wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine-nucleotide-exchange-factor TRIO (Rho family guanine nucleotide exchange factor Trio) (Q9W0L0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDGQRARDLLTLLQERVVFLTGGRDRRGGPLLCFPATPRRDRLKPEDLRRLLSYLISIPSDAAKNLGFTVIIDMRGNGNCSTNAKTILKVLQEHFSANIHNVVIIKPDNFWQKQRASISSHKYKFETTTVSIESLNKIVESHQLTGDFEGQQLYDHQQWTDARLAIEDFFWQAGDMADRIDDLQEDLNRNDFAEDVPLARHAIDHHNEMRKKITKLPIEDLDMQGKKLLAKINAMAPPGGQAPTNSGGPDMDSGPSSAGQQSQPSQQSRSVGGNPDMSAAVNKALRQIELIHTGQEKLLMLWQHKKVKLDQCFQWRLFEQDCEKMFDWILHNRDVFQMSYVEIGHNYSVAKSLQDEHQKFAVASMNVSVNIDRILAVAARLIESQHYAAQHIKTLAQRLDRTWKDFAAGLDERTAVLQLSVLFHHKAEQYCNSVASWAAACQASQPLPSDIQSLETAIRTHQSLYEAMCQAYTEVHSTSKKLLYQLDHLVQVCNQPPPPGVPDHRKNSNNGSFNKYERQNPAADYSEGASHVLAVIHQILSHHRTLEAKWHQERLRLHQTLALRLFQEDVKQVLDWLKNHGEVFLRKNTGIGRNFHKARVYQTSHDNFENVAQNTYSNAQKLLAAADELARSGEADPNEIYSVARELELQVGSFAERVEQRRRRLDMAVIFYTHEKDVTAWIDKLRTDVSTDETRLSQENLEGIERILQQYQRDQQESSVNVCLTTISQGEALLQEMRSLEYADNTGSIAALEATLEKLNKQKVELEELWSARKFRADLILRLRYFERDARLLSVQMEMWSEELQHADLSRDYQKAEQLIRMHNESVTEIQNATYEVVQQGQDLLQLFENAGFISMADATHTAQARIEYLLDFLREREIDLEEMSEAKRAKLEQAVQLCQFQNDANQVISWIRNGEAMLVASFVTPNSLQEAEQLRKGHEQFQIAIEKTHTSAVQVKYRADALINANHYDPLSIDEISDDVTKKWQQLVTYAEERHKLVTASINFYKTAEQVCSVLDSLEREYKREDDWCDGGGGSDKAQAIVQLISKHQEQKEAFLKACTLARRTAETFLKYANRSQQCYQYKGNCEGHVKSKLDKLLTQENQVLDYWTLRKKSLDQCQQFVLFERSAKQAIEWIHNTGEAYLSSRSNLVGISKEETEGLLKEHNEFRSTAKETRERVKLLIQLADSLVEKGHAHASDIKQWVASVDQRYKDFSNRMDSYCEQLEKSLGMSQQQLLLGSDGNSSISSSSGDRHSDPTLEAKLNSSNKENKEINEEKRKSARRKEFIMAELMQTERAYVNDLATCIKCFLEEFRAGKSVPSALIGQEDVIFGNIKEIHHFHQKIFLRELEKYETMPEDVGHCFVTWASKFDMYVHYCKNKPTSNNLLVQHGGSFFEELQRRLEVDHPLPAYLIKPVQRITKYQLLLKDLLSCCEESHGEIKEGLEVMLNVPKKANDAMHLSLLENCDVSVDKLGEVVLQDAFQAWDTKQIIRKGRERRVFLFELYLLFAKEVKESNVVKYQFKSKLMTTDMGITEHIEGDETKFAVWTGRSPMLSDCRIVLKATSLETKQIWVKKLREVMQETCFSGTSLTLPKSPAKHSGSSQRSSRDLDEQLTENDHDRCSLASFGSGNTTDSDNKLGNQEATWVVADYIATSGSNELSVSKGQQVEIVEPPTAGEPDFCLVRLNPQHDDAAVQEGLVPVSVLKPPPGSHKHGSGTAANAASSAGSQKSDMQDQSNRSKADALSSSTKRRGFSGRNWLPLMNRKGTDKPPSSKPLVKKPSEKNLRTPQKHAEELAEQQNQQPGASPATVLPSSQFPSSTQHPGGAGAGDYEPDEEVGLELPPPMKPIQEPHLIANGPPAFAKDAKESSGNMASPGKMDGNPLSEIEEIVKTTTEQHESNSRVDGGGGVENASTNGHGRSHDNNDESHTAVSDKAAALKKRQCVFAELMSTEEAYVQDLHEIVNGYMTEINNTNSDIPMPEDLKGGKMKLVFNNIKDIYEWHRDFFLRALRNCQKSPADLGPLIKRSATKFALYYTYCSNKPLSEYIVSAHYQYFDSIRQKLGHRLDLSNLIIKPVQRITKYELLIKEIIKATEGAGLYKEVPMLQEAYQQMKVVVKTVNDMMVVLRSLQDFDGEITAQGSLLMQGPMNCVVDAAQKHRELQVFLFQQIIIFADIEKTKNQYASPIFKYRSHIQLNHMQMKELGDCRFQIRSTDPKIPEMTIICQAASQENYAGWRDMLNKILQQQNDLIFMLSNPLSTKNK
