wanglab/gogpt-training-data huggingface dataset:
Protein: A-kinase anchor protein 12 (AKAP-12) (Q5QD51)
Organism: Rattus norvegicus (Rat)
Function: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q02952}; Lipid-anchor {ECO:0000250|UniProtKB:Q02952}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Beta-2 adrenergic receptor
- Calmodulin-like protein 4
Sequence:
MGAGSSTEQRSPEQPAGSDTPSELVLSGHGPAAEASGAAGDPADADPATKLPQKNGQLSTVNGVAEQGDVHVQEENQEGQEEEVVDEDVGQRESEDVREKDRVEEMAANSTAVEDITKDGQEETSEIIEQIPASESNVEEMVQPAESQANDVGFKKVFKFVGFKFTVKKDKNEKSDTVQLLTVKKDEGEGAEASVGAGDHQEPSVETAVGESASKESELKQSTEKQEGTLKQEQSSTEIPLQAESDQAAEEEAKDEGEEKQEKEPTKSPESPSSPVSSETTSSFKKFFTHGWAGWRKKTSFKKSKEDDLETAEKRKEQEAEKVDEEEKEKTEPASEEQEPAEDTDQARLSADYEKVELPLEDQVGDLEASSEEKCAPLATEVFDEKMEAHQEVVAEVHVSTVEKTEEEQGGGGEAEGGVVVEGTGESLPPEKLAEPQEVPQEAEPAEELMKSREMCVSGGDHTQLTDLSPEEKTLPKHPEGIVSEVEMLSSQERIKVQGSPLKKLFSSSGLKKLSGKKQKGKRGGGGDEEPGEYQHIHTESPESADEQKGESSASSPEEPEETTCLEKGPLEAPQDGEAEEGTTSDGEKKREGITPWASFKKMVTPKKRVRRPSESDKEEELEKVKSATLSSTDSTVSEMQDEVKTVGEEQKPEEPKRRVDTSVSWEALICVGSSKKRARKASSSDDEGGPRTLGGDSHRAEEASKDKEAGTDAVPASTQEQDQAQGSSSPEPAGSPSEGEGVSTWESFKRLVTPRKKSKSKLEEKAEDSSVEQLSTEIEPSREESWVSIKKFIPGRRKKRADGKQEQATVEDSGPVEINEDDPDVPAVVPLSEYDAVEREKMEAQGNAELPQLLGAVYVSEELSKTLVHTVSVAVIDGTRAVTSVEERSPSWISASVTEPLEHTAGEAMPPVEEVTEKDIIAEETPVLTQTLPEGKDAHDDMVTSEVDFTSEAVTATETSEALRTEEVTEASGAEETTDMVSAVSQLTDSPDTTEEATPVQEVEGGVLDTEEEERQTQAILQAVADKVKEESQVPATQTVQRTGSKALEKVEEVEEDSEVLASEKEKDVMPKGPVQEAGAEHLAQGSETGQATPESLEVPEVTADVDHVATCQVIKLQQLMEQAVAPESSETLTDSETNGSTPLADSDTADGTQQDETIDSQDSKATAAVRQSQVTEEEAATAQKEEPSTLPNNVPAQEEHGEEPGRDVLEPTQQELAAAAVPVLAKTEVGQEGEVDWLDGEKVKEEQEVFVHSGPNSQKAADVTYDSEVMGVAGCQEKESTEVQSLSLEEGEMETDVEKEKRETKPEQVSEEGEQETAAPEHEGTYGKPVLTLDMPSSERGKALGSLGGSPSLPDQDKAGCIEVQVQSLDTTVTQTAEAVEKVIETVVISETGESPECVGAHLLPAEKSSATGGHWTLQHAEDTVPLGPESQAESIPIIVTPAPESTLHPDLQGEISASQRERSEEEDKPDAGPDADGKESTAIEKVLKAEPEILELESKSNKIVLNVIQTAVDQFARTETAPETHAYDSQTQVPAMQADSQGAQQMLDKNESCQDETPSAAAQRGLASPDRSGGMGSASEMLAALAVESAGVKVSIEKLPPQPKDQKEHAADGPQLQSLAQAEASASGNLTKESPDTNGPKLTEEGDAPKVEVQEEEMSTKSVKENKAQAEEDLQEPKGDLAES
