIKFQDGTDFNAAAVKANLDRASDPANHLKRYNLYKNIAKTEAIDPTTVKITLKQPFSAFINILAHPATAMISPAALEKYGKEIGFYPVGTGPYELDTWNQTDFVKVKKFAGYWQPGLPKLDSITWRPVADNNTRAAMLQTGEAQFAFPIPYEQATLLEKNKNIELMASPSIMQRYISMNVTQKPFDNPKVREALNYAINRPALVKVAFAGYATPATGVVPPSIAYAQSYKPWPYDPVKARELLKEAGYPNGFSTTLWSSHNHSTAQKVLQFTQQQLAQVGIKAQVTAMDAGQRAAEVEGKGQKESGVRMFYTGWSASTGEADWALSPLFASQNWPPTLFNTAFYSNKQVDDFLAQALKTNDPAEKTRLYKAAQDIIWQESPWIPLVVEKLVSAHSKNLTGFWIMPDTGFSFEDADLQ
Protein: Iron-sulfur cluster assembly 1 homolog, mitochondrial (HESB-like domain-containing protein 2) (Iron-sulfur assembly protein IscA) (I3ITR1)
Organism: Mus musculus (Mouse)
Interaction partners:
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Cysteine desulfurase
Sequence:
MSASLVRATVWAVSKRKLQPTRAALTLTPSAVNKIKQLLKDKPEHVGLKVGVRTRGCNGLSYSLEYTKTKGDSDEEVIQDGVRVFIEKKAQLTLLGTEMDYVEDKLSSEFVFNNPNIKGTCGCGESFHV
Protein: CUB-like domain-containing protein (G5ECH9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSLYINLLTILTLCSVFSSLIADPYNCAGSQIINPPTNISNPWVYPSTWINKGNPPQYAGGQNCTWTINVPKGMFAIFTLQGITDVSSLLTMQDSVDYVTKFTISDSEPFFLMDPFFVVNLQANTNGTLGMEVRWNPINSGQNSTTYNIHPNSSPLPLFGGDFEDPVIIQSDTQVSLLATLPSIIITDMAPFMRITQVFDGPSINSTHLGNLYQVMASNKNLISSGKSLTLYSLQAGFSNIGYAVILQDYADVKQFNSSYKAINCISILNYCDVKLDASAGTAAAIRYYGLFYVDDFSMPDTNVISVYNDYVTPLHKLADYTSSISKTNTPQKFSGKFTTFVLNKDQATLRMSSAEKTAEWNTAFDSRRGFFTSGNYGLNSSIQNIADQITASKLTNISFTVDRTAIIGGASLTVKITSEQKTVLNNVYTTSNFPGGILYTIGDSISVKYDSNGAVSTGPFVSFGFDRYSSAACNGIFITIIMAIWMGLSL
Protein: Taste receptor type 2 member 60 (T2R60) (Taste receptor type 2 member 56) (T2R56) (P59551)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 1
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
- Extracellular calcium-sensing receptor
Sequence:
MNGDHMVLGSSVTDKKAIILVTILLLLRLVAIAGNGFITAALGVEWVLRRMLLPCDKLLVSLGASRFCLQSVVMGKTIYVFLHPMAFPYNPVLQFLAFQWDFLNAATLWSSTWLSVFYCVKIATFTHPVFFWLKHKLSGWLPWMLFSSVGLSSFTTILFFIGNHRMYQNYLRNHLQPWNVTGDSIRSYCEKFYLFPLKMITWTMPTAVFFICMILLITSLGRHRKKALLTTSGFREPSVQAHIKALLALLSFAMLFISYFLSLVFSAAGIFPPLDFKFWVWESVIYLCAAVHPIILLFSNCRLRAVLKSRRSSRCGTP
Protein: Translation initiation factor eIF2B subunit alpha (eIF2B GDP-GTP exchange factor subunit alpha) (Q64270)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9USP0}.