Protein: Transcription factor VOZ2 (Protein VASCULAR PLANT ONE-ZINC FINGER 2) (AtVOZ2) (Q9SLB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator acting positively in the phytochrome B signaling pathway. Functions redundantly with VOZ1 to promote flowering downstream of phytochrome B (phyB). Down-regulates 'FLOWERING LOCUS C' (FLC) and up-regulates 'FLOWERING LOCUS T' (FT). Binds to the 38-bp cis-acting region of the AVP1 gene. Binds as a dimer to the palindromic sequence 5'-GCGTNNNNNNNACGC-3'. Interacts with phyB in the cytoplasm and is translocated to the nucleus at signal transmission, where it is subjected to degradation in a phytochrome-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22904146}. Nucleus {ECO:0000269|PubMed:22904146}. Note=Cytoplasmic in darkness, and translocated to the nucleus depending on the light quality mediated by phytochromes.
Interaction partners:
- Phytochrome B
- Pirin-1
- TRAF-like family protein
- Gb|AAF32477.1
- Pyrophosphate-energized vacuolar membrane proton pump 1
- DNA ligase-like protein
- Uncharacterized protein At1g23150
- RGS1-HXK1-interacting protein 1
Sequence:
MSNHPKITSAHQNVEEKLRELQERFCHLQAARKEGRHGDLALLEAQISQNIREWQAELTAPSPESSLLGEGISQFLEEFAPLLKLDEEDDATSTLKEHAGAKPDPEGFSQSLCPPEWTSENFSQSPFNGNFSCGFEDALNSTETHGQQLHYGYEGFDPSINSAPDFHDQKLSSNLDITSQYDYIFSEVRQELDNSPSTKLDSSEEIDNFAEFSTPSSVRVPPSAFLGPKCALWDCTRPAQGSEWYLDYCSNYHGTLALNEDSPGTAPVLRPGGISLKDNLLIDALRAKTQGKNVGIPVCEGAVNTKCPWNAAELFHLELVEGETIREWLFFDKPRRAYDSGNRKQRSLPDYSGRGWHESRKQLMKEQEGQKRSYYMDPQPPGPFEWHLFEYQINESDACALYRLELKVGNGKKSPKGKISKDPLADLQKKMGQFKVASDKPSPPTKGRKE
Protein: Tellurite resistance protein TehA homolog (P44741)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Ion channel involved in potassium tellurite resistance.
Subcellular location: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MLHFAHIFQNKVHTMNITKPFPLPTGYFGIPLGLAALSLAWFHLENLFPAARMVSDVLGIVASAVWILFILMYAYKLRYYFEEVRAEYHSPVRFSFIALIPITTMLVGDILYRWNPLIAEVLIWIGTIGQLLFSTLRVSELWQGGVFEQKSTHPSFYLPAVAANFTSASSLALLGYHDLGYLFFGAGMIAWIIFEPVLLQHLRISSLEPQFRATMGIVLAPAFVCVSAYLSINHGEVDTLAKILWGYGFLQLFFLLRLFPWIVEKGLNIGLWAFSFGLASMANSATAFYHGNVLQGVSIFAFVFSNVMIGLLVLMTIYKLTKGQFFLK
Protein: Sulfotransferase 1A1 (ST1A1) (EC 2.8.2.1) (Aryl sulfotransferase) (Phenol sulfotransferase) (Phenol/aryl sulfotransferase) (mSTp1) (ST1A4) (Sulfokinase) (P52840)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (By similarity). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (By similarity). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P17988}.