Protein: Phosphotransferase (EC 2.7.1.-) (C9JQD1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAEMMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Protein: Nuclear hormone receptor family member nhr-49 (O45666)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor. Regulates expression of genes involved in fat metabolism and in maintaining homeostasis of fatty acid saturation, such as lipid desaturase fat-7, and acyl-CoA synthetase acs-2. May form part of a negative feedback loop with fat-7 to limit mitochondrial beta-oxidation, in which it stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation. As part of a lysosome-to-nucleus retrograde lipid signaling pathway, acting in concert with nuclear hormone receptor nhr-80, activates the transcription of genes promoting longevity and mitochondrial beta-oxidation. In concert with nuclear hormone receptor nhr-66, involved in regulating target genes with roles in sphingolipid breakdown and lipid remodeling. Also involved in regulating fatty acid desaturase genes, acting in concert with nuclear hormone receptors nhr-13 and nhr-80. Plays a role in modulating mitochondrial morphology and function. Plays a role in transgenerational lipid accumulation in response to a high-fat diet.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 15
- Sterol regulatory element binding protein sbp-1
- Delta
- Delta
- Delta
- Nuclear hormone receptor family member nhr-80
- Medium-chain acyl-CoA ligase ACSF2
- Lipase lipl-4
- Fatty acid-binding protein homolog 8
- Forkhead box protein O
Sequence:
MDYFLDASKHIQLNQIDEESSDDFMDLVDPLAEPCAVCGDKSTGTHYGVISCNGCKGFFRRTVLRDQKFTCRFNKRCVIDKNFRCACRYCRFQKCVQVGMKREAIQFERDPVGSPTSGASLNGTPFKKDRSPGYENGNSNGVGSNGMGQENMRTVPQSSSVIDALMEMEARVNQEMCNRYRRSQIFANGSGGSNGNDTDIQQGSDSGASAFAPPNRPCTTEVDLNEISRTTLLLMVEWAKTINPFMDLSMEDKIILLKNYAPQHLILMPAFRSPDTTRVCLFNNTYMTRDNNTDLNGFAAFKTSNITPRVLDEIVWPMRQLQMREQEFVCLKALAFLHPEAKGLSNSSQIMIRDARNRVLKALYAFILDQMPDDAPTRYGNILLLAPALKALTQLLIENMTLTKFFGLAEVDSLLSEFILDDINDHSTAPVSLQQHLSSPTTLPTNGVSPLNPAGSVGSVSSVSGITPTGMLSATLAAPLAIHPLQSQDSILNSEQNNHML
Protein: T. brucei spp.-specific protein (Q387F3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDWTDRVLLEDDNDMGKSIVSHHVLMNCSQRSNIKDSNVQTLSTEMLHWDDYREAHGINDGTPKMADTFQNACEPLFQGHVCRSGGSTKRLLSVATKPVLGEGGDRTFCSEMQHWDDYRVKNNIQDGSPAMQCLFRQFDGHDMFILDSGWKLLTLKQMCITSTRQAYGASVNQRVSEMVRWEESQNQQGINCFPASGSAEAVSAITPYNSG
Protein: Amine oxidase [flavin-containing] B (EC 1.4.3.21) (EC 1.4.3.4) (Monoamine oxidase type B) (MAO-B) (P58028)
Organism: Cavia porcellus (Guinea pig)
Function: Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially degrades benzylamine and phenylethylamine.