Interaction partners:
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2, subunit 2
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- eIF-2-alpha kinase GCN2
- Eukaryotic translation initiation factor 2A
Sequence:
MEDGELIKYFKSQMKGDPNMASAVAAIQTLLEFLKRDKGETIQGLRAHLTKAIETLCAVDSSVAVSSGGELFLRFISLTSLEYSDYSKCKKIMIERGELFLSRISLSRTKIASLCHAFIKDGARILTHAYSRVVLRVLEEAVAAKKRFSVYITESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKVDLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKSVQAGQDLKEEHPWVDYTSPSLITLLFTDLGVLTPSAVSDELIKLYL
Protein: MACPF domain-containing protein At4g24290 (Q9STW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negatively controls the salicylic acid (SA)-mediated pathway of programmed cell death in plant immunity.
Interaction partners:
- Glycosyltransferase
- Expressed protein
- Anamorsin homolog
- At3g16350
- MLO-like protein 1
Sequence:
MALRLPASKAAEVAIGSIGCGYDLAIDLRLKYCKGGSKDSRLLDIKEGDDNCEIVLPGGISIPNVSKSIKCDKGERMRFRSDILPFQQMAEQFNQELSLAGKIPSGLFNAMFEFSSCWQKDAAYTKNLAFDGVFISLYSVALDKSQVLLREHVKQAVPSTWDPAALARFIDIYGTHIIVSVKMGGKDVIYAKQQHSSKLQPEDLQKRLKEVADKRFVEASVVHNTGSERVQASSKVETKEQRLRFADTSSLGSYANKEDYVFMCKRRGGNDNRNLMHNEWLQTVQMEPDVISMSFIPITSLLNGVPGSGFLSHAINLYLRYKPPIEELHQFLEFQLPRQWAPVFSELPLGPQRKQQSCASLQFSFFGPKLYVNTTPVDVGKRPITGMRLYLEGRRSNRLAIHLQHLSSLPKIYQLEDDLNRSIRQESHDRRYYEKVNWKNYSHVCTEPVESDDDLSVVTGAQLHVESHGFKNVLFLRLCFSRVVGATLVKNSEWDEAVGFAPKSGLISTLISHHFTAAQKPPPRPADVNINSAIYPGGPPVPTQAPKLLKFVDTSEMTRGPQESPGYWVVSGARLLVEKGKISLKVKYSLFTPILGDEVIEEAYEG
Protein: Kelch-like protein diablo (Q9VGE5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cullin 3, isoform F
- FI23980p1
- RING-box protein 1A
- RING-box protein 1B
- RNA helicase
- Peptidyl-prolyl cis-trans isomerase
- Protein roadkill
- AT19737p
- Succinate--CoA ligase subunit beta, mitochondrial
- Protein germ cell-less
Sequence:
MDLSDNSQVEDQYFVYKHDKLFGESFPLFKEIRRMGKLCDVTLKVEDQTFSAHRVVLAATIPYFYAMFTNNMAESRIKEITMKESAIEPSALESLINYVYSGQVRIDNQNVQNLMVGASFLQLSNVRDACASFLISRFHPHNVLGIRTFADSMICRQLIDAADKYIDQNFAKVSQSEEFLALDCEQLLELMRRDELNVRTEEVIFEACMKWVKYAEDKRSELFPQVLAAVRLPLLSPQFLADRVAREELIRSSHQCRDLLDEAKDFHLMPERRGLLQSFRTRQRSGEFFTGQIYAVGGLASTGESVSTVEIYDPLTKKWKMGEQMSMMRSRVGVAVLNGKLYAFGGFNGTERLSTVEVYDPRKNKWSQGCAMLCKRSAVGVAALDDCIYVCGGYDGVTSLNTVEVYYPKSNTWKTVAQMMKYRSAGGVTQLNGYVYALGGHDGLSIFDSVERYDQAEDVWVKMSPMLNRRCRLGVATLNGKIYVCGGYCGNSFLRSVECYDPQTDTWKLVTPMNCKRSRVALAANMGKLWAIGGYDGESNLSTVEVYDPETDKWTFMPPMCAHSGGVGAGVIRIE
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (Q8LEV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- At1g43860
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL24y
Sequence:
MVSLAKFHYCDQTLHLRLDTHRKPQPKPVSYRILHKPPPSRVIRASSFSSNPKPSFLKTTCVTLTTAAALLSASLHLSTKPVTAATLVSPPPPPSTAADLTSDQISSRPKEEEEEAALEKHLTKNPNDVEALQSLMKIKFQTKNIDHALEILNRLIEIQPEEQEWRILKAQVQTYGGDFDSATKGFEEVLSKDPFRVEAYHGLVMAYSESESKLSEIESRINEAIEKCKKENKKDFRDFMLLIAQIRVIKGNPIEALRVYQELVKDEPKDFRPYLCQGLIYTLMKKKDEAEKQFAEFRRLVPENHPYKEYLDANVLNTNKLFAKNQ
Protein: 9,11-endoperoxide prostaglandin H2 reductase (EC 1.1.1.-) (Prostaglandin F2-alpha synthase) (Q9GV41)
Organism: Trypanosoma brucei brucei
Function: Catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. Has also aldo/ketoreductase activity towards the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11067881}.