Interaction partners:
- Sulfotransferase 1C2
- Sulfotransferase 4A1
- UDP-glucuronosyltransferase 1A1
- Sulfotransferase 1E1
- Cytochrome P450 1A2
Sequence:
MEPLRKPLVPVKGIPLIKYFAETMEQLQNFTAWPDDVLISTYPKSGTNWMSEIMDMIYQGGKLDKCGRAPVYARIPFLEFSCPGVPPGLETLKETPAPRIIKTHLPLSLLPQSLLDQKIKVIYVARNAKDVVVSYYNFYKMAKLHPDPGTWESFLENFMDGKVSYGSWYQHVKEWWELRRTHPVLYLFYEDMKENPKREIKKILEFLGRSLPEETVDLIVHHTSFKKMKENPMANYTTIPTEVMDHTIYPFMRKGTIGDWKNTFTVAQSEHFDAHYAKLMTGCDFTFRCQI
Protein: Lysyl oxidase homolog 3 (EC 1.4.3.-) (EC 1.4.3.13) (Lysyl oxidase-like protein 3) (P58215)
Organism: Homo sapiens (Human)
Function: Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (By similarity). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated. Also able to catalyze deacetylation of lysine residues on STAT3.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:Q9Z175}. Cytoplasm {ECO:0000269|PubMed:28065600}. Nucleus {ECO:0000269|PubMed:28065600}. Note=It is unclear how LOXL3 is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (LOXL2) also has intracellular and extracellular localization despite the presence of a signal sequence (PubMed:28065600). {ECO:0000269|PubMed:28065600}.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17018530}. Secreted, extracellular space {ECO:0000269|PubMed:17018530}.
Interaction partners:
- Bone morphogenetic protein 1
- Elastin
- Fibulin-5
Sequence:
MRPVSVWQWSPWGLLLCLLCSSCLGSPSPSTGPEKKAGSQGLRFRLAGFPRKPYEGRVEIQRAGEWGTICDDDFTLQAAHILCRELGFTEATGWTHSAKYGPGTGRIWLDNLSCSGTEQSVTECASRGWGNSDCTHDEDAGVICKDQRLPGFSDSNVIEVEHHLQVEEVRIRPAVGWGRRPLPVTEGLVEVRLPDGWSQVCDKGWSAHNSHVVCGMLGFPSEKRVNAAFYRLLAQRQQHSFGLHGVACVGTEAHLSLCSLEFYRANDTARCPGGGPAVVSCVPGPVYAASSGQKKQQQSKPQGEARVRLKGGAHPGEGRVEVLKASTWGTVCDRKWDLHAASVVCRELGFGSAREALSGARMGQGMGAIHLSEVRCSGQELSLWKCPHKNITAEDCSHSQDAGVRCNLPYTGAETRIRLSGGRSQHEGRVEVQIGGPGPLRWGLICGDDWGTLEAMVACRQLGLGYANHGLQETWYWDSGNITEVVMSGVRCTGTELSLDQCAHHGTHITCKRTGTRFTAGVICSETASDLLLHSALVQETAYIEDRPLHMLYCAAEENCLASSARSANWPYGHRRLLRFSSQIHNLGRADFRPKAGRHSWVWHECHGHYHSMDIFTHYDILTPNGTKVAEGHKASFCLEDTECQEDVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVKPGNYILQVVINPNFEVAESDFTNNAMKCNCKYDGHRIWVHNCHIGDAFSEEANRRFERYPGQTSNQII
Protein: N(6)-adenine-specific methyltransferase METTL4 (Methyltransferase-like protein 4) (N(6)-adenine-specific DNA methyltransferase METTL4) (EC 2.1.1.72) (snRNA (2'-O-methyladenosine-N(6)-)-methyltransferase METTL4) (EC 2.1.1.-) (Q3U034)
Organism: Mus musculus (Mouse)
Function: N(6)-adenine-specific methyltransferase that can methylate both RNAs and DNA. Acts as a N(6)-adenine-specific RNA methyltransferase by catalyzing formation of N6,2'-O-dimethyladenosine (m6A(m)) on internal positions of U2 small nuclear RNA (snRNA): methylates the 6th position of adenine residues with a pre-deposited 2'-O-methylation (By similarity). Internal m6A(m) methylation of snRNAs regulates RNA splicing (By similarity). Also able to act as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)-methyladenosine). The existence of N(6)-methyladenosine (m6A) on DNA is however unclear in mammals, and additional evidences are required to confirm the role of the N(6)-adenine-specific DNA methyltransferase activity of METTL4 in vivo (By similarity). Acts as a regulator of mitochondrial transcript levels and mitochondrial DNA (mtDNA) copy number by mediating mtDNA N(6)-methylation: m6A on mtDNA reduces transcription by repressing TFAM DNA-binding and bending (By similarity). N(6)-methyladenosine deposition by METTL4 regulates Polycomb silencing by triggering ubiquitination and degradation of sensor proteins ASXL1 and MPND, leading to inactivation of the PR-DUB complex and subsequent preservation of Polycomb silencing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8N3J2}.