Subcellular location: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Interaction partners:
- Catechol O-methyltransferase
- Cytokine-like nuclear factor N-PAC
- catechol O-methyltransferase
- Aldehyde dehydrogenase
- Amine oxidase
- Aldehyde dehydrogenase
- Histamine N-methyltransferase
- Amine oxidase
- aldehyde dehydrogenase
- Amine oxidase
Sequence:
MNSKCDVVVVGGGISGLAAAKLLHDSGLNVVVLEARDCVGGRTYTLRNQNVKYVDLGGAYVGPTQNRILRLAKELGLETYRVNDVERQIHHVKGKSYPFRGPFPPAWNPISYLDHNNLWRTMDDMGKEIPSDAPWKAPLAEEWDHMTMKELLNKICWTNCPRQFGTLFVNLCFTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQISERIMNLLGDRVKLQRPVVYIDQTGESVLVETLNHEIYEAKYVISAIPPALGMKIHFKPPLPMMKNQLVSRVPLGSVIKCIVYYKDPFWRKKDFCGTMVIEGEEAPVLYTMDDTKPDGSYAAIIGFIAAHKARKLARLTKEERLKKLCELYAKVLGSKEALKPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRFLRQPVGRIFFAGTETATHWSGYMEGAVEAGERAAREVLNAIGKIPEDEIWQPEPESVDVPAQPITTTFLERHLPSVPGLLRLIRLTTVVSAVALGFLAQKRGLLLRI
Protein: Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase (EC 2.7.1.49) (EC 2.7.4.7) (Hydroxymethylpyrimidine kinase) (HMP kinase) (Hydroxymethylpyrimidine phosphate kinase) (HMP-P kinase) (HMP-phosphate kinase) (HMPP kinase) (P76422)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
Interaction partners:
- Phosphomethylpyrimidine synthase
- Thiamine-phosphate synthase
- Hydroxyethylthiazole kinase
- Thiazole synthase
- Sulfur carrier protein ThiS adenylyltransferase
- 2-iminoacetate synthase
- Thiamine-monophosphate kinase
- Sulfur carrier protein ThiS
- tRNA sulfurtransferase
- HTH-type transcriptional regulator GgaR
Sequence:
MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAERLQRYQIQNVVLDTVMLAKSGDPLLSPSAVATLRSRLLPQVSLITPNLPEAAALLDAPHARTEQEMLEQGRSLLAMGCGAVLMKGGHLDDEQSPDWLFTREGEQRFTAPRIMTKNTHGTGCTLSAALAALRPRHTNWADTVQEAKSWLSSALAQADTLEVGHGIGPVHHFHAWW
Protein: Neurogranin (Protein kinase C substrate, RC3) b isoform X2 (Sperm autoantigenic protein 17) (F1QK17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Coiled-coil domain-containing 135.
- Ras association domain family member 4.
- Adenylate kinase 8
- Transmembrane protein 119b.
- Coiled-coil domain-containing 170.
- Ras association domain family member 4a
- Ankyrin repeat and death domain-containing 1A.
- Transmembrane protein 151A.
- Transmembrane protein 151A.
- Si:ch211-250g4.3.
Sequence:
MAVPFSNTHLRIPRGFGNLLEGLTREVLREQPEDIATFAAVYFTELLKAREESGLDPAEWGAKLEDRFYNNHSFKGTSLQGNIISPKINTRINAESSSETLGNNETQLSALKDLDTDNSVGSEVNLDKKFDEESGEKERGHAEDILPAETADGDKCAEELKDTNEIPGETSEVAKEEVDVDICRSELEPTPLPSFGGHANVDVCAEEINLQSESSKSKEELVSPKPLFLNKDQSESQDEIHSHTEQDASKQANEMSDHGDDDDAEDPEEEVSEIADNLLEDIDPEEKSTEQVYAEESTESTIEKYITESVAGQESEDAINEDQEETNYEYTSTNDFVEDAGDSTSDINSRSLMEMKDTHVDYSDEIHDSKSEVVDVLDEVHHQCDTRTGEEEAENSSDEENTSKILDALNEEDFLETPKPVSQMNDSEAEASNEILNADAFEKDLNTENVNEGSDLDSDGFEAEEMDLDISNVLQPNEEKTEDEGNHDPEPEEDAFSEAEQANPEPLENETVVVNEELFESQEQTENTENDVDQEDQLEEQRDKIQEMTLESENLENTDISEPKEECSQPQEEEDIMDIPLDDPEANKAAAKIQAGFRGHMTRKKMKPGEKPGEEVSSSGEALNGSQGDSGGTDGVETDGTSGPEQ
Protein: Homeobox protein cut-like 2 (Homeobox protein cux-2) (O14529)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in the control of neuronal proliferation and differentiation in the brain. Regulates dendrite development and branching, dendritic spine formation, and synaptogenesis in cortical layers II-III. Binds to DNA in a sequence-specific manner.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374}.