Interaction partners:
Sequence:
MALTQSLKLSNGVMMPVLGFGMWKLQDGNEAETATMWAIKSGYRHIDTAAIYKNEESAGRAIASCGVPREELFVTTKLWNSDQGYESTLSAFEKSIKKLGLEYVDLYLIHWPGKDKFIDTWKAFEKLYADKKVRAIGVSNFHEHHIEELLKHCKVAPMVNQIELHPLLNQKALCEYCKSKNIAVTAWSPLGQGHLVEDARLKAIGGKYGKTAAQVMLRWEIQAGVITIPKSGNEARIKENGNIFDFELTAEDIQVIDGMNAGHRYGPDPEVFMNDF
Protein: Probable lipase C14C8.15 (EC 3.1.1.-) (O60095)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable lipase.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized membrane protein C30D10.09c
- Uncharacterized membrane protein C18H10.18c
- Uncharacterized protein C594.02c
- Putative mannan endo-1,6-alpha-mannosidase C1198.07c
- TBC domain-containing protein C23D3.03c
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- GTPase-activating protein gyp3
- Multifunctional tryptophan biosynthesis protein
Sequence:
MTLNGNIMKYCLEKGEILISFLLIALESMFRICTVILPSPLRNWFYEQSKKVYSYFLPELLVDDNANKLTDARDTIDLCALHGYDLEEHFVRTTDGYLLGLHRVYKKKKGKIEELNYLPPVLFIHGLMMNSESWVCNLKKEDAIPFALVEQGYDVWLGNLRGNKYSIKNIKFSSQNPKFWDFSLDSIAIFDIPSIVKYILSVNSFDSISLVGFSQGAILAFAALSIDTELRNSVRAFIALAPAIAPKKYSGRTVKSIIHANSQLLYLMFGRNSMLGSAVFWQAVLYPPVFAKIVDLFLRFFLSWTGKNISETQKIVAYSHLYSFTSVKCFVHWAQITRRKVLQMYDDSPGFKPSYYTNLNRIARYPIENIRLPITLVYGSNDNMVDIETLKTQLPPLSQCIQIPNYEHLDIIMGDTKKDIVIQQVVEQLNHVIAGDYFESIKEEFGLDTELVDGVMNHTI
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (P83129)
Organism: Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MALKAVCVLKGAGETSGTVHFEQEDN
Protein: Subtilisin-like protease 1 (EC 3.4.21.62) (PfSUB-1) (O61142)
Organism: Plasmodium falciparum
Function: Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.
Subcellular location: Secreted {ECO:0000269|PubMed:9722575}. Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:Q8I0V0}. Note=At the schizont stage, in merozoites, localizes to dense secretory granules called exonemes (PubMed:9722575). Just prior to egress secreted into the parasitophorous vacuole (By similarity). {ECO:0000250|UniProtKB:Q8I0V0, ECO:0000269|PubMed:9722575}.