Interaction partners:
- N
- Pre-mRNA-splicing regulator WTAP
- Protein virilizer homolog
- N
- RNA-binding protein 15
- Methyltransferase HEMK2
- RNA N
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- Nucleic acid dioxygenase ALKBH1
- RNA demethylase ALKBH5
Sequence:
MSVVHHLPPGWLLDHLSFINKVNYQLCQHQESFCSKNNPTSSVYMDSLQLDPGSPFGAPAMCFAPDFTTVSGNDDEGSCEVITEKYVFRSELFNVTKPYIVPAVHKERQQSNKNENLVTDYKQEVSVSVGKKRKRCIAFNQGELDAMEYHTKIRELILDGSSKLIQEGLRSGFLYPLVEKQDGSSGCITLPLDACNLSELCEMAKHLPSLNEMELQTLQLMGDDVSVIELDLSSQIIENNSSFSKMITLMGQKYLLPPQSSFLLSDISCMQPLLNCGKTFDAIVIDPPWENKSVKRSNRYSSLSPQQIKRMPIPKLAAADCLIVTWVTNRQKHLCFVKEELYPSWSVEVVAEWYWVKITNSGEFVFPLDSPHKKPYECLVLGRVKEKTPLALRNPDVRIPPVPDQKLIVSVPCVLHSHKPPLTEVLRDYIKPGGQCLELFARNLQPGWMSWGNEVLKFQHMDYFIALESGC
Protein: Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (hPlk2) (Serine/threonine-protein kinase SNK) (hSNK) (Serum-inducible kinase) (Q9NYY3)
Organism: Homo sapiens (Human)
Function: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15242618, ECO:0000269|PubMed:19001868}. Cell projection, dendrite {ECO:0000250}. Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase.
Interaction partners:
- Centrosomal P4.1-associated protein
- Separin
- Cellular tumor antigen p53
- Nucleophosmin
- Disintegrin and metalloproteinase domain-containing protein 17
- Alpha-synuclein
- Serine/threonine-protein phosphatase 4 catalytic subunit
Sequence:
MELLRTITYQPAASTKMCEQALGKGCGADSKKKRPPQPPEESQPPQSQAQVPPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYIDTHNRVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPTTTVARSGTPAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICSQNEEYLLTYINEDRISTTFRLTTLLMSGCSSELKNRMEYALNMLLQRCN
Protein: Uncharacterized protein (A0A178UH48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MQSLTSNEVAGLAVGALLLGATIAAPKVDAFIAASQRRSLGMCRKCGDLKNVACGRCKGTGTIKSGGFFGFSDSSNTRSVACDNCQAKGCFPCPECSKS
Protein: Actin-interacting protein 3 homolog (O13735)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the organization and/or function of the actin cytoskeleton.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Actin
- Formin-3
- Uncharacterized protein C3G9.05