Interaction partners:
- Sesquipedalian-1
- Fez family zinc finger protein 2
Sequence:
MAANVGSMFQYWKRFDLRRLQKELNSVASELSARQEESEHSHKHLIELRREFKKNVPEEIREMVAPVLKSFQAEVVALSKRSQEAEAAFLSVYKQLIEAPDPVPVFEAARSLDDRLQPPSFDPSGQPRRDLHTSWKRNPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLACCSPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKFLLEKPSLLASPEEDPSEDDSIKDSLGTEQSYPSPQQLPPPPGPEDPLSPSPGQPLLGPSLGPDGTRTFSLSPFPSLASGERLMMPPAAFKGEAGGLLVFPPAFYGAKPPTAPATPAPGPEPLGGPEPADGGGGGAAGPGAEEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEPFIKMKQFLSDEQNVLALRTIQVRQRGSITPRIRTPETGSDDAIKSILEQAKKEIESQKGGEPKTSVAPLSIANGTTPASTSEDAIKSILEQARREMQAQQQALLEMEVAPRGRSVPPSPPERPSLATASQNGAPALVKQEEGSGGPAQAPLPVLSPAAFVQSIIRKVKSEIGDAGYFDHHWASDRGLLSRPYASVSPSLSSSSSSGYSGQPNGRAWPRGDEAPVPPEDEAAAGAEDEPPRTGELKAEGATAEAGARLPYYPAYVPRTLKPTVPPLTPEQYELYMYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLSDQLGQAVGQQPGASQASPTEPRSSPSPPPSPTEPEKSSQEPLSLSLESSKENQQPEGRSSSSLSGKMYSGSQAPGGIQEIVAMSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREPFVRMQLWLNDPHNVEKLRDMKKLEKKAYLKRRYGLISTGSDSESPATRSECPSPCLQPQDLSLLQIKKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEPDLDPSGGPGILPPGHSHPDPTPQSPDSETEDQKPTVKELELQEGPEENSTPLTTQDKAQVRIKQEQMEEDAEEEAGSQPQDSGELDKGQGPPKEEHPDPPGNDGLPKVAPGPLLPGGSTPDCPSLHPQQESEAGERLHPDPLSFKSASESSRCSLEVSLNSPSAASSPGLMMSVSPVPSSSAPISPSPPGAPPAKVPSASPTADMAGALHPSAKVNPNLQRRHEKMANLNNIIYRVERAANREEALEWEF
Protein: Tyrosyl-DNA phosphodiesterase 1 (G3V5F9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQEGDYGRWTISSSDESEEEKPKPDKPSTSSLLCARQGAANEPRYTCSEAQKAAHKRKISPVKFSNTDSVLPPKRQKSGSQEDLGWCLSSSDDELQPEMPQKQAEKVVIKKEKDISAPNDGTAQRTENHGAPACHRLKEEEDEYET
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 3) (Q15120)
Organism: Homo sapiens (Human)
Function: Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Small muscular protein
- [Pyruvate dehydrogenase
- Integrin beta-1-binding protein 2
- [Pyruvate dehydrogenase
- [Pyruvate dehydrogenase
Sequence:
MRLFRWLLKQPVPKQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRKELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDPQVLDNFLQVLIKVRNRHNDVVPTMAQGVIEYKEKFGFDPFISTNIQYFLDRFYTNRISFRMLINQHTLLFGGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQYYLVAPELEVEEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDRKEGYPAVKTLVTLGKEDLSIKISDLGGGVPLRKIDRLFNYMYSTAPRPSLEPTRAAPLAGFGYGLPISRLYARYFQGDLKLYSMEGVGTDAVIYLKALSSESFERLPVFNKSAWRHYKTTPEADDWSNPSSEPRDASKYKAKQ
Protein: Mal d 1-associated protein (Q9SJ60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Adenosine kinase 1
Sequence:
MGWIWIDDSSASKAGADLTDKPLGDSAAAAENCSTTTVVRSQCKTEEVEPGKFVRKCDKTEEILRHCFGKPSEVVQSNTEHTEEDVTDQMVGRSALPNQFEDKNPLNFPGLRRDVDAIERHFLSGMKSFFDAAEEMTSSLFDIMGDHHPSTRRGGIPIENHPKVEEHRNDETAPTRPHSSGEIDLSGLAKDV