Interaction partners:
Sequence:
MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH
Protein: Coordinator of PRMT5 and differentiation stimulator (H9KV77)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGDAGDREPGPAARSLGEGQAGFATADHSSQERETEKAMDRLARGTQSIPNDSPARGEGTHSEEEGFAMDEEDSDGELNTWELSEGTNCPPKEQPGDLFNEDWDSELKADQGNPYDADDIQESISQELKPWVCCAPQGDMIYDPSWHHPPPLIPYYSKMVFETGQFDDAED
Protein: DNA polymerase iota (J3KTN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISNPELKDKPLGVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIAAEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIPGIGYKTAKCLEALGINSVRDLQTFS
Protein: 2-hydroxyacylsphingosine 1-beta-galactosyltransferase (EC 2.4.1.47) (Ceramide UDP-galactosyltransferase) (CGalT) (Cerebroside synthase) (UDP-galactose-ceramide galactosyltransferase) (Q09426)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. Galactosylates both hydroxy- and non-hydroxy fatty acid-containing ceramides and diglycerides.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:8713090}.
Interaction partners:
- Galactocerebrosidase
- Ceramide glucosyltransferase
- Galactose-3-O-sulfotransferase 1
- Ceramide kinase
- Arylsulfatase A
- Ceramide synthase 2
- Non-lysosomal glucosylceramidase
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Acid ceramidase
Sequence:
MKSYTPYFMLLWSAVGIARAAKIIIVPPIMFESHLYIFKTLASALHERGHHTVFLLSEGRDIDPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAVELVDILDHYTKNCDMMVGNQALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEFNSLLTDRMNFLERMKNTGVYLISRMGVSFLVLPKYERIMQKYNLLPAKSMYDLVHGSSLWMLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVDGAQEHGFVLVSFGAGVKYLSEDIANKLAGALGRLPQKVIWRFSGTKPKNLGNNTKLIEWLPQNDLLGHSNIRAFLSHGGLNSIFETMYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWNTVTEGELYDALVKVINNPSYRQRAQKLSEIHKDQPGHPVNRTTYWIDYILRHDGAHHLRSAVHQISFCQYFLLDIAFVLLLGAVALYFIVSYVTKFIYRKVKSLCSRSTHSTVNGHYQNGILNGRYKGNGHIKHEKKVK
Protein: Ras-specific guanine nucleotide-releasing factor 2 (Ras-GRF2) (Ras guanine nucleotide exchange factor 2) (O14827)
Organism: Homo sapiens (Human)
Function: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation.
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Translocates to membranes when activated. Found both at cell periphery and along the axon of neurons (By similarity). {ECO:0000250}.
Interaction partners:
- GTPase KRas
- Ras-specific guanine nucleotide-releasing factor 1
- Ras-related protein R-Ras
- Ras-related protein R-Ras2
- GTPase NRas
- GTPase HRas
- Calmodulin-1
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 3
Sequence:
MQKSVRYNEGHALYLAFLARKEGTKRGFLSKKTAEASRWHEKWFALYQNVLFYFEGEQSCRPAGMYLLEGCSCERTPAPPRAGAGQGGVRDALDKQYYFTVLFGHEGQKPLELRCEEEQDGKEWMEAIHQASYADILIEREVLMQKYIHLVQIVETEKIAANQLRHQLEDQDTEIERLKSEIIALNKTKERMRPYQSNQEDEDPDIKKIKKVQSFMRGWLCRRKWKTIVQDYICSPHAESMRKRNQIVFTMVEAESEYVHQLYILVNGFLRPLRMAASSKKPPISHDDVSSIFLNSETIMFLHEIFHQGLKARIANWPTLILADLFDILLPMLNIYQEFVRNHQYSLQVLANCKQNRDFDKLLKQYEANPACEGRMLETFLTYPMFQIPRYIITLHELLAHTPHEHVERKSLEFAKSKLEELSRVMHDEVSDTENIRKNLAIERMIVEGCDILLDTSQTFIRQGSLIQVPSVERGKLSKVRLGSLSLKKEGERQCFLFTKHFLICTRSSGGKLHLLKTGGVLSLIDCTLIEEPDASDDDSKGSGQVFGHLDFKIVVEPPDAAAFTVVLLAPSRQEKAAWMSDISQCVDNIRCNGLMTIVFEENSKVTVPHMIKSDARLHKDDTDICFSKTLNSCKVPQIRYASVERLLERLTDLRFLSIDFLNTFLHTYRIFTTAAVVLGKLSDIYKRPFTSIPVRSLELFFATSQNNRGEHLVDGKSPRLCRKFSSPPPLAVSRTSSPVRARKLSLTSPLNSKIGALDLTTSSSPTTTTQSPAASPPPHTGQIPLDLSRGLSSPEQSPGTVEENVDNPRVDLCNKLKRSIQKAVLESAPADRAGVESSPAADTTELSPCRSPSTPRHLRYRQPGGQTADNAHCSVSPASAFAIATAAAGHGSPPGFNNTERTCDKEFIIRRTATNRVLNVLRHWVSKHAQDFELNNELKMNVLNLLEEVLRDPDLLPQERKAAANILRALSQDDQDDIHLKLEDIIQMTDCMKAECFESLSAMELAEQITLLDHVIFRSIPYEEFLGQGWMKLDKNERTPYIMKTSQHFNDMSNLVASQIMNYADVSSRANAIEKWVAVADICRCLHNYNGVLEITSALNRSAIYRLKKTWAKVSKQTKALMDKLQKTVSSEGRFKNLRETLKNCNPPAVPYLGMYLTDLAFIEEGTPNFTEEGLVNFSKMRMISHIIREIRQFQQTSYRIDHQPKVAQYLLDKDLIIDEDTLYELSLKIEPRLPA
Protein: Brevinin-1AVb (P86160)
Organism: Rana arvalis (Moor frog)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000269|PubMed:18280749, ECO:0000269|PubMed:19308951, ECO:0000269|PubMed:35820801}.
Interaction partners:
Sequence:
FVPLLVSKLVCVVTKKC
Protein: Sensor protein kinase PmrB (EC 2.7.13.3) (Q9HV31)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PmrA/PmrB that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+). Autoregulates also its own pmrAB operon under Mg(2+)-limiting conditions. May function as a membrane-associated protein kinase that phosphorylates PmrA in response to environmental signals leading to activation of specific gene promoters (Probable).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Response regulator protein PmrA
- Two-component response regulator PhoP
- DUF155 domain-containing protein
- Two-component response regulator KdpE
- Two-component response regulator, ParR
- Polyamine aminopropyltransferase 2
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- UDP-glucose 6-dehydrogenase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Sequence:
MSRAAVPSVRRRLLVNLLVGFVLCWLSVAALTYHLSLKQVNRLFDDDMVDFGEAALRLLDLATEDQAGEDGSITEIIERSREAIQGLPLLRRESALGYALWRDGQPLLSSLNLPPEITAQGPGFSTVEAQGTHWRVLQLNIDGFQIWISENLIYRQHTMNLLLFYSLFPLLLALPLLGGLVWFGVARGLAPLREVQAEVQQRSARHLQPIAVEAVPLEIRGLIDELNLLLERLRTALEAERRLTSDAAHEIRTPLASLRTHAQVALRSEDPKAHARGLLQVSRSVERISTLMEQILLLARLDGDALLEQFHPVNLATLAEDVLSELARQAIDKDIELSLHQETVYVMGIDLWLKAMVGNLVGNALRYTPAGGQVEIRVENRAQHAVLRVRDNGPGVALEEQQAIFTRFYRSPATSSGEGSGLGLPIVKRIVELHFGSIGLGKGLEGKGLEVQVFLPKTQPDATRPPARGPDSGRSHI
Protein: Probable conserved proline, glycine, valine-rich secreted protein (O06823)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Aromatic amino acid aminotransferase
- Conserved protein
- Uncharacterized transporter Rv0917
- Probable oxidoreductase
- Uncharacterized HIT-like protein Rv0759c
- Probable para-aminobenzoate synthase component I PABD
- Salicylate synthase
- Anthranilate synthase component 1
- Uncharacterized protein Rv1403c
- Probable sugar-transport integral membrane protein SugI
Sequence:
MTLMAIVNRFNIKVIAGAGLFAAAIALSPDAAADPLMTGGYACIQGMAGDAPVAAGDPVAAGGPAAAGACSAALTDMAGVPFVAPGPVPAAAPVPIGAPVPIPGAPVPIPGAPVPIPGGPVPIPGAPVPVPAVPAPVIPVGTPLIALGPVLAGAPGDGVVSAPIIGMSGVKDALTDPAPAGGPVPGQPVLPGPSASAPAGAR