- Tip elongation aberrant protein 1
- Tip elongation aberrant protein Tea4
- Cell division control protein 42 homolog
- Profilin
- Tip elongation protein 1
- Microtubule integrity protein mal3
- Tip elongation aberrant protein 3
Sequence:
MFNNGDNMSRERFSSNHSMQRQKTESRANFSRRLVPSDSNRKPVPNGASNSPLSRDAASHLISTIETSIMKLLVVTKELLESLTNWSKGTVNDSAVSSVYVTLIGEFLQTTKSFHEAGIETADLNDFPLELRSVLEQTLEKTPSSDALETNLPNVRELVMHLLQSLKYKQSLVKSRLNQSRSNLPQMTREANDNDVNRRNSRGSSQGSISSFRNPDSRKQYEETTSASLSAPGAFDALKQTNALERRASKRLSHMVKDQQNNEGSSQNLRNITVESVRGFLRDSSKPDNIMDSPSPKVSKRPSIVRQDSHDSNKLSRRPTINTSFDRKFSPKLTRTPSLTKSLDPGTPTSLKSPSLRKSPSSFVQKDVYSRSNSLRISQANRSNVFPGATDVTRSVSDHRILSSSTINDGEVAPPLPQRSRTISSPNSPLSATVLPSSTPILLPRGRSSTLSVNKKQFNADDGSTLNSPNSIRETEEYAASPKLEDIADEVETDATSQRELLERQIQKAESSEDTSEIESLQGKLSLPQVSSTQQEIQPSSSVPEAASNEIAEKEPAVTAIESITERKEEAPVISSSEKIESGTSISTSDTKGGLANFENDSLEELERLIQQNNAEQDEPSYKFHKYEYSSEESGSEDEFKSEKDTKGYVISNDDSTQVEEDSEDKSTPNTGASAKLINDPSSTITVSDVYPKKPASPVEITEPPSSALVSATSPTTNVPIVPEAVHLSTAFSTAPVSTIVSNISPLPTVAPPNVSGSPSETPISKPEKVPVVSQTEKALPKPLGVDTEKYYFLRYNNQTRKVKVESPLSNANELGELFSNVYKISFSGDSYELNIEDPDTKISYLLEDLSDLKYKSLVSFMFKEQDANKKREDFHSGEVSAIQHSSAQNTLDDHVNTTTHESPSSAFTEILERLKAIEQNISTNHTNDSAALKSSEDHSKLANNFSVPDSIDHKFYQQVKNMQLELASLKQISAAFFTRIPLKIKDFKKEINAFNEKGSLDFQFGRGFVLSSKDRIEREVKNVVEKFDEVNDQIELMRSDVLLRKVRPGLDQTSQLNEESAYLEKRIQTLERSLEEVTPIWKKQWERELNAIVQEQEFLDSHTVLISDLKRDLSALSTVLSNVSAIAELQAKSSIKSKPLTLKTATESEIKGYRDQIQLEVLNLKPDSEARLQAIERSELLQKKRLLQRVDEFSKEVKTFVENEKLNKIGGAEEADRIRTIQDEKVRKILWDDFVSSKRNGKNGGSFIEESSDTVLDEHVVPDNSAKATVAEIDYGSQVDTENFMLERSPLATPKPLKQPDFNIYETPIVRSTAHETDDEQTPSKYSDNRVESSSDTVFENTDLKYDNNVQMSKVTHHVRHDTISTDDYDAYEDAEDVEETSLT
Protein: Polyamine oxidase 7 (OsPAO7) (EC 1.5.3.-) (Q0J290)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives. Substrate preference is spermine > spermidine > N(1)-acetylspermine > N(1)-acetylspermidine > norspermine > thermospermine. No activity detected when putrescine is used as substrate. May play a role in producing hydrogen peroxide for secondary wall thickening through lignin formation during anther development (Probable).
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:24634478}.