Protein: Transient receptor potential cation channel subfamily A member 1 (dTRPA1) (Ankyrin-like with transmembrane domains protein 1) (dANKTM1) (Q7Z020)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for thermotaxis by sensing environmental temperature. Receptor-activated non-selective cation channel involved in detection of sensations such as temperature. Involved in heat nociception by being activated by warm temperature of about 24-29 degrees Celsius.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12815418}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transient receptor potential cation channel trpm
- SD02261p
- Transient-receptor-potential-like protein
- MIP30126p
- Putative gustatory receptor 28b
- Dopamine receptor 1
- Amiloride-sensitive Na+ channel
- Transient receptor potential-gamma protein
- Gustatory receptor for bitter taste 66a
- Gustatory receptor 5a for trehalose
Sequence:
MTSGDKETPKREDFASALRFLMGGCAREPEMTAMAPLNLPKKWARILRMSSTPKIPIVDYLEAAESGNLDDFKRLFMADNSRIALKDAKGRTAAHQAAARNRVNILRYIRDQNGDFNAKDNAGNTPLHIAVESDAYDALDYLLSIPVDTGVLNEKKQAPVHLATELNKVKSLRVMGQYRNVIDIQQGGEHGRTALHLAAIYDHEECARILITEFDACPRKPCNNGYYPIHEAAKNASSKTMEVFFQWGEQRGCTREEMISFYDSEGNVPLHSAVHGGDIKAVELCLKSGAKISTQQHDLSTPVHLACAQGAIDIVKLMFEMQPMEKRLCLSCTDVQKMTPLHCASMFDHPDIVSYLVAEGADINALDKEHRSPLLLAASRSGWKTVHLLIRLGACISVKDAAARNVLHFVIMNGGRLTDFAEQVANCQTQAQLKLLLNEKDSMGCSPLHYASRDGHIRSLENLIRLGACINLKNNNNESPLHFAARYGRYNTVRQLLDSEKGSFIINESDGAGMTPLHISSQQGHTRVVQLLLNRGALLHRDHTGRNPLQLAAMSGYTETIELLHSVHSHLLDQVDKDGNTALHLATMENKPHAISVLMSMGCKLVYNVLDMSAIDYAIYYKYPEAALAMVTHEERANEVMALRSDKHPCVTLALIASMPKVFEAVQDKCITKANCKKDSKSFYIKYSFAFLQCPFMFAKIDEKTGESITTASPIPLPALNTMVTHGRVELLAHPLSQKYLQMKWNSYGKYFHLANLLIYSIFLVFVTIYSSLMMNNIELKAGDNKTMSQYCNMGWEQLTMNLSQNPSVASQIRLDSCEERINRTTAILFCAVVIVVYILLNSMRELIQIYQQKLHYILETVNLISWVLYISALVMVTPAFQPDGGINTIHYSAASIAVFLSWFRLLLFLQRFDQVGIYVVMFLEILQTLIKVLMVFSILIIAFGLAFYILLSKIIDPQPNHLSFSNIPMSLLRTFSMMLGELDFVGTYVNTYYRDQLKVPMTSFLILSVFMILMPILLMNLLIGLAVGDIESVRRNAQLKRLAMQVVLHTELERKLPHVWLQRVDKMELIEYPNETKCKLGFCDFILRKWFSNPFTEDSSMDVISFDNNDDYINAELERQRRKLRDISRMLEQQHHLVRLIVQKMEIKTEADDVDEGISPNELRSVVGLRSAGGNRWNSPRVRNKLRAALSFNKSM
Protein: Calcineurin B-like protein 3 (SOS3-like calcium-binding protein 6) (Q8LEM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binds calcium ions. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Negatively regulates the enzyme activity of MTN1 in the presence of calcium.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}; Lipid-anchor {ECO:0000269|PubMed:19832944, ECO:0000269|PubMed:23109687, ECO:0000269|PubMed:23184060, ECO:0000269|PubMed:23482856}. Note=Tonoplast localization abolished by 2-bromopalmitate (2-BP) treatment.
Interaction partners:
- CBL-interacting serine/threonine-protein kinase 9
- CBL-interacting serine/threonine-protein kinase 3
- CBL-interacting serine/threonine-protein kinase 21
- CBL-interacting serine/threonine-protein kinase 6
- CBL-interacting serine/threonine-protein kinase 23
- CBL-interacting serine/threonine-protein kinase 24
- CBL-interacting serine/threonine-protein kinase 1
- CBL-interacting serine/threonine-protein kinase 11
- CBL-interacting serine/threonine-protein kinase 14
- 5'-methylthioadenosine nucleosidase
Sequence:
MSQCIDGFKHVCSSFFRCFDIDIYKQSGGLGDPELLARETVFSVSEIEALYELFKKISSAVIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPIEDKIDFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLSDEIIESIIDKTFEEADTKHDGRIDKEEWRTLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVEDT
Protein: Invasin CotH3 (Spore coat protein homolog 3) (I1CFE1)
Organism: Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Function: Promotes invasion of host epithelial cells by adhering to receptors on the host cell surface to facilitate endocytosis of the pathogen into host cells. Binds HSPA5/BiP protein on the cell surface of host nasal epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24355926}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- MHD domain-containing protein
- Clathrin adaptor alpha/beta/gamma-adaptin appendage Ig-like subdomain domain-containing protein
- Protein kinase domain-containing protein
Sequence:
MKLSIISAAFLVAITHAASIKFNVIAPNATDVKVSVNGQQVTLTASDANVPYFTGSAEVGASKTYKYVAGGTEESFDRSLDGITNSTLNDFYNRPVTYANLPQLPWPIEKDPQWTRSGSKADIFDDNYIPSVFFHGDDSQVQNVVKNVPADRISGTLTFIGSNYVYSFQNVSFGIHGAGKKHNNAKQSWNWILSGSDTMGNRNFFKLRHMEEDPTQIRERLYSDILHAMGTYANDATMVRLFINNQGFGTFNMLDDITQFSYINAKFYNGKPPATLGPLYDGASGADFLYHPGNLDGYSSWVANTANPNGEAYEALDPLCKAWNETTYTDNTAIANFEKMFDLDRFMRFMVIEYLTADWDGYWMGQTNDGAYRDPTDNNKWYFLDQDFDGTFGVNLAAPEGNAFLDVSYKDFPSRYPGAVMINNLLQNADKKATFEKYLTETVRVLFNNVTLTNRVLALHNFLLPDLEWDRSIVQQSPGINFGWTFDQVTQNLWQGVTAPNNNGGGAAFGLVEYIAAKAQAVAKEFNISIVSQPVGPPSANGTTAAAPAPAAGNSTGKGGNQSISSSASSNKTSAQSTSGASRSKTAPIVLAISALALLVF
Protein: Diacylglycerol kinase 2 (AtDGK2) (DAG kinase 2) (EC 2.7.1.107) (Diglyceride kinase 2) (DGK 2) (Q9FFN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack (Probable). May be involved in the accumulation of PA during cold stress (Probable). Involved in response to freezing stress by modulating the accumulation of PA. Exhibits high specificity for the unsaturated DAG analogs 1-stearoyl-2-arachidonoyl-sn-glycerol (1,2-SAG) and 1,2-dioleoyl-sn-glycerol (1,2-DOG). Exhibits high specificity for 1-palmitoyl, 2-oleoyl-sn-glycerol (1,2 POG), 1-stearoyl, 2-linoleoyl-sn-glycerol (1,2-SLG) and 1-oleoyl, 2-palmitoyl-sn-glycerol (1,2-OPG). Has almost no activity toward 1,2-dioctanoyl-sn-glycerol (1,2-DOCG), 1,2-dipalmitoyl-sn-glycerol (1,2-DPG), 1,2-dimyristoyl-sn-glycerol (1,2-DMG) and 1-oleoyl-2-acetyl-sn-glycerol (1,2-OAG). Functions together with DGK4 in male gametophyte development and biosynthesis of phosphatidylglycerol and phosphatidylinositol in the endoplasmic reticulum (ER). Involved in PA production for pollen grain growth, as well as leaf and root growth.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:32471859}.