Interaction partners:
- Aminopropyl transferase
- Spermidine synthase 1
- Polyamine oxidase 3
- Polyamine oxidase 5
- Polyamine oxidase 4
- Os02g0254700 protein
- Polyamine oxidase 1
- Amine oxidase
- Amine oxidase
- Amine oxidase
Sequence:
MTKPTTMAIFLSIVLLSMAQLPSLVAGTGRPRVIIIGAGISGISAGKRLSEAGITDILILEATDHIGGRMHKQRFAGVNVEIGANWVEGVNGEKMNPIWPIVNSTLKLRNFLSDFDSLAQNVYKDGGLCDAAYVQKRIDLADEADKSGENLSATLHPSGRDDMSILSMQRLNNHLPNGPSSPVDMVVDYFTYDYEFAEPPRVTSLRNTVPLPTFTDFGDDNYFVADQRGYEAVVYYLAGQYLEADKSGNIVDARLQLNKVVREISYSSTGVTVKTEDNSTYQADYVMVSASLGVLQSDLIQFKPQLPSWKILAIYQFDMAVYTKIFVKFPKKFWPEGAGREFFLYASTRRGYYGVWQEFEKQYPDANVLLVTVTDEESRRIEQQPDSQTKAEIMEVVRSMFPDEDVPDATDILVPRWWSDRFFQGSFSNWPIGVSRYEHDQLRAPVGRVYFTGEHTSERYNGYVHGAYLAGIYA
Protein: Elongator complex protein 1 (Gamma-toxin target 1) (Protein IKI3) (Q06706)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. Functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitivity to Pichia inositovora toxin. ELP1/IKI3 binds to tRNA, mediating interaction of the elongator complex with tRNA. Independently, may be involved in polarized exocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15780940, ECO:0000269|PubMed:24750273}. Nucleus {ECO:0000269|PubMed:10024884, ECO:0000269|PubMed:24750273}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:24750273}.
Interaction partners:
- Elongator complex protein 5
- Elongator complex protein 6
- Elongator complex protein 3
- Elongator complex protein 2
- Elongator complex protein 4
- Protein KTI12
- Adenylyltransferase and sulfurtransferase UBA4
- Diphthamide biosynthesis protein 3
- Cytoplasmic tRNA 2-thiolation protein 1
- Casein kinase I homolog HRR25
Sequence:
MVEHDKSGSKRQELRSNMRNLITLNKGKFKPTASTAEGDEDDLSFTLLDSVFDTLSDSITCVLGSTDIGAIEVQQFMKDGSRNVLASFNIQTFDDKLLSFVHFADINQLVFVFEQGDIITATYDPVSLDPAETLIEIMGTIDNGIAAAQWSYDEETLAMVTKDRNVVVLSKLFEPISEYHLEVDDLKISKHVTVGWGKKETQFRGKGARAMEREALASLKASGLVGNQLRDPTMPYMVDTGDVTALDSHEITISWRGDCDYFAVSSVEEVPDEDDETKSIKRRAFRVFSREGQLDSASEPVTGMEHQLSWKPQGSLIASIQRKTDLGEEDSVDVIFFERNGLRHGEFDTRLPLDEKVESVCWNSNSEALAVVLANRIQLWTSKNYHWYLKQELYASDISYVKWHPEKDFTLMFSDAGFINIVDFAYKMAQGPTLEPFDNGTSLVVDGRTVNITPLALANVPPPMYYRDFETPGNVLDVACSFSNEIYAAINKDVLIFAAVPSIEEMKKGKHPSIVCEFPKSEFTSEVDSLRQVAFINDSIVGVLLDTDNLSRIALLDIQDITQPTLITIVEVYDKIVLLRSDFDYNHLVYETRDGTVCQLDAEGQLMEITKFPQLVRDFRVKRVHNTSAEDDDNWSAESSELVAFGITNNGKLFANQVLLASAVTSLEITDSFLLFTTAQHNLQFVHLNSTDFKPLPLVEEGVEDERVRAIERGSILVSVIPSKSSVVLQATRGNLETIYPRIMVLAEVRKNIMAKRYKEAFIVCRTHRINLDILHDYAPELFIENLEVFINQIGRVDYLNLFISCLSEDDVTKTKYKETLYSGISKSFGMEPAPLTEMQIYMKKKMFDPKTSKVNKICDAVLNVLLSNPEYKKKYLQTIITAYASQNPQNLSAALKLISELENSEEKDSCVTYLCFLQDVNVVYKSALSLYDVSLALLVAQKSQMDPREYLPFLQELQDNEPLRRKFLIDDYLGNYEKALEHLSEIDKDGNVSEEVIDYVESHDLYKHGLALYRYDSEKQNVIYNIYAKHLSSNQMYTDAAVAYEMLGKLKEAMGAYQSAKRWREAMSIAVQKFPEEVESVAEELISSLTFEHRYVDAADIQLEYLDNVKEAVALYCKAYRYDIASLVAIKAKKDELLEEVVDPGLGEGFGIIAELLADCKGQINSQLRRLRELRAKKEENPYAFYGQETEQADDVSVAPSETSTQESFFTRYTGKTGGTAKTGASRRTAKNKRREERKRARGKKGTIYEEEYLVQSVGRLIERLNQTKPDAVRVVEGLCRRNMREQAHQIQKNFVEVLDLLKANVKEIYSISEKDRERVNENGEVYYIPEIPVPEIHDFPKSHIVDF
Protein: Serine/threonine-protein kinase pak-2 (EC 2.7.11.1) (p21-activated kinase 2) (G5EFU0)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which plays a redundant role with pak-1 in embryogenesis but, in contrast to pak-1, is not involved in commissural axon guidance of ventral cord motoneurons or in distal tip cell (DTC) migration.