Interaction partners:
- Sulfoquinovosyl transferase SQD2
- Choline/ethanolaminephosphotransferase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Putative phospholipid:diacylglycerol acyltransferase 2
- Choline/ethanolaminephosphotransferase 1
- Triacylglycerol lipase SDP1
- Triacylglycerol lipase SDP1L
- Phosphoinositide phospholipase C 5
- Phosphoinositide phospholipase C 1
- Phosphoinositide phospholipase C 4
Sequence:
MMEVGFSLIQWLISSGADSPFIFGWLVTGSVGLLAVIYTFLKWQKKTSLNWVKAAAREKKKVWKRLRVPLSHHQWTDDYGYGQQPSTCCVCLYSLVPGQNVSNKASLSIPVHRCAVCGVAAHFYCSSSAAKDCKCVAQAGSDHVRHHWSERWVNMDDNADMTAFCFYCDEPCGIPFIEASPMWHCLWCQRLIHVKCHMIMSKESGDACDLGSLRRVILSPVHVKLNEANGVDGVLTTIKNELASIRGHVRRKRHRGKNGNGQSLNGKLLEDSVSDPVKTVVNGLVVKKLRRDRSIDCLKQVSDMPNAKGLQNGIGGHKRNKSAALNFMKKFSLVDLPPDARPLLVFINAKSGGQLGPFLHRRLNMLLNPVQVFELGSCQGPDAGLDLCSKVKYFRVLVCGGDGTVAWVLDAIEKRNFESPPPVAILPLGTGNDLSRVLQWGRGISVVDGQGSLRTFLQDIDHAAVTMLDRWSVKIVEESTEKFPAREGHKFMMNYLGIGCDAKVAYEFHMMRQEKPEKFCSQFVNKLRYAKEGARDIMDRACADLPWQVWLEVDGKDIEIPKDSEGLIVLNIGSYMGGVDLWQNDYEHDDNFSIQCMHDKTLEVVCVRGAWHLGKLQVGLSQARRLAQGKVIRIHVSSPFPVQIDGEPFIQQPGCLEITHHGQVFMLRRASDEPRGHAAAIMNEVLLDAECKGVINASQKKVLLQQMALHLS
Protein: PDZ domain-containing protein (D3YT29)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MMSSSYPTGSDLISSVIYFAPSTSSSTVFNTPASRYSTATQTTFDGGSNRHKGFVSFRSQDEDQNEDDCEEGALLLKAVQHTSSAKNHINRKTQYERPYGFGGSSATIDQPVKYGTLPSSTNHNHNNIYSHYNSGTLKSSSSPRDSGFDSSPTRYRKFGDPPETATSSADYDHHSKMFSRSSNPLFTTDPARLGGELISTKIVKGAKGLGFTLIGNDSSSRGDEFIQVKSVLSGGPAAANGVLRSGDILVRVNGRLLLGATQKEACDVFVAIPVNEAVDIQVCRGYELFIDPANRIVTENVYAAAKSRDLHEIDIFKGSEGFGFTIADNLNGQRIKKILFPSQCPNLMEGDTIVELDGRNVRPIPHTQLVDMLRERPIGYRGKLVVKRGSPKTRSRTPSAAFRYGEPQTNMMDSAAPLPVRSKTPAERQTSRTEEDQNVRNTLQRQPAVTSEWEGMSSAIPASRMRPSSTTLGFATPNYIPLSQYNQKPSDLITVSLIRKPVGFGFRLLGGVESKTPLSVGQIVIGGAAEEDGRLQEGDEIVEIDGHNVEGASHSEAVVLLEAAAQNKHVKLIVRRPSRTDPARRGSLNSAGPSGSYDVLLHRNENDGFGFVLMSSQHKNGSTVGQIQPGSPAARCGRLSVGDRVIAVNGIDILSLSHPDTISLIKDSGLSVRLTIAPPNTAGPVLPMVSATLGRNFTMNGHYESNYGLPPPPPSVYEKHPPPSYLAFDGLSINDRMSMNGNLIDVTLERGTKGFGFSIRGGQEFGSMPLFVLRIADDGPAKADGRLQVGDQLTTINGQSTKGMSHDDAIRIIKQHTMVNLTVLRNRLP
Protein: Squamosa promoter binding protein-like 7 (F4JZI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSLSQSPPPPEMDIQPPALVNDDPSTYSSALWDWGDLLDFAADERLLVDQIHFPPVLSPPLPPLIPTQTPAESELDPSPEESGSGSDRVRKRDPRLICSNFIEGMLPCSCPELDQKLEDAELPKKKRVRGGSGVARCQVPDCEADISELKGYHKRHRVCLRCATASFVVLDGENKRYCQQCGKFHLLPDFDEGKRSCRRKLERHNNRRKRKPVDKGGVAAEQQQVLSQNDNSVIDVEDGKDITCSSDQRAEEEPSLIFEDRHITTQGSVPFTRSINADNFVSVTGSGEAQPDEGMNDTKFERSPSNGDNKSAYSTVCPTGRISFKLYDWNPAEFPRRLRHQIFQWLANMPVELEGYIRPGCTILTVFIAMPEIMWAKLSKDPVAYLDEFILKPGKMLFGRGSMTVYLNNMIFRLIKGGTTLKRVDVKLESPKLQFVYPTCFEAGKPIELVVCGQNLLQPKCRFLVSFSGKYLPHNYSVVPAPDQDGKRSCNNKFYKINIVNSDPSLFGPAFVEVENESGLSNFIPLIIGDAAVCSEMKLIEQKFNATLFPEGQEVTACSSLTCCCRDFGERQSTFSGLLLDIAWSVKVPSAERTEQPVNRCQIKRYNRVLNYLIQNNSASILGNVLHNLETLVKKMEPDSLVHCTCDCDVRLLHENMDLASDIHRKHQSPIESKVNPPSSGCCCVSSQKDIPSRILNFNKDPEAGLDCKERIQADCSPDSGGKETDPLLNKEVVMNVNDIGDWPRKSCIKTHSALAFRSRQTMFLIATFAVCFAVCAVLYHPNKVTQLAVAIRMRLCSTELSHNSFSESFPSERDRI
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase) (P79023)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Interaction partners:
- Pentafunctional AROM polypeptide
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Chorismate mutase
- Chorismate synthase
- aromatic-amino-acid transaminase
- Aromatic-amino-acid:2-oxoglutarate transaminase
Sequence:
MSKTPVPTEYDDTRILGYDPLVPPALLQHEIKASAESLDVVIKGRYDSAQILKGNDDRCIVIVGPCSIHDPPQALEYGKRLKKLADELKDDLVIIMRAYLEKPRTTVGWKGLINDPDVDNSFDINRGLKISRQLYSDLTSVVGLPIGSEMLDTISPQYFSDFLSFGAIGARTTESQLHRELASGLSFPIGFKNGTDGGLAVALDAVQASSKGHHFMGVTKNGMAAITTTKGNDCCFIILRGGKKITNYDVESVKAAKEAIAKCTDPSIKLMVDCSHDNSRKDYRNQPQVLDSVAEQISNGEDSIIGVMIESNIHEGKQPMPPAGSGKEALKYGVSITDGCVSWETTVEMLTKLSQAVQTRRSLKKQKVSN