Interaction partners:
- NCK adaptor protein family
- Serine/threonine-protein kinase pak-1
- Ras-like GTP-binding protein rhoA
- Ras-related protein ced-10
- Cell division control protein 42 homolog
- Rac-like GTPase
- CHp/Wrch Rho-like protein homolog
- Ras-related protein rac-2
- Integrin beta pat-3
- Cdc-42 Related Protein
Sequence:
MNRTFSLRRKVKKSEISTPSNFEHRIHAGFDARSGTYTGLPKQWQALLGPPRSISRPKPMVDPSCITPVDVAELKTVIRGPSSSFRYNSPLPFGMTNSPMPSVARSNSLRISATASPVVNVSSARHSFRPTLPPVSQRGYPFNDPSYAPLPLRNQKPPMSTTFGVEKPHQYQQIITIVAPSRTTTPQLQPKSPSTPQAMRQQPKCTEGVSDEEFRNALKFVVDGTDPRSDLTDYKQIGEGSTGVVEAAYKISTKQIVAVKRMNLRKQQRRELLFNEVSILRQYQHPNIVRFFSSHLVDDELWVVMEFMEGGSLTDIVTATRMTEPQIATISRQVLGALDFLHARKVIHRDIKSDSILLKRDGTVKLTDFGFCGQLSEEVPRRRSLVGTPYWTAAEVIAREPYDTRADIWSFGIMLIEMVEGEPPFFNDQPFQAMKRIRDEHEARFSRHAKVSVELSELLSHCIVKDVNKRWPAKDLLRHPFFAKAQHSSSIAPLLLQLQGNTINGNNPPTHHHSSQITTVIQ
Protein: TcpH (Probable pore-forming membrane protein) (Q1PLH3)
Organism: Clostridium perfringens
Interaction partners:
Sequence:
MENVKINIYSKFLYLKNKLTYKNILKAIVIIATIVIAYNCLTKIAYADGFLSYGNSDDPYKNIPEGWGMFISEKYRNNYALDIIDTHGWELIDKAITGLTNIVFSGIVMISWFGVNIFRFCFTNDIAAGFANQLNSVLGSLNNGIFNNFFMIVFMISLFSIVYNLYKKNFSAIGSQILAVAIIYATTAFLSNGAVGFLSKTTEFSKTIGTSAIVAINGKDNNEGSLEDYSKTVVGTLWGNFVQQPWVMLEFDGKVPLNDENMTTKNSINEEALNYSKDILSEPYGSDEREKALESINEKFNKELFSKNGINTKLVSVCVLFVITLIKMIILIAVGMIQIGFQLMSILLILLLPFIMLIAIVPFFGGTNIIKGIARKYLGTQLGIIVSSFVLALLVLVDTVTLTMFQAWGANLIIALLMQCTCWIMVIAFRKQLMNGLINLQNRIAPGTAGAFRFGAKPLDKGADIAKEYAVNPAMDRAYDIGDNLITKAQYAKEYTKGNLSLYKDRKVAQAIDFLGSKYDNLKNNKPEDIENANNPKENIDGVKDTKNKVNSNENINKKPVEKFDLNGVKATKPSNITSENIPNKNINGENKPNIDEDAVTKNDIKDPIENKDIAPKTIDENIKNNGNDNGTIQDKSPGSKENKTISEDEEITTKPEEIKTPEKTINKENLNELKNENTSADKKNNDSNSSNISVTEIPEDLVEEKSVEAINKAKNDVKANKEKINNNINSKNVESNPEVKENIEVASSPEVTEIKKKSTKKVENIKNNGQPKEKSADKKEIKEVSTKERVERVKSFMGVSNKDIKSKEKHLENKLEYIKKGNSKNFKKKGS